The Aston Centre for Membrane Protein & Lipid Research (AMPL) is a collaborative team of six principal investigators in biochemistry, pharmacology, protein/lipid chemistry and polymer science. We study the structure and function of membrane proteins and associated lipids, using interdisciplinary approaches and our novel technologies. Our aim is to understand the molecular basis of how cells communicate with their environment and each other, facilitating drug discovery for patient benefit and driving advances in industrial biotechnology. Membrane proteins are the targets of 60% of all pharmaceutical drugs including all top 10 selling prescription drugs, as well as targets for breeding drought- and disease-tolerant crops and generating new industrial microorganisms. Our activities to date show our ability and expertise in creating synergistic projects over a range of scales with demonstrable real-world impact.
Our work is funded by BBSRC (responsive mode, GCRF, iCASE), EPSRC (iCASE), The Wellcome Trust, IB Catalyst, the European Commission (FP6, FP7, H2020, IMI, STREP and International Incoming Fellowships.
MemTrain (Cell Membranes in Industrial Processes Training)
The department of Biosciences at Aston University has recently been awarded the EU Marie Skłodowska-Curie funded COFUND Doctoral Programme entitled MemTrain (Cell Membranes in Industrial Processes Training). The Programme is coordinated by Dr Alan Goddard who is a member of the Aston Membrane Protein and Lipid Research Group (AMPL). Please see the projects available under the Opportunities tab below and click here to apply.
Professor Roslyn Bill
Roslyn is Professor of Biotechnology. Her research team characterizes and engineers yeast cells to make recombinant membrane proteins, (especially aquaporins, G protein-coupled receptors and tetraspanins) for biochemical, biophysical and structural analysis. Roslyn has a particular interest in AQP protein chemistry, which she has worked on for 20 years. She discovered the novel pathway whereby a hypotonic stimulus directly induces intracellular calcium elevations through transient receptor potential channels, which trigger AQP relocalization. Her team has published a series of articles describing this regulatory mechanism for human AQPs1, 3, 4 and 5. Roslyn also uses yeast to make a range of soluble proteins, such as enzymes, for biotechnological applications. Examples include the conversion of glucose from waste products into high-value platform chemicals such as malic acid.
Dr Alan Goddard
Alan is a Lecturer in Biochemistry. His research interests all revolve around the cell membrane, modulating both the lipid and protein components to alter the function of the cell. Much of this is done in conjunction with industrial partners including those involved in biotechnology and drug development. Alan is currently the Project Co-ordinator of the H2020 ERA CoBioTech project MeMBrane (MEmbrane Modulation for BiopRocess enhAncemEnt) which involves five academic and two industrial partners focussing on alteration of the cell membrane to reduce the toxicity of high-value chemicals produced by fermentation. Alan also works closely with Green Biologics Ltd. to improve their processes for making butanol using Clostridia. He uses a variety of techniques ranging from protein expression and purification through lipid biophysics to molecular microbiology.
Professor David Poyner
David is Professor of Pharmacology. He is interested in the structure and function of G protein-coupled receptors (GPCRs). In the past he has specialised in the molecular pharmacology of calcitonin gene-related peptide (CGRP), which has a particularly interesting receptor made of a GPCR and an accessory protein called RAMP1. His activities have now expanded to include other receptors in the same family as the CGRP receptor as well as the adenosine 2a receptor. He isolates and purifies GPCRs, studies their function in cells by mutagenesis and pharmacological inhibitors and probes their dynamics by biophysics and molecular modelling.
Dr Alice Rothnie
Alice is a Lecturer in Biochemistry. Her research interests lie in elucidating the mechanistic functional details of transmembrane and membrane associated proteins, which do important jobs in the cell, both in health and disease. Alice is particularly interested in membrane transporters of the ABC (ATP Binding Cassette) superfamily, but her group also works on proteins involved in cellular trafficking, secondary active transporters, ion channels, tetraspanins and GPCRs (G-protein coupled receptors). By fully understanding exactly how a protein works, we can begin to understand how it goes wrong in disease states and how we might be able to target it therapeutically. To carry out this work Alice is keen to develop new methods and techniques that enable us to answer important questions about the target protein; as such she has collaborations with industrial partners examining novel detergents for membrane protein extraction and she has played a major role in developing the ‘detergent free’ SMALP (styrene maleic acid lipid particle) technology for membrane protein extraction, purification, structural and functional characterization.
Professor Corinne Spickett
Corinne is a Professor of Biochemistry. Her research centres on the analysis of protein and lipid modifications in response to oxidative stress. She uses liquid chromatography mass spectrometry for ox-lipidomics and ox-proteomics, which she has applied to studies of LDL in chronic kidney disease, pancreatitis, diabetes, as well as yeast membrane changes under stress. Currently Corinne is the Coordinator of a Horizon-2020 Innovative Training Network “MASTRPLAN”, a MASS spectrometry TRaining network for Protein Lipid adduct Analysis, which involves developing label-free, semi-targeted approaches to identifying oxidized lipid-protein adducts in biological samples. Corinne is also interested in the signalling effects of oxidized membrane phospholipids and proteins, especially in relation to inflammatory diseases.
Prof Andrew Devitt
Andrew is an inflammatory cell biologist whose research over 20 years has focused on the innate immune system and its role in protection and tissue repair through the study of phagocyte clearance of dying (apoptotic) cells and microbial challenge. His focus has been the study of membrane receptors/ligands and cell communication in this clearance process. Current work is now focused on defining the mechanisms by which apoptotic cells communicate via extracellular vesicles (EV). This BBSRC-funded work is revealing novel EV structure-function relationships that underpin tissue repair and regeneration capacity of EV from both apoptotic and viable cells, including mesenchymal stem cells. This has introduced the concept that EV are an active extracellular metabolic compartment capable of modulating inflammation. The ultimate aim of Andrew’s research is to modify inflammation for therapeutic gain either through the inhibition of inflammation (e.g. in cardiovascular disease and regenerative medicine applications) or promoting inflammation (e.g. in tumours).
Dr Zita Balklava
Zita is a Lecturer in Cell Biology. She is interested in deciphering how cell signalling and vesicular trafficking crosstalk by regulating each other. One intriguing example of this crosstalk is provided by the Fibroblast Growth Factor Receptor signalling pathway, which plays an important role in development, tissue homeostasis and cancer. The main theme of her research focuses on decoding the trafficking and downstream signalling of Amyloid Precursor Protein, which plays a key role in Alzheimer’s disease. Most research is carried out in the model organism C. elegans. In collaboration with Prof. Roslyn Bill, she is studying the role of vesicular trafficking in the translocation of aquaporins in mammalian tissue culture systems.
Catarina Afonso is in the final year of her PhD, studying oxidative damage to lipoproteins in health and disease. She is looking at novel approaches to separate lipoproteins containing adducts of oxidized phospholipids and investigating their potential as biomarkers for inflammatory conditions such as diabetes and cardiovascular disease. Her project is supported by the EU Horizon 2020 ITN MASSTRPLAN.
Hoor’s research project aims to study the association between proteins and lipids in the cell membrane. She is particularly focussed on the role of surrounding lipids in the structure and function of the membrane protein, CD81.
Aiman is a 2nd year PhD student. She is investigating the application of SMA polymer derivatives and novel polymers for the solubilisation and purification of membrane proteins.
David is a final year PhD student supported by a BBSRC iCASE studentship in collaboration with Calixar. He is examining the use of novel solubilising agents, calixarenes and SMA (styrene maleic acid co-polymer), to stabilise the ABC transporter MRP4 (multidrug resistance protein 4/ABCC4) during solubilisation and purification.
Rav is a BBSRC CASE student working with Chemoxy Ltd on developing a cell-free cascade to facilitate the conversion of glucose to malic acid. Along with Dr Pinar Karagoz, she is also working on the immobilization of the cascade enzymes to aid enzyme recovery and recyclability.
John’s research focusses on the modulation of the membrane components of industrially-relevant Clostridia strains with the aim to increase their resistance to high value chemicals. His project focusses on the production of butanol and is undertaken in conjunction with Green Biologics Ltd.
Floren is a final year PhD student who is investigating the role of ABC transporters MRP1/ABCC1 and MRP4/ABCC4 in the development and progression of breast cancer.
Jaimin is a 2nd year PhD student. He is using SMA to solubilise and purify large human membrane proteins (MRP1/ABBC1 and BK channel) in order to investigate their function and structure and their interactions with lipids.
Bebiana Sousa’s research is on the effects of oxidized and chlorinated lipid products, their reactions with proteins and how to analyse this by liquid chromatography mass spectrometry. She is a 3rd year PhD student and research associate funded by the Horizon 2020 innovative training network MASSTRPLAN.
Romez solubilises membranes expressing either the adenosine 2a receptor or the calcitonin gene related peptide receptor to form styrene-maleic acid lipid particles (SMALPs). Phage display is being used to generate pharmacologically-active nanobodies against the receptor-SMALPs.
Daniel’s research revolves around the interactions between the calcitonin family of G protein-coupled receptors (GPCRs) and a family of accessory proteins called the receptor activity modifying proteins (RAMPs); these form physiologically relevant, functional units for which there are few drugs available. He is particularly interested in determining the binding interface between these two membrane proteins, with eventual application to drug discovery.
Charlie’s project is centred around understanding the mechanistic role of the transmembrane water channel, aquaporin 4, in the pathological brain swelling caused by traumatic injury and stroke. She uses cell-based and imaging techniques to explore the relocalization of the protein, working as part of #teamaquaporin to identify drug targets and therapies that prevent brain oedema.
Aquaporin 4 (AQP4) is the channel responsible for water flow in and out of the central nervous system (CNS). After traumatic brain injury and ischaemic stroke, it allows water into the CNS and causes cytotoxic brain injury. Abir’s project is designed to aid the understanding of the complete mechanism of AQP4 regulation and specifically to identify steps that can be targeted for inhibition, as well as identifying and validating novel inhibitors of this process.
Monse Román Lara
One of the main challenges in the industrialization of biobased high-value chemicals is the organism’s low tolerance to toxicity as it destroys the cell membrane. Monse’s research focusses on the creation of Clostridial strains that are more resistant to product toxicity through membrane modifications in order to generate improved bioprocesses. Her project is undertaken in conjunction with Green Biologics Ltd. Her PhD is funded by the Mexican National Council for Science and Technology.
Dr Joyce Bennett
Joyce is the Project Manager on the MeMBrane project, responsible for day-to-day running of the projects, organising meetings and reporting on the project.
Dr Michelle Clare
Michelle’s research aims to determine the structural characteristics of a tetraspanin, CD81, that is involved in many biological functions such as cell adhesion, tissue differentiation, immune cell maturation and host-parasite interactions. Michelle is supported by a BBSRC responsive mode grant (to Roslyn Bill), on which she is the researcher co-investigator.
Dr Pinar Karagoz
Pinar is currently working on a BBSRC GCRF project (to Roslyn Bill), on which she is the researcher co-investigator. The project concerns developing a cell-free malic acid production process. She immobilizes key enzymes onto different support materials and analyzes their activities and re-usability.
Dr Philip KitchenPhil is an Aston 50th Anniversary Research Fellow. His research interests are in understanding the structure, function, and physiological roles of the aquaporin family of water channel proteins. Current work is focused on aquaporin-4, the water channel protein that facilitates excessive water entry into the brain and spinal cord following head injury or stroke.
He is characterising the interactions of human aquaporin-4 with proteins involved in intracellular vesicle traffic using cell biology and biophysical techniques, and using organ-on-a-chip technology to study the subcellular localisation of aquaporin-4 in a realistic cell culture model of the human blood-brain barrier, both with the goal of developing new treatments for people who have had a brain injury or stroke.
If you are a PhD qualified researcher from outside of the UK and are interested in applying for a Marie-Curie Fellowship to come and work at Aston on projects of mutual interest (related membrane proteins and lipids or industrial biotechnology) please contact us for further details (also see here).
Interns and Volunteers
Please contact us directly if you are interested in volunteering as a researcher with the AMPL Research group.
If you are interested in applying for a PhD to work with one of us, please contact us directly by email for further details of potential project
MemTrain (Cell Membranes in Industrial Processes Training) Projects
1. Characterisation of extracellular vesicles using microfluidic approaches (uFraction8).
Extracellular vesicles (EV) are released from cells and act as a conduit for transfer of signals between them. However, relatively little is known about how EV act or the key modulators that underpin their function. Due to their small nature, traditional purification methods generally involve high-force regimes e.g. ultracentrifugation. Coupled to this, populations of EV are highly heterogeneous both in terms of size and composition. A key area for understanding is the varying functional effects of these different EV and the molecular basis underpinning their activity.
This project will utilise bespoke proprietary microfluidic chip technology to separate EV from cells and to sub-fractionate them by size under low-force regimes. These chips have been developed by the industrial partner, uFraction8, and have been demonstrated to be capable of separating biological particles on the nanoscale. Once separated, EV population will be subjected to rigorous biochemical (e.g. lipid and protein composition), biophysical (e.g. size, surface charge, membrane fluidity) and functional assays (e.g. control of inflammation). Taken together, these analyses will reveal the underlying properties of different EV populations that are responsible for their activities. This will pave the way to a better understanding of both normal and disease-state EV activity as well as the development of novel EV-based therapeutics.
Academic: Dr Alan Goddard, Aston University: firstname.lastname@example.org
Industrial: Dr Monika Tomecka: email@example.com
2. Optimisation of membrane protein expression and purification (Peak Proteins Ltd)
Peak Proteins Ltd. is involved in the production and supply of bespoke high-quality protein reagents to clients and the delivery of macromolecular structure solutions of client targets, largely to aid pharmaceutical and drug discovery research.
The student will be helping to expand Peak Proteins capabilities to handle membrane protein targets. They will be involved in the development of a rapid, simple and generic approach to membrane protein stability assessment using fluorescent protein tags. The project will include the expression of a number of therapeutically relevant membrane protein targets from different classes, with the initial focus on a serotonin receptor (GPCR) and an iron-sulphur cluster transporter (ABC transporter). Appropriate expression systems will be used, including E. coli, insect cell and HEK systems. New approaches will be benchmarked against traditional methods for assessing membrane protein quality, such as radioligand binding assays, protein activity assays and transport assays.
The student will gain a broad overview of protein production pipelines, from gene construct design, through expression, to protein purification methods. Furthermore, the student will gain specific skills such as tissue culture, membrane protein solubilisation, and biophysical assays for membrane protein assessment. Finally, the student will gain a unique perspective on a career in commercial research from a contract research organisation perspective, including risk management and business development skills.
Academic: Prof Roslyn Bill, Aston University: R.M.Bill@aston.ac.uk
Industrial: Dr Mark Abbott: firstname.lastname@example.org
3. Membrane proteins as antifungal drug targets (F2G)
An estimated 1.5 million people die from invasive fungal infections each year. With limited treatment options and increasing resistance to available therapies, there is an urgent need for new antifungal drugs acting via novel mechanisms of action. To address this issue, this project will investigate membrane proteins as antifungal drug targets. F2G Ltd have antifungal programmes at different stages that target membrane proteins. The phase 2 antifungal compound olorofim acts by inhibiting the mitochondrial membrane protein dihydroorotate dehydrogenase. Additionally, a multi-spanning membrane protein has been identified as the target of a preclinical series of antifungals. Further potential membrane protein targets will also be assessed in this project.
Traditionally, membrane proteins have been difficult to work with so that preparation of recombinant versions of potential drug targets for inhibitor screening has not always been possible. However, the use of innovative purification techniques including SMA lipid particles (SMALPs) has enabled difficult membrane proteins to be purified in their native form allowing their activity to be studied.
This project will apply cutting edge membrane protein technology to the exploration of antifungal drug targets, with the aim of supporting existing drug programmes and identifying potential novel targets.
Academic: Dr Alice Rothnie, Aston University: email@example.com
Industrial: Dr Jason Oliver: firstname.lastname@example.org
4. Development of antibody-based drugs targeting ion channels (Iontas).
Ion channels represent the second largest family of human cell surface proteins and are implicated in a number of diseases including cancer, autoimmunity and chronic pain. To date, most of ion channel drug discovery focused on developing small molecules and peptides as therapeutics. These drug modalities often suffer from poor selectivity for the target ion channel leading to severe side effects and poor efficacy in patients. An attractive alternative is the use of antibody-based therapeutics which can demonstrate superior affinity, selectivity and in vivo half-life. However, the efforts to generate monoclonal antibodies against ion channels are hampered by the difficulties in expression and purification of ion channels in a format suitable for antibody isolation and screening.
Iontas is an innovative antibody-drug discovery company developing a novel platform technology (KnotBodyTM) targeting ion channels using antibody-like molecules. As part of the development of this technology, purified ion channels are extremely desirable. As such, this project will focus on expression, purification and functional analysis of ion channels, using cutting-edge polymer-based technology developed at Aston University. Following this, there will be the opportunity to undertake a substantial placement at Iontas to generate and validate antibodies against the ion channel(s) of interest using phage and/or mammalian display technology. Ultimately, this will aid the development of novel therapeutics.
Industrial: Aneesh Karatt Vellatt: email@example.com
5. Approaches for stabilising wild type membrane proteins for structural and functional characterisation (Calixar)
Membrane proteins are important drug discovery targets for a wide range of diseases. However elucidating the structure and function of native membrane proteins is notoriously challenging. Detergents have been used to solubilize membrane proteins from the lipid bilayer with varying degrees of success concerning protein stability. To try to improve stability many studies use mutagenesis approaches to further stabilise the protein, but this can often affect the structure and function of the protein. CALIXAR is a French SME which specialises in purification technologies for membrane proteins. They have developed a series of stabilising detergents and additives which have been shown to stabilise extracted membrane proteins, maintaining the native conformation in solution.
This collaborative project will include cryo-electron microscopy structural characterization of human transporter protein MRP4 (multidrug resistance protein 4/ABCC4), solubilised and purified using calixarene-based detergents and /or styrene maleic acid (SMA) polymers. In addition novel reconstitution approaches will be investigated to monitor MRP4 function. Finally the project will involve testing of novel polymers and additives developed by Calixar/Aston to evaluate their potential in terms of solubilisation efficiency, stabilization, function and compatibility with downstream techniques. The project will likely involve placements of 1-3 months at Calixar.
Industrial: Anass Jawhari: firstname.lastname@example.org
6. New methods for the analysis of lipids and lipoxidation products using ion mobility mass spectrometry (Waters Ltd).
Aston will be the first academic institution in the UK to take delivery of the new generation cyclic ion mobility mass spectrometry (cIM-MS) instrument from Waters Ltd. This instrument offers a step-change in mass spectrometry capability in a number of areas, but especially in multipass, high-resolution (>500) cIM-MS and multidimensional ion-mobility (cIM-MS)n. The project will exploit the potential of this new technology by developing novel methodologies for ion-mobility separation, characterization and identification of lipids (especially oxidised lipids) and post-translationally modified proteins. The project will run with support and collaboration from scientists at Waters. Initially commercially available lipids and in-house generated samples will be used to establish the new methods. The project will then develop the analysis of complex lipid samples from two biological areas: i) Analysis of membrane lipid profiles and lipids associated with membrane proteins. The focus will be to understand the changes in membrane lipids are responsible for altered tolerance to biofuels and bio-feedstocks in the producing microorganisms, and how changes in lipids associated with membrane proteins affect their activity, using samples being generated in parallel MemTrain projects; and ii) Lipid oxidation in autoimmune diseases. Autoimmune diseases are difficult to treat, and often the epitopes that the autoantibodies recognise that are responsible for the immune response are often unknown. Identification of the epitopes would provide a route to understanding the disease aetiology and may provide a route for intervention. Oxidised gangliosides (glycolipids) may be partly responsible for the development of autoimmune diseases of the nervous system, such as multiple sclerosis and Guillaine-Barre syndrome. The project will develop the analysis of oxidised gangliosides to help to understand their role in disease.
Academic: Prof Andy Pitt, Aston University: email@example.com
If you would like to apply for one of these projects available click here.
Professor Roslyn Bill's publications:
Arif, M, Kitchen, P, Conner, M, Hill, E, Nagel, D, Bill, R, Dunmore, S, Armesilla, A, Gross, S, Carmichael, A, Conner, A & Brown, J 2018, 'Downregulation of aquaporin 3 inhibits cellular proliferation, migration and invasion in the MDA-MB-231 breast cancer cell line' Oncology Letters, vol. 16, no. 1, pp. 713-720. DOI:10.3892/ol.2018.8759
Dilworth, MV, Piel, MS, Bettaney, KE, Ma, P, Luo, J, Sharples, D, Poyner, DR, Gross, SR, Moncoq, K, J. F. Henderson, P, Miroux, B & Bill, RM 2018, 'Microbial expression systems for membrane proteins'Methods. DOI:10.1016/j.ymeth.2018.04.009
Salman, MM, Kitchen, P, Woodroofe, MN, Bill, RM, Conner, AC, Heath, PR & Conner, MT 2017, 'Transcriptome Analysis of Gene Expression Provides New Insights into the Effect of Mild Therapeutic Hypothermia on Primary Human Cortical Astrocytes Cultured under Hypoxia' Frontiers in Cellular Neuroscience, vol. 11, pp. 386. DOI:10.3389/fncel.2017.00386
Salman, MM, Kitchen, P, Woodroofe, MN, Brown, JE, Bill, RM, Conner, AC & Conner, MT 2017, 'Hypothermia increases aquaporin 4 (AQP4) plasma membrane abundance in human primary cortical astrocytes via a calcium/transient receptor potential vanilloid 4 (TRPV4)- and calmodulin-mediated mechanism' European Journal of Neuroscience, vol. 46, no. 9, pp. 2542-2547. DOI:10.1111/ejn.13723
Grove, J, Hu, K, Farquhar, MJ, Goodall, M, Walker, L, Jamshad, M, Drummer, HE, Bill, RM, Balfe, P & McKeating, JA 2017, 'A new panel of epitope mapped monoclonal antibodies recognising the prototypical tetraspanin CD81' Wellcome Open Research, vol. 2, pp. 82. DOI:10.12688/wellcomeopenres.12058.1
Salman, MM, Sheilabi, MA, Bhattacharyya, D, Kitchen, P, Conner, AC, Bill, RM, Woodroofe, MN, Conner, MT & Princivalle, AP 2017, 'Transcriptome analysis suggests a role for the differential expression of cerebral aquaporins and the MAPK signalling pathway in human temporal lobe epilepsy'European Journal of Neuroscience, vol. 46, no. 5, pp. 2121-2132. DOI:10.1111/ejn.13652
Cartwright, S, Bill, RM, Bui, ST, Van, HT & Nguyen, HM 2017, 'Rapid expression and purification of the hepatitis delta virus antigen using the methylotropic yeast Pichia pastoris' BMC Research Notes, vol. 10, 340. DOI:10.1186/s13104-017-2692-8
Tran, A-M, Nguyen, T-T, Nguyen, C-T, Huynh-Thi, X-M, Nguyen, C-T, Trinh, M-T, Tran, L-T, Cartwright, SP, Bill, RM & Tran-Van, H 2017, 'Pichia pastorisversusSaccharomyces cerevisiae: a case study on the recombinant production of human granulocyte-macrophage colony-stimulating factor' BMC Research Notes, vol. 10, no. 1, 148. DOI:10.1186/s13104-017-2471-6
Cartwright, SP, Darby, RAJ, Sarkar, D, Bonander, N, Gross, SR, Ashe, MP & Bill, RM 2017, 'Constitutively-stressed yeast strains are high-yielding for recombinant Fps1: implications for the translational regulation of an aquaporin' Microbial Cell Factories, vol. 16, no. 1, 41. DOI:10.1186/s12934-017-0656-2
Cartwright, SP, Mikaliunaite, L & Bill, RM 2016,Membrane protein production in the Yeast,S. cerevisiae. in I Mus-Veteau (ed.),Heterologous expression of membrane proteins.Methods in Molecular Biology, vol. 1432, Springer, New York (US), pp. 23-35. DOI:10.1007/978-1-4939-3637-3_2
Hardy, D, Bill, RM, Jawhari, A & Rothnie, AJ 2016, 'Overcoming bottlenecks in the membrane protein structural biology pipeline' Biochemical Society Transactions, vol. 44, no. 3, pp. 838-844. DOI:10.1042/BST20160049
Wheatley, M, Charlton, J, Jamshad, M, Routledge, SJ, Bailey, S, La-Borde, PJ, Azam, MT, Logan, RT, Bill, RM, Dafforn, TR & Poyner, DR 2016, 'GPCR-styrene maleic acid lipid particles (GPCR-SMALPs): their nature and potential' Biochemical Society Transactions, vol. 44, no. 2, pp. 619-623. DOI:10.1042/BST20150284
Kitchen, P, Conner, MT, Bill, RM & Conner, AC 2016, 'Structural determinants of oligomerization of the aquaporin-4 channel' Journal of Biological Chemistry, vol. 291, no. 13, pp. 6858-6871. DOI:10.1074/jbc.M115.694729
Routledge, S, Mikaliunaite, L, Patel, A, Clare, M, Cartwright, SP, Bawa, Z, Wilks, MDB, Low, F, Hardy, D, Rothnie, AJ & Bill, RM 2016, 'The synthesis of recombinant membrane proteins in yeast for structural studies' Methods, vol. 95, pp. 26-37. DOI:10.1016/j.ymeth.2015.09.027
Kitchen, P, Day, RE, Salman, MM, Conner, MT, Bill, RM & Conner, AC 2015, 'Beyond water homeostasis: diverse functional roles of mammalian aquaporins' BBA - General Subjects, vol. 1850, no. 12, pp. 2410-2421. DOI:10.1016/j.bbagen.2015.08.023
Kitchen, P, Öberg, F, Sjöhamn, J, Hedfalk, K, Bill, RM, Conner, AC, Conner, MT & Törnroth-Horsefield, S 2015, 'Plasma membrane abundance of human aquaporin 5 is dynamically regulated by multiple pathways' PLoS ONE, vol. 10, no. 11, e0143027. DOI:10.1371/journal.pone.0143027
Day, R, Kitchen, P, Salman, M, Bill, R, Conner, A & Conner, M 2015, 'Rapid tonicity induced re-localisation of endogenous aquaporin 4 in primary rat astrocytes - a therapeutic target for cytotoxic brain oedema?' GLIA, vol. 63, no. Suppl.S1, T13-01B, pp. E406-E407. DOI:10.1002/glia.22870
Kitchen, P, Day, RE, Taylor, LHJ, Salman, MM, Bill, RM, Conner, MT & Conner, AC 2015, 'Identification and molecular mechanisms of the rapid tonicity-induced relocalization of the aquaporin 4 channel'Journal of Biological Chemistry, vol. 290, pp. 16873-16881. DOI:10.1074/jbc.M115.646034
Booe, JM, Walker, CS, Barwell, J, Kuteyi, G, Simms, J, Jamaluddin, MA, Warner, ML, Bill, RM, Harris, PW, Brimble, MA, Poyner, DR, Hay, DL & Pioszak, AA 2015, 'Structural basis for receptor activity-modifying protein-dependent selective peptide recognition by a G protein-coupled receptor' Molecular Cell, vol. 58, no. 6, pp. 1040-1052. DOI:10.1016/j.molcel.2015.04.018
Berger, I & Bill, RM 2015, 'Editorial overview: new protein production tools for structural biology' Current Opinion in Structural Biology, vol. 32, pp. v–vii. DOI:10.1016/j.sbi.2015.05.006
Bill, RM & von der Haar, T 2015, 'Hijacked then lost in translation: the plight of the recombinant host cell in membrane protein structural biology projects' Current Opinion in Structural Biology, vol. 32, pp. 147-155. DOI:10.1016/j.sbi.2015.04.003
Prielhofer, R, Cartwright, S, Graf, AB, Valli, M, Bill, R, Mattanovich, D & Gasser, B 2015, 'Pichia pastorisregulates its gene-specific response to different carbon sources at the transcriptional, rather than the translational, level' BMC Genomics, vol. 16, no. 1, 167. DOI:10.1186/s12864-015-1393-8
Jamshad, M, Charlton, J, Lin, Y-P, Routledge, SJ, Bawa, Z, Knowles, TJ, Overduin, M, Dekker, N, Dafforn, TR, Bill, RM, Poyner, DR & Wheatley, M 2015, 'G-protein-coupled receptor solubilization and purification for biophysical analysis and functional studies, in the total absence of detergent' Bioscience Reports, vol. 35, no. 2, e00188. DOI:10.1042/BSR20140171
Bill, RM 2015, 'Recombinant protein subunit vaccine synthesis in microbes: a role for yeast?' Journal of Pharmacy and Pharmacology, vol. 67, no. 3, pp. 319-328. DOI:10.1111/jphp.12353
Bill, R 2015, ' Recombinant protein subunit vaccine synthesis in microbes: a role for yeast? ' Journal of pharmacy and pharmacology .
Bawa, Z, Routledge, SJ, Jamshad, M, Clare, M, Sarkar, D, Dickerson, I, Ganzlin, M, Poyner, DR & Bill, RM 2014, 'Functional recombinant protein is present in the pre-induction phases ofPichia pastoriscultures when grown in bioreactors, but not shake-flasks' Microbial Cell Factories, vol. 13, no. 1, 127. DOI:10.1186/s12934-014-0127-y
Day, RE, Kitchen, P, Owen, D, Bland, C, Marshall, L, Conner, AC, Bill, RM & Conner, MT 2014, 'Human aquaporins: regulators of transcellular water flow' BBA - General Subjects. DOI:10.1016/j.bbagen.2013.09.033
Bill, RM 2014, 'Playing catch-up withEscherichia coli: using yeast to increase success rates in recombinant protein production experiments' Frontiers in Microbiology, vol. 5, 85. DOI:10.3389/fmicb.2014.00085
Routledge, SJ, Poyner, DR & Bill, RM 2014, 'Antifoams: the overlooked additive?' Pharmaceutical Bioprocessing, vol. 2, no. 2, pp. 103-106. DOI:10.4155/pbp.14.17
Bonander, N, Jamshad, M, Oberthür, D, Clare, M, Barwell, J, Hu, K, Farquhar, MJ, Stamataki, Z, Harris, HJ, Dierks, K, Dafforn, TR, Betzel, C, McKeating, JA & Bill, RM 2013, 'Production, purification and characterization of recombinant, full-length human claudin-1' PLoS ONE, vol. 8, no. 5, e64517. DOI:10.1371/journal.pone.0064517
Hipkiss, AR, Cartwright, SP, Bromley, C, Gross, SR & Bill, RM 2013, 'Carnosine: can understanding its actions on energy metabolism and protein homeostasis inform its therapeutic potential?' Chemistry Central Journal, vol. 7, no. 1, 38. DOI:10.1186/1752-153X-7-38
Conner, AC, Bill, RM & Conner, MT 2013, 'An emerging consensus on aquaporin translocation as a regulatory mechanism' Molecular Membrane Biology, vol. 30, no. 1, pp. 101-112. DOI:10.3109/09687688.2012.743194
Bill, RM & Byrne, B 2013, 'Foreword for EDICT Special Edition, volume 2' Molecular Membrane Biology, vol. 30, no. 2, pp. 113. DOI:10.3109/09687688.2013.761918
Bill, RM & Byrne, B 2012, 'Introduction to EDICT volume 1' Molecular Membrane Biology, vol. 30, no. 1, pp. 2. DOI:10.3109/09687688.2013.742252
Cartwright, SP, Bill, RM & Hipkiss, AR 2012, 'L-carnosine affects the growth of Saccharomyces cerevisiae in a metabolism-dependent manner' PLoS ONE, vol. 7, no. 9, e45006. DOI:10.1371/journal.pone.0045006
Bora, N, Bawa, Z, Bill, RM & Wilks, MDB 2012,The implementation of a design of experiments strategy to increase recombinant protein yields in yeast (review). in RM Bill (ed.),Recombinant protein production in yeast: methods and protocols.Methods in molecular biology, vol. 866, Springer protocols, Humana Press, pp. 115-127. DOI:10.1007/978-1-61779-770-5_11
Routledge, SJ & Bill, RM 2012,The effect of antifoam addition on protein production yields. in RM Bill (ed.),Recombinant protein production in yeast: methods and protocols.Methods in molecular biology, vol. 866, Springer protocols, Humana Press, pp. 87-97. DOI:10.1007/978-1-61779-770-5_9
Conner, MT, Conner, AC, Bland, CE, Taylor, LHJ, Brown, J, Parri, HR & Bill, RM 2012, 'Rapid aquaporin translocation regulates cellular water flow: the mechanism of hypotonicity-induced sub-cellular localization of the aquaporin 1 water channel' Journal of Biological Chemistry, vol. 287, no. 14, pp. 11516-11525. DOI:10.1074/jbc.M111.329219
Bill, RM (ed.) 2012,Recombinant protein production in yeast: methods and protocols. Methods in molecular biology, vol. 866, Springer protocols, Humana Press. DOI:10.1007/978-1-61779-770-5
Bill, RM 2012,Preface. in RM Bill (ed.),Recombinant protein production in yeast: methods and protocols.Methods in molecular biology, vol. 866, Springer protocols, Humana Press, pp. vii.
Bonander, N & Bill, RM 2012,Optimising yeast as a host for recombinant protein production (review). in RM Bill (ed.),Recombinant protein production in yeast: methods and protocols.Methods in molecular biology, vol. 866, Springer protocols, Humana Press, pp. 1-9. DOI:10.1007/978-1-61779-770-5_1
Darby, RAJ, Cartwright, SP, Dilworth, MV & Bill, RM 2012,Which yeast species shall I choose? Saccharomyces cerevisiae versus Pichia pastoris (review). in RM Bill (ed.),Recombinant protein production in yeast: methods and protocols.Methods in molecular biology, vol. 866, Springer protocols, Humana Press, pp. 11-23. DOI:10.1007/978-1-61779-770-5_2
Kitson, SM, Mullen, W, Cogdell, RJ, Bill, RM & Fraser, NJ 2011, 'GPCR production in a novel yeast strain that makes cholesterol-like sterols' Methods, vol. 55, no. 4, pp. 287-292. DOI:10.1016/j.ymeth.2011.09.023
Öberg, F, Sjöhamn, J, Conner, MT, Bill, RM & Hedfalk, K 2011, 'Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: the importance of codon optimization and clone selection'Molecular Membrane Biology, vol. 28, no. 6, pp. 398-411. DOI:10.3109/09687688.2011.602219
Jamshad, M, Lin, Y-P, Knowles, TJ, Parslow, RA, Harris, C, Wheatley, M, Poyner, DR, Bill, RM, Thomas, ORT, Overduin, M & Dafforn, TR 2011, 'Surfactant-free purification of membrane proteins with intact native membrane environment' Biochemical Society Transactions, vol. 39, no. 3, pp. 813-818. DOI:10.1042/BST0390813
Ashe, MP & Bill, RM 2011, 'Mapping the yeast host cell response to recombinant membrane protein production: relieving the biological bottlenecks' Biotechnology Journal, vol. 6, no. 6, pp. 707-714. DOI:10.1002/biot.201000333
Bawa, Z, Bland, CE, Bonander, N, Bora, N, Cartwright, SP, Clare, M, Conner, MT, Darby, RAJ, Dilworth, MV, Holmes, WJ, Jamshad, M, Routledge, SJ, Gross, SR & Bill, RM 2011, 'Understanding the yeast host cell response to recombinant membrane protein production' Biochemical Society Transactions, vol. 39, no. 3, pp. 719-723. DOI:10.1042/BST0390719
Bill, RM, Henderson, PJF, Iwata, S, Kunji, ERS, Michel, H, Neutze, R, Newstead, S, Poolman, B, Tate, CG & Vogel, H 2011, 'Overcoming barriers to membrane protein structure determination' Nature Biotechnology, vol. 29, no. 4, pp. 335-340. DOI:10.1038/nbt.1833
Bonander, N, Jamshad, M, Hu, K, Farquhar, MJ, Stamataki, Z, Balfe, P, McKeating, JA & Bill, RM 2011, 'Structural characterization of CD81-Claudin-1 hepatitis C virus receptor complexes' Biochemical Society Transactions, vol. 39, no. 2, pp. 537-540. DOI:10.1042/BST0390537
Garcia-Caballero, A, Gavira, JA, Pineda-Molina, E, Chayen, NE, Govada, L, Sheikh, KA, Saridakis, E, Boudjemline, A, Swann, MJ, Shaw Stewart, P, Briggs, RA, Kolek, SA, Oberthuer, D, Dierks, K, Betzel, C, Santana, M, Hobbs, JR, Thaw, P, Savill, TJ, Mesters, JR, Hilgenfeld, R, Bonander, N & Bill, R 2011, 'Optimization of protein crystallization: the OptiCryst project' Crystal Growth and Design, vol. 11, no. 6, pp. 2112–2121. DOI:10.1021/cg1013768
Routledge, SJ, Hewitt, CJ, Bora, N & Bill, RM 2011, 'Antifoam addition to shake flask cultures of recombinantPichia pastorisincreases yield' Microbial Cell Factories, vol. 10, no. 17, 17. DOI:10.1186/1475-2859-10-17
Ferndahl, C, Bonander, N, Logez, C, Wagner, R, Gustafsson, L, Larsson, C, Hedfalk, K, Darby, RAJ & Bill, RM 2010, 'Increasing cell biomass in Saccharomyces cerevisiae increases recombinant protein yield: the use of a respiratory strain as a microbial cell factory' Microbial Cell Factories, vol. 9, 47, pp. 47. DOI:10.1186/1475-2859-9-47
Conner, MT, Conner, AC, Brown, J & Bill, RM 2010, 'Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity' Biochemistry, vol. 49, no. 5, pp. 821-823. DOI:10.1021/bi902068b
Darby, RAJ, Jamshad, M, Grgic, L, Holmes, WJ & Bill, RM 2010,Production of recombinant G protein-coupled receptor in yeast for structural and functional analysis. in DR Poyner & M Wheatley (eds),G protein-coupled receptors: essential methods.Wiley-Blackwell, pp. 85-110. DOI:10.1002/9780470749210.ch5
Bonander, N & Bill, RM 2009, 'Relieving the first bottleneck in the drug discovery pipeline: using array technologies to rationalize membrane protein production' Expert Review of Proteomics, vol. 6, no. 5, pp. 501-505. DOI:10.1586/epr.09.65
Holmes, WJ, Darby, RAJ, Wilks, MDB, Smith, R & Bill, RM 2009, 'Developing a scalable model of recombinant protein yield from Pichia pastoris: the influence of culture conditions, biomass and induction regime' Microbial Cell Factories, vol. 8, no. 35, 35, pp. 35. DOI:10.1186/1475-2859-8-35
Chan, KLA, Govada, L, Bill, RM, Chayen, NE & Kazarian, SG 2009, 'Attenuated total reflection-FT-IR spectroscopic imaging of protein crystallization' Analytical Chemistry, vol. 81, no. 10, pp. 3769-3775. DOI:10.1021/ac900455y
Bonander, N, Darby, RAJ, Grgic, L, Bora, N, Wen, J, Brogna, S, Poyner, DR, O' Neill, MAA & Bill, RM 2009, 'Altering the ribosomal subunit ratio in yeast maximizes recombinant protein yield' Microbial Cell Factories, vol. 8, no. 10, 10. DOI:10.1186/1475-2859-8-10
Bonander, N, Ferndahl, C, Mostad, P, Wilks, MDB, Chang, C, Showe, L, Gustafsson, L, Larsson, C & Bill, RM 2008, 'Transcriptome analysis of a respiratory Saccharomyces cerevisiae strain suggests the expression of its phenotype is glucose insensitive and predominantly controlled by Hap4, Cat8 and Mig1' BMC Genomics, vol. 9, no. 365, 365. DOI:10.1186/1471-2164-9-365
Bonander, N, Darby, R, Bill, R & Grgic, L 2008,BMS1 protein expression system, Patent No. GB 0813253.2, IPC No. C12N1/19.
Roach, PCJ, O' Reilly, J, Norbertczak, HT, Hope, RJ, Venter, H, Patching, SG, Jamshad, M, Stockley, PG, Baldwin, SA, Herbert, RB, Rutherford, NG, Bill, RM & Henderson, PJF 2008,Equipping a Research Scale Fermentation Laboratory for Production of Membrane Proteins. inPractical Fermentation Technology.Wiley, pp. 37-67. DOI:10.1002/9780470725306.ch3
Jamshad, M, Rajesh, S, Stamataki, Z, McKeating, JA, Dafforn, T, Overduin, M & Bill, RM 2008, 'Structural characterization of recombinant human CD81 produced in Pichia pastoris' Protein Expression and Purification, vol. 57, no. 2, pp. 206-216. DOI:10.1016/j.pep.2007.10.013
Dr Alan Goddard's publications:
Castell, OK, Dijkman, PM, Wiseman, D & Goddard, A 2018, 'Single molecule fluorescence for membrane proteins' Methods. DOI:10.1016/j.ymeth.2018.05.024
Eales, MG, Ferrari, E, Goddard, A, Lancaster, L, Sanderson, P & Miller, C 2018, 'Mechanistic and phenotypic studies of bicarinalin, BP100 and colistin action on Acinetobacter baumannii' Research in Microbiology. DOI:10.1016/j.resmic.2018.04.005
Dijkman, PM, Castell, OK, Goddard, A, Munoz-Garcia, JC, de Graaf, C, Wallace, MI & Watts, A 2018, 'Dynamic tuneable G protein-coupled receptor monomer-dimer populations' Nature Communications, vol. 9, 1710. DOI:10.1038/s41467-018-03727-6
Bird, JL, Simpson, R, Vllasaliu, D & Goddard, AD 2017, 'Neurotensin receptor 1 facilitates intracellular and transepithelial delivery of macromolecules' European Journal of Pharmaceutics and Biopharmaceutics, vol. 119, pp. 300-309. DOI:10.1016/j.ejpb.2017.06.027
Goddard, AD, Bali, S, Mavridou, DAI, Luque-Almagro, VM, Gates, AJ, Roldán, MD, Newstead, S, Richardson, DJ & Ferguson, SJ 2017, 'TheParacoccus denitrificansNarK-like nitrate and nitrite transporters—probing nitrate uptake and nitrate/nitrite exchange mechanisms' Molecular Microbiology, vol. 103, no. 1, pp. 117-133. DOI:10.1111/mmi.13546
Goddard, AD, Dijkman, PM, Adamson, RJ, dos Reis, RI & Watts, A 2015, 'Reconstitution of membrane proteins: a GPCR as an example' Methods in Enzymology, vol. 556, pp. 405-424. DOI:10.1016/bs.mie.2015.01.004
Basu, S, Leonard, JC, Desai, N, Mavridou, DAI, Tang, KH, Goddard, AD, Ginger, ML, Lukeš, J & Allen, JWA 2013, 'Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists' Eukaryotic Cell, vol. 12, no. 2, pp. 343-355. DOI:10.1128/EC.00304-12
Goddard, AD, Dijkman, PM, Adamson, RJ & Watts, A 2013,Lipid-dependent GPCR dimerization. in PM Conn (ed.),Receptor-receptor interactions.vol. 117, Methods in Cell Biology, vol. 117, Academic Press, London (UK), pp. 341-357. DOI:10.1016/B978-0-12-408143-7.00018-9
Goddard, AD & Watts, A 2012, 'Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerisation' Biophysical Reviews, vol. 4, no. 4, pp. 291-298. DOI:10.1007/s12551-012-0073-z
Goddard, AD & Watts, A 2012, 'Regulation of G protein-coupled receptors by palmitoylation and cholesterol' BMC Biology, vol. 10, 27. DOI:10.1186/1741-7007-10-27
Stevens, JM, Mavridou, DAI, Hamer, R, Kritsiligkou, P, Goddard, AD & Ferguson, SJ 2011, 'Cytochrome c biogenesis System I' FEBS journal, vol. 278, no. 22, pp. 4170-4178. DOI:10.1111/j.1742-4658.2011.08376.x
Mavridou, DAI, Saridakis, E, Kritsiligkou, P, Goddard, AD, Stevens, JM, Ferguson, SJ & Redfield, C 2011, 'Oxidation state-dependent protein-protein interactions in disulfide cascades' Journal of Biological Chemistry, vol. 286, no. 28, pp. 24943-24956. DOI:10.1074/jbc.M111.236141
Tapaneeyakorn, S, Goddard, AD, Oates, J, Willis, CL & Watts, A 2011, 'Solution- and solid-state NMR studies of GPCRs and their ligands' BBA -Biomembranes, vol. 1808, no. 6, pp. 1462-1475. DOI:10.1016/j.bbamem.2010.10.003
Gates, AJ, Luque-Almagro, VM, Goddard, AD, Ferguson, SJ, Roldán, MD & Richardson, DJ 2011, 'A composite biochemical system for bacterial nitrate and nitrite assimilation as exemplified byParacoccus denitrificans' Biochemical Journal, vol. 435, no. 3, pp. 743-753. DOI:10.1042/BJ20101920
Selmi, DN, Adamson, RJ, Attrill, H, Goddard, AD, Gilbert, RJC, Watts, A & Turberfield, AJ 2011, 'DNA-templated protein arrays for single-molecule imaging' Nano Letters, vol. 11, no. 2, pp. 657-660. DOI:10.1021/nl1037769
Goddard, AD, Stevens, JM, Rao, F, Mavridou, DAI, Chan, W, Richardson, DJ, Allen, JWA & Ferguson, SJ 2010, 'c-Type cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE' Journal of Biological Chemistry, vol. 285, no. 30, pp. 22882-22889. DOI:10.1074/jbc.M110.133421
Goddard, AD, Stevens, JM, Rondelet, A, Nomerotskaia, E, Allen, JWA & Ferguson, SJ 2010, 'Comparing the substrate specificities of cytochromecbiogenesis Systems I and II' FEBS journal, vol. 277, no. 3, pp. 726-737. DOI:10.1111/j.1742-4658.2009.07517.x
Hill, C, Goddard, A, Ladds, G & Davey, J 2009, 'The cationic region of Rhes mediates its interactions with specific Gß subunits' Cellular Physiology and Biochemistry, vol. 23, no. 1-3, pp. 1-8. DOI:10.1159/000204075
Mavridou, DAI, Stevens, JM, Goddard, AD, Willis, AC, Ferguson, SJ & Redfield, C 2009, 'Control of periplasmic interdomain thiol: disulfide exchange in the transmembrane oxidoreductase DsbD' Journal of Biological Chemistry, vol. 284, no. 5, pp. 3219-3226. DOI:10.1074/jbc.M805963200
Professor David Poyner's publications:
Uddin, R, Simms, J & Poyner, D 2018, 'Functional characterisation of G protein-coupled receptors'Methods. DOI:10.1016/j.ymeth.2018.02.018
Hay, DL, Garelja, ML, Poyner, DR & Walker, CS 2017, 'Update on the pharmacology of calcitonin/CGRP family of peptides: IUPHAR Review 25' British Journal of Pharmacology, vol. In press. DOI:10.1111/bph.14075
Woolley, MJ, Simms, J, Uddin, S, Poyner, DR & Conner, AC 2017, 'Relative antagonism of mutants of the CGRP receptor extracellular loop 2 domain (ECL2) using a truncated competitive antagonist (CGRP8-37): evidence for the dual involvement of ECL2 in the two-domain binding model' Biochemistry, vol. 56, no. 30, pp. 3877-3880. DOI:10.1021/acs.biochem.7b00077
Woolley, MJ, Reynolds, CA, Simms, J, Walker, CS, Mobarec, JC, Garelja, ML, Conner, AC, Poyner, DR & Hay, DL 2017, 'Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs'Biochemical Pharmacology, vol. in press. DOI:10.1016/j.bcp.2017.07.005
Woolley, MJ, Simms, J, Mobarec, JC, Reynolds, CA, Poyner, DR & Conner, AC 2017, 'Understanding the molecular functions of the second extracellular loop (ECL2) of the calcitonin gene-related peptide (CGRP) receptor using a comprehensive mutagenesis approach' Molecular and Cellular Endocrinology, vol. in press. DOI:10.1016/j.mce.2017.05.034
Routledge, SJ, Ladds, G & Poyner, DR 2017, 'The effects of RAMPs upon cell signalling' Molecular and Cellular Endocrinology, vol. in press. DOI:10.1016/j.mce.2017.03.033
Weston, C, Winfield, I, Harris, M, Hodgson, R, Shah, A, Dowell, SJ, Mobarec, JC, Woodlock, DA, Reynolds, CA, Poyner, DR, Watkins, HA & Ladds, G 2016, 'Receptor activity-modifying protein-directed G protein signaling specificity for the calcitonin gene-related peptide family of receptors' Journal of Biological Chemistry, vol. 291, no. 42, pp. 21925-21944. DOI:10.1074/jbc.M116.751362
Watkins, HA, Chakravarthy, M, Abhayawardana, RS, Gingell, JJ, Garelja, M, Pardamwar, M, McElhinney, JMWR, Lathbridge, A, Constantine, A, Harris, PWR, Yuen, T-Y, Brimble, MA, Barwell, J, Poyner, DR, Woolley, MJ, Conner, AC, Pioszak, AA, Reynolds, CA & Hay, DL 2016, 'Receptor activity-modifying proteins 2 and 3 generate adrenomedullin receptor subtypes with distinct molecular properties' Journal of Biological Chemistry, vol. 291, no. 22, pp. 11657-11675. DOI:10.1074/jbc.M115.688218
Gingell, JJ, Simms, J, Barwell, J, Poyner, DR, Watkins, HA, Pioszak, AA, Sexton, PM & Hay, DL 2016, 'An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology' Cell Discovery, vol. 2, 16012. DOI:10.1038/celldisc.2016.12
Hay, DL, Walker, CS, Gingell, JJ, Ladds, G, Reynolds, CA & Poyner, DR 2016, 'Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins' Biochemical Society Transactions, vol. 44, no. 2, pp. 568-573. DOI:10.1042/BST20150237
Weston, C, Lu, J, Li, N, Barkan, K, Richards, GO, Roberts, DJ, Skerry, TM, Poyner, D, Pardamwar, M, Reynolds, CA, Dowell, SJ, Willars, GB & Ladds, G 2015, 'Modulation of glucagon receptor pharmacology by Receptor Activity-modifying Protein-2 (RAMP2)' Journal of Biological Chemistry, vol. 290, no. 38, pp. 23009-23022. DOI:10.1074/jbc.M114.624601
Weston, C, Poyner, D, Patel, V, Dowell, S & Ladds, G 2014, 'Investigating G protein signalling bias at the glucagon-like peptide-1 receptor in yeast' British Journal of Pharmacology, vol. 171, no. 15, pp. 3651-3665. DOI:10.1111/bph.12716
Watkins, HA, Walker, CS, Ly, KN, Bailey, RJ, Barwell, J, Poyner, DR & Hay, DL 2014, 'Receptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: implications for adrenomedullin and calcitonin gene-related peptide pharmacology' British Journal of Pharmacology, vol. 171, no. 3, pp. 772-788. DOI:10.1111/bph.12508
Hay, DL, Harris, PWR, Kowalczyk, R, Brimble, MA, Rathbone, DL, Barwell, J, Conner, AC & Poyner, DR 2014, 'Structure-activity relationships of the N-terminus of calcitonin gene-related peptide: key roles of alanine-5 and threonine-6 in receptor activation' British Journal of Pharmacology, vol. 171, no. 2, pp. 415-426. DOI:10.1111/bph.12464
Watkins, HA, Rathbone, DL, Barwell, J, Hay, DL & Poyner, DR 2013, 'Structure-activity relationships for a-calcitonin gene-related peptide' British Journal of Pharmacology, vol. 170, no. 7, pp. 1308-1322. DOI:10.1111/bph.12072
Woolley, MJ, Watkins, HA, Taddese, B, Karakullukcu, ZG, Barwell, J, Smith, KJ, Hay, DL, Poyner, DR, Reynolds, CA & Conner, AC 2013, 'The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach' Journal of the Royal Society Interface, vol. 10, no. 88, 20130589. DOI:10.1098/rsif.2013.0589
Kuteyi, G, Barwell, J & Poyner, D 2013, 'Identifying key residues important for CGRP binding to its receptor' FEBS journal, vol. 280, no. S1, SW04.S18-20, pp. 405. DOI:10.1111/febs.12340
Hay, DL, Conner, AC & Poyner, DR 2013,Calcitonin Gene-Related Peptide and Adrenomedullin Receptors. inEncyclopedia of Biological Chemistry: Second Edition.Elsevier, pp. 265-269. DOI:10.1016/B978-0-12-378630-2.00363-7
Vohra, S, Taddese, B, Conner, AC, Poyner, DR, Hay, DL, Barwell, J, Reeves, PJ, Upton, GJG & Reynolds, CA 2013, 'Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies' Journal of the Royal Society Interface, vol. 10, no. 79, 20120846. DOI:10.1098/rsif.2012.0846
Wootten, D, Lindmark, H, Kadmiel, M, Willcockson, H, Caron, KM, Barwell, J, Drmota, T & Poyner, D 2013, 'Receptor Activity Modifying Proteins (RAMPs) interact with the VPAC2Receptor and CRF1receptors and modulate their function' British Journal of Pharmacology, vol. 168, no. 4, pp. 822-834. DOI:10.1111/j.1476-5381.2012.02202.x
Chini, B, Parenti, M, Poyner, DR & Wheatley, M 2013, 'G-protein-coupled receptors: from structural insights to functional mechanisms' Biochemical Society Transactions, vol. 41, no. 1, pp. 135–136. DOI:10.1042/BST20120344
Barwell, J, Wheatley, M, Conner, AC, Taddese, B, Vohra, S, Reynolds, CA & Poyner, DR 2013, 'The activation of the CGRP receptor' Biochemical Society Transactions, vol. 41, no. 1, pp. 180-184. DOI:10.1042/BST20120251
Barwell, J, Gingell, JJ, Watkins, HA, Archbold, JK, Poyner, DR & Hay, DL 2012, 'Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?' British Journal of Pharmacology, vol. 166, no. 1, pp. 51-65. DOI:10.1111/j.1476-5381.2011.01525.x
Hong, Y, Hay, DL, Quirion, R & Poyner, DR 2012, 'The pharmacology of adrenomedullin 2/intermedin'British Journal of Pharmacology, vol. 166, no. 1, pp. 110-120. DOI:10.1111/j.1476-5381.2011.01530.x
Poyner, DR & Hay, DL 2012, 'Secretin family (Class B) G protein-coupled receptors - from molecular to clinical perspectives' British Journal of Pharmacology, vol. 166, no. 1, pp. 1-3. DOI:10.1111/j.1476-5381.2011.01810.x
Barwell, J, Woolley, MJ, Wheatley, M, Conner, AC & Poyner, DR 2012, 'The role of the extracellular loops of the CGRP receptor, a family B GPCR' Biochemical Society Transactions, vol. 40, no. 2, pp. 433-437. DOI:10.1042/BST20110726
Wheatley, M, Wootten, D, Conner, MT, Simms, J, Kendrick, R, Logan, RT, Poyner, DR & Barwell, J 2012, 'Lifting the lid on GPCRs: the role of extracellular loops' British Journal of Pharmacology, vol. 165, no. 6, pp. 1688-1703. DOI:10.1111/j.1476-5381.2011.01629.x
Barwell, J, Wootten, D, Simms, J, Hay, DL & Poyner, DR 2012, 'RAMPs and CGRP receptors' Advances in Experimental Medicine and Biology, vol. 744, pp. 13-24. DOI:10.1007/978-1-4614-2364-5_2
Sexton, PM, Poyner, DR, Simms, J, Christopoulos, A & Hay, DL 2012, 'RAMPs as drug targets'Advances in Experimental Medicine and Biology, vol. 744, pp. 61-74. DOI:10.1007/978-1-4614-2364-5_6
Barwell, J, Conner, AC & Poyner, DR 2011, 'Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function'BBA - Molecular Cell Research, vol. 1813, no. 10, pp. 1906-1916. DOI:10.1016/j.bbamcr.2011.06.005
Conner, AC, Barwell, J, Poyner, DR & Wheatley, M 2011,The use of site-directed mutagenesis to study GPCRs. in GB Willars & RAJ Challiss (eds),Receptor signal transduction protocols.3rd ed edn, Methods in molecular biology, vol. 746, Humana Press, pp. 85-98. DOI:10.1007/978-1-61779-126-0_5
Qi, T, Ly, K, Poyner, DR, Christopoulos, G, Sexton, PM & Hay, DL 2011, 'Structure-function analysis of amino acid 74 of human RAMP1 and RAMP3 and its role in peptide interactions with adrenomedullin and calcitonin gene-related peptide receptors' Peptides, vol. 32, no. 5, pp. 1060-1067. DOI:10.1016/j.peptides.2011.03.004
Hay, DL, Walker, CS & Poyner, DR 2011, 'Adrenomedullin and calcitonin gene-related peptide receptors in endocrine-related cancers: opportunities and challenges' Endocrine-related Cancer, vol. 18, no. 1, pp. C1-14. DOI:10.1677/ERC-10-0244
Qi, T, Simms, J, Bailey, RJ, Wheatley, M, L. Rathbone, D, Hay, DL & Poyner, DR 2010, 'Structure-function analysis of RAMP1-RAMP3 chimeras' Biochemistry, vol. 49, no. 3, pp. 522-531. DOI:10.1021/bi9019093
Walker, CS, Conner, AC, Poyner, DR, Hay, DL & Conner, AC 2010, 'Regulation of signal transduction by calcitonin gene-related peptide receptors' Trends in Pharmacological Sciences, vol. 31, no. 10, pp. 476-483. DOI:10.1016/j.tips.2010.06.006
Chugunov, AO, Simms, J, Poyner, DR, Dehouck, Y, Rooman, M, Gilis, D & Langer, I 2010, 'Evidence that interaction between conserved residues in transmembrane helices 2, 3, and 7 are crucial for human VPAC1 receptor activation' Molecular Pharmacology, vol. 78, no. 3, pp. 394-401. DOI:10.1124/mol.110.063578
Bailey, RJ, Bradley, JWI, Poyner, DR, L. Rathbone, D & Hay, DL 2010, 'Functional characterization of two human receptor activity-modifying protein 3 variants' Peptides, vol. 31, no. 4, pp. 579-584. DOI:10.1016/j.peptides.2009.12.016
Poyner, DR & Wheatley, M (eds) 2010,G protein-coupled receptors: essential methods. Wiley-Blackwell. DOI:10.1002/9780470749210
Miller, PS, Barwell, J, Poyner, DR, Wigglesworth, MJ, Garland, SL & Donnelly, D 2010, 'Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74' Biochemical and Biophysical Research Communications, vol. 391, no. 1, pp. 437-442. DOI:10.1016/j.bbrc.2009.11.076
Barwell, J, Miller, PS, Donnelly, D & Poyner, DR 2010, 'Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor' Peptides, vol. 31, no. 1, pp. 170-176. DOI:10.1016/j.peptides.2009.10.021
Poyner, DR & Wheatley, M 2010,Preface. in DR Poyner & M Wheatley (eds),G protein-coupled receptors: essential methods.Wiley-Blackwell. DOI:10.1002/9780470749210
Poyner, DR, Hay, DL & Conner, AC 2009, 'CGRP receptor antagonists: design and screening' Expert Opinion on Drug Discovery, vol. 4, no. 12, pp. 1253-1265. DOI:10.1517/17460440903413496
Robinson, SD, Aitken, JF, Bailey, RJ, Poyner, DR & Hay, DL 2009, 'Novel peptide antagonists of adrenomedullin and calcitonin gene-related peptide receptors: identification, pharmacological characterization, and interactions with position 74 in receptor activity-modifying protein 1/3' Journal of Pharmacology and Experimental Therapeutics, vol. 331, no. 2, pp. 513-521. DOI:10.1124/jpet.109.156448
Hay, DL & Poyner, DR 2009, 'Calcitonin gene-related peptide, adrenomedullin and flushing' Maturitas, vol. 64, no. 2, pp. 104-108. DOI:10.1016/j.maturitas.2009.08.011
Sexton, PM, Poyner, DR, Simms, J, Christopoulos, A & Hay, DL 2009, 'Modulating receptor function through RAMPs: can they represent drug targets in themselves?' Drug Discovery Today, vol. 14, no. 7-8, pp. 413-419. DOI:10.1016/j.drudis.2008.12.009
Simms, J, Hay, DL, Bailey, RJ, Konycheva, G, Bailey, G, Wheatley, M & Poyner, DR 2008, 'Structure-function analysis of RAMP1 by Alanine Mutagenesis' Biochemistry, vol. 48, no. 1, pp. 198-205. DOI:10.1021/bi801869n
Conner, M, Hicks, MR, Dafforn, T, Knowles, TJ, Ludwig, C, Staddon, S, Overduin, M, Günther, UL, Thome, J, Wheatley, M, Poyner, DR & Conner, AC 2008, 'Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR' Biochemistry, vol. 47, no. 32, pp. 8434-8444. DOI:10.1021/bi8004126
Hay, DL, Poyner, DR & Quirion, R 2008, 'International Union of Pharmacology. LXIX. Status of the calcitonin gene-related peptide subtype 2 receptor' Pharmacological Reviews, vol. 60, no. 2, pp. 143-145. DOI:10.1124/pr.108.00372
Poyner, DR 2008,RAMPs and the modulation of G-protein coupled receptors. inProceeedings of the XXVIII European Section Meeting of the International Society gor Heart Research.Monduzzi, Bologna (IT), pp. 9-11.
Dr Alice Rothnie's publications:
Hall, SCL, Tognoloni, C, Charlton, J, Bragginton, ÉC, Rothnie, AJ, Sridhar, P, Wheatley, M, Knowles, TJ, Arnold, T, Edler, KJ & Dafforn, TR 2018, 'An acid-compatible co-polymer for the solubilization of membranes and proteins into lipid bilayer-containing nanoparticles' Nanoscale, pp. 10609-10619. DOI:10.1039/C8NR01322E
Hardy, D, Desuzinges Mandon, E, Rothnie, A & Jawhari, A 2018, 'The yin and yang of solubilization and stabilization for wild-type and full-length membrane protein' Methods. DOI:10.1016/j.ymeth.2018.02.017
Dannhauser, PN, Camus, SM, Sakamoto, K, Sadacca, LA, Torres, JA, Camus, MD, Briant, K, Vassilopoulos, S, Rothnie, A, Smith, CJ & Brodsky, FM 2017, 'CHC22 and CHC17 clathrins have distinct biochemical properties and display differential regulation and function' Journal of Biological Chemistry, vol. 292, no. 51, pp. 20834-20844. DOI:10.1074/jbc.M117.816256
Pollock, NL, Lee, SC, Patel, JH, Gulamhussein, AA & Rothnie, AJ 2017, 'Structure and function of membrane proteins encapsulated in a polymer-bound lipid bilayer' BBA -Biomembranes, vol. in press. DOI:10.1016/j.bbamem.2017.08.012
Morrison, KA, Akram, A, Mathews, A, Khan, ZA, Patel, JH, Zhou, C, Hardy, DJ, Moore-Kelly, C, Patel, R, Odiba, V, Knowles, T, Javed, M-H, Chmel, NP, Dafforn, TR & Rothnie, AJ 2016, 'Membrane protein extraction and purification using styrene-maleic acid (SMA) co-polymer: effect of variations in polymer structure' Biochemical Journal, vol. 473, no. 23, pp. 4349-4360. DOI:10.1042/BCJ20160723
Rothnie, AJ 2016,Detergent-free membrane protein purification. in I Mus-Veteau (ed.),Heterologous expression of membrane proteins: methods and protocols.2nd edn, Methods in Molecular Biology, vol. 1432. DOI:10.1007/978-1-4939-3637-3
Lee, SC, Khalid, S, Pollock, NL, Knowles, TJ, Edler, K, Rothnie, AJ, Thomas, ORT & Dafforn, TR 2016, 'Encapsulated membrane proteins: a simplified system for molecular simulation' BBA -Biomembranes, vol. In press. DOI:10.1016/j.bbamem.2016.02.039
Currinn, H, Guscott, B, Balklava, Z, Rothnie, A & Wassmer, T 2016, 'APP controls the formation of PI(3,5)P2vesicles through its binding of the PIKfyve complex' Cellular and Molecular Life Sciences, vol. 73, no. 2, pp. 393-408. DOI:10.1007/s00018-015-1993-0
Lin, Y-H, Currinn, H, Pocha, SM, Rothnie, A, Wassmer, T & Knust, E 2015, 'AP-2 complex-mediated endocytosis of Drosophila Crumbs regulates polarity via antagonizing Stardust' Journal of Cell Science, vol. 128, no. 24, pp. 4538-4549. DOI:10.1242/jcs.174573
Gulati, S, Jamshad, M, Knowles, TJ, Morrison, KA, Downing, R, Cant, N, Collins, R, Koenderink, JB, Ford, RC, Overduin, M, Kerr, ID, Dafforn, TR & Rothnie, AJ 2014, 'Detergent-free purification of ABC (ATP-binding-cassette) transporters' Biochemical Journal, vol. 461, no. 2, pp. 269-278. DOI:10.1042/BJ20131477
Wong, K, Ma, J, Rothnie, A, Biggin, PC & Kerr, ID 2014, 'Towards understanding promiscuity in multidrug efflux pumps' Trends in Biochemical Sciences, vol. 39, no. 1, pp. 8-16. DOI:10.1016/j.tibs.2013.11.002
Young, A, Stoilova-McPhie, S, Rothnie, A, Vallis, Y, Harvey-Smith, P, Ranson, N, Kent, H, Brodsky, FM, Pearse, BMF, Roseman, A & Smith, CJ 2013, 'Hsc70-induced changes in clathrin-auxilin cage structure suggest a role for clathrin light chains in cage disassembly' Traffic, vol. 14, no. 9, pp. 987-996. DOI:10.1111/tra.12085
Rothnie, A, Clarke, AR, Kuzmic, P, Cameron, A & Smith, CJ 2011, 'A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin' Proceedings of the National Academy of Sciences, vol. 108, no. 17, pp. 6927-6932. DOI:10.1073/pnas.1018845108
Maeno, K, Nakajima, A, Conseil, G, Rothnie, A, Deeley, RG & Cole, SPC 2009, 'Molecular basis for reduced estrone sulfate transport and altered modulator sensitivity of transmembrane helix (TM) 6 and TM17 mutants of multidrug resistance protein 1 (ABCC1)' Drug Metabolism and Disposition, vol. 37, no. 7, pp. 1411-1420. DOI:10.1124/dmd.109.026633
Heikal, A, Box, K, Rothnie, A, Storm, J, Callaghan, R & Allen, M 2009, 'The stabilisation of purified, reconstituted P-glycoprotein by freeze drying with disaccharides' Cryobiology, vol. 58, no. 1, pp. 37-44. DOI:10.1016/j.cryobiol.2008.10.125
Conseil, G, Rothnie, AJ, Deeley, RG & Cole, SPC 2009, 'Multiple roles of charged amino acids in cytoplasmic loop 7 for expression and function of the multidrug and organic anion transporter MRP1 (ABCC1)' Molecular Pharmacology, vol. 75, no. 2, pp. 397-406. DOI:10.1124/mol.108.052860
Rothnie, A, Conseil, G, Lau, AYT, Deeley, RG & Cole, SPC 2008, 'Mechanistic differences between GSH transport by multidrug resistance protein 1 (MRP1/ABCC1) and GSH modulation of MRP1-mediated transport' Molecular Pharmacology, vol. 74, no. 6, pp. 1630-1640. DOI:10.1124/mol.108.049080
Proffesor Corrinne Spickett's publications:
Pietrzak, J, Spickett, CM, Ploszajc, T, Virág, L & Robaszkiewicz, A 2018, 'PARP1 promoter links cell cycle progression with adaptation to oxidative environment' Redox biology, vol. 18, pp. 1-5. DOI:10.1016/j.redox.2018.05.017
Spickett, CM, Bhurrut, EJ, Sousa, BC, Afonso, CB, Durand, T & Pitt, AR 2018, 'Developing targeted mass spectrometry approaches for the identification of protein lipoxidation' Free Radical Biology and Medicine, vol. 120, no. Suppl 1, pp. S86-S87. DOI:10.1016/j.freeradbiomed.2018.04.286
Afonso, CB, Pitt, AR & Spickett, CM 2018, 'YO-1 Synthesis and separation of peptide-oxidized phospholipid adducts, a potential lipoxidation marker' Free Radical Biology and Medicine, vol. 120, no. Suppl 1, pp. S27. DOI:10.1016/j.freeradbiomed.2018.04.096
Sousa, BC, Ashman, J, Spickett, CM & Pitt, AR 2018, 'Effect of short-chain aldehydes on the enzymatic activity of pyruvate kinase' Free Radical Biology and Medicine, vol. 120, no. Suppl 1, pp. S32. DOI:10.1016/j.freeradbiomed.2018.04.110
Campos-pinto, I, Wilkins, J, Schouten, J, Pitt, A, Spickett, C & Davis, P 2018, 'Immunodetecting lipoxidation: epitope mapping of HNE-modified human serum albumin using two different anti-HNE pAbs' Free Radical Biology and Medicine, vol. 120, no. Suppl 1, pp. S50-S51. DOI:10.1016/j.freeradbiomed.2018.04.167
Baetta, R, Pontremoli, M, Fernandez, AM, Spickett, CM & Banfi, C 2018, 'Reprint of: Proteomics in cardiovascular diseases:: Unveiling sex and gender differences in the era of precision medicine'Journal of Proteomics, vol. 178, pp. 57-72. DOI:10.1016/j.jprot.2018.03.017
Afonso, CB, Sousa, BC, Pitt, AR & Spickett, CM 2018, 'A mass spectrometry approach for the identification and localization of small aldehyde modifications of proteins' Archives of Biochemistry and Biophysics. DOI:10.1016/j.abb.2018.03.026
Knight, AR, Taylor, E, Lukaszewski, R, Tveen Jensen, K, Jones, HE, Carré, JE, supov, MNI, Littlechild, JA, Bailey, SJ, Brewer, E, McDonald, TJ, Pitt, AR, Spickett, CM & Winyard, PG 2018, 'A high-sensitivity electrochemiluminescence-based ELISA for the measurement of the oxidative stress biomarker, 3-nitrotyrosine, in human blood serum and cells' Free Radical Biology and Medicine. DOI:10.1016/j.freeradbiomed.2018.03.026
Verrastro, I, Tveen Jensen, K, Spickett, CM & Pitt, AR 2018, 'The effect of HOCl-induced modifications on phosphatase and tensin homolog (PTEN) structure and function' Free Radical Research, pp. 1-471. DOI:10.1080/10715762.2018.1424333
Campos-Pinto, I, Wilkins, J, Schouten, J, Davis, P & Spickett, CM 2018, 'Detecting lipoxidation: diagnostic tools for the translation and commercial application' Free Radical Biology and Medicine. DOI:10.1016/j.freeradbiomed.2018.05.034
Spickett, CM, Sousa, BC & Pitt, AR 2018, 'Analysis of phospholipid peroxidation and protein lipoxidation products by LC-MS' Free Radical Biology and Medicine. DOI:10.1016/j.freeradbiomed.2018.05.017
Baetta, R, Pontremoli, M, Fernandez, AM, Spickett, CM & Banfi, C 2017, 'Proteomics in cardiovascular diseases: Unveiling sex and gender differences in the era of precision medicine' Journal of Proteomics, vol. Early online. DOI:10.1016/j.jprot.2017.11.012
Egea, J, Fabregat, I, Frapart, YM, Ghezzi, P, Görlach, A, Kietzmann, T, Kubaichuk, K, Knaus, UG, Lopez, MG, Olaso-Gonzalez, G, Petry, A, Schulz, R, Vina, J, Winyard, P, Abbas, K, Ademowo, OS, Afonso, CB, Andreadou, I, Antelmann, H, Antunes, F, Aslan, M, Bachschmid, MM, Barbosa, RM, Belousov, V, Berndt, C, Bernlohr, D, Bertrán, E, Bindoli, A, Bottari, SP, Brito, PM, Carrara, G, Casas, AI, Chatzi, A, Chondrogianni, N, Conrad, M, Cooke, MS, Costa, JG, Cuadrado, A, My-Chan Dang, P, De Smet, B, Debelec-Butuner, B, Dias, IHK, Dunn, JD, Edson, AJ, El Assar, M, El-Benna, J, Ferdinandy, P, Fernandes, AS, Fladmark, KE, Förstermann, U, Giniatullin, R, Giricz, Z, Görbe, A, Griffiths, H, Hampl, V, Hanf, A, Herget, J, Hernansanz-Agustín, P, Hillion, M, Huang, J, Ilikay, S, Jansen-Dürr, P, Jaquet, V, Joles, JA, Kalyanaraman, B, Kaminskyy, D, Karbaschi, M, Kleanthous, M, Klotz, LO, Korac, B, Korkmaz, KS, Koziel, R, Kracun, D, Krause, KH, Kren, V, Krieg, T, Laranjinha, J, Lazou, A, Li, H, Martínez-Ruiz, A, Matsui, R, McBean, GJ, Meredith, SP, Messens, J, Miguel, V, Mikhed, Y, Milisav, I, Milkovic, L, Miranda-Vizuete, A, Mojovic, M, Monsalve, M, Mouthuy, PA, Mulvey, J, Münzel, T, Muzykantov, V, Nguyen, ITN, Oelze, M, Oliveira, NG, Palmeira, CM, Papaevgeniou, N, Pavicevic, A, Pedre, B, Peyrot, F, Phylactides, M, Pircalabioru, GG, Pitt, AR, Poulsen, HE, Prieto, I, Rigobello, MP, Robledinos-Antón, N, Rodríguez-Mañas, L, Rolo, AP, Rousset, F, Ruskovska, T, Saraiva, N, Sasson, S, Schröder, K, Semen, K, Seredenina, T, Shakirzyanova, A, Smith, GL, Soldati, T, Sousa, BC, Spickett, CM, Stancic, A, Stasia, MJ, Steinbrenner, H, Stepanic, V, Steven, S, Tokatlidis, K, Tuncay, E, Turan, B, Ursini, F, Vacek, J, Vajnerova, O, Valentová, K, Van Breusegem, F, Varisli, L, Veal, EA, Yalçin, AS, Yelisyeyeva, O, Žarkovic, N, Zatloukalová, M, Zielonka, J, Touyz, RM, Papapetropoulos, A, Grune, T, Lamas, S, Schmidt, HHHW, Di Lisa, F & Daiber, A 2017, 'Corrigendum to "European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)" [Redox Biol. 13 (2017) 94-162]' Redox Biology, vol. In press. DOI:10.1016/j.redox.2017.10.001
Egea, J, Fabregat, I, Frapart, YM, Ghezzi, P, Görlach, A, Kietzmann, T, Kubaichuk, K, Knaus, UG, Lopez, MG, Olaso-Gonzalez, G, Petry, A, Schulz, R, Vina, J, Winyard, P, Abbas, K, Ademowo, S, Afonso, CB, Andreadou, I, Antelmann, H, Antunes, F, Aslan, M, Bachschmid, MM, Barbosa, RM, Belousov, V, Berndt, C, Bernlohr, D, Bertrán, E, Bindoli, A, Bottari, SP, Brito, PM, Carrara, G, Casas, AI, Chatzi, A, Chondrogianni, N, Conrad, M, Cooke, MS, Costa, JG, Cuadrado, A, My-Chan Dang, P, De Smet, B, Debelec–butuner, B, Dias, I, Dunn, JD, Edson, AJ, El Assar, M, El-Benna, J, Ferdinandy, P, Fernandes, AS, Fladmark, KE, Förstermann, U, Giniatullin, R, Giricz, Z, Görbe, A, Griffiths, H, Hampl, V, Hanf, A, Herget, J, Hernansanz-Agustín, P, Hillion, M, Huang, J, Ilikay, S, Jansen-Dürr, P, Jaquet, V, Joles, JA, Kalyanaraman, B, Kaminskyy, D, Karbaschi, M, Kleanthous, M, Klotz, L-O, Korac, B, Korkmaz, KS, Koziel, R, Kracun, D, Krause, K-H, Kren, V, Krieg, T, Laranjinha, J, Lazou, A, Li, H, Martínez-Ruiz, A, Matsui, R, Mcbean, GJ, Meredith, SP, Messens, J, Miguel, V, Mikhed, Y, Milisav, I, Milkovic, L, Miranda-Vizuete, A, Mojovic, M, Monsalve, M, Mouthuy, P-A, Mulvey, J, Münzel, T, Muzykantov, V, Nguyen, ITN, Oelze, M, Oliveira, NG, Palmeira, CM, Papaevgeniou, N, Pavicevic, A, Pedre, B, Peyrot, F, Phylactides, M, Pircalabioru, GG, Pitt, AR, Poulsen, HE, Prieto, I, Rigobello, MP, Robledinos-Antón, N, Rodríguez-mañas, L, Rolo, AP, Rousset, F, Ruskovska, T, Saraiva, N, Sasson, S, Schröder, K, Semen, K, Seredenina, T, Shakirzyanova, A, Smith, GL, Soldati, T, Sousa, BC, Spickett, CM, Stancic, A, Stasia, MJ, Steinbrenner, H, Stepanic, V, Steven, S, Tokatlidis, K, Tuncay, E, Turan, B, Ursini, F, Vacek, J, Vajnerova, O, Valentová, K, van Breusegem, F, Varisli, L, Veal, EA, Yalçin, AS, Yelisyeyeva, O, Žarkovic, N, Zatloukalová, M, Zielonka, J, Touyz, RM, Papapetropoulos, A, Grune, T, Lamas, S, Schmidt, HHHW, di Lisa, F & Daiber, A 2017, 'European contribution to the study of ROS: a summary of the findings and prospects for the future from the COST Action BM1203 (EU-ROS)' Redox biology, vol. 13, pp. 94-162. DOI:10.1016/j.redox.2017.05.007
Sousa, BC, Pitt, AR & Spickett, CM 2017, 'Chemistry and analysis of HNE and other prominent carbonyl-containing lipid oxidation compounds' Free Radical Biology and Medicine, vol. In press. DOI:10.1016/j.freeradbiomed.2017.02.003
Popat, RJ, Hakki, S, Thakker, A, Coughlan, AM, Watson, J, Little, MA, Spickett, CM, Lavender, P, Afzali, B, Kemper, C & Robson, MG 2017, 'Anti-myeloperoxidase antibodies attenuate the monocyte response to LPS and shape macrophage development' JCI insight, vol. 2, no. 2, e87379. DOI:10.1172/jci.insight.87379
Kativu, P, Pitt, AR & Spickett, CM 2016, 'The effect of cellular oxidative stress on PTEN interactions' pp. S57-S58. DOI:10.1016/j.freeradbiomed.2016.04.123
Ali, AY, Meredith, SP & Spickett, CM 2016, 'Testing anti-sera raised against synthetic fibrinogen peptides with oxidative modifications' pp. S47. DOI:10.1016/j.freeradbiomed.2016.04.098
Dias, IH, Milic, I, Devitt, A, Spickett, CM, Pitt, AR & Griffiths, HR 2016, 'Mass spectrometry based method for measurement of oxysterols' pp. S27. DOI:10.1016/j.freeradbiomed.2016.04.183
Meredith, SP, Parekh, G, Schouten, J, Wilkins, J, Griffiths, HR, Davis, P & Spickett, CM 2016, 'Generation of antibodies with varying sequence specifity for Oxidatively-modified peptides from human fibrinogen' pp. S28. DOI:10.1016/j.freeradbiomed.2016.04.185
Verrastro, I, Tveen-Jensen, K, Woscholski, R, Spickett, CM & Pitt, AR 2016, 'Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins'Free Radical Biology and Medicine, vol. 90, pp. 24-34. DOI:10.1016/j.freeradbiomed.2015.11.004,10.1016/j.freeradbiomed.2015.11.004
Greig, FH, Ewart, M-A, McNaughton, E, Cooney, J, Spickett, CM & Kennedy, S 2015, 'The hypotensive effect of acute and chronic AMP-activated protein kinase activation in normal and hyperlipidemic mice'Vascular Pharmacology, vol. 74, pp. 93-102. DOI:10.1016/j.vph.2015.07.010
Fauzi, NM & Spickett, CM 2015,Lipid oxidation. in SM Roberts, JP Kehrer & L-O Klotz (eds),Studies on experimental toxicology and pharmacology.Oxidative stress in applied basic research and clinical practice, Springer, Cham (CH), pp. 43-79. DOI:10.1007/978-3-319-19096-9_4
Thakker, A, Spickett, C & Pitt, A 2015, 'Optimisation of chromatographic separation of oxidised phospholipids and detection with targeted approaches provides greater coverage of the oxidised lipidome' Free Radical Biology and Medicine, vol. 86, no. Suppl.1, PP18, pp. S25. DOI:10.1016/j.freeradbiomed.2015.07.093
Spickett, CM, Verrastro, I & Pitt, AR 2015, 'Uncovering changes in the redox protein interactome of PTEN' Free Radical Biology and Medicine, vol. 86, no. Suppl.1, OP15, pp. S9. DOI:10.1016/j.freeradbiomed.2015.07.042
Meredith, S, Spickett, C, Parekh, G, Schouten, J, Griffiths, H & Davis, P 2015, 'Investigating the ability of antibodies to recognize specific oxidized protein epitopes' Free Radical Biology and Medicine, vol. 86, no. Suppl.1, PP36, pp. S31. DOI:10.1016/j.freebiomed.2015.07.0111
Aldini, G, Domingues, MR, Spickett, CM, Domingues, P, Altomare, A, Sánchez-Gómez, FJ, Oeste, CL & Pérez-Sala, D 2015, 'Protein lipoxidation: detection strategies and challenges' Redox biology, vol. 5, pp. 253-266. DOI:10.1016/j.redox.2015.05.003
Spickett, CM & Pitt, AR 2015, 'Oxidiative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology' Antioxidants and Redox Signaling, vol. 22, no. 18, pp. 1646-1666. DOI:10.1089/ars.2014.6098
Spickett, CM & Pitt, AR 2015, ' Oxidative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology ' Antioxidants and redox signaling , vol 22, no. 18, pp. 1646-1666., 10.1089/ars.2014.6098
Tveen Jensen, K, Gesellchen, F, Wilson, R, Spickett, C, Cooper, JM & Pitt, A 2015, 'Interfacing low-energy SAW nebulization with liquid chromatography-mass spectrometry for the analysis of biological samples' Scientific Reports, vol. 5, 9736. DOI:10.1038/srep09736
Greig, FH, Hutchison, L, Spickett, CM & Kennedy, S 2015, 'Differential effects of chlorinated and oxidized phospholipids in vascular tissue: implications for neointima formation' Clinical Science, vol. 128, no. 9, pp. 579-592. DOI:10.1042/CS20140578
Parsons, BJ & Spickett, CM 2015, 'Special issue on "analytical methods for the detection of oxidized biomolecules and antioxidants"' Free Radical Research, vol. 49, no. 5, pp. 473-476. DOI:10.3109/10715762.2015.1024678
Verrastro, I, Pasha, S, Jensen, KT, Pitt, AR & Spickett, CM 2015, 'Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges' Biomolecules, vol. 5, no. 2, pp. 378-411. DOI:10.3390/biom5020378
Reis , A, Rudnitskaya, A, Chariyavilaskul, P, Dhaun, N, Melville, V, Goddard, J, Webb, DJ, Pitt, AR & Spickett, CM 2015, 'Top-down lipidomics of low density lipoprotein reveal altered lipid profiles in advanced chronic kidney disease' Journal of Lipid Research, vol. 56, no. 2, pp. 413-422. DOI:10.1194/jlr.M055624
Houée-Lévin, C, Bobrowski, K, Horakova, L, Karademir, B, Schöneich, C, Davies, MJ & Spickett, CM 2015, 'Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences' Free Radical Research, vol. 49, no. 4, pp. 347-373. DOI:10.3109/10715762.2015.1007968
Dunbar, L, Sowden, RJ, Trotter, KD, Taylor, MK, Smith, D, Kennedy, AR, Reglinski, J & Spickett, CM 2015, 'Copper complexes as a source of redox active MRI contrast agents' BioMetals, vol. 28, no. 5, pp. 903-912. DOI:10.1007/s10534-015-9875-3
Rezende Valim, L, Davies, JA, Tveen Jensen, K, Guo, R, Willison, KR, Spickett, CM, Pitt, AR & Klug, DR 2014, 'Identification and relative quantification of tyrosine nitration in a model peptide using two-dimensional infrared spectroscopy' Journal of Physical Chemistry: Part B, vol. 118, no. 45, pp. 12855-12864. DOI:10.1021/jp509053q
Tveen-Jensen, K, Reis, A, Spickett, CM & Pitt, AR 2014, 'Targeted mass spectrometry methods for detecting oxidative post-translational modifications' Free Radical Biology and Medicine, vol. 75, no. Suppl.1, P93, pp. S52-S53. DOI:10.1016/j.freeradbiomed.2014.10.825
Pasha, S, Tveen Jensen, K, Pitt, AR & Spickett, CM 2014, 'Detection and quantification of protein oxidation in sarcopenic models: a mass spectrometry study' Free Radical Biology and Medicine, vol. 75, no. Suppl.1, P68, pp. S44. DOI:10.1016/j.freeradbiomed.2014.10.800
Dias, IHK, Mistry, J, Fell, S, Reis, A, Spickett, CM, Polidori, MC, Lip, GYH & Griffiths, HR 2014, 'Oxidised LDL-lipids increase beta amyloid production by SH-SY5Y cells through glutathione depletion and lipid raft formation' Free Radical Biology and Medicine, vol. 75, pp. 48–59. DOI:10.1016/j.freeradbiomed.2014.07.012
Griffiths, H, Dias, I, Lip, GYH, Spickett, C & Polidori, C 2014, 'Oxidised LDL lipids, statins and a blood-brain barrier' Free Radical Biology and Medicine, vol. 75, no. Suppl.1, OP2-3, pp. S15-S16. DOI:10.1016/j.freeradbiomed.2014.10.591
Meredith, S, Parekh, G, Towler, J, Schouten, J, Davis, P, Griffiths, H & Spickett, C 2014, 'Mapping nitro-tyrosine modifications in fibrinogen by mass spectrometry as a biomarker for inflammatory disease'Free Radical Biology and Medicine, vol. 75, no. Suppl.1, P87, pp. S50. DOI:10.1016/j.freeradbiomed.2014.10.819
Maciel, E, Neves, BM, Santinha, D, Reis, A, Domingues, P, Cruz, MT, Pitt, AR, Spickett, CM & Domingues, MRM 2014, 'Detection of phosphatidylserine with a modified polar head group in human keratinocytes exposed to the radical generator AAPH' Archives of Biochemistry and Biophysics, vol. 548, pp. 38–45. DOI:10.1016/j.abb.2014.02.002
Robaszkiewicz, A, Bartosz, G, Pitt, AR, Thakker, A, Armstrong, RA, Spickett, CM & Soszynski, M 2014, 'HOCl-modified phosphatidylcholines induce apoptosis and redox imbalance in HUVEC-ST cells'Archives of Biochemistry and Biophysics, vol. 548, pp. 1-10. DOI:10.1016/j.abb.2014.02.013
Silva, AMN, Vitorino, R, Domingues, MRM, Spickett, CM & Domingues, P 2013, 'Post-translational modifications and mass spectrometry detection' Free Radical Biology and Medicine, vol. 65, pp. 925-941. DOI:10.1016/j.freeradbiomed.2013.08.184
Calimport, S, Pitt, AR & Spickett, CM 2013, 'Residue-specific investigation of the relationship between oxidation and activity of a dual specificity phosphatase by mass spectrometry' Free Radical Biology and Medicine, vol. 65, no. Suppl.2, PSS110, pp. S57. DOI:10.1016/j.freeradbiomed.2013.10.527
Domingues, MR, Domingues, P, Melo, T, Pérez-Sala, D, Reis, A & Spickett, CM 2013, 'Lipoxidation adducts with peptides and proteins: deleterious modifications or signalling mechanisms?' Journal of Proteomics, vol. 92, pp. 110-131. DOI:10.1016/j.jprot.2013.06.004
Tveen Jensen, K, Reis, A, Mouls, L, Pitt, AR & Spickett, CM 2013, 'Reporter ion-based mass spectrometry approaches for the detection of non-enzymatic protein modifications in biological samples' Journal of Proteomics, vol. 92, pp. 71-79. DOI:10.1016/j.jprot.2013.03.033
Spickett, CM, Tveen-jensen, K, Reis, A & Pitt, AR 2013, 'Protein modification and phospholipid oxidation' Free Radical Biology and Medicine, vol. 65, no. Suppl.1, pp. S15. DOI:10.1016/j.freeradbiomed.2013.08.140
Horáková, L, Strosova, MK, Spickett, CM & Blaskovic, D 2013, 'Impairment of calcium ATPases by high glucose and potential pharmacological protection' Free Radical Research, vol. 47, no. S1, pp. 81-92. DOI:10.3109/10715762.2013.807923
Reis, A, Rudnitskaya, A, Blackburn, GJ, Fauzi, NM, Pitt, AR & Spickett, CM 2013, 'A comparison of five lipid extraction solvent systems for lipidomic studies of human LDL' Journal of Lipid Research, vol. 54, no. 7, pp. 1812-1824. DOI:10.1194/jlr.M034330
Spickett, CM, Reis, A & Pitt, AR 2013, 'Use of narrow mass-window, high-resolution extracted product ion chromatograms for the sensitive and selective identification of protein modifications' Analytical Chemistry, vol. 85, no. 9, pp. 4621-4627. DOI:10.1021/ac400131f
Jové, M, Ayala, V, Ramírez-Núñez, O, Naudí, A, Cabré, R, Spickett, CM, Portero-Otin, M & Pamplona, R 2013, 'Specific lipidome signatures in central nervous system from methionine-restricted mice' Journal of Proteome Research, vol. 12, no. 6, pp. 2679-2689. DOI:10.1021/pr400064a
Sowden, RJ, Trotter, KD, Dunbar, L, Craig, G, Erdemli, O, Spickett, CM & Reglinski, J 2013, 'Reactions of copper macrocycles with antioxidants and HOCl: potential for biological redox sensing' BioMetals, vol. 26, no. 1, pp. 85-96. DOI:10.1007/s10534-012-9596-9
Spickett, CM 2013, 'The lipid peroxidation product 4-hydroxy-2-nonenal: advances in chemistry and analysis' Redox biology, vol. 1, no. 1, pp. 145-152. DOI:10.1016/j.redox.2013.01.007
Hermetter, A, Kinnunen, P & Spickett, C 2012, 'Oxidized phospholipids: their properties and interactions with proteins' BBA -Biomembranes, vol. 1818, no. 10, pp. 2373. DOI:10.1016/j.bbamem.2012.06.009
Reis Pereira, A & Spickett, CM 2012, 'Chemistry of phospholipid oxidation' BBA -Biomembranes, vol. 1818, no. 10, pp. 2374–2387. DOI:10.1016/j.bbamem.2012.02.002
Pasha, S, Mahalka, AK, Reis, A, Pitt, AR, Kinnunen, PKJ & Spickett, CM 2012, 'Mass spectrometry analysis of modified bee venom phospholipase A2 in correlation with increased activity' Free Radical Biology and Medicine, vol. 53, no. Supplement 1, 0578, pp. S213-S214. DOI:10.1016/j.freeradbiomed.2012.08.447
Tveen Jensen, K, Calimport, SRG, Verrastro, I, Spickett, CM & Pitt, AR 2012, 'Mapping oxidative modifications of PTEN' Free Radical Biology and Medicine, vol. 53, no. Supplement 1, 0576, pp. S213. DOI:10.1016/j.freeradbiomed.2012.08.446
Li, Y, Wright, HJ, Pitt, AR, Chapple, ILC & Spickett, CM 2012, 'Proteomic and oxPTM analysis of neutrophil extracellular traps' Free Radical Biology and Medicine, vol. 53, no. Supplement 1, 0583, pp. S170. DOI:10.1016/j.freeradbiomed.2012.08.356
Reis, A, Spickett, CM & Rudnitskaya, A 2012, 'Integrated Omics for the global mapping of biomolecules in LDL' Free Radical Biology and Medicine, vol. 53, no. Supplement 1, 0560, pp. S212. DOI:10.1016/j.freeradbiomed.2012.08.445
Reis, A & Spickett, CM 2012, 'Mass spectrometry based strategies in the mapping of modified LDL' Free Radical Biology and Medicine, vol. 53, no. Supplement 1, HNE.P.17 , pp. S252. DOI:10.1016/j.freeradbiomed.2012.08.047
Fauzi, NM, Torrance, E, Neamatallah, T, Ho, HK, Spickett, CM & Plevin, R 2012, 'Effects of oxidized and chlorinated phospholipids on signaling pathways in endothelial cells' Vascular Pharmacology, vol. 56, no. 5-6, P.13.7, pp. 373. DOI:10.1016/j.vph.2011.08.182
Greig, FH, Kennedy, S & Spickett, CM 2012, 'Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation' Free Radical Biology and Medicine, vol. 52, no. 2, pp. 266-280. DOI:10.1016/j.freeradbiomed.2011.10.481
Spickett, CM & Pitt, AR 2012, 'Protein oxidation: role in signalling and detection by mass spectrometry'Amino Acids, vol. 42, no. 1, pp. 5-21. DOI:10.1007/s00726-010-0585-4
Spickett, CM, Reis, A & Pitt, AR 2011, 'Identification of oxidized phospholipids by electrospray ionization mass spectrometry and LC-MS using a QQLIT instrument' Free Radical Biology and Medicine, vol. 51, no. 12, pp. 2133-2149. DOI:10.1016/j.freeradbiomed.2011.09.003
Spickett, CM & Fauzi, NM 2011, 'Analysis of oxidized and chlorinated lipids by mass spectrometry and relevance to signalling' Biochemical Society Transactions, vol. 39, no. 5, pp. 1233-1239. DOI:10.1042/BST0391233
Winyard, PG, Spickett, CM & Griffiths, HR 2011, 'Analysis of radicals and radical reaction products in cell signalling and biomolecular damage: the long hard road to gold-standard measures' Biochemical Society Transactions, vol. 39, no. 5, pp. 1217-1220. DOI:10.1042/BST0391217
Kwolek-Mirek, M, Bartosz, G & Spickett, CM 2011, 'Sensitivity of antioxidant-deficient yeast to hypochlorite and chlorite' Yeast, vol. 28, no. 8, pp. 595-609. DOI:10.1002/yea.1889
Strosova, MK, Karlovska, J, Zizkova, P, Kwolek-Mirek, M, Ponist, S, Spickett, CM & Horakova, L 2011, 'Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis' Archives of Biochemistry and Biophysics, vol. 511, no. 1-2, pp. 40-47. DOI:10.1016/j.abb.2011.04.011
Spickett, CM, Wiswedel, I, Siems, W, Zarkovic, K & Zarkovic, N 2010, 'Advances in methods for the determination of biologically relevant lipid peroxidation products' Free Radical Research, vol. 44, no. 10, pp. 1172-1202. DOI:10.3109/10715762.2010.498476
Breusing, N, Grune, T, Andrisic, L, Atalay, M, Bartosz, G, Biasi, F, Borovic, S, Bravo, L, Casals, I, Casillas, R, Dinischiotu, A, Drzewinska, J, Faber, H, Fauzi, NM, Gajewska, A, Gambini, J, Gradinaru, D, Kokkola, T, Lojek, A, Luczaj, W, Margina, D, Mascia, C, Mateos, R, Meinitzer, A, Mitjavila, MT, Mrakovcic, L, Munteanu, MC, Podborska, M, Poli, G, Sicinska, P, Skrzydlewska, E, Vina, J, Wiswedel, I, Zarkovic, N, Zelzer, S & Spickett, CM 2010, 'An inter-laboratory validation of methods of lipid peroxidation measurement in UVA-treated human plasma samples' Free Radical Research, vol. 44, no. 10, pp. 1203-1215. DOI:10.3109/10715762.2010.499907
Robaszkiewicz, A, Greig, FH, Pitt, AR, Spickett, CM, Bartosz, G & Soszynski, M 2010, 'Effect of phosphatidylcholine chlorohydrins on human erythrocytes' Chemistry and Physics of Lipids, vol. 163, no. 7, pp. 639-647. DOI:10.1016/j.chemphyslip.2010.05.201
Trotter, KD, Taylor, MK, Forgie, JC, Reglinski, J, Berlouis, LEA, Kennedy, AR, Spickett, CM & Sowden, RJ 2010, 'The structural and electrochemical consequences of hydrogenating Copper N2S2Schiff base macrocycles' Inorganica Chimica Acta, vol. 363, no. 7, pp. 1529-1538. DOI:10.1016/j.ica.2010.01.012
Strosova, M, Karlovska, J, Spickett, CM, Orszagova, Z, Ponist, S, Bauerova, K, Mihalova, D & Horakova, L 2009, 'Modulation of SERCA in the chronic phase of adjuvant arthritis as a possible adaptation mechanism of redox imbalance' Free Radical Research, vol. 43, no. 9, pp. 852-864. DOI:10.1080/10715760903089708
Trotter, KD, Reglinski, J, Robertson, K, Forgie, JC, Parkinson, JA, Kennedy, AR, Armstrong, DR, Sowden, RJ & Spickett, CM 2009, 'Structural studies of trans-N2S2 copper macrocycles' Inorganica Chimica Acta, vol. 362, no. 11, pp. 4065-4072. DOI:10.1016/j.ica.2009.05.060
Spickett, CM & Pitt, AR 2009, 'Redox signalling and detection of protein oxidation by mass spectrometry' 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom,3/08/09 -7/08/09 , pp. 33.
Strosova, M, Karlovska, J, Spickett, CM, Grune, T, Orszagova, Z & Horakova, Z 2009, 'Oxidative injury induced by hypochlorous acid to Ca-ATPase from sarcoplasmic reticulum of skeletal muscle and protective effect of trolox' General Physiology and Biophysics, vol. 28, no. 2, pp. 195-209. DOI:10.4149/gpb_2009_02_195
Mouls, L, Silajdzic, E, Haroune, N, Spickett, CM & Pitt, AR 2009, 'Development of novel mass spectrometric methods for identifying HOCl-induced modifications to proteins' Proteomics, vol. 9, no. 6, pp. 1617-1631. DOI:10.1002/pmic.200800391
Strosova, M, Karlovska, J, Spickett, CM & Horakova, L 2009, 'Mechanism of serca modulation from rats with adjuvant arthritis' SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy,27/09/09 , .
Spickett, CM, Silajdzic, E, Mouls, L, Thomson, K & Pitt, A 2009, 'Protein oxidative modifications: new mass spectrometry approaches to detection in biological samples' SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy,27/09/09 , pp. 43.
Strosova, M, Tomaskova, I, Ponist, S, Bauerova, K, Karlovska, J, Spickett, CM & Horakova, L 2008, 'Oxidative impairment of plasma and skeletal muscle sarcoplasmic reticulum in rats with adjuvant arthritis - effects of pyridoindole antioxidants' Neuroendocrinology Letters, vol. 29, no. 5, pp. 706-711.
Erridge, C, Burdess, A, Jackson, AJ, Murray, C, Riggio, M, Lappin, D, Milligan, S, Spickett, CM & Webb, DJ 2008, 'Vascular cell responsiveness to toll-like receptor ligands in carotid atheroma' European journal of clinical investigation, vol. 38, no. 10, pp. 713-720. DOI:10.1111/j.1365-2362.2008.02010.x
Pitt, AR & Spickett, CM 2008, 'Mass spectrometric analysis of HOCl- and free-radical-induced damage to lipids and proteins' Biochemical Society Transactions, vol. 36, no. 5, pp. 1077-82. DOI:10.1042/BST0361077
Erridge, C, Kennedy, S, Spickett, CM & Webb, DJ 2008, 'Oxidized phospholipid inhibition of toll-like receptor (TLR) signaling is restricted to TLR2 and TLR4 roles for cd14, lps-binding protein, and md2 as targets for specificity of inhibition' Journal of Biological Chemistry, vol. 283, no. 36, pp. 24748-24759. DOI:10.1074/jbc.M800352200
Erridge, C, Spickett, CM, Attina, T & Webb, DJ 2008, 'Reply to J Rood and SR Smith' American Journal of Clinical Nutrition, vol. 88, no. 1, pp. 249-250.
Spickett, CM 2008, 'Chlorinated and oxidized lipids in inflammation' Meeting of the Society-for-Free-Radical-Research-Europe, Berlin, Germany,5/07/09 -9/07/09 , pp. S43.
Taylor, MK, Trotter, KD, Reglinski, J, Berlouis, LEA, Kennedy, AR, Spickett, CM & Sowden, RJ 2008, 'Copper N2S2Schiff base macrocycles: the effect of structure on redox potential' Inorganica Chimica Acta, vol. 361, no. 9-10, pp. 2851-2862. DOI:10.1016/j.ica.2008.02.021
Dever, G, Benson, R, Wainwright, CL, Kennedy, S & Spickett, CM 2008, 'Phospholipid chlorohydrin induces leukocyte adhesion to Apoe(-/-) mouse arteries via upregulation of P-selectin' Free Radical Biology and Medicine, vol. 44, no. 3, pp. 452-463. DOI:10.1016/j.freeradbiomed.2007.10.038
Dr Zita Balklava's publications:
Balklava Z, Rathnakumar ND, Vashist S, Schweinsberg PJ, Grant BD. (2016). Linking Gene Expression in the Intestine to Production of Gametes Through the Phosphate Transporter PITR-1 in Caenorhabditis elegans. Genetics. 204,153-62. doi: 10.1534/genetics.116.188532.
Guscott B, Balklava Z, Safrany ST, Wassmer T. (2016). A cell-permeable tool for analysing APP intracellular domain function and manipulation of PIKfyve activity. Biosci Rep. doi: 10.1042/BSR20160040.
Currinn H, Guscott B, Balklava Z, Rothnie A, Wassmer T. (2016). APP controls the formation of PI(3,5)P2 vesicles through its binding of the PIKfyve complex. Cell Mol Life Sci. 73, 393-408. doi: 10.1007/s00018-015-1993-0.
Balklava Z, Niehage C, Currinn H, Mellor L, Guscott B, Poulin G, Hoflack B, Wassmer T. (2015). The Amyloid Precursor Protein Controls PIKfyve Function. PLoS One. 10(6):e0130485. doi: 10.1371/journal.pone.0130485.
Balklava Z, Sztul E. (2013). Studying Membrane Trafficking in the Worm C. elegans by RNA Interference. Methods Cell Biol. 118, 51-68. doi: 10.1016/B978-0-12-417164-0.00004-5.
Grabski R, Balklava Z, Wyrozumska P, Szul T, Brandon E, Alvarez C, Holloway ZG, Sztul E. (2012). Identifying a novel functional domain within the p115 tethering factor required for Golgi ribbon assembly and membrane trafficking. J Cell Sci. 125, 1896-1909. doi: 10.1242/jcs.090571.
Morohashi Y, Balklava Z, Ball M, Hughes H, Lowe M. (2010). Phosphorylation and membrane dissociation of the ARF exchange factor GBF1 in mitosis. Biochem J. 427, 401-412. doi: 10.1042/BJ20091681.
Shi A, Pant S, Balklava Z, Chen CC, Figueroa V, Grant BD. (2007). A novel requirement for C. elegans Alix/ALX-1 in RME-1-mediated membrane transport.Curr Biol. 17, 1913-1924.
Balklava Z, Pant S, Fares H, Grant BD. (2007). Genome-wide analysis of membrane transport in C. elegans identifies a general requirement for polarity proteins in endocytosis. Nat. Cell Biol. 9, 1066-1073.
Balklava Z, Grant BD. (2005). The regulation of endocytosis by kinases: cell biology meets genomics. Genome Biol., 6 , 245.
Nur-E-Kamal A, Gross SR, Pan Z, Balklava Z, Ma J, Liu LF. (2004). Nuclear Translocation of Cytochrome C During Apoptosis. J.Biol. Chem. 279, 24911-24914.
Gross SR, Balklava Z, Griffin M. (2003). Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source. J. Invest. Dermat., 121, 412-423.
Balklava Z, Verderio E, Collighan RJ, Gross SR, Adams J, Griffin M. (2002). Analysis of tissue transglutaminase in the migration of Swiss 3T3 fibroblasts: The active-state conformation of the enzyme does not affect cell motility but it is important for its secretion. J. Biol. Chem., 277, 16567-16575.
Licis N, Balklava Z, Van Duin J. (2000). Forced retroevolution of an RNA bacteriophage. Virology, 271, 298-306.
Licis N, van Duin J, Balklava Z, Berzins V. (1998). Long-range translational coupling in single-stranded RNA bacteriophages: an evolutionary analysis. Nucl. Acids Res., 26, 3242-3246.
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