Mark’s research focuses on the 29-amino-acid endocrine peptide glucagon. Glucagon is responsible for elevating blood glucose through stimulation of its cognate, G-protein coupled receptor, the glucagon receptor (GCGR). As the worldwide prevalence of diabetes is increasing, pharmacological intervention of glucagon’s effect as a novel treatment for attaining prolonged glucose homeostasis in diabetic patients is receiving greater attention. By combining molecular biology techniques with characterisation via native mass spectrometry Mark hopes to better understand glucagon peptide-receptor interactions, and how other membrane components (for example, lipids, G-proteins, and accessory proteins) allosterically influence binding properties.
Mark graduated from the University of California San Diego and completed his PhD studies at the University of Arizona. He joined the Robinson group in 2017.
Jani Reddy Bolla
Jani employs native mass spectrometry techniques and X-ray crystallography to characterise the multiprotein machineries involved in peptidoglycan and outer membrane biogenesis in Gram-negative bacteria. The goal of his research is to provide useful information for the development of more effective vaccines as well as targets for new drug design against bacterial infections. A full list of Jani's publications can be found here
Jani studied chemical sciences at Pondicherry University, India and then moved to Iowa State University for his doctoral studies under the supervision of Prof. Edward Yu. He joined the Robinson group in 2015.
Dror’s background is in cell signaling and the isolation and analysis of cell-adhesion related protein complexes using cell biological and mass spectrometry approaches. He is now working on developing novel approaches for detergent-free native mass spectrometry of membrane proteins.
Dror obtained his MSc from the Israeli Institute of Technology (Technion) and his PhD from the Weizmann Institute of Science. He joined the Robinson group in 2015.
Joe’s research aims to unravel the complex structural changes involved as ligand binding is translated into functional effect. He is developing new instrumentation and native mass spectrometry platforms for NativeOmics – the complete characterisation of multiproteoform-ligand complexes. He is also exploring how top-down mass spectrometry, novel fragmentation techniques, such as SID, and high-resolution imaging can be used to provide a more in-depth structural characterisation of membrane protein assemblies.
A full list of Joe's publications can be found here.
Joe completed his MSci in Chemistry at Imperial College London. He obtained his PhD from Ecole Polytechnique (l’X) & Institut Pasteur, France. He joined the Robinson group in 2014 and is currently a Junior Research Fellow at The Queen’s College.
Lucia Geis Asteggiante
Lucia is currently exploring protein-protein interactions and the effect of small molecule binding to membrane proteins. She has a broad background in mass spectrometry and proteomics. Her experience ranges from using mass spectrometry to determine agricultural and urban pollution sources to applying bottom-up and top-down qualitative and quantitative proteomic approaches to determine the role of exosomes released from myeloid-derived suppressor cells in mediating immune suppression.
Lucia studied Chemistry at the University of the Republic of Uruguay (Uruguay) followed by an MSc in the Department of Civil and Environmental Engineering at the University of Maryland (USA); she remained in Maryland for her PhD studies which she completed under the supervision of Professor Catherine Fenselau. Lucia joined the Robinson Group in 2017
LinkedIn profile: https://www.linkedin.com/in/lucia-geis-asteggiante-0b596026
ResearchGate profile: https://www.researchgate.net/profile/Lucia_Geis-Asteggiante
Kallol’s research interest lies in understanding how lipids can act as a regulator of membrane protein assemblies and developing mass spectrometric platform to deconvolute such chemical synergies. Details of his publications can be found here:
Kallol joined the lab as a fellow of Royal Commission for the Exhibition of 1851 and is a Junior Research Fellow at the St. Catherine’s College, Oxford.
Max Felix Hantke
Max works at the interface of physics and biology. His PhD studies focused on high-throughput flash X-ray imaging enabled by X-ray free-electron lasers (XFEL). His interests lie in method development and structural studies of inherently heterogeneous biological entities such as proteins, protein complexes, organelles, and virions. Max is now working towards combining the methodology of X-ray laser imaging and mass spectrometry to study transient interactions of proteins in evaporating nanodroplets.
Max completed his doctoral studies in biophysics at the University of Uppsala, Sweden and was awarded a Sir Henry Wellcome Postdoctoral Fellowship to continue his research in Oxford. He joined the Robinson group in 2017.
Shahid’s research focuses on membrane protein biophysical characterisation using native, and hydrogen deuterium exchange, mass spectrometry. He is currently using mass spectrometry based techniques to understand the dynamics of several antibiotic efflux pumps and off-target drug binding interactions . He is also developing native mass spectrometry methods to better study challenging membrane proteins.
Shahid completed his PhD at the University of Grenoble, France and joined the Robinson Group in 2012.
Di is interested in understanding lipid micro-environment of membrane proteins and dynamic protein post-translational modifications by integrative mass spectrometry based approaches, including native MS, metabolomics, proteomics and biochemistry. He is developing new methods for quantitative analysis of membrane ion channel-lipid interaction. He is also using high resolution native MS to elucidate the importance of glycosylation in protein-protein/drug interactions.
Di obtained his BSc and MSc from Wuhan University, China and completed his PhD at the University of Dundee. He joined the Robinson group in 2015.
DPhil title: The development and applications of a desorption electrospray interface
Stephen’s research focuses on the application of ambient ionisation techniques for analysing soluble and membrane proteins by mass spectrometry. Using a custom desorption electrospray ionisation (DESI) source and novel methods, he has succeeded in measuring large protein complexes and their native interactions with bioactive molecules. He is currently working on extending this technique to samples that cannot be studied by conventional ionization techniques.
Stephen completed his undergraduate studies at the University of Oxford and joined the Robinson Group for his DPhil in 2014.
DPhil title: The study of protein complexes by proteomics and native mass spectrometry
Victoria uses a combination of native mass spectrometry, cross-linking and proteomics to probe the structure and function of Eukaryotic Translation Initiation Factors and ATP synthases.
Victoria studied Chemistry (MChem) at the University of Oxford. She started her DPhil studies in the Robinson group in 2013.
DPhil title: Uncovering the lipid effect on GPCR signalling and capturing protein-lipid interactions using native MS of membrane memetics
Hugh is investigating membrane protein-lipid interactions, in particular those of the GPCR family. The primary goal of his research is to probe GPCR-lipid interactions and their effects on GPCR signalling. In addition, he is also exploring the use of various membrane mimetics, such as nanodisc and SMALP, to capture membrane protein-lipid interactions in the context of the lipid bilayer.
Hugh completed his undergraduate studies at the Queensland University of Technology, Australia, followed by his MSc at the University of Melbourne. He joined the Robinson group in 2014.
DPhil title: Probing Interactions between Membrane Proteins and Lipids by Native Mass Spectrometry
Jingwen’s DPhil studies concentrate on using native mass spectrometry techniques to probe interactions between membrane proteins and lipids in order to understand the specific regulation between lipids and protein conformations. This information will then allow her to investigate the effect on function. To aid her research she is developing a detergent-free strategy to interrogate the lipid dynamics of membrane proteins.
Jingwen graduated from the University of Birmingham, UK and joined the Robinson group in 2014.
DPhil title: Investigating the regulation of membrane protein assemblies by lipids and other small molecules using native mass spectrometry
Denis employs native mass spectrometry, in combination with Surface-Induced Dissociation (SID), to obtain positional information on lipids and ligands bound to membrane protein complexes. His current goal is to locate interfacial lipids that are involved in membrane protein oligomerisation.
Denis completed his undergraduate studies at the University of Oxford. He started his DPhil studies in the Robinson group in 2016.