Thermo Scientific Tandem Mass Tag Research Awards
Describe how you will use Thermo Scientific tandem mass tag (including amine-, sulfhydryl-, or carbonyl-reactive) labeling reagents and Thermo Scientific mass spectrometry (MS) reagents in your research, and you could receive one of three awards that provide up to $10,000 worth of these reagents, free for use in your doctoral or post-doctoral research. Applications will be accepted from September 30, 2018 through February 28, 2019.
The research awards include eligible Thermo Scientific MS reagents, with up to 50% of each grant available for tandem mass tag labeling reagents. See program flier, including a complete list of eligible products. Official rules here.
The top three recipients will be selected by a panel of judges from Thermo Fisher Scientific and Proteome Sciences, based on the recipient’s innovative and impactful intended use of the TMT reagents. Award recipients will be recognized during a Thermo Scientific sponsored event at ASMS in Atlanta, Georgia
Learn more about past award recipients
David-Paul Minde, University of Cambridge, Cambridge, UK
Dr. Minde works as postdoc in the Cambridge Centre for Proteomics with Prof. Kathryn Lilley in the Department of Biochemistry. His research explores protein dynamics using a variety of techniques. During his PhD on cancer-related Wnt signaling scaffolds, he developed a fast proteolysis assay (FASTpp) to determine protein stability and validated a 2000 residue large predicted disordered region in APC in vitro. Subsequent in singulo optical tweezers studies contributed to a paradigm shift in understanding possible cellular roles of Hsp70 chaperone systems. His current work focuses on in vivo dynamics of membrane proteins in the bacterial cell envelope specifically under poisoning conditions as part of the BBSRC-funded DETOX consortium.
Sandipan Ray, Francis Crick Institute and University College London, London, UK
Dr. Ray is a postdoctoral research associate at the UCL Institute of Neurology and a visiting scientist at The Francis Crick Institute, UK. He is working in the Biological Clocks and Sleep Group headed by Prof. Akhilesh B. Reddy. He has substantial expertise in cutting-edge proteomics technologies and big-data analysis skills with a very solid record of scientific publications in reputed journals. His current research interests are to understand the cross-talks among circadian clocks, sleep-wake cycles, and diverse signaling networks using systems-level approaches. By combining multiplexed quantitative proteomics and Thermal Proteome Profiling (TPP) he is investigating mechanisms of action of circadian period altering drugs in mammalian cells. This is critical in clearly defining molecular targets in order to modulate daily rhythms for therapeutic benefit (e.g. in shift work disorder, jet lag and sleep disorders).
Sarah Peck, Indiana University School of Medicine, Indianapolis, IN
Sarah is a graduate student in the lab of Amber Mosley in the Department of Biochemistry and Molecular Biology at Indiana University School of Medicine. The Mosley lab utilizes both proteomic and genomic approaches to study the regulation of transcription by RNA polymerase II in Saccharomyces cerevisiae. Sarah is currently developing a quantitative proteomics approach that couples an adapted cellular thermal shift assay to high resolution mass spectrometry to profile the thermal stability of proteins with missense mutations. This application provides a high throughput method to characterize the impacts of disease-associated missense mutations in proteins on the global proteome.
Edward Emmott, Northeastern University, Boston, MA
Dr Emmott is working in the quantitative biology group headed by Dr Nikolai Slavov at Northeastern University. The group currently studies ribosome heterogeneity and the refinement of single cell mass spectrometry methods (SCoPE-MS). Ed has a background in applying mass spectrometry-based quantitative proteomics to the study of virus-host interactions. His current research covers the interaction between the immune system and ribosomes, as well as helping develop SCoPE-MS for the investigation of post-translational modifications. He is also an ASAPbio and eLife ambassador, supporting the use of preprints in the life sciences, and initiatives to aid data reproducibility and reuse.
Roman Fischer, University of Oxford, Oxford, UK
Dr. Fischer leads the Discovery Proteomics Facility and is a principal investigator at the University of Oxford, UK. His lab focusses on proteomic strategies to access the deep proteome from minimal sample materials, such as cells harvested by laser-capture-microdissection. Employing a series of recently published techniques (GASP, CHOPIN) they aim at not only comprehensive proteome-, but also proteome sequence coverage to detect protein isoforms and PTMs in the context of tumor biology and drug target.
Kathryn Lilley, University of Cambridge, Cambridge, UK
Dr. Lilley is a research group leader in the Department of Biochemistry, University of Cambridge, UK. She is also the Director, Cambridge Centre for Proteomics and Head of Cambridge Systems Biology Centre. She has been at the forefront of technology development enabling mapping of the spatial proteome. Her current work investigates the implications of where transcripts are translated upon the spatial proteome and protein structure and how this process is controlled.
Kilian Huber, University of Oxford, Oxford, UK
Dr. Huber is a Principal Investigator at the Structural Genomics Consortium and Target Discovery Institute at the Nuffield Department of Clinical Medicine. His research laboratory uses a combination of chemistry and biology to develop small molecule tool compounds to explore protein function and probe cellular signaling networks related to human disease research. A second key area of interest is the development of chemical biology approaches to investigate the mechanism of action of drugs and other pharmacologically active compounds to identify future novel therapeutic targets.
Ashok Reddy, Oregon Health & Sciences University, Portland, OR
Dr. Ashok Reddy is the associate director of the Oregon Health & Sciences University Proteomics Shared Resource, and is responsible for managing proteomics projects across the entire university. He has 15 years of experience conducting cancer research and proteomics/biomarker discovery studies in human body fluids. He has managed these proteomics projects from conception to discovery as demonstrated by the discovery of candidate biomarkers of infection for pre-term birth, preeclampsia, and neonatal sepsis. His research interests are in discovery and validation of disease biomarkers in body fluids, tissues and exosomes.
Noah Dephoure, Weill Cornell Medical College,
New York, NY
Dr. Dephoure is an Assistant Professor at the Sandra and Edward Meyer Cancer Center at Weill Cornell Medical College. His lab develops and refines proteomic tools and uses them to study signaling events that underlie basic cellular biology and human disease research. A long-term goal of the lab is to understand the complex roles of posttranslational protein modifications (PTMs) in cellular growth and proliferation. By combining multiplexed quantitative and temporal analysis of PTMs with novel methods for studying changes in protein interactions and subcellular localization, they are decoding the mechanisms by which these simple chemical changes impact oncogenesis and tumor progression.
Domitille Schvartz, University of Geneva, Geneva, Switzerland
Dr. Schvartz is working in the Translational Biomarker Group headed by Pr. Jean-Charles Sanchez at the University of Geneva. The group has conducted studies over the years for the discovery of diagnostic and prognostic biomarkers of brain injuries using proteomic approaches on body fluids. She has applied many “omics” approaches to her own research projects, mainly on type 2 diabetes. She is also the chair of a worldwide initiative of the Human Proteome Organization, gathering researchers in the field of diabetes and proteomics. She is now involved in a project aimed at discovering early biomarkers of drug-induced liver injury (DILI) by quantitative “omics”.
Sina Ghaemmaghami, University of Rochester, Rochester, NY
Sina Ghaemmaghami is an assistant professor of biology at the University of Rochester. His research focuses on understanding the mechanisms of cellular protein folding and degradation with a special focus on neurodegenerative disorders. He has authored more than 30 publications in journals such as Science, Nature, and PNAS. His laboratory has developed a number of commonly used proteomic methodologies for global analyses of cellular protein homeostasis.
Matthias Trost, University of Dundee, Scotland
His lab focuses on using proteomics to understand cell signaling via phosphorylation and ubiquitylation in vesicle trafficking in macrophages. They use their expertise in this area to characterize molecular mechanisms in Parkinson’s disease. Recently, they started developing mass spectrometry tools for identification of potential drug targets and drug discovery.
Jun Qu, SUNY, Buffalo, NY
His lab develops and applies LC/MS-based strategies for research in the fields of proteomics and pharmaceutical analysis, involving high-resolution and large-scale expression profiling of pathological proteomes (e.g., for cardiovascular diseases, colon cancer, and infectious diseases) for the discovery of disease/therapeutic biomarkers; identification, localization, and quantification of post-translational modifications in complex proteomes; and targeted quantification of regulatory marker proteins for research study.
Jon Reed, Roskamp Institute, Sarasota, FL
His MS lab uses integrative -omic approaches (proteomics, lipidomics, metabolomics) as well as DMPK analyses to elucidate the underlying mechanisms of several neurodegenerative diseases, and to facilitate the development of therapeutic approaches. The use of stable isotope tagging such as the TMT reagents is integral to day-to-day operations, owing to the increases in throughput and assay standardization observed relative to other techniques.
For Research Use Only. Not for use in diagnostic procedures.