Target- based drug design

Our Lab

Thompson LabChemical Biology of Arginine Modifying Enzymes

Welcome to the Thompson Lab! The major focus of our group is the target-based design of novel anti-cancer and anti-rheumatoid arthritis chemotherapeutics. Currently we are focusing our efforts on the development of potent and selective inhibitors of enzymes whose activities are involved in modulating chromatin structure.

 

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Research Focus

Thompson Lab

Chemical Biology of Arginine Modifying Enzymes

Our major focus is the target-based design of novel anti-cancer and anti-rheumatoid arthritis chemotherapeutics. Currently we are focusing our efforts on the development of potent and selective inhibitors of enzymes whose activities are involved in modulating chromatin structure. The modulation of chromatin structure can have drastic effects on the transcription of particular genes. Our lab uses kinetic and structural analyses to guide the design of small molecule inhibitors, which we then synthesize and evaluate as inhibitors of these enzymes. Protein Arginine Methyl-Transferases (PRMTs) catalyze the mono-, asymmetric di-, and symmetric di-methylation of Arginine residues in a number of proteins including the core histone proteins.

 

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Publications

Thompson Lab Members

Total: 1 results
  • Diverse stimuli engage different neutrophil extrac...

    Friday, June 02, 2017
    Source: Elife

    Neutrophils release neutrophil extracellular traps (NETs) which ensnare pathogens and have pathogenic functions in diverse diseases. We examined the NETosis pathways induced by five stimuli; PMA, the calcium ionophore A23187, nigericin, Candida albicans and Group B Streptococcus. We studied NET production in neutrophils from healthy donors with inhibitors of molecules crucial to PMA induced NETs including protein kinase C, calcium, reactive oxygen species, the enzymes myeloperoxidase (MPO) and neutrophil elastase. Additionally, neutrophils from chronic granulomatous disease patients, carrying mutations in the NADPH oxidase complex or a MPO-deficient patient were examined. We show that PMA, C. albicans and GBS use a related pathway for NET induction whereas ionophores require an alternative pathway but that NETs produced by all stimuli are proteolytically active, kill bacteria and composed mainly of chromosomal DNA. Thus, we demonstrate that NETosis occurs through several signalling mechanisms, suggesting that extrusion of NETs is important in host defence.

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Contact

Office:

Lazare Research Building  LRB825
Campus Map (pdf)

Phone:
508.856.8333 (Admin. Assistant)
508.856.8874 (lab)

Email:
Paul.Thompson@umassmed.edu

Mailing Address:
UMASS Medical School
Paul Thompson, Ph.D.
Department of Biochemistry and Molecular Pharmacology
364 Plantation Street, LRB825
Worcester, MA 01605-4321

Join Us

We are always interested in applications from qualified candidates at graduate student, postdoctoral, and research associate levels.

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