Bishop, Anthony - Amherst College - Biochemistry-Biophysics

个人简介

Ph.D., Princeton University (2000) B.A., University of California, San Diego (1993) I teach courses in Organic Chemistry, Biochemistry, and Chemical Biology. Faculty Member, Molecular and Cellular Biology Program, University of Massachusetts Amherst, 2003-Present.

研究领域

Many bacterial species use carefully regulated attachment and virulence mechanisms to colonize and sometimes sicken their eukaryotic hosts. My laboratory aims to understand the complex molecular ‘conversations’ that underlie these interactions by studying Vibrio cholerae, the Gram-negative bacterium that causes cholera, an acute diarrheal disease that affects hundreds of thousands of people each year. Vibrio cholerae is naturally found in aquatic environments, often attached to phytoplankton, aquatic arthropods such as copepods, and larger organisms. V. cholerae also can be carried by terrestrial arthropods such as houseflies. Our laboratory explores interactions between V. cholerae and arthropods using Drosophila melanogaster, the common fruit fly, as a model system. In the course of our work, we have discovered specific V. cholerae genes that are required for virulence and colonization in Drosophila. These include genes that likely initiate signal transduction cascades that regulate expression of V. cholerae genes in the fly. Our lab is interested in understanding how these regulatory cascades work; that is, what genes do they regulate? What environmental signals do they sense? How are they turned on and off? Ultimately, this project will reveal the genetic mechanisms that allow V. cholerae to associate with arthropods in order to survive and spread in the rivers, lakes, ponds, and oceans that let the disease persist in areas where it is endemic, and spread to distant locales. Our ultimate goal is to better understand the ecology and evolution of a pathogen of major public health importance by integrating genomic, genetic, molecular and environmental approaches.

近期论文

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Bishop AC. A missense methionine mutation augments catalytic activity but reduces thermal stability in two protein tyrosine phosphatases. Biochemical and Biophysical Research Communications 481, 153-158 (2016). Chio CM,* Cheng KW* & Bishop AC. Direct chemical activation of a rationally engineered signaling enzyme. ChemBioChem 16, 1735-1739 (2015). Chio CM,* Yu X* & Bishop AC. Rational design of allosteric-inhibition sites in classical protein tyrosine phosphatases. Bioorganic & Medicinal Chemistry 23, 2828-2838 (2015). Pomorski A, Adamczyk J, Bishop AC & Krężel A. Probing the target-specific inhibition of sensitized protein tyrosine phosphatases with biarsenical probes. Organic & Biomolecular Chemistry 13, 1395-1403 (2015). Chio CM,* Lim CS* & Bishop AC. Targeting a cryptic allosteric site for selective inhibition of the oncogenic protein tyrosine phosphatase Shp2. Biochemistry 54, 497-504 (2015). Harris LK,* Frumm SM* & Bishop AC. A general assay for monitoring the activities of protein tyrosine phosphatases in living eukaryotic cells. Analytical Biochemistry 435, 99-105 (2013). Davis OB* & Bishop AC. Inhibition of sensitized protein tyrosine phosphatase 1B (PTP1B) with a biarsenical probe. Bioconjugate Chemistry 23, 272-278 (2012). Walton ZE* & Bishop AC. Target-specific control of lymphoid-specific protein tyrosine phosphatase (Lyp) activity. Bioorganic & Medicinal Chemistry 18, 4884-4891 (2010). Chen VL* & Bishop AC. Chemical rescue of protein tyrosine phosphatase activity. Chemical Communications 46, 637-639 (2010). Bishop AC & Chen VL.* Brought to life: Targeted activation of enzyme function with small molecules. Journal of Chemical Biology (Invited Review) 2, 1-9 (2009). Zhang XY, Chen VL,* Rosen MS,* Blair ER,* Lone AM* & Bishop AC. Allele-specific inhibition of divergent protein tyrosine phosphatases with a single small molecule. Bioorganic & Medicinal Chemistry 16, 8090-8097 (2008). Zhang XY & Bishop AC. Engineered inhibitor sensitivity in the WPD loop of a protein tyrosine phosphatase. Biochemistry 47, 4491-4500 (2008). Zhang XY & Bishop AC. Site-specific incorporation of allosteric-inhibition sites in a protein tyrosine phosphatase. Journal of the American Chemical Society 129, 3812-3813 (2007). Bishop AC, Zhang XY & Lone AM.* Generation of inhibitor-sensitive protein tyrosine phosphatases via active-site mutations. Methods (Invited Article) 42, 278-288 (2007). Savage DF,* de Crécy-Lagard V & Bishop AC. Molecular determinants of dihydrouridine synthase activity. FEBS Letters 580, 5198-5202 (2006). Bishop AC & Blair ER.* A gatekeeper residue for inhibitor sensitization of protein tyrosine phosphatases. Bioorganic & Medicinal Chemistry Letters 16, 4002-4006 (2006). Blair ER,* Hoffman HE* & Bishop AC. Engineering non-natural inhibitor sensitivity in protein tyrosine phosphatase H1. Bioorganic & Medicinal Chemistry 14, 464-471 (2006). Hoffman HE,* Blair ER,* Johndrow JE* & Bishop AC. Allele-specific inhibitors of protein tyrosine phosphatases. Journal of the American Chemical Society 127, 2824-2825 (2005). Bishop AC, Xu J, Johnson RC, Schimmel P & de Crécy-Lagard V. Identification of the tRNA-Dihydrouridine Synthase Family. Journal of Biological Chemistry 277, 25090-25095 (2002). Bishop AC, Nomanbhoy TK & Schimmel P. Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America 99, 585-590 (2002). Bishop AC, Ubersax JA, Petsch DT, Matheos DP, Gray NS, Blethrow J, Shimizu E, Tsien JZ, Schultz PG, Rose MD, Wood JL, Morgan DO & Shokat KM. A chemical switch for inhibitor-sensitive alleles of any protein kinase. Nature 407, 395-401 (2000). Bishop AC, Kung C-Y, Shah K, Witucki L, Shokat KM & Liu Y. Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach. Journal of the American Chemical Society 121, 627-631 (1999). Bishop AC, Shah K, Liu Y, Witucki L, Kung C-Y & Shokat KM. Design of allele-specific inhibitors to probe protein kinase signaling. Current Biology 8, 257-266 (1998).