Notes: Asterisk (*) indicates Amherst College undergraduate co-author. Publications are peer-reviewed original-research articles unless otherwise noted.
Plaman BA,* Chan WC* & Bishop AC. Chemical activation of divergent protein tyrosine phosphatase domains with cyanine-based biarsenicals. Scientific Reports 9, 16148. doi: 10.1038/s41598-019-52002-1 (2019).
Marsh-Armstrong B,* Fajnzylber JM,* Korntner S,* Plaman BA* & Bishop AC. The allosteric site on SHP2’s protein tyrosine phosphatase domain is targetable with druglike small molecules. ACS Omega 3, 15763-15770 (2018).
Korntner S,* Pomorski A, Krężel A & Bishop AC. Optimized allosteric inhibition of engineered protein tyrosine phosphatases with an expanded palette of biarsenical small molecules. Bioorganic & Medicinal Chemistry 26, 2610-2620 (2018).
Chan WC,* Knowlton GS* & Bishop AC. Activation of engineered protein tyrosine phosphatases with the biarsenical compound AsCy3-EDT2. ChemBioChem 18, 1950-1958 (2017).
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, Beebe K & Schimmel PR. Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America 100, 490-494 (2003).
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).
Weiss EL, Bishop AC, Shokat KM & Drubin DG. Chemical genetic analysis of the budding-yeast p21-activated kinase Cla4p. Nature Cell Biology 2, 677-685 (2000).
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).