M
Mary E. McGrath
Researcher at Celera Corporation
Publications - 41
Citations - 3191
Mary E. McGrath is an academic researcher from Celera Corporation. The author has contributed to research in topics: Serine protease & Proteases. The author has an hindex of 29, co-authored 41 publications receiving 2999 citations. Previous affiliations of Mary E. McGrath include University of California, San Francisco & Sunesis Pharmaceuticals.
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Journal ArticleDOI
A structural role for hormone in the thyroid hormone receptor
Richard L. Wagner,James W. Apriletti,Mary E. McGrath,Brian L. West,John D. Baxter,Robert J. Fletterick +5 more
TL;DR: A structural role for ligand is suggested, in establishing the active conformation of the receptor, that is likely to underlie hormonal regulation of gene expression for the nuclear receptors.
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Structural basis for RNA replication by the hepatitis C virus polymerase.
Todd Appleby,Jason K. Perry,Eisuke Murakami,Ona Barauskas,Joy Y. Feng,Aesop Cho,David A. Fox,Diana R. Wetmore,Mary E. McGrath,Adrian S. Ray,Michael J. Sofia,S. Swaminathan,Thomas E. Edwards +12 more
TL;DR: The details of HCV RNA replication are studied by determining crystal structures of stalled polymerase ternary complexes with enzymes, RNA templates, RNA primers, incoming nucleotides, and catalytic metal ions during both primed initiation and elongation of RNA synthesis.
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The crystal structure of cruzain: a therapeutic target for Chagas' disease.
Mary E. McGrath,Ann E. Eakin,Juan C. Engel,James H. McKerrow,Charles S. Craik,Robert J. Fletterick +5 more
TL;DR: X-ray crystal structure of cruzain complexed with the potent inhibitor Z-Phe-Ala-fluoromethyl ketone shows that a biotinylated form of the bound inhibitor does not effectively reach host proteases in their lysosomal compartment, but is selectively taken up by the parasite.
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Structural, Biochemical, and Biophysical Characterization of Idelalisib Binding to Phosphoinositide 3-Kinase δ
John R. Somoza,David Koditek,Armando G. Villaseñor,Nikolai Novikov,Melanie H. Wong,Albert Liclican,Weimei Xing,Leanna Lagpacan,Ruth Wang,Brian E. Schultz,Giuseppe A. Papalia,Dharmaraj Samuel,Latesh Lad,Mary E. McGrath +13 more
TL;DR: The data show that idelalisib is a potent and selective inhibitor of the kinase activity of PI3Kδ, and a crystal structure of idELalisib bound to the p110δ subunit ofPI3K δ furthers the understanding of the binding interactions that confer the potency and selectivity of the compound.
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Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex
C. J. Linnevers,Mary E. McGrath,Randall Armstrong,F. R. Mistry,M. G. Barnes,J L Klaus,James T. Palmer,Bradley A. Katz,Dieter Brömme +8 more
TL;DR: The wild‐type sequence of the protease has been mutated so as to replace a potential N‐glycosylation site in cathepsin K to facilitate structural studies of the protein.