T
Thomas J. McMurry
Researcher at Stanford University
Publications - 25
Citations - 1016
Thomas J. McMurry is an academic researcher from Stanford University. The author has contributed to research in topics: G protein-coupled receptor & Allosteric regulation. The author has an hindex of 14, co-authored 25 publications receiving 985 citations.
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Journal ArticleDOI
Structural characterization of horseradish peroxidase using EXAFS spectroscopy: evidence for Fe=O ligation in compounds I and II
James E. Penner-Hahn,K S Eble,Thomas J. McMurry,Mark W. Renner,Alan L. Balch,Jay T. Groves,John H. Dawson,Keith O. Hodgson +7 more
TL;DR: The present work demonstrates unambiguously that a short, ca.
Journal ArticleDOI
Ferric ion sequestering agents. 22. Synthesis and characterization of macrobicyclic iron(III) sequestering agents
Thomas M. Garrett,Thomas J. McMurry,Mir Wais Hosseini,Zelideth E. Reyes,F. Ekkehardt Hahn,Kenneth N. Raymond +5 more
Journal ArticleDOI
Preparation and Characterization of a Dialkoxyiron(IV) Porphyrin
TL;DR: In this article, a precurseur radicalaire cationique d'une porphyrine de Fer(III) is presented, a partir d'un precurseurs radicalaire Cationique de Fer (III).
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Discovery of a CXCR4 agonist pepducin that mobilizes bone marrow hematopoietic cells
Boris Tchernychev,Yong Ren,Pallavi Sachdev,Jay M. Janz,Lynn Haggis,Adam O'Shea,Ed McBride,Richard J. Looby,Qing Deng,Thomas J. McMurry,Manija A. Kazmi,Thomas P. Sakmar,Stephen W. Hunt,Kenneth E. Carlson +13 more
TL;DR: ITA-2341 is a potent and efficacious mobilizer of bone marrow PMNs and HSPCs and could represent a previously undescribed therapeutic approach for the recruitment of HSPC collection before autologous bone marrow transplantation (ABMT).
Journal ArticleDOI
X-ray absorption spectroscopic studies of high valent iron porphyrins. Horseradish peroxidase compounds I and II and synthetic models.
James E. Penner-Hahn,Thomas J. McMurry,Mark W. Renner,L Latos-Grazynsky,K S Eble,I. M. Davis,Alan L. Balch,John T. Groves,John H. Dawson,Keith O. Hodgson +9 more
TL;DR: The shapes of the absorption edges further support the assignment of HRP-I and one of the model compounds as Fe(IV)-porphyrin pi-cations and demonstrate that the iron sites in the model porphyrins are not identical to the iron Sites in the enzyme.