B
Brent R. Martin
Researcher at University of Michigan
Publications - 50
Citations - 3764
Brent R. Martin is an academic researcher from University of Michigan. The author has contributed to research in topics: Palmitoylation & Protein palmitoylation. The author has an hindex of 24, co-authored 50 publications receiving 3351 citations. Previous affiliations of Brent R. Martin include Life Sciences Institute & University of California, San Diego.
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Journal ArticleDOI
New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications.
Stephen R. Adams,Robert E. Campbell,Larry A. Gross,Brent R. Martin,Grant K. Walkup,Yong Yao,Juan Llopis,Roger Y. Tsien +7 more
TL;DR: Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed alpha-helix.
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Large-scale profiling of protein palmitoylation in mammalian cells
TL;DR: It is demonstrated that the commercially available compound 17-octadecynoic acid (17-ODYA) can serve as a bioorthogonal, click chemistry probe for in situ labeling, identification and verification of palmitoylated proteins in human cells.
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Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity.
TL;DR: Improved biarsenical-tetracysteine motifs should enable detection of a much broader spectrum of cellular proteins, culminating in a >20-fold increase in contrast.
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Global profiling of dynamic protein palmitoylation
TL;DR: The metabolic incorporation of the palmitic acid analog 17-octadecynoic acid (17-ODYA) in combination with stable-isotope labeling with amino acids in cell culture and pulse-chase methods is reported to generate a global quantitative map of dynamic protein palmitoylation events in cells.
Journal ArticleDOI
Click-generated triazole ureas as ultrapotent in vivo–active serine hydrolase inhibitors
Alexander Adibekian,Brent R. Martin,Chu Wang,Ku-Lung Hsu,Daniel A. Bachovchin,Sherry Niessen,Heather Hoover,Benjamin F. Cravatt +7 more
TL;DR: 1,2,3-triazole ureas is designated as a pharmacologically privileged chemotype for SH inhibition that shows broad activity across the SH class coupled with tunable selectivity for individual enzymes.