H
Howard C. Hang
Researcher at Rockefeller University
Publications - 138
Citations - 9170
Howard C. Hang is an academic researcher from Rockefeller University. The author has contributed to research in topics: Palmitoylation & Fatty acylation. The author has an hindex of 48, co-authored 124 publications receiving 7922 citations. Previous affiliations of Howard C. Hang include Scripps Health & Torrey Pines Institute for Molecular Studies.
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Journal ArticleDOI
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Hong Jiang,Saba Khan,Yi Wang,Guillaume Charron,Bin He,Carlos Sebastian,Jintang Du,Raymond J. Kim,Eva J. Ge,Raul Mostoslavsky,Howard C. Hang,Quan Hao,Hening Lin +12 more
TL;DR: It is shown that human SIRT6 efficiently removes long-chain fatty acyl groups, such as myristoyl, from lysine residues and promotes the secretion of tumour necrosis factor-α (TNF-α) by removing the fatty acy modification on K19 and K20 of TNF- α.
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A chemical approach for identifying O-GlcNAc-modified proteins in cells
TL;DR: A chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro is described, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification, tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
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A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
TL;DR: A method for labeling mucin-type O-linked glycoproteins with a unique chemical tag, the azide, which permits their selective covalent modification from complex cell lysates, and was validated by labeling a recombinant glycoprotein that is known to possess O- linked glycans with GalNAz.
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Palmitoylome profiling reveals S-palmitoylation–dependent antiviral activity of IFITM3
Jacob S. Yount,Bruno Moltedo,Yu-Ying Yang,Guillaume Charron,Thomas M. Moran,Carolina B. López,Howard C. Hang +6 more
TL;DR: In this paper, the antiviral activity of interferon-induced transmembrane protein 3 (IFITM3) is post-translationally regulated by S-palmitoylation.