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Reversible acetylation in the regulation of protein function is a ubiquitous posttranslational modification that rivals phosphorylation in its scope. Rooted in the discovery of histone acetylation more than 50 years ago, lysine acetylation-deacetylation cycles are now known to regulate the cellular functions of nuclear and cytoplasmic proteins in epigenetics, cell signaling, metabolism, and other biological processes. Thus, acetylation in biology is not limited solely to histone proteins in the nucleus.
Three classes of proteins are involved in the chemical biology of the acetylome: “writers”, or histone acetylases (also known as lysine acetyltransferases); “readers”, i.e., bromodomain-containing proteins that specifically recognize the acetyllysine moiety; and “erasers”, or histone deacetylases (HDACs, also known more generally as lysine deacetylases since both histone and nonhistone proteins are substrates). Our group focuses on the metal-dependent HDACs, which typically require a single zinc ion for catalytic activity in the hydrolysis of acetyllysine
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论文共 504 篇作者统计合作学者相似作者
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ACS Medicinal Chemistry Letters (2024)
Matthew N Gaynes,David W Christianson
Methods in enzymology (2024): 1-23
ACCOUNTS OF CHEMICAL RESEARCHno. 8 (2024): 1135-1148
JOURNAL OF BIOLOGICAL CHEMISTRYno. 10 (2023)
Frontiers in ethology (2023)
Beate Ko''nig,Paris R. Watson,Nina Ressing,Abigail D. Cragin, Linda Scha''ker-Hu''bner,David W. Christianson,Finn K. Hansen
crossref(2023)
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#Papers: 504
#Citation: 27214
H-Index: 91
G-Index: 152
Sociability: 7
Diversity: 0
Activity: 2
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