Is acetylation the key to opening locked gates?

Research output: Contribution to journalShort survey

2 Citations (Scopus)

Abstract

Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.

Original languageEnglish (US)
Pages (from-to)298-300
Number of pages3
JournalNature Structural and Molecular Biology
Volume11
Issue number4
DOIs
StatePublished - Apr 1 2004

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Acetyltransferases
Acetylation
Protein Kinases
Catalytic Domain
Proteins

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

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title = "Is acetylation the key to opening locked gates?",
abstract = "Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.",
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Is acetylation the key to opening locked gates? / Pugh, B. Franklin.

In: Nature Structural and Molecular Biology, Vol. 11, No. 4, 01.04.2004, p. 298-300.

Research output: Contribution to journalShort survey

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AB - Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.

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