The DOI matches its Crossref record; 163 of the 163 references it cites were found in a registry or an index.
Writers and Readers of Histone Acetylation: Structure, Mechanism, and Inhibition
Open accessAbstract
Histone acetylation marks are written by histone acetyltransferases (HATs) and read by bromodomains (BrDs), and less commonly by other protein modules. These proteins regulate many transcription-mediated biological processes, and their aberrant activities are correlated with several human diseases. Consequently, small molecule HAT and BrD inhibitors with therapeutic potential have been developed. Structural and biochemical studies of HATs and BrDs have revealed that HATs fall into distinct subfamilies containing a structurally related core for cofactor binding, but divergent flanking regions for substrate-specific binding, catalysis, and autoregulation. BrDs adopt a conserved left-handed four-helix bundle to recognize acetyllysine; divergent loop residues contribute to substrate-specific acetyllysine recognition.
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“However, significant hCD1 activity in Y782F hCD12 was observed with C-terminal acetyllysine peptide substrates 9 and 10 , indicating that hCD1 was indeed catalytically active, but exhibited strict substrate specificity for substrates bearing C-terminal acetyllysine residues (Fig.”
Metadata
- Authors
- Marmorstein, R., & Zhou, M.-M.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2014-07-01
- Volume
- 6
- Issue
- 7
- Pages
- a018762-a018762
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2143277424
- Cited by
- 638
- References
- 163
- Type
- posted content
- Language
- en
- Open access
- bronze
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