Structure of a Ternary Naa50p (NAT5/SAN) N-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation
Journal Article
·
· Journal of Biological Chemistry
- Research Organization:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE SC OFFICE OF SCIENCE (SC)
- DOE Contract Number:
- DE-AC02-98CH10886
- OSTI ID:
- 1069414
- Report Number(s):
- BNL-99986-2013-JA
- Journal Information:
- Journal of Biological Chemistry, Vol. 286, Issue 42; ISSN 0021--9258
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structural Basis of Substrate-Binding Specificity of Human Arylamine N-acetyltransferases
System-wide Studies of N-Lysine Acetylation in Rhodopseudomonas palustris Reveals Substrate Specificity of Protein Acetyltransferases
Crystal Structures of Murine Carnitine Acetyltransferase in Ternary Complexes with Its Substrates
Journal Article
·
Mon Jan 01 00:00:00 EST 2007
· Journal of Biological Chemistry
·
OSTI ID:1069414
+5 more
System-wide Studies of N-Lysine Acetylation in Rhodopseudomonas palustris Reveals Substrate Specificity of Protein Acetyltransferases
Journal Article
·
Sun Jan 01 00:00:00 EST 2012
· Journal of Biological Chemistry
·
OSTI ID:1069414
Crystal Structures of Murine Carnitine Acetyltransferase in Ternary Complexes with Its Substrates
Journal Article
·
Sun Jan 01 00:00:00 EST 2006
· Journal of Biological Chemistry
·
OSTI ID:1069414