Structure and functions of the GNAT superfamily of acetyltransferases.

By M. Vetting, Luiz Pedro S de Carvalho, Michael Yu, S. Hegde, S. Magnet, S. Roderick, J. Blanchard. Archives of Biochemistry and Biophysics, 2005

618 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/7b9d61fc45ad93097b3fc14fb63e8cb7ef378ed4

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1. Gerard D. Wright

Citations in the corpus

• The antibiotic resistome: the nexus of chemical and genetic diversity (2007, background): “This protein scaffold seems to be particularly malleable, with functions of member enzmyes ranging from small-molecule acetylation (for example, AACs) to protein modification (for example, histone acetyltransferases”
• Aminoglycoside Modifying Enzymes (2010, background): “Aminoglycoside modifying enzymes: aminoglycoside N-acetyltransferases (AACs) AACs belong to the ubiquitous GCN5-related N-acetyltransferase (GNAT) superfamily of proteins, which include about 10,000 proteins (Vetting et al., 2005).”