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Nature Structural Biology

Volumn 8, Issue 11, 2001, Pages 947-952

Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity

(4) Stevens, Shawn Y a Sanker, Subramaniam a,b Kent, Claudia a Zuiderweg, Erik R P a

a UNIVERSITY OF MICHIGAN (United States)

b LERNER RESEARCH INSTITUTE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; ENERGY TRANSFER; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SUBSTITUTION; ARGININE; CYTIDINE TRIPHOSPHATE; DIMERIZATION; ENTROPY; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEOTIDYLTRANSFERASES; PROTEIN BINDING; PROTEIN CONFORMATION; TITRIMETRY;

EID: 0034765285 PISSN: 10728368 EISSN: None Source Type: Journal
DOI: 10.1038/nsb1101-947 Document Type: Article

Times cited : (88)

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