Crystallographic and kinetic analyses of human IPMK reveal disordered domains modulate ATP binding and kinase activity.

Seacrist CD, Blind RD
Sci Rep. 2018 8 (1): 16672

PMID: 30420721 · PMCID: PMC6232094 · DOI:10.1038/s41598-018-34941-3

MeSH Terms (10)

Adenosine Triphosphate Crystallography Humans Inositol Phosphates Kinetics Phosphorylation Phosphotransferases (Alcohol Group Acceptor) Protein Binding Protein Structure, Secondary Signal Transduction

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