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A Myosin V Inhibitor Based on Privileged Chemical Scaffolds
Author(s) -
Islam Kabirul,
Chin Harvey F.,
Olivares Adrian O.,
Saunders Lauren P.,
De La Cruz Enrique M.,
Kapoor Tarun M.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201004026
Subject(s) - myosin , adenosine triphosphate , nucleotide , motor protein , adenosine , intracellular , adenosine diphosphate , chemistry , molecular motor , key (lock) , biochemistry , computer science , computational biology , microbiology and biotechnology , biology , gene , microtubule , platelet , platelet aggregation , immunology , computer security
Switching the motor off : Privileged chemical scaffolds were used as a starting point for the development of a specific chemical inhibitor 1 of myosin V, a key motor protein required for intracellular transport (see picture; ADP=adenosine diphosphate, ATP=adenosine triphosphate). The potency of 1 , which does not compete directly with nucleotide binding, is comparable to that of other known motor‐protein inhibitors used as probes in chemical biology.