105108-59-6Relevant articles and documents
The First Direct Evaluation of the Two-Active Site Mechanism for Chitin Synthase
Yeager, Adam R.,Finney, Nathaniel S.
, p. 613 - 618 (2004)
Chitin synthase polymerizes UDP-GlcNAc to form chitin (poly-β (1,4)-GlcNAc) and is essential for fungal cell wall biosynthesis. The alternating orientation of the GlcNAc residues within the chitin chain has led to the proposal that chitin synthase possesses two active sites. We report the results of the first direct test of this possibility. Two simple uridine-derived dimeric inhibitors are shown to exhibit 10-fold greater inhibition than a monomeric control, consistent with the presence of two active sites. This observation has important implications for the development of antifungal agents, as well as the understanding of polymerizing glycosyltransferases.
PRODRUGS OF THE TYROSINE KINASE INHIBITOR FOR TREATING CANCER
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Paragraph 00151-00152, (2021/03/05)
There are provided compounds of Formula (I), and pharmaceutically acceptable salts and esters thereof, and pharmaceutical compositions thereof, useful for inhibition or modulation of the activity of tyrosine kinases and treatment of disease states or conditions mediated by tyrosine kinases, including cancers. (I)
PEPTIDE DERIVATIVES
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, (2008/06/13)
The invention concerns pharmaceutically useful trifluoromethyl ketone substituted di-, tri-and tetra-peptide derivatives of the formulae Ia, Ib, Ic set out hereinafter, and salts thereof, which are inhibitors of human leukocyte elastase. Also described herein are pharmaceutical compositions containing a peptide derivative and processes and intermediates for use in the manufacture of the peptide derivatives.
