Development of Inhibitors That Selectively Disrupt Substrate Recognition by Cyclin-Dependent Kinases

2002 ◽  
Author(s):  
James Wohlschlegel ◽  
Anindya Dutta
Keyword(s):  
Substrate Recognition ◽  
Cyclin Dependent Kinases

scholarly journals Structure-function relationships of the yeast cyclin-dependent kinase Pho85.

1995 ◽  
Vol 15 (10) ◽  
pp. 5482-5491 ◽  
Author(s):  
R C Santos ◽  
N C Waters ◽  
C L Creasy ◽  
L W Bergman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Structure Function ◽  
Cell Cycle Progression ◽  
Substrate Recognition ◽  
The Other ◽  
Cyclin Dependent Kinase ◽  
Cycle Progression ◽  
Cyclin Dependent Kinases ◽  
Induced Mutagenesis

The PHO85 gene of Saccharomyces cerevisiae encodes a cyclin-dependent kinase involved in both transcriptional regulation and cell cycle progression. Although a great deal is known concerning the structure, function, and regulation of the highly homologous Cdc28 protein kinase, little is known concerning these relationships in regard to Pho85. In this study, we constructed a series of Pho85-Cdc28 chimeras to map the region(s) of the Pho85 molecule that is critical for function of Pho85 in repression of acid phosphatase (PHO5) expression. Using a combination of site-directed and ethyl methanesulfonate-induced mutagenesis, we have identified numerous residues critical for either activation of the Pho85 kinase, interaction of Pho85 with the cyclin-like molecule Pho80, or substrate recognition. Finally, analysis of mutations analogous to those previously identified in either Cdc28 or cdc2 of Schizosaccharomyces pombe suggested that the inhibition of Pho85-Pho80 activity in mechanistically different from that seen in the other cyclin-dependent kinases.

scholarly journals A Bipartite Substrate Recognition Motif for Cyclin-dependent Kinases

2000 ◽  
Vol 276 (3) ◽  
pp. 1993-1997 ◽  
Author(s):  
David Y. Takeda ◽  
James A. Wohlschlegel ◽  
Anindya Dutta
Keyword(s):  
Substrate Recognition ◽  
Cyclin Dependent Kinases ◽  
Recognition Motif

Cyclin-dependent kinases: inhibition and substrate recognition

1999 ◽  
Vol 9 (6) ◽  
pp. 738-744 ◽  
Author(s):  
Jane A Endicott ◽  
Martin EM Noble ◽  
Julie A Tucker
Keyword(s):  
Substrate Recognition ◽  
Cyclin Dependent Kinases

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

Phosphorylation of androgen receptor at serine 81 by cyclin-dependent kinases

2016 ◽  
Author(s):  
Zuzana Skraškova ◽  
Radek Jorda ◽  
Eva Řezničkova ◽  
Vladimir Kryštof
Keyword(s):  
Androgen Receptor ◽  
Cyclin Dependent Kinases
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