Flexibility and inhibitor binding in cdc25 phosphatases.
about
Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.Overexpression of p42.3 promotes cell growth and tumorigenicity in hepatocellular carcinomaIdentification of the quinolinedione inhibitor binding site in Cdc25 phosphatase B through docking and molecular dynamics simulations.Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases.Modeling loop backbone flexibility in receptor-ligand docking simulations.
P2860
Flexibility and inhibitor binding in cdc25 phosphatases.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-hans
2010年学术文章
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2010年学术文章
@zh-sg
2010年學術文章
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2010年學術文章
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2010年學術文章
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name
Flexibility and inhibitor binding in cdc25 phosphatases.
@en
Flexibility and inhibitor binding in cdc25 phosphatases.
@nl
type
label
Flexibility and inhibitor binding in cdc25 phosphatases.
@en
Flexibility and inhibitor binding in cdc25 phosphatases.
@nl
prefLabel
Flexibility and inhibitor binding in cdc25 phosphatases.
@en
Flexibility and inhibitor binding in cdc25 phosphatases.
@nl
P2860
P356
P1433
P1476
Flexibility and inhibitor binding in cdc25 phosphatases.
@en
P2860
P304
P356
10.1002/PROT.22826
P407
P577
2010-11-01T00:00:00Z