Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132.
about
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilisEssential role of protein kinase C zeta in transducing a motility signal induced by superoxide and a chemotactic peptide, fMLP.The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamicsThe role of low-molecular-weight protein tyrosine phosphatase (LMW-PTP ACP1) in oncogenesis.Low Mr phosphotyrosine protein phosphatase associates and dephosphorylates p125 focal adhesion kinase, interfering with cell motility and spreading.The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases.
P2860
Low molecular weight protein-tyrosine phosphatase controls the rate and the strength of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132.
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
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2000年論文
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2000年论文
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2000年论文
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2000年论文
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name
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@en
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@nl
type
label
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@en
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@nl
prefLabel
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@en
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@nl
P2093
P2860
P356
P1476
Low molecular weight protein-t ...... lation on tyrosine 131 or 132.
@en
P2093
Buricchi F
Chiarugi P
P2860
P304
37619-37627
P356
10.1074/JBC.M006375200
P407
P577
2000-12-01T00:00:00Z