A heteromorphic protein-tyrosine phosphatase, PTP phi, is regulated by CSF-1 in macrophages.
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Biology and action of colony--stimulating factor-1GLEPP1/protein-tyrosine phosphatase phi inhibitors block chemotaxis in vitro and in vivo and improve murine ulcerative colitisGenome-wide review of transcriptional complexity in mouse protein kinases and phosphatases.Protein tyrosine phosphatase (PC12, Br7,S1) family: expression characterization in the adult human and mouseAssociation of the T-cell protein tyrosine phosphatase with nuclear import factor p97Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signallingAltered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rateIdentification of a receptor-type protein tyrosine phosphatase expressed in postmitotic maturing neurons: its structure and expression in the central nervous systemPhosphorylation of CSF-1R Y721 mediates its association with PI3K to regulate macrophage motility and enhancement of tumor cell invasion.A novel macrophage actin-associated protein (MAYP) is tyrosine-phosphorylated following colony stimulating factor-1 stimulationExpression of PTPRO in the interneurons of adult mouse olfactory bulbDifferential use of signal peptides and membrane domains is a common occurrence in the protein output of transcriptional units.Roles of protein tyrosine phosphatases in cell migration and adhesion.Structural and evolutionary relationships among protein tyrosine phosphatase domainsRegulation of tyrosine phosphorylation in macrophage phagocytosis and chemotaxis.Protein tyrosine phosphatase phi regulates paxillin tyrosine phosphorylation and mediates colony-stimulating factor 1-induced morphological changes in macrophages.A functional nuclear localization sequence in the C-terminal domain of SHP-1.Expression of a structurally unique osteoclastic protein-tyrosine phosphatase is driven by an alternative intronic, cell type-specific promoter.An osteoclastic protein-tyrosine phosphatase may play a role in differentiation and activity of human monocytic U-937 cell-derived, osteoclast-like cells.Functional involvement of PTP-U2L in apoptosis subsequent to terminal differentiation of monoblastoid leukemia cells.The PTPROt tyrosine phosphatase functions as an obligate haploinsufficient tumor suppressor in vivo in B-cell chronic lymphocytic leukemia.
P2860
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P2860
A heteromorphic protein-tyrosine phosphatase, PTP phi, is regulated by CSF-1 in macrophages.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@ast
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@en
type
label
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@ast
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@en
prefLabel
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@ast
A heteromorphic protein-tyrosi ...... lated by CSF-1 in macrophages.
@en
P2093
P2860
P356
P1476
A heteromorphic protein-tyrosi ...... ulated by CSF-1 in macrophages
@en
P2093
D B Einstein
E R Stanley
M G Dominguez
P2860
P304
27339-27347
P356
10.1074/JBC.270.45.27339
P407
P50
P577
1995-11-01T00:00:00Z