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In a model of spinal cord injury, blocking PTPalpha and LAR receptors promotes oligodendrogenesis.
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PTPalpha coordinates oligodendroglial and neuronal development and myelination.
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RPTPalpha mediates proinflammatory and proinvasive signaling in rheumatoid arthritis fibroblast-like synoviocytes (FLS), correlating with the promotion of disease in an FLS-dependent model of rheumatoid arthritis.
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Ptpra coordinates the regulation of the Fyn signaling pathway in corpus striatum.
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PTPs alpha and epsilon play distinct roles in osteoclasts.
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PTP-alpha promotes profibrotic signaling pathways in fibroblasts through control of cellular responsiveness to TGF-beta.
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The focal adhesion targeting domain of FAK interacts with protein-tyrosine phosphatase-alpha to restrict IL1-induced Ca2+ release, ERK activation, and MMP-9 expression.
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PTPalpha may be involved in the formation of axoglial junctions and ensheathment in small axons during myelination of the spinal cord.
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Findings indicate Grb2 as a new FAK activator and in coordinating PTPalpha tyrosine phosphorylation to enable downstream integrin signaling and migration.
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Results suggest that inhibition of PTPalpha can have a beneficial effect on HER2-positive breast cancers, but that inhibition of additional targets is needed to block breast tumorigenesis.
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Inflammation-induced connective tissue degradation involving fibroblasts requires functionally active PTPalpha.
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study described a molecular complex of PTPalpha-BCAR3-Cas-Src; this complex forms in response to PTPalpha Tyr789 phosphorylation and mediates Cas localization to focal adhesions and Cas downstream signaling to promote cell migration
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Protein-tyrosine phosphatase alpha acts in oligodendrocyte progenitor cells to limit self-renewal and facilitate differentiation.
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protein kinase C and protein tyrosine phosphatase alpha participate in Src activation by 1alpha,25OH2 vitamin D3 in C2C12 skeletal muscle cells
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the PTPalpha-mediated increase of NB-3 level at the cell surface represents a novel function of PTPalpha in NB-3 signaling in neural development
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these findings indicate that PTPalpha acts as an Ag-stimulated Lyn-Fyn phosphatase and a critical positive regulator of these Src family kinases in FcepsilonRI signaling
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The results suggest that transformation by PTPalpha involves at least one function other than, or in addition to, its activation of Src and that this depends on PTPalpha's extracellular domain.
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Expression of CD45RA and -RC isoforms is increased 20- to 200-fold on T cells from mice with a loss-of-function mutation in RNA-binding protein heterogeneous nuclear ribonucleoprotein L-like, although total CD45 expression is unaltered.
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Results describe the role of nitric oxide in regulating the focal adhesion proteins, Src, FAK, p130 Cas, and PTP-alpha.
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IL-1-induced signaling through focal adhesions leading to MMP3 release and interactions between SHP-2 and PTPalpha are dependent on the integrity of the catalytic domains of PTPalpha.