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The protein encoded by PTPRE is a member of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen PTPRE Antikörper (132) und und viele weitere Produktgruppen zu diesem Protein an.
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these data demonstrate that HCV infection reduces PTPRE expression in the liver and peripheral blood mononuclear cell sof infected humans
Epidermal growth factor receptor (EGFR)-mediated positive feedback of protein-tyrosine phosphatase epsilon (PTPepsilon) on ERK1/2 and AKT protein pathways is required for survival of human breast cancer cells.
Studies indicate that RAD50 and PTPRE of crude associations with asthma at a Bonferroni-corrected level of significance, while IL4R, CCL5 and TBXA2R of nominal significance.
Transfection of cells with different PTPepsilon constructs and activator protein-1 reporter gene indicates that the catalytic activity of PTPepsilon is involved in the regulation of the mitogen-activated protein kinase cascade.
Characterization, expression and functional aspects of an alternative spliced isoform of protein tyrosine phosphatase epsilon
interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs
Functions to prevent inappropriate activation and to terminate prolonged, rather than acute, activation of ERK in the cytosol.
cyt-PTP epsilon is dimerized and phosphorylated in the absence of direct interaction between the PTP and extracellular molecules
Transgenic mice overexpressing catalytically inactive transmembrane protein tyrosine phosphatase epsilon provide unexpected insight into the cell-cell interactions that occur between oligodendrocytes and the cells which they myelinate.
Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling
GRB2 physically links cyt-PTPe with Src and enables cyt-PTPe to activate Src downstream of activated integrins in osteoclast-like cells.
PTPs alpha and epsilon play distinct roles in osteoclasts.
Multifaceted modulation of K+ channels by protein-tyrosine phosphatase epsilon tunes neuronal excitability.
Integrin activation regulates cyt-PTPe via Src-dependent Y638 phosphorylation. cyt-PTPe affects osteoclast podosome stability by a feedback loop ensuring proper Src activation downstream of integrins, linking their signaling with Src activation.
Findings demonstrate that PTPalpha is a critical regulator of Fyn activation and of specific Fyn signaling events during differentiation, and is essential for promoting OPC differentiation and central nervous system myelination.
RPTPepsilon is a physiological activator of Src in Neu-induced mammary tumors.
PTPepsilon as a phosphatase required for optimal structure, subcellular organization, and function of osteoclasts
Receptor-like protein tyrosine phosphatase zeta/RPTP beta is expressed on tangentially aligned neurons in early mouse neocortex.
Protein tyrosine phosphatase epsilon activates Yes and Fyn in mammary tumor cells.
We conclude that PTPepsilon and PTPalpha differ significantly in their regulation of Kv channels and Src in the system examined and that similarity between PTPs does not necessarily result in full functional redundancy in vivo.
Data show that association of protein tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor.
cytosolic PTPepsilon serves as another major candidate negative regulator of insulin receptor signaling in skeletal muscle
findings show that PTPe is expressed in erythrocytes & is involved in red cell signaling networks
Data suggest that PTPepsilon negatively regulates FcepsilonRI-mediated signalling pathways and thus constitutes a novel target for ameliorating allergic conditions.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Two alternatively spliced transcript variants of this gene have been reported, one of which encodes a receptor-type PTP that possesses a short extracellular domain, a single transmembrane region, and two tandem intracytoplasmic catalytic domains\; Another one encodes a PTP that contains a distinct hydrophilic N-terminus, and thus represents a nonreceptor-type isoform of this PTP. Studies of the similar gene in mice suggested the regulatory roles of this PTP in RAS related signal transduction pathways, cytokines induced SATA signaling, as well as the activation of voltage-gated K+ channels.
protein tyrosine phosphatase, receptor type, A
, receptor-type tyrosine-protein phosphatase epsilon
, protein tyrosine phosphatase, receptor type, epsilon polypeptide
, protein-tyrosine phosphatase epsilon
, protein tyrosine phosphatase epsilon
, protein tyrosine phosphatase epsilon-like 1
, protein tyrosine phosphatase epsilon-like 2
, protein tyrosine phosphatase, receptor type, epsilon