A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain
about
Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasmA novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphataseThe protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cellsPTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agentsProtein tyrosine phosphatase (PC12, Br7,S1) family: expression characterization in the adult human and mouseThe MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTPPhosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathwayERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Inhibitor of the tyrosine phosphatase STEP reverses cognitive deficits in a mouse model of Alzheimer's diseaseProtein tyrosine phosphatases as negative regulators of mitogenic signalingSynaptic plasticity: one STEP at a time.Regulation of stress-activated protein kinase signaling pathways by protein phosphatases.Follicle-stimulating hormone activates extracellular signal-regulated kinase but not extracellular signal-regulated kinase kinase through a 100-kDa phosphotyrosine phosphataseResting and active states of the ERK2:HePTP complex.Latent herpes simplex virus infection of sensory neurons alters neuronal gene expression.Down-regulation of BDNF in cell and animal models increases striatal-enriched protein tyrosine phosphatase 61 (STEP61 ) levels.Structural basis of p38α regulation by hematopoietic tyrosine phosphatase.Long-term dynamics of multisite phosphorylationThe differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular studyPTPRR protein tyrosine phosphatase isoforms and locomotion of vesicles and mice.Toward an in situ phospho-protein atlas: phospho- and site-specific antibody-based spatio-temporally systematized detection of phosphorylated proteins in vivo.Molecular basis of MAP kinase regulation.Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.Molecular cloning of a mouse epithelial protein-tyrosine phosphatase with similarities to submembranous proteins.Characterization of multiple transcripts and isoforms derived from the mouse protein tyrosine phosphatase gene Ptprr.The mouse Ptprr gene encodes two protein tyrosine phosphatases, PTP-SL and PTPBR7, that display distinct patterns of expression during neural development.
P2860
Q22010423-958BBE2C-8BE3-4DBD-B9BE-9135B2926D35Q22010940-9C67717B-55E9-422B-9837-A5804A27EA49Q24294952-3E9A559C-5A46-487D-9FD3-C2A33C35C5D3Q24533479-3EC5303B-6018-4ED9-AA55-8217BEE82FC3Q28116921-B157CFF0-CF3C-408A-8E92-2183C227FEFAQ28137874-0A3EE4E8-45B0-4125-97D1-02194ED8C573Q28145888-D77D51C9-D834-43A7-807F-B4EF635FFE49Q28202064-B0A34646-5A4A-49FA-BF71-F5BF92A4CB4AQ28271104-44694089-DCC4-4ED6-8114-AE1FEE5F9DE8Q28541603-0A719F44-1B65-4C22-BB5F-16FC99A625AAQ29013218-1B2AD123-C5CB-453A-8652-C01E1494C5B2Q30541159-4CA97D4D-E166-4F5B-ADB4-60B34A23C13BQ34539377-4539E8C1-32F5-4358-813E-990CAC601663Q35024993-834FCECF-A319-43C1-BEB2-1638DEEB7086Q35534815-F2A524F6-98CB-423B-A43E-1B65759CB5A6Q35803233-73491055-08B9-404E-8E61-B2E0A32A9E75Q36627183-8690E3C4-E3CA-455C-A0AD-8C42589C7D35Q36852670-3B08AEB3-EFD2-40EA-A246-C94892162105Q37095279-3932976A-AC2D-402D-A12D-F73114E67444Q37161124-3663D07E-D911-4135-B936-1C62FE7493E9Q37223796-BC17AD41-7170-4F6C-9D3B-84DFAD8DFEDFQ37538635-D92043D1-3E0C-4967-BFC5-EE0F9F467379Q38151621-A9040F97-9D0E-4B3E-A790-6332DFE3C686Q40768240-C3FD4A6E-CF3E-4EF0-A86D-A33920F18372Q42635881-4EAFFC7A-B745-48A4-A194-C1CF9AC438F8Q45088264-BD3807A2-561D-4D11-8F1F-605B92DB3CECQ52172816-112BFFA1-FA67-46ED-B0E0-8537EDB04132
P2860
A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain
description
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1995
@ast
im Januar 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/01/15)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/01/15)
@nl
наукова стаття, опублікована в січні 1995
@uk
مقالة علمية نشرت في 15-1-1995 حول موضوع: دماغ
@ar
name
A novel receptor-type protein ...... cally expressed in mouse brain
@ast
A novel receptor-type protein ...... cally expressed in mouse brain
@en
A novel receptor-type protein ...... cally expressed in mouse brain
@nl
type
label
A novel receptor-type protein ...... cally expressed in mouse brain
@ast
A novel receptor-type protein ...... cally expressed in mouse brain
@en
A novel receptor-type protein ...... cally expressed in mouse brain
@nl
prefLabel
A novel receptor-type protein ...... cally expressed in mouse brain
@ast
A novel receptor-type protein ...... cally expressed in mouse brain
@en
A novel receptor-type protein ...... cally expressed in mouse brain
@nl
P2093
P2860
P3181
P356
P1433
P1476
A novel receptor-type protein ...... cally expressed in mouse brain
@en
P2093
B. Wieringa
C. Brugman
J. Schepens
P. Zeeuwen
W. Hendriks
P2860
P304
P3181
P356
10.1042/BJ3050499
P407
P478
305 ( Pt 2)
P577
1995-01-15T00:00:00Z