Regulation of cellular protein phosphatase-1 (PP1) by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors
about
SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscleCalcium Sensitization Mechanisms in Gastrointestinal Smooth MusclesThe Function of Rho-Associated Kinases ROCK1 and ROCK2 in the Pathogenesis of Cardiovascular DiseaseThe role of actin filament dynamics in the myogenic response of cerebral resistance arteriesEndogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling.Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractilityIntegrin-linked kinase is a functional Mn2+-dependent protein kinase that regulates glycogen synthase kinase-3β (GSK-3beta) phosphorylationMechanical activation of angiotensin II type 1 receptors causes actin remodelling and myogenic responsiveness in skeletal muscle arterioles.Nuclear localization of CPI-17, a protein phosphatase-1 inhibitor protein, affects histone H3 phosphorylation and corresponds to proliferation of cancer and smooth muscle cells.Protein Ser/Thr phosphatases--the ugly ducklings of cell signalling.Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1).Role of PKC and RhoA/ROCK pathways in the spontaneous phasic activity in the rectal smooth muscle.Cholangiocyte myosin IIB is required for localized aggregation of sodium glucose cotransporter 1 to sites of Cryptosporidium parvum cellular invasion and facilitates parasite internalizationA bioinformatic and computational study of myosin phosphatase subunit diversity.Myosin phosphatase isoforms and related transcripts in the pig coronary circulation and effects of exercise and chronic occlusion.Neural programming of mesenteric and renal arteries.G protein-mediated Ca²+-sensitization of CPI-17 phosphorylation in arterial smooth muscleVascular smooth muscle phenotypic diversity and functionProtein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunitRole of rho kinase in the functional and dysfunctional tonic smooth muscles.The extended PP1 toolkit: designed to create specificity.Inside-out Regulation of Ectodomain Cleavage of Cluster-of-Differentiation-44 (CD44) and of Neuregulin-1 Requires Substrate Dimerization.Tra2β protein is required for tissue-specific splicing of a smooth muscle myosin phosphatase targeting subunit alternative exon.Reciprocal regulation controlling the expression of CPI-17, a specific inhibitor protein for the myosin light chain phosphatase in vascular smooth muscle cells.The effect of inhibition of PP1 and TNFα signaling on pathogenesis of SARS coronavirusThe stress of maternal separation causes misprogramming in the postnatal maturation of rat resistance arteries.Involvement of transglutaminase 2 and voltage-gated potassium channels in cystamine vasodilatation in rat mesenteric small arteries.Regulated ADAM17-dependent EGF family ligand release by substrate-selecting signaling pathwaysSmooth muscle-selective CPI-17 expression increases vascular smooth muscle contraction and blood pressureRole of CPI-17 in restoring skin homoeostasis in cutaneous field of cancerization: effects of topical application of a film-forming medical device containing photolyase and UV filters.Retromer in Osteoblasts Interacts With Protein Phosphatase 1 Regulator Subunit 14C, Terminates Parathyroid Hormone's Signaling, and Promotes Its Catabolic Response.Altered contractile phenotypes of intestinal smooth muscle in mice deficient in myosin phosphatase target subunit 1Cohesin Removal along the Chromosome Arms during the First Meiotic Division Depends on a NEK1-PP1γ-WAPL Axis in the Mouse.Smooth muscle contractile diversity in the control of regional circulations.STRIPAK components determine mode of cancer cell migration and metastasis.Integrin-linked kinase: not so 'pseudo' after all.Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention.Peripheral circulation.Myosin phosphatase isoforms as determinants of smooth muscle contractile function and calcium sensitivity of force production.
P2860
Q24307960-C1BBE45F-9878-4F8E-84A6-E5EFA698AE54Q24631228-40433017-E401-4B1C-9A51-E3A9C27CFEDFQ26772115-6B22D8A1-AC46-485E-B7B8-DB373F984C88Q26774795-AD1408C8-015C-4C20-978C-53902D99638DQ26829930-F99FDC26-9E59-44D5-9C9A-80829238394BQ26849244-57590F15-D2BC-486D-A5D9-FC6E42AF0B3EQ27693957-A0C5585B-C8F2-4805-BE70-EA76B9D000C8Q28749480-B729B33F-996D-484A-9C58-3FD4314DB673Q30276108-F4F509AE-F048-4B1A-9544-0C2588582D14Q30413663-C0C33AA6-3F3B-445E-8D41-AD93FE7B50F0Q30455386-9194FCB2-D72B-4FC2-9828-E6D22E2291D4Q33719596-7F1D8BC0-93C5-4110-BCCB-029ADFC0409DQ33816566-F967B110-13E0-4C15-8F22-7651CA7D4C6DQ33963033-3F4D01F8-B684-4361-9EEA-E36A923DB650Q34001586-4502CFE0-0C79-439B-BF81-AA9CB226079AQ34051651-3F9F32DB-8525-4482-BA56-9B3AD16D5AE7Q34062825-68F8A829-55B4-46E1-B807-BF7E835E8C0DQ34213553-66DD0A85-D7F5-4B92-8BD9-9BEB1762C5A5Q34432730-055134A8-7EA0-40E5-A29C-5154997A59AEQ34990649-11340AFB-A853-409F-9F4A-D3D25A0C3B1BQ35083933-BEDE010B-E20B-4B71-9A38-9E86FF068575Q35092072-BA702A21-C93D-46B8-961A-1AF5AD8D0E5FQ35837076-BB1D55A3-2760-445F-A3E6-59C66BA19C26Q35956484-6668EE1A-F311-4CFC-A18D-252E7873C5C4Q36114698-123584A6-DF9D-4225-A095-1D9390940246Q36143370-004372FF-50CE-47A8-B5EA-50EB7A4D831BQ36339435-99B42A14-E55E-42E9-B8F5-9176DF9508A2Q36599656-39F267DB-8CFB-45FD-B40D-AFBD025FEA59Q36932188-CD6A3F47-4D9C-40E8-912E-360E9AE42B61Q37054951-245B1BB2-8A0C-49E0-A645-2AFBD3760210Q37108899-A57C8CC0-7F1F-4A06-9E04-F9F96959B4FCQ37149901-E8E34F7F-423D-4B96-AFDB-C91B5635A432Q37196730-79612FE7-A31F-48C5-9070-F74D0BF70C31Q37441692-7BD469DB-C031-4F2B-A8CA-1C7EF6B07F7AQ37575852-E76F6B3E-F0BA-4526-BEE5-A926B277A501Q37705440-6457DADD-F218-40AD-BA92-78BCB96B9040Q37878251-0DFFA805-8ED5-4A75-B7EF-8356E70EDA0BQ37984815-E3341C95-8083-4DF8-A020-59A88EA24763Q38111280-D00AA69E-AB5B-43AD-8AE9-0079001FA85CQ38151237-133592EF-0CD9-4E82-9FB1-32B39BE841B7
P2860
Regulation of cellular protein phosphatase-1 (PP1) by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@ast
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@en
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@nl
type
label
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@ast
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@en
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@nl
prefLabel
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@ast
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@en
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@nl
P2860
P3181
P356
P1476
Regulation of cellular protein ...... inase-activated PP1 inhibitors
@en
P2860
P304
P3181
P356
10.1074/JBC.R109.059972
P407
P50
P577
2009-12-18T00:00:00Z