Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
about
Novel interactors and a role for supervillin in early cytokinesis.Stretch activates human myometrium via ERK, caldesmon and focal adhesion signalingA possible mechanism behind autoimmune disorders discovered by genome-wide linkage and association analysis in celiac diseaseSupervillin reorganizes the actin cytoskeleton and increases invadopodial efficiency.The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility.Supervillin couples myosin-dependent contractility to podosomes and enables their turnoverLIM-domain proteins TRIP6 and LPP associate with shelterin to mediate telomere protectionThe transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.TRIP6: an adaptor protein that regulates cell motility, antiapoptotic signaling and transcriptional activity.Gamma-sarcoglycan is required for the response of archvillin to mechanical stimulation in skeletal muscle.An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.The lysophosphatidic acid type 2 receptor is required for protection against radiation-induced intestinal injury.Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stressSupervillin-mediated suppression of p53 protein enhances cell survival.Role of the retinal vascular endothelial cell in ocular diseaseOverexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion proteinPTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration.PTPN13/PTPL1: an important regulator of tumor aggressiveness.Defining the role of TRIP6 in cell physiology and cancer.Building tolerance by dismantling synapses: inhibitory receptor signaling in natural killer cells.Gelsolin: the tail of a molecular gymnast.Modulation of Rho guanine exchange factor Lfc activity by protein kinase A-mediated phosphorylation.Preparation and Affinity-Purification of Supervillin Isoform 4 (SV4) Specific Polyclonal Antibodies.PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration.The adaptor protein TRIP6 antagonizes Fas-induced apoptosis but promotes its effect on cell migration.Zyxin is involved in regulation of mechanotransduction in arteriole smooth muscle cells.Supervillin binds the Rac/Rho-GEF Trio and increases Trio-mediated Rac1 activation.Emerging roles for LPP in metastatic cancer progression.TRIP6 regulates neural stem cell maintenance in the postnatal mammalian subventricular zone.Supervillin promotes epithelial-mesenchymal transition and metastasis of hepatocellular carcinoma in hypoxia via activation of the RhoA/ROCK-ERK/p38 pathway.
P2860
Q24304327-3BACE542-A2C9-43F0-BC15-1F5D49622E39Q28476312-0E1EC179-7C21-42E2-97AD-E928B714825BQ28943417-52AB8C50-E6E3-44B8-BFB4-12AD3E86C13DQ30485711-C7803E2B-E45A-4277-B47D-D8F4E7036968Q30494945-E0A8EDAA-CFD7-48D9-A082-D9AF09A7482BQ30514839-04219DE1-F7DD-4CC3-8CB7-4F88D67B79FCQ33633718-D7CF76D0-796F-46A2-A97A-4D9385414DC1Q34742453-CBBCCB1D-C505-40E1-810A-E22E534FE55BQ35165077-DDF5340E-4513-460B-82E5-60A4068F6191Q35253089-1044E85C-7724-4796-94E7-145CBF1376BCQ35679463-293BA665-5B85-4A8C-9ACC-1662636B7D35Q35784690-980984AB-1B9E-4D8B-87FE-4C88EDFF0317Q36246898-80974AD6-55B7-45B0-8179-1C5D609BDF44Q36449448-733473A7-0BFD-4F88-BFCF-898058D631DAQ36685259-5BF1CCD1-1144-483A-8759-7236EB16332AQ36919959-AB33AB4D-900A-414E-BB57-358A79F09522Q36994662-E654BC00-8C47-45EE-B2DC-1C1E05299657Q37582782-C9854732-4E65-48A6-8BA1-30835F2F83F9Q37828546-64051C81-B611-4327-AF56-90C0FCE63698Q37952876-04BCC7F8-A4A6-4059-9F50-22B22E6739EDQ38070790-7D3A2875-95BE-4B7D-A188-C4B906539D15Q38113172-CFD38FCF-210C-4670-8CBA-435615349648Q38471795-FC91A0B3-F240-4432-901C-6F354F677050Q38783121-7B7E25A4-2B6D-4F93-BA08-A6AC25A473A5Q38788774-3C600959-1F4B-47B9-BF67-1DC594C85454Q39650793-BB4AA6F2-940B-4703-9B5D-B402DF39DEB7Q42147327-ECE85A5A-5506-43C1-8B7D-D59ED3D6AC77Q43187995-F8B3AAC6-02E8-4F6C-B5A5-D4F7E68279ECQ47658713-79954B7F-1E9E-463A-B4FA-C5C8D80C8F4FQ48648082-198CEEA0-4A8C-4A3A-BD17-945034202F5FQ55515806-92D1D962-3D6B-4D66-8AE2-3C9D99BC6FAD
P2860
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
description
2006 nî lūn-bûn
@nan
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@ast
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en-gb
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@nl
type
label
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@ast
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en-gb
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@nl
prefLabel
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@ast
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en-gb
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@nl
P2093
P2860
P356
P1476
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
@en
P2093
Anka G Ehrhardt
Elizabeth J Luna
Jessica L Crowley
Laura M Hoffman
Lawrence M Lifshitz
Mary C Beckerle
Norio Takizawa
Stephen J Palmieri
Tara C Smith
P2860
P304
P356
10.1083/JCB.200512051
P407
P50
P577
2006-07-01T00:00:00Z