A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
about
sameAs
Cloning and characterization of SCHIP-1, a novel protein interacting specifically with spliced isoforms and naturally occurring mutant NF2 proteinsIntegrating the biophysical and molecular mechanisms of auditory hair cell mechanotransductionProteomic analysis of the enterocyte brush borderTwo independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domainCloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1A novel role for BRCA1 in regulating breast cancer cell spreading and motilityEzrin is a cyclic AMP-dependent protein kinase anchoring proteinHeterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteinsStructural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domainEzrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding siteThe effect of overexpression of the protein tyrosine phosphatase PTPMEG on cell growth and on colony formation in soft agar in COS-7 cellsPrognostic value of tumor microinvasion and metalloproteinases expression in intracranial pediatric ependymomasRegulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathwayPhysical association of moesin and CD46 as a receptor complex for measles virusEzrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosisRho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail associationIdentification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin familyMoesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarizationModel membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesinStructural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Conditional biallelic Nf2 mutation in the mouse promotes manifestations of human neurofibromatosis type 2.Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletonsThe LIM and SH3 domain protein family: structural proteins or signal transducers or both?Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein moesinDistinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin.Submembranous junctional plaque proteins include potential tumor suppressor moleculesRadixin deficiency causes deafness associated with progressive degeneration of cochlear stereocilia.Neurofibromatosis type 2 protein co-localizes with elements of the cytoskeleton.Germ-line mutations in the neurofibromatosis 2 gene: correlations with disease severity and retinal abnormalities.A molecular analysis of desiccation tolerance mechanisms in the anhydrobiotic nematode Panagrolaimus superbus using expressed sequenced tags.A mutation in the neurofibromatosis type 2 tumor-suppressor gene, giving rise to widely different clinical phenotypes in two unrelated individualsRadixin is involved in lamellipodial stability during nerve growth cone motilityOocytes of baboon fetal primordial ovarian follicles express estrogen receptor beta mRNAEzrin is highly expressed in early thymocytes, but dispensable for T cell development in mice.Maternal control of early mouse development.Enteropathogenic Escherichia coli activates ezrin, which participates in disruption of tight junction barrier function.Ezrin promotes invasion and metastasis of pancreatic cancer cells.Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury.Moesin is not a receptor for measles virus entry into mouse embryonic stem cells.
P2860
Q22253159-F4DD4754-BC9A-4369-BFE6-F474BBE4E3F4Q22337239-359EBD3A-AE39-4E63-B5B8-F8FF659C46BDQ24293478-B2E62F97-5226-4CE9-AE98-77C577835E67Q24321386-081E23F0-DD84-40D9-A3CC-94972CAAAE99Q24328861-5A719EE6-641C-4E56-9CFA-EE22E1372283Q24338824-CF902A76-7572-49B2-BA94-21F3D1809903Q24532065-C3CCEB62-76FE-4EFE-8AAD-14993E70BC6AQ24564097-491D1C44-44D4-459A-B863-E5CF63911EF6Q24598762-C7703A09-69E6-4C37-AE4C-425D3FEEC005Q24617964-D2E0CF19-5129-4DEA-A4C9-8B11759E4BE3Q24647975-EA5ECFAA-4101-4D47-8A2D-CF3588A3425EQ24656634-9FB630E4-DDF1-4BE8-93D9-C9203B361716Q24671083-7D49B0FD-B8E5-42DD-A18E-9FCA50D937E1Q24675691-1BD07431-27DC-44EB-BD1F-E94E9AFE123FQ24676628-06F7BF93-8C24-4827-A98A-03A94530703FQ24676652-A73C6F7A-1528-4594-A4C2-58DBBDBB6C9DQ24678197-EFD4B91E-6EFC-445C-A45C-DDF7BD2874CFQ24678695-D7AB5C45-BC57-4D3C-AD11-9D571FD638D3Q24683747-8B3024C7-393C-4F20-B99C-4AD8183C6ED4Q27004665-0629FC7F-F1F7-450A-9177-7818BF772004Q27640373-CFB9681E-CF89-415E-A2E0-C0844AFAB92DQ28507503-ECDB7D19-CEA1-4B1E-A9F5-DF5F95F89663Q28582916-24B12CFB-2B4C-4A5F-924C-403757C54A72Q30157698-94072687-F87A-404F-8E74-CE110915276EQ30372875-095B9CD6-DAB8-45EC-B1D1-A90B300080FAQ30494553-740777C8-7F2E-49A1-A5F7-21CD64168D99Q30494561-F3D24516-EF61-45B8-B563-CDA6B785F871Q30496716-8DF211A2-1678-4A2C-A280-C134F59DB5ABQ30498854-DD221469-2288-4418-A0AA-DAC9C079732FQ30502813-E43341BC-35FF-4A08-815F-08C85012602CQ30506753-F2A6C6F6-5148-428F-B7AE-FA4349D10E38Q30544702-7FC02FC1-DE95-467B-B40A-496E4E8142C0Q30629181-AEC835CB-F91A-4CC0-A173-16512D907961Q33335201-CE4D2388-CCF6-4D5F-8727-A131F3E2C57DQ33678939-2962485A-3EA5-429A-B341-0E13E4290613Q33710885-5EBAC519-8195-4F80-8EE8-AC51795269A8Q34009023-90952A60-B32E-4148-B794-101406604AE2Q34047483-21500435-B7EA-41AB-BA31-A06E1CFDC2F9Q34060749-4E2AB42E-57A6-42A8-B2B4-E5CB9FF0357DQ34070151-98CE80BE-AE7A-458A-8BF2-F9081728B2D8
P2860
A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
description
1992 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1992
@ast
im September 1992 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: September 1992)
@en
vedecký článok (publikovaný 1992-09)
@sk
vědecký článek publikovaný v roce 1992
@cs
wetenschappelijk artikel (gepubliceerd in 1992-09)
@nl
наукова стаття, опублікована у вересні 1992
@uk
научни чланак (објављен 1992-09)
@sr
name
A gene family consisting of ez ...... sma membrane association sites
@ast
A gene family consisting of ez ...... sma membrane association sites
@en
A gene family consisting of ez ...... sma membrane association sites
@nl
type
label
A gene family consisting of ez ...... sma membrane association sites
@ast
A gene family consisting of ez ...... sma membrane association sites
@en
A gene family consisting of ez ...... sma membrane association sites
@nl
prefLabel
A gene family consisting of ez ...... sma membrane association sites
@ast
A gene family consisting of ez ...... sma membrane association sites
@en
A gene family consisting of ez ...... sma membrane association sites
@nl
P2093
P3181
P1476
A gene family consisting of ez ...... sma membrane association sites
@en
P2093
P304
P3181
P407
P478
103 ( Pt 1)
P577
1992-09-01T00:00:00Z