Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein - Test2 - elhamkhani - TriplyDB

Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein

Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein

http://www.wikidata.org/entity/Q28248311

about

MIR is a novel ERM-like protein that interacts with myosin regulatory light chain and inhibits neurite outgrowth The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho CD44 binds to the Shigella IpaB protein and participates in bacterial invasion of epithelial cells Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase The complex of Arl2-GTP and PDE delta: from structure to function The role of ezrin-associated protein network in human sperm capacitation Androgen regulation of the human FERM domain encoding gene EHM2 in a cell model of steroid-induced differentiation Identification of a novel brain-specific and Reelin-regulated gene that encodes a protein colocalized with synapsin Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes.Magicin, a novel cytoskeletal protein associates with the NF2 tumor suppressor merlin and Grb2 Podocalyxin EBP50 ezrin molecular complex enhances the metastatic potential of renal cell carcinoma through recruiting Rac1 guanine nucleotide exchange factor ARHGEF7 Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304 Ezrin tunes T-cell activation by controlling Dlg1 and microtubule positioning at the immunological synapse.Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains RhoGDI: multiple functions in the regulation of Rho family GTPase activities Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain The 'invisible hand': regulation of RHO GTPases by RHOGDIs Ezrin, a plasma membrane-microfilament linker, signals cell survival through the phosphatidylinositol 3-kinase/Akt pathway Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane Podoplanin - a small glycoprotein with many faces The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI.Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms.PIP kinases define PI4,5P₂signaling specificity by association with effectors Protein phosphatase 2C inactivates F-actin binding of human platelet moesin Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large Rho GTPase activity zones and transient contractile arrays Organizing the cell cortex: the role of ERM proteins Networking with AKAPs: context-dependent regulation of anchored enzymes Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association Arabidopsis thaliana Rop GTPases are localized to tips of root hairs and control polar growth FERM domain containing protein 7 interacts with the Rho GDP dissociation inhibitor and specifically activates Rac1 signaling The headpiece domain of dematin regulates cell shape, motility, and wound healing by modulating RhoA activation Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors

P2860

Q22010916-602BFB5C-DFCC-45E7-8381-9B3DAEF4DF9A Q22254081-ACE9EC18-BF3A-4E29-80F8-B25CA4CF15F0 Q24290851-2B8ED5A1-65FF-4AF5-9283-E2729BDC1BD6 Q24294818-0E1480B9-4742-4342-ABCC-EE425366E9A9 Q24295264-901810F1-3FFA-4E21-B229-EF60455942FA Q24296013-D6693EBF-241E-4999-82F5-8AB972C6B83F Q24296691-CDFFEABA-0E87-49B7-B90A-B6A8209E9080 Q24299394-773E94A3-D189-4E29-97D2-1B6B5F1A54E0 Q24300262-D1CB9EF9-4FF2-4F68-8CAC-BE1DBCCC1963 Q24306359-8A685FE7-57AA-432A-B198-D4722D5B2492 Q24306767-469B3728-D56C-476E-BCB4-31C3C8BF7574 Q24313074-DFDAB597-99EB-40AB-9AD4-0FB809A19E55 Q24321953-C2B64EFD-497F-4271-8301-6598959EB87D Q24533435-AC3EA151-62C3-4C75-B39C-3F195F8DB30E Q24534900-66F1EA66-95B8-499A-944C-C200EC4E322A Q24598762-A5B2FF10-A400-4555-B10C-9EC1F98ACB1D Q24606819-49538804-333C-4126-8F88-0E0709FC093C Q24648522-EC771225-45E1-48DA-80CD-AD7FF2776DD3 Q24654170-47E9516A-E59B-4F40-91C1-9614DE5A2AA6 Q24678197-65CB7FFC-224D-4F92-917F-D3D20632EFF4 Q24683879-8A80606E-0A1D-4F75-840E-16DDBB834C85 Q26749146-7FE7E75A-1B70-4D4C-8FD2-BED2AAF93654 Q27919637-4967BDEF-7D60-4840-B8BB-106A160A8BFC Q27931452-2A7F1F35-CA1E-4EF7-8B04-7F82ACA9D0F0 Q27939498-48DE662D-397D-44B5-9C23-A1433CC73833 Q28083975-89D20DA4-84C7-485D-AE95-E7CF5FAEB8E0 Q28144127-1C2B16C8-DC97-4A5C-96ED-55EA5BE67B7B Q28144320-A803BB05-0892-43D3-9B99-CD58A57E9F02 Q28261201-8C27817E-A177-4DB1-82AB-300B9DA8873D Q28265366-ED8427D5-D1DF-4CC9-B1E5-C206D9F68167 Q28277373-5F33B27E-DE1A-43A6-8DC9-676B5D56417A Q28278715-A994E0DB-3340-4CFD-9901-BD5AF04A7BAF Q28290396-33E6C14D-ED4E-44C3-AFA6-72BE27CD6D87 Q28344277-EC124747-4EE9-4540-AF3E-EAE1CC4F53E4 Q28365540-F2F7F228-F9FC-41F2-9EEF-847EE7DD5059 Q28366139-D6BE9220-8017-420F-89BD-ADCE3E49E9AF Q28506649-AD04448A-E7BD-4AAD-A51A-E8AD9DA9082D Q28507036-B4D11C00-F912-4A00-8AE9-2471D38CA151 Q28508442-58ADF634-C91E-47F1-ACE2-6C73113C5E00 Q28510087-4203368F-F86A-49F5-AF3F-FEEDD845E1A7

P2860

Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein

http://www.wikidata.org/entity/Q28248311

description

1997 nî lūn-bûn

@nan

1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

Direct interaction of the Rho ...... ion of the Rho small G protein

@ast

Direct interaction of the Rho ...... ion of the Rho small G protein

@en

Direct interaction of the Rho ...... ion of the Rho small G protein

@nl

type

label

Direct interaction of the Rho ...... ion of the Rho small G protein

@ast

Direct interaction of the Rho ...... ion of the Rho small G protein

@en

Direct interaction of the Rho ...... ion of the Rho small G protein

@nl

prefLabel

Direct interaction of the Rho ...... ion of the Rho small G protein

@ast

Direct interaction of the Rho ...... ion of the Rho small G protein

@en

Direct interaction of the Rho ...... ion of the Rho small G protein

@nl

P1433

Q28248311-B1B5EF76-C2D4-4AB9-9EE1-1FB0982CEAFD

P1476

Q28248311-DC86160F-85A1-450D-86CF-0935397F348C

P2093

Q28248311-040D8A28-8173-4387-83F0-50DF3B28A96E

Q28248311-62F12AA3-8A48-4FDB-B035-D4DD9AD5281C

Q28248311-764A4CF1-EF1B-481A-8D1C-7A13FAB3A6E9

Q28248311-8225AD22-EEE3-4AC1-8C70-16E0C82A783A

Q28248311-C33DCBE4-8DD0-4498-907C-F809921390C4

Q28248311-CCE169D5-A2F2-4B35-9381-344F28429F60

Q28248311-EE7146BF-1054-42AE-A895-4D64752F51B2

P304

Q28248311-A248BD23-D486-4CE1-8FEF-9FDC2FC3A160

P31

Q28248311-01A7387F-6805-40CC-8D3D-DA61102BCB8A

P356

Q28248311-3C88181C-7828-4AA4-B136-8BCDF180F351

P407

Q28248311-BE25EE84-EEB9-4D2B-81A5-5784B2BCBF20

P433

Q28248311-F1DD3A63-B8CA-4D4B-ACC3-03115FE84FEB

P478

Q28248311-FA38DF3E-963C-486D-8ED6-2E5EAA54C29C

P577

Q28248311-3E827579-DDC4-4CD6-9E9D-F3ABBE782A17

P698

Q28248311-4039C6D5-0CA5-4BA8-B90D-8D75DCE25EB5

P356

JBC.272.37.23371

P1433

Journal of Biological Chemistry

P1476

Direct interaction of the Rho ...... ion of the Rho small G protein

@en

P2093

A Mammoto

http://www.w3.org/2001/XMLSchema#string

K Takahashi

http://www.w3.org/2001/XMLSchema#string

K Takaishi

http://www.w3.org/2001/XMLSchema#string

S Tsukita

http://www.w3.org/2001/XMLSchema#string

T Kameyama

http://www.w3.org/2001/XMLSchema#string

T Sasaki

http://www.w3.org/2001/XMLSchema#string

Y Takai

http://www.w3.org/2001/XMLSchema#string

P304

23371-5

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.272.37.23371

http://www.w3.org/2001/XMLSchema#string

P407

P433

37

http://www.w3.org/2001/XMLSchema#string

P478

272

http://www.w3.org/2001/XMLSchema#string

P577

1997-09-12T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

9287351

http://www.w3.org/2001/XMLSchema#string