The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane
about
Differential effects of MYH9 and APOL1 risk variants on FRMD3 Association with Diabetic ESRD in African AmericansEvolution and origin of merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor geneResidue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alphaThe TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase RhoGAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytesConformation, localization, and integrin binding of talin depend on its interaction with phosphoinositidesIdentification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARPSpectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissuesWSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci.FERM domain-containing unconventional myosin VIIA interacts with integrin β5 subunit and regulates αvβ5-mediated cell adhesion and migrationMSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chainThe parathyroid hormone 1 receptor directly binds to the FERM domain of ezrin, an interaction that supports apical receptor localization and signaling in LLC-PK1 cellsInteraction proteome of human Hippo signaling: modular control of the co-activator YAP1A novel role for BRCA1 in regulating breast cancer cell spreading and motilityCytoskeletal protein 4.1G binds to the third intracellular loop of the A1 adenosine receptor and inhibits receptor actionLoss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndromeBinding 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 domainsThe 4.1/ezrin/radixin/moesin domain of the DAL-1/Protein 4.1B tumour suppressor interacts with 14-3-3 proteinsSorting nexin 17 accelerates internalization yet retards degradation of P-selectinVezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complexStructural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domainProtein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transductionJanus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transductionCoupling of STIM1 to store-operated Ca2+ entry through its constitutive and inducible movement in the endoplasmic reticulum.Structural basis for the autoinhibition of focal adhesion kinaseThe protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-cateninThe tumor suppressor DAL-1/4.1B and protein methylation cooperate in inducing apoptosis in MCF-7 breast cancer cells.Recycling Endosomes and Viral InfectionFAK and paxillin, two potential targets in pancreatic cancerFRMD3 gene: its role in diabetic kidney disease. A narrative reviewHow PI3K-derived lipids control cell divisionUbiquitin ligases in cholesterol metabolismModel membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesinPhosphoinositides: tiny lipids with giant impact on cell regulationRegulation of brain tumor dispersal by NKCC1 through a novel role in focal adhesion regulationStructural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domainStructural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Structural Basis of Tumor Suppressor in Lung Cancer 1 (TSLC1) Binding to Differentially Expressed in Adenocarcinoma of the Lung (DAL-1/4.1B)Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPasesStructural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)
P2860
Q21144945-69CB9349-1749-45CA-8CC2-8CA77C4114FBQ21283962-9E360804-22C5-44F7-B302-8F30BF7D9903Q22253482-C28B5921-86FF-4B08-927E-1B80B0ED817BQ22254081-54AC1E21-817D-4E09-8742-47E2CFEDDDB9Q22254279-5045C161-90C2-4C36-A1E3-56DA445D95B5Q24291063-C2071FA8-BD13-4F68-84CB-E79BCECF857AQ24291083-E4C192CA-01E1-47BC-A3CA-AC546EBE5C6CQ24291372-07B477C4-DDF1-4837-AFDB-06347B3BF987Q24295285-5E58462C-7D4E-45FA-9322-85FDAB0E1F40Q24300327-F474465C-DBBF-4466-8DD2-C0418C556621Q24306325-2042F08E-CDB9-4BD2-A5C7-1ED143FF38BDQ24315599-6490684E-AD3B-41CA-8C49-2ACFCC736968Q24316087-E3A86F58-365F-4A4F-8C90-CF0C4D89DBE1Q24338824-95880595-DC75-4AE8-B80F-92BF99D9613BQ24530574-0924F75C-A89A-4F80-A573-F5C8FFBCD6D4Q24532354-CD43B3FD-9D19-420D-B1E2-077EC73AD583Q24533435-F0F93C1D-099B-4B9E-B200-7F80ABEDBE0CQ24534317-8BA248F1-562B-4799-8C25-B4AD2A51609CQ24561629-974EA3A8-A983-4F3A-AA99-D51D3CC8AD40Q24597349-E7B745B1-477F-4904-8FE2-70B81ADFD559Q24598762-BDC89643-DC6E-4C2B-AA9B-0D0D0D0EB125Q24622527-742EBFC7-9E9B-4195-B742-1B80FBB8D826Q24654170-28E4330F-E687-4C39-AE11-220DAB3D33F3Q24672652-C63237D1-EA03-451B-AF95-A3F1E56A2006Q24678318-5313B546-31CB-43F8-9356-594E19114078Q24679774-EB029447-920F-4064-A510-D90D33086E57Q25257451-9D63FFB7-72AF-4B2F-92AC-6646F1329AA2Q26752566-570BF55F-F566-4E2F-97B1-C830DCE605A2Q26765360-2D183E89-EAFC-483E-A18A-59E8F2AC9D16Q26771495-A2807A46-7BC1-4D09-ACD6-339C2799FCEDQ26781315-C5D52969-B70A-4889-B7F1-E7946963786BQ26998402-FEEC25A0-D0D5-4E22-9C0D-F6BEC0FAB50DQ27004665-497DD482-2274-420E-A8B8-28C2E00A99DCQ27012953-B0EF5D24-6258-4458-B4A4-6CA53A592C75Q27319526-39DDF8AB-B483-498A-8AAB-E4B7DA4D70C8Q27637088-76973416-CB08-4F5D-B606-A8EFC62D6E13Q27640373-C1BDD62B-05CB-4611-B678-4D3882134AA3Q27666177-36D46B92-86A2-4EF0-B01E-907A4CC56B53Q27667515-860FA80C-5071-4B9D-8E4C-933C35C8E9EFQ27684808-8DF255CD-1030-4B63-9AEC-C2B85A7C340A
P2860
The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The FERM domain: a unique modu ...... asmic proteins to the membrane
@ast
The FERM domain: a unique modu ...... asmic proteins to the membrane
@en
The FERM domain: a unique modu ...... asmic proteins to the membrane
@nl
type
label
The FERM domain: a unique modu ...... asmic proteins to the membrane
@ast
The FERM domain: a unique modu ...... asmic proteins to the membrane
@en
The FERM domain: a unique modu ...... asmic proteins to the membrane
@nl
prefLabel
The FERM domain: a unique modu ...... asmic proteins to the membrane
@ast
The FERM domain: a unique modu ...... asmic proteins to the membrane
@en
The FERM domain: a unique modu ...... asmic proteins to the membrane
@nl
P2093
P1476
The FERM domain: a unique modu ...... asmic proteins to the membrane
@en
P2093
A Bretscher
A H Chishti
G A Rouleau
J A Chasis
J G Conboy
K B Hoover
P356
10.1016/S0968-0004(98)01237-7
P407
P577
1998-08-01T00:00:00Z