About: Characterization of an Actin-binding Site within the Talin FERM Domain

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rdf:type	Item
description	article (en) wetenschappelijk artikel (nl) article scientifique publié en 2004 (fr) наукова стаття, опублікована в жовтні 2004 (uk) im Oktober 2004 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q58321657-E2517DB0-6869-4493-870C-F26B3969F3F9
publication date	2004-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58321657-B4A53A15-48DE-447F-8AEE-8988874911D6
language of work or name	English
cites work	wds:Q58321657-05EE5CBC-5ED6-47B6-90C6-0F7DD6E27990
cites work	EMAN: semiautomated software for high-resolution single-particle reconstructions
author name string	wds:Q58321657-0EBEB3ED-4B9B-4FD5-AA3B-CB553C093E52 wds:Q58321657-16521820-510C-4420-BD97-D69ABADC9E21 wds:Q58321657-2EAD0369-83E9-42C0-AD4C-D2837227C010 wds:Q58321657-4A7085F7-417F-4311-B20F-B06CAED05184 wds:Q58321657-53B0B0FC-C163-46D9-82DF-AF802AA0BCA1 wds:Q58321657-8FD8A2E5-912E-4EC5-8553-7FB0011ECCEF wds:Q58321657-BE15538D-7C86-4DD3-BDDF-A13ED80E257B wds:Q58321657-D4C992E0-5FAE-457F-B345-0A571555877E wds:Q58321657-D5EF72AE-FCAE-47C5-88EF-F77941A06FA9 wds:Q58321657-FB69459F-DAE7-4139-9397-ED1B630E3630 wds:Q58321657-FDA23C5C-3947-4F52-A621-36E5A97323A8
author name string	Robert C Liddington Bipin Patel David R Critchley Dorit Hanein Niels Volkmann Hongjun Liu Ho-Sup Lee Richard M Robson Robert M Bellin Diane L Walker Pam Powers
rdfs:label	Characterization of an Actin-binding Site within the Talin FERM Domain (en) Characterization of an Actin-binding Site within the Talin FERM Domain (nl)
skos:prefLabel	Characterization of an Actin-binding Site within the Talin FERM Domain (en) Characterization of an Actin-binding Site within the Talin FERM Domain (nl)
name	Characterization of an Actin-binding Site within the Talin FERM Domain (en) Characterization of an Actin-binding Site within the Talin FERM Domain (nl)
author	wds:Q58321657-16C27C87-681D-4B98-B412-4EBCDF4CEE87 wds:Q58321657-F06B9204-2C5C-45EF-9DAF-BAFBAE1E28F7
author	José M de Pereda Begoña Garcia-Alvarez
title	wds:Q58321657-A79BB1DC-DC6E-4964-8F44-D2F99F162891
title	Characterization of an actin-binding site within the talin FERM domain (en)
page(s)	wds:Q58321657-655FD209-AD50-4FE9-95B6-575211520A3E
page(s)	771-784
instance of	wds:Q58321657-2F4EC5B5-A893-4258-BFB0-4E230ADD79AF
instance of	scholarly article
PubMed ID	wds:Q58321657-5EE7BE85-B56F-42D7-A1FB-5503B7163784
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15465061
PubMed ID	15465061
published in	wds:Q58321657-0B7AAECB-01D4-4546-A033-8E908A85D305
published in	Journal of Molecular Biology
issue	wds:Q58321657-2DCFB594-AC9B-4F9B-969E-D485354EBB6F
volume	wds:Q58321657-DCEAFE6A-1520-4AFC-B8B9-78C74102569E
issue	3
volume	343
DOI	wds:Q58321657-F9AE5369-425F-49D6-ACEC-014B511809C0
DOI	http://dx.doi.org/10.1016/J.JMB.2004.08.069
DOI	10.1016/J.JMB.2004.08.069
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58321657
is cites work of	Vinculin controls focal adhesion formation by direct interactions with talin and actin. Mechanisms of talin-dependent integrin signaling and crosstalk Plekhh2, a novel podocyte protein downregulated in human focal segmental glomerulosclerosis, is involved in matrix adhesion and actin dynamics The structure of the C-terminal actin-binding domain of talin Structural and biophysical properties of the integrin-associated cytoskeletal protein talin Extracellular alkaline pH leads to increased metastatic potential of estrogen receptor silenced endocrine resistant breast cancer cells Subcellular localization of talin is regulated by inter-domain interactions Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1. Mechanical integration of actin and adhesion dynamics in cell migration Assembly and signaling of adhesion complexes The conserved C-terminal I/LWEQ module targets Talin1 to focal adhesions Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas Actin co-sedimentation assay; for the analysis of protein binding to F-actin Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod. Structural model and functional significance of pH-dependent talin-actin binding for focal adhesion remodeling Dysregulated pH: a perfect storm for cancer progression. Central Region of Talin Has a Unique Fold That Binds Vinculin and Actin Myosin genes in Tetrahymena Distinct developmental roles for direct and indirect talin-mediated linkage to actin Ligation of erythrocyte CR1 induces its clustering in complex with scaffolding protein FAP-1 Talin contains a C-terminal calpain2 cleavage site important in focal adhesion dynamics Talin 2 is a large and complex gene encoding multiple transcripts and protein isoforms Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions. Intracellular pH sensors: design principles and functional significance The expanding family of FERM proteins. How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism Directed motility of phagosomes in Tetrahymena thermophila requires actin and Myo1p, a novel unconventional myosin A novel 4.1 ezrin radixin moesin (FERM)-containing protein, 'Willin'. Talin and signaling through integrins Talin is required to position and expand the luminal domain of the Drosophila heart tube. Kindlin-2 directly binds actin and regulates integrin outside-in signaling Getting a GRASP on CASP: properties and role of the cytohesin-associated scaffolding protein in immunity Role of vinculin in cellular mechanotransduction Talin - the master of integrin adhesions. Myo1 localizes to phagosomes, some of which traffic to the nucleus in a Myo1-dependent manner in Tetrahymena thermophila

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