About: Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle

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About: Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 1988

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1988 (uk) artículu científicu espublizáu n'avientu de 1988 (ast) scientific article published on 01 December 1988 (en)
publication date	wds:Q70416395-0A743A51-A782-4256-9FB6-55F6C42A2B1D
publication date	1988-12-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q70416395-3547DE4C-405F-499C-BA12-52117E373FC8 wds:Q70416395-4D178D1E-BF5A-4822-9725-B76F35503978 wds:Q70416395-D7031A86-F088-46DB-855D-C00D1B2FCA03
author name string	M Wilchek B Geiger T Miron
rdfs:label	Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (en) Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (nl)
skos:prefLabel	Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (en) Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (nl)
name	Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (en) Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (nl)
title	wds:Q70416395-1E2C3C2B-7FB8-47B8-BE84-11719A050317
title	Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle (en)
page(s)	wds:Q70416395-401CF25E-AE23-450E-B620-2872012D66FB
page(s)	543-553
instance of	wds:Q70416395-E95B3113-990F-4B25-8BDA-08D3476FEB37
instance of	scholarly article
PubMed ID	wds:Q70416395-C89FD7DB-8C41-479D-9526-FFA9772B49B6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3145203
PubMed ID	3145203
published in	wds:Q70416395-8D1A42A6-46A1-4BCF-9593-9B0CE7CE4DDD
published in	FEBS Journal
issue	wds:Q70416395-84FC3560-A514-4C51-9F53-E3D500BC9048
volume	wds:Q70416395-C5729010-9773-4FCE-87D4-4710E3D930E2
issue	2
volume	178
DOI	wds:Q70416395-55F1254B-D095-4C76-AE44-C3F64857A30D
DOI	http://dx.doi.org/10.1111/J.1432-1033.1988.TB14481.X
DOI	10.1111/J.1432-1033.1988.TB14481.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70416395
is cites work of	Focal adhesion as a signal transduction organelle A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance Inhibition of Daxx-mediated apoptosis by heat shock protein 27 Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions Altered expression of glomerular heat shock protein 27 in experimental nephrotic syndrome Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets Identification of proteins that modify cataract of mouse eye lens Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27 alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner Actin cytoskeleton and small heat shock proteins: how do they interact? Critical role for heat shock protein 20 (HSP20) in migration of malarial sporozoites Vinculin Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics. Influence of phosphorylation and oligomerization on the protective role of the small heat shock protein 27 in rat adult cardiomyocytes Heat shock proteins in the retina: Focus on HSP70 and alpha crystallins in ganglion cell survival Disruption of the gene for hsp30, an alpha-crystallin-related heat shock protein of Neurospora crassa, causes defects in thermotolerance Small heat shock proteins in smooth muscle Structure and properties of avian small heat shock protein with molecular weight 25 kDa. The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Thiol/disulfide exchange between small heat shock protein 25 and glutathione Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion Endothelium-targeted overexpression of heat shock protein 27 ameliorates blood-brain barrier disruption after ischemic brain injury. HSPB7 is indispensable for heart development by modulating actin filament assembly Mechanical signals activate p38 MAPK pathway-dependent reinforcement of actin via mechanosensitive HspB1. Purification and characterization of an 85 kDa talin-binding fragment of vinculin Cyclosporine-induced renal artery smooth muscle contraction is associated with increases in the phosphorylation of specific contractile regulatory proteins Thrombin activates MAPKAP2 kinase in vascular smooth muscle. Hsp27-actin interaction Heat shock protein 25 plays multiple roles during mouse skin development Carp liver actin: isolation, polymerization and interaction with deoxyribonuclease I (DNase I)
is cites work of	wds:Q44214861-D74C8A53-7FBD-4528-8E65-DB33FEA96FEC wds:Q34966102-14EB6898-A9E8-4251-9A32-BB35BE8643D1 wds:Q27934278-3CEBC085-1656-49F1-8C51-299FD5B44741 wds:Q34153266-DC6EAFD7-6237-4B9D-BF68-2A7C3B9399F0 wds:Q34285127-3168D0C4-CB55-4D76-A796-776A0E8212A8 wds:Q40733286-99B8B4D2-5AEE-4F63-AA82-F114DBED7A8E wds:Q44684922-DEE8A0CC-37C2-46D0-8BE9-2B23C7857D0A wds:Q47139116-3DCCD3E1-7FAD-48E7-9655-089B95CC9B6D wds:Q24290301-B31536A8-3702-4FBC-837A-4E436698EB69 wds:Q36530055-6A46C735-CF08-48F5-BFE8-3E7D1278B740 wds:Q46316541-8F250424-013F-4A53-AF4F-D27B204E6744 wds:Q57243698-C443CE32-53EE-4537-B3B7-F1056607B8F7 wds:Q74026482-59EC4C0D-9A93-43FD-99EF-1FAFEC23B21C wds:Q36829093-109D0E2D-F51E-45AF-A518-2B47F8505DB8 wds:Q42048403-65EA68A0-B00E-4427-93F4-812F81ED8287 wds:Q74603004-4B260BA3-FB6B-4898-8C7A-36E172716FFC wds:Q24641828-3B38A693-16E2-4957-AE97-7E8B7B9776DA wds:Q43728190-22186645-98A1-4C86-8A7D-B0044A4F07BD wds:Q47994357-221EEC1F-80D2-49BC-9207-C79ADD73C257 wds:Q24646796-6CE5C37F-0EF5-4AE2-83F6-79F975E4D15A wds:Q28204103-F3300DAD-D917-4D05-82CA-37898BAE7F27 wds:Q34477202-A7EB39B7-0F16-4EE1-BB05-694ED7A3667A wds:Q35325518-33F55A8D-174D-46FB-8C85-67428E7A9F79 wds:Q47897069-E3EB2039-6090-43A4-99FE-3726B4CC5FE5 wds:Q78122997-C3BFBC50-2E1E-47E8-B156-6727EB48F589 wds:Q67266976-719CB417-6237-4E89-B5B0-AAC1F9B94FDC wds:Q37728818-A8395D46-2713-43FA-8861-DAB600F1991D wds:Q37356213-55CB1574-E9A5-4DAD-B754-02FF564F1DCF

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