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000019044 0247_ $$2DOI$$a10.1073/pnas.1110109108
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000019044 084__ $$2WoS$$aMultidisciplinary Sciences
000019044 1001_ $$0P:(DE-HGF)0$$aGalkin, V.E.$$b0
000019044 245__ $$aRemodeling of actin filaments by ADF/cofilin proteins
000019044 260__ $$aWashington, DC$$bAcademy$$c2011
000019044 300__ $$a20568 - 20572
000019044 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000019044 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v108$$x0027-8424$$y51
000019044 500__ $$3POF3_Assignment on 2016-02-29
000019044 500__ $$aThis work was supported by National Institutes of Health Grants GM081303 (E. H. E.) and GM077190 (E.R.).
000019044 520__ $$aCofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.
000019044 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000019044 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000019044 588__ $$aDataset connected to Web of Science, Pubmed
000019044 65320 $$2Author$$acytoskeleton
000019044 65320 $$2Author$$aelectron microscopy
000019044 65320 $$2Author$$ahelical polymers
000019044 650_2 $$2MeSH$$aActin Depolymerizing Factors: chemistry
000019044 650_2 $$2MeSH$$aActins: chemistry
000019044 650_2 $$2MeSH$$aCofilin 2: chemistry
000019044 650_2 $$2MeSH$$aCryoelectron Microscopy: methods
000019044 650_2 $$2MeSH$$aCytoskeleton: chemistry
000019044 650_2 $$2MeSH$$aGene Library
000019044 650_2 $$2MeSH$$aHumans
000019044 650_2 $$2MeSH$$aMicroscopy, Electron: methods
000019044 650_2 $$2MeSH$$aModels, Molecular
000019044 650_2 $$2MeSH$$aMolecular Conformation
000019044 650_2 $$2MeSH$$aMuscle, Skeletal: metabolism
000019044 650_2 $$2MeSH$$aPolymers: chemistry
000019044 650_2 $$2MeSH$$aProtein Conformation
000019044 650_2 $$2MeSH$$aProtein Structure, Secondary
000019044 650_7 $$00$$2NLM Chemicals$$aActin Depolymerizing Factors
000019044 650_7 $$00$$2NLM Chemicals$$aActins
000019044 650_7 $$00$$2NLM Chemicals$$aCofilin 2
000019044 650_7 $$00$$2NLM Chemicals$$aPolymers
000019044 650_7 $$2WoSType$$aJ
000019044 7001_ $$0P:(DE-HGF)0$$aOrlova, A.$$b1
000019044 7001_ $$0P:(DE-HGF)0$$aKudryashov, D.S.$$b2
000019044 7001_ $$0P:(DE-HGF)0$$aSolodukhin, A.$$b3
000019044 7001_ $$0P:(DE-HGF)0$$aReisler, E.$$b4
000019044 7001_ $$0P:(DE-Juel1)132018$$aSchröder, G.F.$$b5$$uFZJ
000019044 7001_ $$0P:(DE-HGF)0$$aEgelman, E.H.$$b6
000019044 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.1110109108$$gVol. 108, p. 20568 - 20572$$p20568 - 20572$$q108<20568 - 20572$$tProceedings of the National Academy of Sciences of the United States of America$$v108$$x0027-8424$$y2011
000019044 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3251117
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000019044 9132_ $$0G:(DE-HGF)POF3-559H$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vAddenda$$x0
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