guest ::
| Home > Publications database > Remodeling of actin filaments by ADF/cofilin proteins > print |
| 001 | 19044 | ||
| 005 | 20200402210140.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:22158895 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC3251117 |
| 024 | 7 | _ | |2 DOI |a 10.1073/pnas.1110109108 |
| 024 | 7 | _ | |2 WOS |a WOS:000298289400064 |
| 024 | 7 | _ | |a altmetric:490426 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-19044 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 000 |
| 084 | _ | _ | |2 WoS |a Multidisciplinary Sciences |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Galkin, V.E. |b 0 |
| 245 | _ | _ | |a Remodeling of actin filaments by ADF/cofilin proteins |
| 260 | _ | _ | |a Washington, DC |b Academy |c 2011 |
| 300 | _ | _ | |a 20568 - 20572 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 5100 |a Proceedings of the National Academy of Sciences of the United States of America |v 108 |x 0027-8424 |y 51 |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 500 | _ | _ | |a This work was supported by National Institutes of Health Grants GM081303 (E. H. E.) and GM077190 (E.R.). |
| 520 | _ | _ | |a Cofilin/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. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK409 |2 G:(DE-HGF) |a Funktion und Dysfunktion des Nervensystems |c P33 |x 0 |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |2 G:(DE-HGF) |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Actin Depolymerizing Factors: chemistry |
| 650 | _ | 2 | |2 MeSH |a Actins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Cofilin 2: chemistry |
| 650 | _ | 2 | |2 MeSH |a Cryoelectron Microscopy: methods |
| 650 | _ | 2 | |2 MeSH |a Cytoskeleton: chemistry |
| 650 | _ | 2 | |2 MeSH |a Gene Library |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Microscopy, Electron: methods |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Molecular Conformation |
| 650 | _ | 2 | |2 MeSH |a Muscle, Skeletal: metabolism |
| 650 | _ | 2 | |2 MeSH |a Polymers: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Secondary |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Actin Depolymerizing Factors |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Actins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cofilin 2 |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Polymers |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a cytoskeleton |
| 653 | 2 | 0 | |2 Author |a electron microscopy |
| 653 | 2 | 0 | |2 Author |a helical polymers |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Orlova, A. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Kudryashov, D.S. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Solodukhin, A. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Reisler, E. |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)132018 |a Schröder, G.F. |b 5 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Egelman, E.H. |b 6 |
| 773 | _ | _ | |0 PERI:(DE-600)1461794-8 |a 10.1073/pnas.1110109108 |g Vol. 108, p. 20568 - 20572 |p 20568 - 20572 |q 108<20568 - 20572 |t Proceedings of the National Academy of Sciences of the United States of America |v 108 |x 0027-8424 |y 2011 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3251117 |
| 909 | C | O | |o oai:juser.fz-juelich.de:19044 |p VDB |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK409 |a DE-HGF |b Gesundheit |k P33 |l Funktion und Dysfunktion des Nervensystems |v Funktion und Dysfunktion des Nervensystems |x 0 |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK505 |a DE-HGF |b Schlüsseltechnologien |k P45 |l Biologische Informationsverarbeitung |v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |x 1 |
| 913 | 2 | _ | |a DE-HGF |b Key Technologies |l BioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences |1 G:(DE-HGF)POF3-550 |0 G:(DE-HGF)POF3-559H |2 G:(DE-HGF)POF3-500 |v Addenda |x 0 |
| 914 | 1 | _ | |y 2011 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)ICS-6-20110106 |g ICS |k ICS-6 |l Strukturbiochemie |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)133773 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|