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| Hauptseite > Publikationsdatenbank > Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16 > print |
| Hauptseite > Publikationsdatenbank > Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16 > print |
| 001 | 7510 | ||
| 005 | 20200402205733.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:19533740 |
| 024 | 7 | _ | |2 DOI |a 10.1002/prot.22477 |
| 024 | 7 | _ | |2 WOS |a WOS:000270849900013 |
| 037 | _ | _ | |a PreJuSER-7510 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-Juel1)VDB77156 |a Thielmann, Y. |b 0 |u FZJ |
| 245 | _ | _ | |a Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16 |
| 260 | _ | _ | |a New York, NY |b Wiley-Liss |c 2009 |
| 300 | _ | _ | |a 637 - 646 |
| 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 21902 |a Proteins: Structure, function and Bioinformatics |v 77 |x 0887-3585 |y 3 |
| 500 | _ | _ | |a Grant sponsor: Deutsche Forschungsgememschaft (DFG); Grant number: Wil472/5. |
| 520 | _ | _ | |a Vesicular trafficking is an important homeostatic process in eukaryotic cells which critically relies on membrane fusion. One of the essential components of the universal membrane fusion machinery is NSF (N-ethylmaleimide-sensitive factor), a large hexameric ATPase involved in disassembly of SNARE (soluble NSF attachment protein receptor) complexes. To improve our understanding of this sophisticated molecular machine, we have modeled the structure of the NSF hexamer in two alternative assemblies. Our data suggest a mechanistic concept of the operating mode of NSF which helps to explain the functional impact of post-translational modifications and mutations reported previously. Furthermore, we propose a binding site for the ubiquitin-like proteins GABARAP and GATE-16, which is supported by experimental evidence, yielding a complex with favorable surface complementarity. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK443 |2 G:(DE-HGF) |a Programm Biosoft |c N03 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Adaptor Proteins, Signal Transducing: chemistry |
| 650 | _ | 2 | |2 MeSH |a Adenosine Triphosphate: chemistry |
| 650 | _ | 2 | |2 MeSH |a Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Hydrolysis |
| 650 | _ | 2 | |2 MeSH |a Microfilament Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Microtubule-Associated Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a N-Ethylmaleimide-Sensitive Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Peptides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Phosphorylation |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Protein Interaction Mapping |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Ubiquitin: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Adaptor Proteins, Signal Transducing |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a GABARAP protein, human |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a GABARAPL2 protein, human |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Microfilament Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Microtubule-Associated Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Peptides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Ubiquitin |
| 650 | _ | 7 | |0 56-65-5 |2 NLM Chemicals |a Adenosine Triphosphate |
| 650 | _ | 7 | |0 EC 3.6.4.6 |2 NLM Chemicals |a N-Ethylmaleimide-Sensitive Proteins |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a N-ethylmaleimide-sensitive factor |
| 653 | 2 | 0 | |2 Author |a GABARAP |
| 653 | 2 | 0 | |2 Author |a comparative modeling |
| 653 | 2 | 0 | |2 Author |a structure model |
| 653 | 2 | 0 | |2 Author |a protein-protein interaction |
| 700 | 1 | _ | |0 P:(DE-Juel1)131988 |a Weiergräber, O.H. |b 1 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB84828 |a Ma, P. |b 2 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132019 |a Schwarten, M. |b 3 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132012 |a Mohrlüder, J. |b 4 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 5 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)1475032-6 |a 10.1002/prot.22477 |g Vol. 77, p. 637 - 646 |p 637 - 646 |q 77<637 - 646 |t Proteins |v 77 |x 0887-3585 |y 2009 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1002/prot.22477 |
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| 914 | 1 | _ | |y 2009 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)ISB-2-20090406 |d 31.12.2010 |g ISB |k ISB-2 |l Molekulare Biophysik |x 0 |
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