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| 001 | 55021 | ||
| 005 | 20200402210300.0 | ||
| 024 | 7 | _ | |2 WOS |a WOS:000236290300001 |
| 037 | _ | _ | |a PreJuSER-55021 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |a Lemaitre, V. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy |
| 260 | _ | _ | |a Guilderland, NY |b Adenine Press |c 2006 |
| 300 | _ | _ | |a 485 - 496 |
| 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 | |a Journal of Biomolecular Structure & Dynamics |x 0739-1102 |0 16381 |v 23 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Based on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV- 1) and closely related simian immunodeficiency viruses (SIVs). Its role is to amplify viral release. Upon phosphorylation, the cytoplasmic domain adopts a more compact shape with helices 2 and 3 becoming almost parallel to each other. A loss of helicity for several residues belonging to the helices adjacent to both ends of the loop region containing serines 53 and 57 is observed. A fourth helix, present in one of: the NMR-based Structures of the cytoplasmic domain and located near the C-terminus, is lost upon phosphorylation. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a Vpu |
| 653 | 2 | 0 | |2 Author |a HIV-1 |
| 653 | 2 | 0 | |2 Author |a membrane protein |
| 653 | 2 | 0 | |2 Author |a molecular dynamics simulations |
| 653 | 2 | 0 | |2 Author |a NMR spectroscopy |
| 700 | 1 | _ | |a Wray, V. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Willbold, D. |b 2 |u FZJ |0 P:(DE-Juel1)132029 |
| 700 | 1 | _ | |a Watts, A. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Fischer, W. B. |b 4 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |g Vol. 23, p. 485 - 496 |p 485 - 496 |q 23<485 - 496 |0 PERI:(DE-600)2085732-9 |t Journal of biomolecular structure & dynamics |v 23 |y 2006 |x 0739-1102 |
| 909 | C | O | |o oai:juser.fz-juelich.de:55021 |p VDB |
| 913 | 1 | _ | |k P33 |v Funktion und Dysfunktion des Nervensystems |l Funktion und Dysfunktion des Nervensystems |b Gesundheit |0 G:(DE-Juel1)FUEK409 |x 0 |
| 914 | 1 | _ | |y 2006 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 920 | 1 | _ | |k JARA-SIM |l Jülich-Aachen Research Alliance - Simulation Sciences |g JARA |0 I:(DE-Juel1)VDB1045 |x 1 |
| 970 | _ | _ | |a VDB:(DE-Juel1)85880 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a I:(DE-Juel1)VDB1045 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)VDB1045 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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