000013094 001__ 13094
000013094 005__ 20200402205938.0
000013094 0247_ $$2pmid$$apmid:20529298
000013094 0247_ $$2pmc$$apmc:PMC2894018
000013094 0247_ $$2DOI$$a10.1186/1743-422X-7-119
000013094 0247_ $$2WOS$$aWOS:000244272500011
000013094 037__ $$aPreJuSER-13094
000013094 041__ $$aeng
000013094 082__ $$a610
000013094 084__ $$2WoS$$aVirology
000013094 1001_ $$0P:(DE-HGF)0$$aVenkatachari, N.J.$$b0
000013094 245__ $$aHuman immunodeficiency virus type 1 Vpr: Oligomerization is an essential feature for its incorporation into virus particles
000013094 260__ $$aSan Diego, Calif. [u.a.]$$bElsevier$$c2010
000013094 300__ $$a119
000013094 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000013094 3367_ $$2DataCite$$aOutput Types/Journal article
000013094 3367_ $$00$$2EndNote$$aJournal Article
000013094 3367_ $$2BibTeX$$aARTICLE
000013094 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000013094 3367_ $$2DRIVER$$aarticle
000013094 440_0 $$023403$$aVirology$$v7$$x0042-6822
000013094 500__ $$aRecord converted from VDB: 12.11.2012
000013094 520__ $$aHIV-1 Vpr, a nonstructural viral protein associated with virus particles, has a positive role in the efficient transport of PIC into the nucleus of non-dividing target cells and enhances virus replication in primary T cells. Vpr is a 96 amino acid protein and the structure by NMR shows three helical domains. Vpr has been shown to exist as dimers and higher order oligomers. Considering the multifunctional nature of Vpr, the contribution of distinct helical domains to the dimer/oligomer structure of Vpr and the relevance of this feature to its functions are not clear. To address this, we have utilized molecular modeling approaches to identify putative models of oligomerization. The predicted interface residues were subjected to site-directed mutagenesis and evaluated their role in intermolecular interaction and virion incorporation. The interaction between Vpr molecules was monitored by Bimolecular Fluorescence complementation (BiFC) method. The results show that Vpr forms oligomers in live cells and residues in helical domains play critical roles in oligomerization. Interestingly, Vpr molecules defective in oligomerization also fail to incorporate into the virus particles. Based on the data, we suggest that oligomerization of Vpr is essential for virion incorporation property and may also have a role in the events associated with virus infection.
000013094 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000013094 588__ $$aDataset connected to Web of Science, Pubmed
000013094 650_2 $$2MeSH$$aAmino Acid Sequence
000013094 650_2 $$2MeSH$$aCell Line
000013094 650_2 $$2MeSH$$aHIV-1: chemistry
000013094 650_2 $$2MeSH$$aHIV-1: genetics
000013094 650_2 $$2MeSH$$aHIV-1: metabolism
000013094 650_2 $$2MeSH$$aHumans
000013094 650_2 $$2MeSH$$aMolecular Conformation
000013094 650_2 $$2MeSH$$aMolecular Sequence Data
000013094 650_2 $$2MeSH$$aProtein Structure, Tertiary
000013094 650_2 $$2MeSH$$aSequence Alignment
000013094 650_2 $$2MeSH$$aVirion: chemistry
000013094 650_2 $$2MeSH$$aVirion: genetics
000013094 650_2 $$2MeSH$$aVirion: metabolism
000013094 650_2 $$2MeSH$$avpr Gene Products, Human Immunodeficiency Virus: chemistry
000013094 650_2 $$2MeSH$$avpr Gene Products, Human Immunodeficiency Virus: genetics
000013094 650_2 $$2MeSH$$avpr Gene Products, Human Immunodeficiency Virus: metabolism
000013094 650_7 $$00$$2NLM Chemicals$$avpr Gene Products, Human Immunodeficiency Virus
000013094 650_7 $$2WoSType$$aJ
000013094 65320 $$2Author$$aHIV-1 Vpr
000013094 65320 $$2Author$$aCD28
000013094 65320 $$2Author$$aCTLA-4
000013094 65320 $$2Author$$aIFN-gamma
000013094 65320 $$2Author$$aNF-kappa B
000013094 65320 $$2Author$$aimmune activation
000013094 7001_ $$0P:(DE-HGF)0$$aWalker, L.A.$$b1
000013094 7001_ $$0P:(DE-HGF)0$$aTastan, O.$$b2
000013094 7001_ $$0P:(DE-HGF)0$$aLe, T.$$b3
000013094 7001_ $$0P:(DE-HGF)0$$aDempsey, T.M.$$b4
000013094 7001_ $$0P:(DE-HGF)0$$aLi, Y.$$b5
000013094 7001_ $$0P:(DE-HGF)0$$aYanamala, N.$$b6
000013094 7001_ $$0P:(DE-HGF)0$$aSrinivasan, A.$$b7
000013094 7001_ $$0P:(DE-Juel1)VDB44599$$aKlein-Seetharaman, J.$$b8$$uFZJ
000013094 7001_ $$0P:(DE-HGF)0$$aMontelaro, R.C.$$b9
000013094 7001_ $$0P:(DE-HGF)0$$aAyyavoo, V.$$b10
000013094 773__ $$0PERI:(DE-600)1471925-3$$a10.1186/1743-422X-7-119$$gVol. 7, p. 119$$p119$$q7<119$$tVirology$$v7$$x0042-6822$$y2010
000013094 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2894018
000013094 909CO $$ooai:juser.fz-juelich.de:13094$$pVDB
000013094 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000013094 9132_ $$0G:(DE-HGF)POF3-551$$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$$vFunctional Macromolecules and Complexes$$x0
000013094 9141_ $$y2010
000013094 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000013094 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
000013094 970__ $$aVDB:(DE-Juel1)124921
000013094 980__ $$aVDB
000013094 980__ $$aConvertedRecord
000013094 980__ $$ajournal
000013094 980__ $$aI:(DE-Juel1)ICS-6-20110106
000013094 980__ $$aUNRESTRICTED
000013094 981__ $$aI:(DE-Juel1)IBI-7-20200312
000013094 981__ $$aI:(DE-Juel1)ICS-6-20110106
000013094 981__ $$aI:(DE-Juel1)ISB-2-20090406