Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr.

Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr.

Item
http://www.wikidata.org/entity/Q33787316
The Vpr protein from HIV-1: distinct roles along the viral life cycleAnalysis of HIV-1 Vpr determinants responsible for cell growth arrest in Saccharomyces cerevisiaeStructure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solutionCharacterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assayThe inhibition of assembly of HIV-1 virus-like particles by 3-O-(3',3'-dimethylsuccinyl) betulinic acid (DSB) is counteracted by Vif and requires its Zinc-binding domain.The immunosuppressive properties of the HIV Vpr protein are linked to a single highly conserved residue, R90HIV-1 Vpr oligomerization but not that of Gag directs the interaction between Vpr and Gag.Development of a robust cell-based high-throughput screening assay to identify targets of HIV-1 viral protein R dimerization.HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic interventionA comprehensive analysis of the naturally occurring polymorphisms in HIV-1 Vpr: potential impact on CTL epitopesHIV-1 Vpr-a still "enigmatic multitasker".HIV1-viral protein R (Vpr) mutations: associated phenotypes and relevance for clinical pathologies.Proline 35 of human immunodeficiency virus type 1 (HIV-1) Vpr regulates the integrity of the N-terminal helix and the incorporation of Vpr into virus particles and supports the replication of R5-tropic HIV-1 in human lymphoid tissue ex vivo.Human immunodeficiency virus type 1 Vpr: oligomerization is an essential feature for its incorporation into virus particles.Specific amino acids in HIV-1 Vpr are significantly associated with differences in patient neurocognitive status.Direct Vpr-Vpr interaction in cells monitored by two photon fluorescence correlation spectroscopy and fluorescence lifetime imaging.Structural characterization of the HIV-1 Vpr N terminus: evidence of cis/trans-proline isomerism.
P2860

Functional role of residues corresponding to helical domain II (amino acids 35 to 46) of human immunodeficiency virus type 1 Vpr.

Item
http://www.wikidata.org/entity/Q33787316
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@ast
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@en
type
label
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@ast
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@en
prefLabel
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@ast
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Functional role of residues co ...... nodeficiency virus type 1 Vpr.
@en
P2093
P2860
P304
P31
P356
10.1128/JVI.74.22.10650-10657.2000
P433
P478
P577
P5875
P698
P932