The cationic amphipathic alpha-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells.
about
The Vpr protein from HIV-1: distinct roles along the viral life cycleHuman immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145Activation of the ATR pathway by human immunodeficiency virus type 1 Vpr involves its direct binding to chromatin in vivoPathway for polyarginine entry into mammalian cellsPP2A1 binding, cell transducing and apoptotic properties of Vpr(77-92): a new functional domain of HIV-1 Vpr proteins.Targeted Vpr-derived peptides reach mitochondria to induce apoptosis of alphaVbeta3-expressing endothelial cells.The progestin-only contraceptive medroxyprogesterone acetate, but not norethisterone acetate, enhances HIV-1 Vpr-mediated apoptosis in human CD4+ T cells through the glucocorticoid receptor.Polyanions and the proteome.Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides.A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsid-condensed RNA to Vpr-bridged DNA.Human immunodeficiency virus viral protein R as an extracellular protein in neuropathogenesis.Cell-surface processing of extracellular human immunodeficiency virus type 1 Vpr by proprotein convertases.HIV-1 Vpr-a still "enigmatic multitasker".Roles of Vpr and Vpx in modulating the virus-host cell relationship.HIV1-viral protein R (Vpr) mutations: associated phenotypes and relevance for clinical pathologies.Activation of JNK-dependent pathway is required for HIV viral protein R-induced apoptosis in human monocytic cells: involvement of antiapoptotic BCL2 and c-IAP1 genes.Synthetic Vpr protein activates activator protein-1, c-Jun N-terminal kinase, and NF-kappaB and stimulates HIV-1 transcription in promonocytic cells and primary macrophages.The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain.Polyarginine as a multifunctional fusion tag.Crotamine mediates gene delivery into cells through the binding to heparan sulfate proteoglycans.
P2860
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P2860
The cationic amphipathic alpha-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeabilizes membranes, and efficiently transfects cells.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The cationic amphipathic alpha ...... efficiently transfects cells.
@en
type
label
The cationic amphipathic alpha ...... efficiently transfects cells.
@en
prefLabel
The cationic amphipathic alpha ...... efficiently transfects cells.
@en
P2093
P2860
P356
P1476
The cationic amphipathic alpha ...... d efficiently transfects cells
@en
P2093
Antoine Kichler
Dominique Coulaud
Emmanuel Coeytaux
Olivier Danos
P2860
P304
18110-18116
P356
10.1074/JBC.M300248200
P407
P50
P577
2003-03-14T00:00:00Z