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.

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.

Item

http://www.wikidata.org/entity/Q39565551

Q39565551

about

Solution structure of the Equine Infectious Anemia Virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein Characterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assay The 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 intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.The host-pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains A comprehensive analysis of the naturally occurring polymorphisms in HIV-1 Vpr: potential impact on CTL epitopes Human immunodeficiency virus type 1 Vpr: oligomerization is an essential feature for its incorporation into virus particles.Virion encapsidated HIV-1 Vpr induces NFAT to prime non-activated T cells for productive infection.Dual role of the chromatin-binding factor PHF13 in the pre- and post-integration phases of HIV-1 replication.

P2860

Q27658675-5824022A-C835-4827-90FA-8EAEFAD0567F Q28477791-9FEB4789-6F29-4A59-B8E5-4EA7F5372438 Q30440445-C7922C77-6623-4CB4-8E2B-CFA9E667A825 Q33710135-B5D104BB-839B-4C9C-800D-F865029CFCF7 Q34106660-270804B5-32D1-4B6C-9EDE-DDE3D537A506 Q36908259-DC2EB11C-A549-42A0-8363-107AFFBA932B Q39696115-3686E981-5BF5-4037-B792-151C6641BD42 Q40623679-76587DAC-ADE9-43CA-8DF1-8CDD15AE8597 Q41918811-408B82C6-CBAA-4936-8D9B-4F269A9A4BEF

P2860

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.

Item

http://www.wikidata.org/entity/Q39565551

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

Proline 35 of human immunodefi ...... human lymphoid tissue ex vivo.

@en

Proline 35 of human immunodeficiency virus type 1

@nl

type

Item

label

Proline 35 of human immunodefi ...... human lymphoid tissue ex vivo.

@en

Proline 35 of human immunodeficiency virus type 1

@nl

prefLabel

Proline 35 of human immunodefi ...... human lymphoid tissue ex vivo.

@en

Proline 35 of human immunodeficiency virus type 1

@nl

P1476

Proline 35 of human immunodefi ...... human lymphoid tissue ex vivo.

@en

P2093

Alok Sharma

http://www.w3.org/2001/XMLSchema#string

Bernhard Schick

http://www.w3.org/2001/XMLSchema#string

Elke Rücker

http://www.w3.org/2001/XMLSchema#string

Jan Münch

http://www.w3.org/2001/XMLSchema#string

Jörg Votteler

http://www.w3.org/2001/XMLSchema#string

Karsten Bruns

http://www.w3.org/2001/XMLSchema#string

Nicole Studtrucker

http://www.w3.org/2001/XMLSchema#string

Peter Henklein

http://www.w3.org/2001/XMLSchema#string

Stefan Sörgel

http://www.w3.org/2001/XMLSchema#string

Torgils Fossen

http://www.w3.org/2001/XMLSchema#string

P2860

The Vpr protein from HIV-1: distinct roles along the viral life cycle

NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr

NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains

NMR structure of the HIV-1 regulatory protein VPR

Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone

Interaction with the p6 domain of the gag precursor mediates incorporation into virions of Vpr and Vpx proteins from primate lentiviruses

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

Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells

A conserved dileucine-containing motif in p6(gag) governs the particle association of Vpx and Vpr of simian immunodeficiency viruses SIV(mac) and SIV(agm)

Preferential coreceptor utilization and cytopathicity by dual-tropic HIV-1 in human lymphoid tissue ex vivo.

P304

9572-9576

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/JVI.02803-06

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Frank Kirchhoff

P577

2007-06-06T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

17553868

http://www.w3.org/2001/XMLSchema#string

P932

1951402

http://www.w3.org/2001/XMLSchema#string

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.

about

P2860

P2860

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.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932