Evidence map›Paper›PMID 9463369›Full record

ArticleThe EMBO journal1998

Viral protein R regulates nuclear import of the HIV-1 pre-integration complex.

S Popov, M Rexach, G Zybarth, N Reiling, M A Lee, L Ratner, C M Lane, M S Moore, G Blobel, M Bukrinsky

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed
7.9field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

135 citing papers in PubMed, 321 citations in OpenAlex.

  1. HIV-1 Vif and Vpr cooperatively modulate the cell cycle to maximize per-cell virion production.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  14. Frontiers in microbiology · 2021
    Article
  15. Article
  16. Review
  17. Protein ArginineViruses · 2020
    Article
  18. Article
  19. Review
  20. Nuclear landscape of HIV-1 infection and integration.Nature reviews. Microbiology · 2017
    Review

75 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

S PopovThe Picower Institute for Medical Research, Manhasset, NY 11030, USA.
M Rexach
G Zybarth
N Reiling
M A Lee
L Ratner
C M Lane
M S Moore
G Blobel
M Bukrinsky

Funding

VPR AND HIV1 NUCLEAR TRANSLOCATIONR01AI033776 · NIAID · PICOWER INSTITUTE FOR MEDICAL RESEARCH · PI BUKRINSKY, MICHAEL ILYA · 1998 to 2006
$2.0M
HIV VPX/VPR STRUCTURE/FUNCTIONR01AI036071 · NIAID · WASHINGTON UNIVERSITY · PI RATNER, LEE · 1995 to 2001
$557k
Role of Vpr in HIV-1 Nuclear TranslocationR21AI033776 · NIAID · GEORGE WASHINGTON UNIVERSITY · PI BUKRINSKY, MICHAEL ILYA · 2001 to 2001
$215k
MATRIX PROTEIN (MAP17) AND HIV-1 LIFE CYCLER29AI033776 · NIAID · PICOWER INSTITUTE FOR MEDICAL RESEARCH · PI BUKRINSKY, MICHAEL ILYA · 1993 to 1997
–
NIAID NIH HHS AI 33776NIAID NIH HHS AI 36071
6 · The paper itself

Abstract

Replication of human immunodeficiency virus type 1 (HIV-1) in non-dividing cells critically depends on import of the viral pre-integration complex into the nucleus. Genetic evidence suggests that viral protein R (Vpr) and matrix antigen (MA) are directly involved in the import process. An in vitro assay that reconstitutes nuclear import of HIV-1 pre-integration complexes in digitonin-permeabilized cells was used to demonstrate that Vpr is the key regulator of the viral nuclear import process. Mutant HIV-1 pre-integration complexes that lack Vpr failed to be imported in vitro, whereas mutants that lack a functional MA nuclear localization sequence (NLS) were only partially defective. Strikingly, the import defect of the Vpr- mutant was rescued when recombinant Vpr was re-added. In addition, import of Vpr- virus was rescued by adding the cytosol of HeLa cells, where HIV-1 replication had been shown to be Vpr-independent. In a solution binding assay, Vpr associated with karyopherin alpha, a cellular receptor for NLSs. This association increased the affinity of karyopherin alpha for basic-type NLSs, including that of MA, thus explaining the positive effect of Vpr on nuclear import of the HIV-1 pre-integration complex and BSA-NLS conjugates. These results identify the biochemical mechanism of Vpr function in transport of the viral pre-integration complex to, and across, the nuclear membrane.

Indexed as

Viral ProteinsVirus Integrationalpha KaryopherinsBiological TransportCell-Free SystemCell Membrane PermeabilityCell NucleusCytoplasmDefective VirusesDigitoningag Gene Products, Human Immunodeficiency VirusGene Products, gagGene Products, vprHeLa CellsHIV-1HIV Antigensalpha KaryopherinsDigitoningag Gene Products, Human Immunodeficiency VirusGene Products, gagGene Products, vprHIV AntigensNuclear Proteinsp17 protein, Human Immunodeficiency Virus Type 1Viral Proteinsvpr Gene Products, Human Immunodeficiency Virus

Identifiers

PMID9463369
PMCPMC1170440
OpenAlexW2117098951

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.