Evidence map›Paper›PMID 34824204›Full record

ArticleNature communications2021

Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A.

In-Ja L Byeon, Guillermo Calero, Ying Wu, Chang H Byeon, Jinwon Jung, Maria DeLucia, Xiaohong Zhou, Simon Weiss, Jinwoo Ahn, Caili Hao and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
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  7. Review
  8. Article
  9. Article
  10. Biomolecular NMR assignments · 2023
    Article
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

12 authors at 1 institution in 2 countries.

In-Ja L Byeon *Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Guillermo Calero *Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. guc9@pitt.edu.ORCID http://orcid.org/0000-0003-3730-4676
Ying WuPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Chang H ByeonDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID http://orcid.org/0000-0001-9997-7708
Jinwon JungDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID http://orcid.org/0000-0002-7981-3316
Maria DeLuciaPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Xiaohong ZhouPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID http://orcid.org/0000-0003-0519-2550
Simon WeissDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Jinwoo AhnPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID http://orcid.org/0000-0003-4339-0515
Caili HaoPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Jacek SkowronskiPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Angela M GronenbornPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. amg100@pitt.edu.ORCID http://orcid.org/0000-0001-9072-3525
University of Pittsburgh · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CHRISTOPHER J. BAKKENIST · 1988 to 2026
$158.0M
Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIONG, YONG · 2019 to 2021
$14.1M
A low volume isothermal titration calorimeter for structure-function studies of biological macromoleculesS10OD023481 · OD · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2017 to 2017
$127k
NCI NIH HHS P30 CA047904NIAID NIH HHS P50 AI150481NIH HHS S10 OD023481
6 · The paper itself

Abstract

HIV-1 Vpr is a prototypic member of a large family of structurally related lentiviral virulence factors that antagonize various aspects of innate antiviral immunity. It subverts host cell DNA repair and protein degradation machineries by binding and inhibiting specific post-replication repair enzymes, linking them via the DCAF1 substrate adaptor to the Cullin 4 RING E3 ligase (CRL4

Indexed as

Crystallography, X-RayDNA-Binding ProteinsDNA RepairDNA Repair EnzymesHIV-1Host-Pathogen InteractionsHumansNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesProtein Structure, SecondaryUbiquitin-Protein Ligasesvpr Gene Products, Human Immunodeficiency VirusDCAF1 protein, humanDNA-Binding ProteinsDNA Repair EnzymesProtein Serine-Threonine KinasesRAD23A protein, humanRAD23B protein, humanUbiquitin-Protein Ligasesvpr Gene Products, Human Immunodeficiency Virusvpr protein, Human immunodeficiency virus 1XPC protein, human

Identifiers

PMID34824204
PMCPMC8617076
OpenAlexW3187417685

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.