Evidence map›Paper›PMID 28606917›Full record

ArticleMolecular & cellular proteomics : MCP2017

Quantitative Temporal Viromics of an Inducible HIV-1 Model Yields Insight to Global Host Targets and Phospho-Dynamics Associated with Protein Vpr.

John D Lapek, Mary K Lewinski, Jacob M Wozniak, John Guatelli, David J Gonzalez

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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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

5 authors at 2 institutions in 1 country.

John D LapekFrom the ‡Department of Pharmacology.
Mary K Lewinski§Skaggs School of Pharmacy and Pharmaceutical Sciences.
Jacob M WozniakFrom the ‡Department of Pharmacology.
John Guatelli¶San Diego Veterans Affairs Healthcare System, San Diego, California 92161, and.
David J GonzalezFrom the ‡Department of Pharmacology, djgonzalez@ucsd.edu.
University of Montana · USVA San Diego Healthcare System · US

Funding

VirologyP30AI036214 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Maile Ann Young Karris · 1994 to 2026
$78.4M
UCSD/SDSU IRACDAK12GM068524 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TREJO, JOANN · 2003 to 2025
$24.4M
GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
HIV-1 Vpu and BST-2/CD317R37AI081668 · NIAID · VETERANS MEDICAL RESEARCH FDN/SAN DIEGO · PI GUATELLI, JOHN C. · 2014 to 2023
$4.8M
HIV-1 Modulation of the Ubiquitinome and Its Effects on Cell-to-Cell TransmissionK08AI112394 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LEWINSKI, MARY KATHLEEN · 2015 to 2019
$971k
NIAID NIH HHS K08 AI112394NIAID NIH HHS P30 AI036214NIAID NIH HHS R37 AI081668NIGMS NIH HHS K12 GM068524NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

The mechanisms by which human immunodeficiency virus (HIV) circumvents and coopts cellular machinery to replicate and persist in cells are not fully understood. HIV accessory proteins play key roles in the HIV life cycle by altering host pathways that are often dependent on post-translational modifications (PTMs). Thus, the identification of HIV accessory protein host targets and their PTM status is critical to fully understand how HIV invades, avoids detection and replicates to spread infection. To date, a comprehensive characterization of HIV accessory protein host targets and modulation of their PTM status does not exist. The significant gap in knowledge regarding the identity and PTMs of HIV host targets is due, in part, to technological limitations. Here, we applied current mass spectrometry techniques to define mechanisms of viral protein action by identifying host proteins whose abundance is affected by the accessory protein Vpr and the corresponding modulation of down-stream signaling pathways, specifically those regulated by phosphorylation. By utilizing a novel, inducible HIV-1 CD4+ T-cell model system expressing either the wild type or a

Indexed as

Host-Pathogen InteractionsAurora Kinase ACD4-Positive T-LymphocytesCell Cycle ProteinsCyclin-Dependent Kinase 4Gene ExpressionGene OntologyHEK293 CellsHIV-1HIV InfectionsHumansJurkat CellsPhosphorylationProtein Processing, Post-TranslationalProteomicsRNA SplicingAurora Kinase ACell Cycle ProteinsCyclin-Dependent Kinase 4vpr Gene Products, Human Immunodeficiency Virus

Identifiers

PMID28606917
PMCPMC5546197
OpenAlexW2624877602

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.