Evidence map›Paper›PMID 21941623›Full record

ArticleViruses2011

A long-awaited structure is rev-ealed.

Myles H Hammarskjold, David Rekosh

Abstract read
In one paragraph

Article in Viruses, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. 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

2 authors.

Myles H HammarskjoldMyles H. Thaler Center for AIDS and Human Retrovirus Research and The Department of Microbiology, University of Virginia, Charlottesville, VA 22908, USA.
David Rekosh

Funding

Women's Interagency HIV Study (WIHS-V)U01AI035004 · NIAID · MONTEFIORE MEDICAL CENTER (BRONX, NY) · PI ANASTOS, KATHRYN M., SHARMA, ANJALI · 1993 to 2018
$65.7M
Engineered gp41 Peptides as HIV-1 Topical MicrobicidesR01AI068591 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI LU, MIN · 2006 to 2009
$1.6M
Compounds That Inhibit HIV Rev FunctionR01AI068501 · NIAID · UNIVERSITY OF VIRGINIA · PI REKOSH, DAVID M · 2006 to 2008
$1.3M
Functional Variation of Rev and RRE Activity During HIV InfectionR01GM110009 · NIGMS · UNIVERSITY OF VIRGINIA · PI HAMMARSKJOLD, MARIE-LOUISE, REKOSH, DAVID M · 2013 to 2016
$1.2M
NXF Proteins, Cofactors and TargetsR01GM087651 · NIGMS · UNIVERSITY OF VIRGINIA · PI HAMMARSKJOLD, MARIE-LOUISE · 2009 to 2012
$1.2M
HIV Rev/RRE Variation and ConstraintsR21AI087505 · NIAID · UNIVERSITY OF VIRGINIA · PI REKOSH, DAVID M · 2010 to 2011
$417k
Therapeutic Antisense RNA and The HIV Rev-RRE PathwayR21AI080411 · NIAID · UNIVERSITY OF VIRGINIA · PI HAMMARSKJOLD, MARIE-LOUISE · 2009 to 2010
$415k
NIAID NIH HHS AI035004NIAID NIH HHS AI068591NIAID NIH HHS AI080411NIAID NIH HHS AI087505NIAID NIH HHS R01 AI068501NIAID NIH HHS R01 AI068591NIAID NIH HHS R21 AI080411NIAID NIH HHS R21 AI087505NIAID NIH HHS U01 AI035004NIGMS NIH HHS GM087651NIGMS NIH HHS R01 GM087651NIGMS NIH HHS R01 GM110009
6 · The paper itself

Abstract

It has been known for some time that the HIV Rev protein binds and oligomerizes on a well-defined multiple stem-loop RNA structure, named the Rev Response Element (RRE), which is present in a subset of HIV mRNAs. This binding is the first step in a pathway that overcomes a host restriction, which would otherwise prevent the export of these RNAs to the cytoplasm. Four recent publications now provide new insight into the structure of Rev and the multimeric RNA-protein complex that forms on the RRE. Two unexpected and remarkable findings revealed in these studies are the flexibility of RNA binding that is demonstrated by the Rev arginine-rich RNA binding motif, and the way that both Rev protein and RRE contribute to the formation of the complex in a highly cooperative fashion. These studies also define the Rev dimerization and oligomerization interfaces to a resolution of 2.5Å, providing a framework necessary for further structural and functional studies. Additionally, and perhaps most importantly, they also pave the way for rational drug design, which may ultimately lead to new therapies to inhibit this essential HIV function.

Indexed as

DimerizationHIV-1HIV InfectionsHumansProtein BindingResponse Elementsrev Gene Products, Human Immunodeficiency VirusRNA, Viralrev Gene Products, Human Immunodeficiency VirusRNA, ViralHIV-1nuclear-cytoplasmic exportprotein structureRevRNA exportRNA-protein bindingRREX-ray crystallography

Identifiers

PMID21941623
PMCPMC3176729

What OpenQuestion holds

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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.