Evidence map›Paper›PMID 30639227›Full record

ReviewStructure (London, England : 1993)2019

HIV-1 Reverse Transcriptase: A Metamorphic Protein with Three Stable States.

Robert E London

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Protease-mediated maturation of M-PMV reverse transcriptase into a functional heterodimer.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Design and discovery of metamorphic proteins.Current opinion in structural biology · 2022
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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

1 author at 1 institution in 1 country.

Robert E LondonGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA. Electronic address: london@niehs.nih.gov.
National Institutes of Health · US

Funding

Aids Related Nmr ResearchZIAES050147 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI LONDON, ROBERT E · 2009 to 2020
$6.3M
Intramural NIH HHS ZIA ES050147
6 · The paper itself

Abstract

There has been a steadily increasing appreciation of the fact that the relationship between protein sequence and structure is often sufficiently ambiguous to allow a single sequence to adopt alternative, stable folds. Living organisms have been able to utilize such metamorphic proteins in remarkable and unanticipated ways. HIV-1 reverse transcriptase is among the earliest such proteins identified and remains a unique example in which a functional heterodimer contains two, alternatively folded polymerase domains. Structural characterization of the p66 precursor protein combined with NMR spectroscopic and molecular modeling studies have provided insights into the factors underlying the metamorphic transition and the subunit-specific programmed unfolding step required to expose the protease cleavage site within the ribonuclease H domain, supporting the conversion of the p66/p66' precursor into the mature p66/p51 heterodimer.

Indexed as

Enzyme StabilityHIV-1HIV Reverse TranscriptaseModels, MolecularMultienzyme ComplexesNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein FoldingHIV Reverse TranscriptaseMultienzyme Complexesreverse transcriptase, Human immunodeficiency virus 1HIV-1 reverse transcriptasemetamorphic proteinmetamorphic transitionprogrammed unfoldingsubunit-specific RH-domain unfolding

Identifiers

PMID30639227
PMCPMC6686890
OpenAlexW2909288089

What OpenQuestion holds

Textmetadata
LicenceTDM
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.