Evidence map›Paper›PMID 22947870›Full record

ArticleBiophysical journal2012

Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release.

James E N Taylor, John Y H Chow, Cy M Jeffries, Ann H Kwan, Anthony P Duff, William A Hamilton, Jill Trewhella

Erratum issuedOpen access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.Proceedings of the National Academy of Sciences of the United States of America · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

James E N TaylorBragg Institute, Australian Nuclear Science and Technology Organisation, New South Wales, Australia; School of Molecular Bioscience, The University of Sydney, New South Wales, Australia.
John Y H ChowSchool of Molecular Bioscience, The University of Sydney, New South Wales, Australia.
Cy M JeffriesSchool of Molecular Bioscience, The University of Sydney, New South Wales, Australia.
Ann H KwanSchool of Molecular Bioscience, The University of Sydney, New South Wales, Australia.
Anthony P DuffBragg Institute, Australian Nuclear Science and Technology Organisation, New South Wales, Australia.
William A HamiltonBragg Institute, Australian Nuclear Science and Technology Organisation, New South Wales, Australia.
Jill TrewhellaSchool of Molecular Bioscience, The University of Sydney, New South Wales, Australia. Electronic address: jill.trewhella@sydney.edu.au.
The University of Sydney · AUAustralian Nuclear Science and Technology Organisation · AU

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

Calmodulin (CaM) expression is upregulated upon HIV-1 infection and interacts with proteins involved in viral processing, including the multifunctional HIV-1 MA protein. We present here the results of studies utilizing small-angle neutron scattering with contrast variation that, when considered in the light of earlier fluorescence and NMR data, show CaM binds MA in an extended open-clamp conformation via interactions with two tryptophans that are widely spaced in sequence and space. The interaction requires a disruption of the MA tertiary fold such that MA becomes highly extended in a long snakelike conformation. The CaM-MA interface is extensive, covering ~70% of the length of the MA such that regions known to be important in MA interactions with critical binding partners would be impacted. The CaM conformation is semiextended and as such is distinct from the classical CaM-collapse about short α-helical targets. NMR data show that upon dissociation of the CaM-MA complex, either by the removal of Ca

Indexed as

HIV-1Protein RefoldingCalmodulingag Gene Products, Human Immunodeficiency VirusHIV AntigensModels, MolecularNeutron DiffractionNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationScattering, Small AngleCalmodulingag Gene Products, Human Immunodeficiency VirusHIV Antigensp17 protein, Human Immunodeficiency Virus Type 1

Identifiers

PMID22947870
PMCPMC3414894
OpenAlexW2080408283

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.