Evidence map›Paper›PMID 29176596›Full record

ArticleNature communications2017

Quenching protein dynamics interferes with HIV capsid maturation.

Mingzhang Wang, Caitlin M Quinn, Juan R Perilla, Huilan Zhang, Randall Shirra, Guangjin Hou, In-Ja Byeon, Christopher L Suiter, Sherimay Ablan, Emiko Urano and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 62 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Synthesis ofMagnetic resonance in chemistry : MRC · 2026
    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

17 authors at 6 institutions in 2 countries.

Mingzhang WangDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Caitlin M QuinnDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Juan R PerillaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA. jperilla@udel.edu.ORCID http://orcid.org/0000-0003-1171-6816
Huilan ZhangDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Randall ShirraPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA, 15261, USA.
Guangjin HouDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.ORCID http://orcid.org/0000-0001-8292-1169
In-Ja ByeonPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA, 15261, USA.
Christopher L SuiterDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA.
Sherimay AblanHIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.
Emiko UranoHIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.
Theodore J NitzDFH Pharma, Gaithersburg, MD, 20886, USA.
Christopher AikenPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA, 15261, USA.
Eric O FreedHIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.
Peijun ZhangPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA, 15261, USA.
Klaus SchultenUniversity of Illinois, Theoretical and Computational Biophysics Group, Urbana, IL, 61801, USA.
Angela M GronenbornPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave., Pittsburgh, PA, 15261, USA. amg100@pitt.edu.
Tatyana PolenovaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA. tpolenov@udel.edu.ORCID http://orcid.org/0000-0002-0346-1131
University of Pittsburgh · USNational Cancer Institute · USCentre for Human Genetics · GBUniversity of Illinois Urbana-Champaign · USUrbana University · USVifor Pharma (United States) · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
The Center for HIV RNA Studies (CRNA)P50GM103297 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAYIE, KWAKU · 2012 to 2016
$21.7M
WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI PATEL, SANDEEP · 2014 to 2018
$5.8M
COBRE on Membrane Protein Production and CharacterizationP30GM103519 · NIGMS · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2012 to 2014
$3.3M
Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
750MHz Wide Bore NMR SpectrometerS10OD012213 · OD · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2013 to 2013
$2.0M
MAS NMR Studies of the NIV-1 Gag Polyprotein Assembled into Virus-Like ParticlesF32GM113452 · NIGMS · UNIVERSITY OF DELAWARE · PI QUINN, CAITLIN · 2015 to 2016
$109k
NIGMS NIH HHS F32 GM113452NIGMS NIH HHS P30 GM103519NIGMS NIH HHS P30 GM110758NIGMS NIH HHS P41 GM104601NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50 GM103297NIGMS NIH HHS R01 GM116961NIH HHS S10 OD012213Wellcome Trust 206422/Z/17/Z
6 · The paper itself

Abstract

Maturation of HIV-1 particles encompasses a complex morphological transformation of Gag via an orchestrated series of proteolytic cleavage events. A longstanding question concerns the structure of the C-terminal region of CA and the peptide SP1 (CA-SP1), which represents an intermediate during maturation of the HIV-1 virus. By integrating NMR, cryo-EM, and molecular dynamics simulations, we show that in CA-SP1 tubes assembled in vitro, which represent the features of an intermediate assembly state during maturation, the SP1 peptide exists in a dynamic helix-coil equilibrium, and that the addition of the maturation inhibitors Bevirimat and DFH-055 causes stabilization of a helical form of SP1. Moreover, the maturation-arresting SP1 mutation T8I also induces helical structure in SP1 and further global dynamical and conformational changes in CA. Overall, our results show that dynamics of CA and SP1 are critical for orderly HIV-1 maturation and that small molecules can inhibit maturation by perturbing molecular motions.

Indexed as

CapsidCapsid ProteinsCell LineHIV-1HIV InfectionsHumansPeptidesVirus AssemblyCapsid ProteinsPeptides

Identifiers

PMID29176596
PMCPMC5701193
OpenAlexW2768954818

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.