Evidence map›Paper›PMID 25646410›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.

Xiancheng Zeng, Suchetana Mukhopadhyay, Charles L Brooks

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Scalable Constant pH Molecular Dynamics in GROMACS.Journal of chemical theory and computation · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Novel Molecular Signatures of Chikungunya Virus in Puerto Rico.Puerto Rico health sciences journal · 2019
    Article
  10. Article
  11. CHARMM-GUI 10 years for biomolecular modeling and simulation.Journal of computational chemistry · 2017
    Review
  12. Review
  13. Article
  14. Computational virology: From the inside out.Biochimica et biophysica acta · 2016
    Review
  15. All-Atom Molecular Dynamics of Virus Capsids as Drug Targets.The journal of physical chemistry letters · 2016
    Article
  16. 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

3 authors at 2 institutions in 1 country.

Xiancheng ZengDepartment of Chemistry and Biophysics Program, University of Michigan, Ann Arbor, MI 48109; and.
Suchetana MukhopadhyayDepartment of Biology, Indiana University, Bloomington, IN 47405-7000.
Charles L BrooksDepartment of Chemistry and Biophysics Program, University of Michigan, Ann Arbor, MI 48109; and brookscl@umich.edu.
University of Michigan–Ann Arbor · USIndiana University Bloomington · US

Funding

Theoretical Studies of Receptor-Ligand InteractionsR01GM037554 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 1987 to 2018
$3.8M
INTERACTIONS IN NONNATIVE STATES OF PROTEINSR01GM057513 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI CASE, DAVID A · 1998 to 2012
$3.3M
Acid-mediated processes in nucleic acids and proteinsR01GM107233 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 2014 to 2017
$1.1M
NIGMS NIH HHS GM037554NIGMS NIH HHS GM057513NIGMS NIH HHS GM107233NIGMS NIH HHS R01 GM037554NIGMS NIH HHS R01 GM057513NIGMS NIH HHS R01 GM107233
6 · The paper itself

Abstract

Alphavirus envelope proteins, organized as trimers of E2-E1 heterodimers on the surface of the pathogenic alphavirus, mediate the low pH-triggered fusion of viral and endosomal membranes in human cells. The lack of specific treatment for alphaviral infections motivates our exploration of potential antiviral approaches by inhibiting one or more fusion steps in the common endocytic viral entry pathway. In this work, we performed constant pH molecular dynamics based on an atomic model of the alphavirus envelope with icosahedral symmetry. We have identified pH-sensitive residues that cause the largest shifts in thermodynamic driving forces under neutral and acidic pH conditions for various fusion steps. A series of conserved interdomain His residues is identified to be responsible for the pH-dependent conformational changes in the fusion process, and ligand binding sites in their vicinity are anticipated to be potential drug targets aimed at inhibiting viral infections.

Indexed as

Hydrogen-Ion ConcentrationMembrane FusionAlphavirusHydrogen BondingThermodynamicsViral Envelope ProteinsViral Envelope Proteinsalphavirusconstant pH molecular dynamicsenvelope proteinmembrane fusionpH

Identifiers

PMID25646410
PMCPMC4343099
OpenAlexW2078298078

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.