Evidence map›Paper›PMID 29708495›Full record

ArticleeLife2018

All-atom molecular dynamics of the HBV capsid reveals insights into biological function and cryo-EM resolution limits.

Jodi A Hadden, Juan R Perilla, Christopher John Schlicksup, Balasubramanian Venkatakrishnan, Adam Zlotnick, Klaus Schulten

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1The journal of physical chemistry. B · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. All-atom MD simulations of the HPV16 capsid.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

6 authors.

Jodi A HaddenDepartment of Chemistry and Biochemistry, University of Delaware, Newark, United States.ORCID 0000-0003-4685-8291
Juan R PerillaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, United States.ORCID 0000-0003-1171-6816
Christopher John SchlicksupDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States.
Balasubramanian VenkatakrishnanDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States.
Adam ZlotnickDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States.ORCID 0000-0001-9945-6267
Klaus SchultenDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, United States.ORCID 0000-0001-7192-9632

Funding

Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI BEEBE, THOMAS PAUL · 2014 to 2018
$5.8M
Graduate Program in Quantitative and Chemical Biology at Indiana University BloomT32GM109825 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 2014 to 2018
$926k
NIGMS NIH HHS P30 GM110758NIGMS NIH HHS T32 GM109825NIH HHS Biomedical Technology Research Resource,9P41GM104601NIH HHS Center of Biomedical Research Excellence Grant,5P30GM110758-04
6 · The paper itself

Abstract

The hepatitis B virus capsid represents a promising therapeutic target. Experiments suggest the capsid must be flexible to function; however, capsid structure and dynamics have not been thoroughly characterized in the absence of icosahedral symmetry constraints. Here, all-atom molecular dynamics simulations are leveraged to investigate the capsid without symmetry bias, enabling study of capsid flexibility and its implications for biological function and cryo-EM resolution limits. Simulation results confirm flexibility and reveal a propensity for asymmetric distortion. The capsid's influence on ionic species suggests a mechanism for modulating the display of cellular signals and implicates the capsid's triangular pores as the location of signal exposure. A theoretical image reconstruction performed using simulated conformations indicates how capsid flexibility may limit the resolution of cryo-EM. Overall, the present work provides functional insight beyond what is accessible to experimental methods and raises important considerations regarding asymmetry in structural studies of icosahedral virus capsids.

Indexed as

Cryoelectron MicroscopyMolecular Dynamics SimulationCapsidHepatitis B virusProtein ConformationCryo-EM resolutionHepatitis B Virusmolecular biophysicsMolecular Dynamics SimulationnoneSingle-Particle Image Reconstructionstructural biologyVirus Capsid

Identifiers

PMID29708495
PMCPMC5927769

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.