Evidence map›Paper›PMID 26266555›Full record

ArticleACS nano2015

Monitoring Assembly of Virus Capsids with Nanofluidic Devices.

Zachary D Harms, Lisa Selzer, Adam Zlotnick, Stephen C Jacobson

Abstract read
In one paragraph

Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Biosensing With Nanofluidics.Exploration (Beijing, China) · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Integrated In-Plane Nanofluidic Devices for Resistive-Pulse Sensing.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Dynamics of Viruslike Capsid Assembly and Disassembly.Journal of the American Chemical Society · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Hepatitis B Core Protein Capsids.Sub-cellular biochemistry · 2021
    Review
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Zachary D HarmsDepartment of Chemistry and ‡Department of Molecular and Cellular Biochemistry, Indiana University , Bloomington, Indiana 47405, United States.
Lisa SelzerDepartment of Chemistry and ‡Department of Molecular and Cellular Biochemistry, Indiana University , Bloomington, Indiana 47405, United States.
Adam ZlotnickDepartment of Chemistry and ‡Department of Molecular and Cellular Biochemistry, Indiana University , Bloomington, Indiana 47405, United States.
Stephen C JacobsonDepartment of Chemistry and ‡Department of Molecular and Cellular Biochemistry, Indiana University , Bloomington, Indiana 47405, United States.
Indiana University Bloomington · US

Funding

Nanofluidic Devices for Studying Assembly of Single Virus ParticlesR01GM100071 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI JACOBSON, STEPHEN C · 2012 to 2015
$1.2M
The Biophysics of Virus Capsid AssemblyR56AI077688 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2014 to 2014
$347k
NIAID NIH HHS R56 AI077688NIGMS NIH HHS R01 GM100071
6 · The paper itself

Abstract

Virus assembly is a coordinated process in which typically hundreds of subunits react to form complex, symmetric particles. We use resistive-pulse sensing to characterize the assembly of hepatitis B virus core protein dimers into T = 3 and T = 4 icosahedral capsids. This technique counts and sizes intermediates and capsids in real time, with single-particle sensitivity, and at biologically relevant concentrations. Other methods are not able to produce comparable real-time, single-particle observations of assembly reactions below, near, and above the pseudocritical dimer concentration, at which the dimer and capsid concentrations are approximately equal. Assembly reactions across a range of dimer concentrations reveal three distinct patterns. At dimer concentrations as low as 50 nM, well below the pseudocritical dimer concentration of 0.5 μM, we observe a switch in the ratio of T = 3 to T = 4 capsids, which increases with decreasing dimer concentration. Far above the pseudocritical dimer concentration, kinetically trapped, incomplete T = 4 particles assemble rapidly, then slowly anneal into T = 4 capsids. At all dimer concentrations tested, T = 3 capsids form more rapidly than T = 4 capsids, suggesting distinct pathways for the two forms.

Indexed as

Virus AssemblyCapsidCapsid ProteinsHepatitis B virusKineticsProtein MultimerizationVirionCapsid Proteinshepatitis B virusin-plane nanochannelnanofluidicsresistive-pulse sensingself-assemblysingle-particle counting

Identifiers

PMID26266555
PMCPMC4753561
OpenAlexW2470584193

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.