Evidence map›Paper›PMID 20371334›Full record

ArticleBiophysical journal2010

Balanced electrostatic and structural forces guide the large conformational change associated with maturation of T = 4 virus.

Tsutomu Matsui, Hiro Tsuruta, John E Johnson

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Unraveling the maturation pathway of a eukaryotic virus through cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015
    Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Confessions of an icosahedral virus crystallographer.Microscopy (Oxford, England) · 2013
    Review
  15. Go hybrid: EM, crystallography, and beyond.Current opinion in structural biology · 2012
    Review
  16. Article
  17. Review
  18. Virus maturation.Annual review of biophysics · 2012
    Review
  19. Subunits fold at position-dependent rates during maturation of a eukaryotic RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

3 authors.

Tsutomu MatsuiDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA.
Hiro Tsuruta
John E Johnson

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Studies of large and small-scale virus capsid dynamicsR01GM054076 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI JOHNSON, JOHN EMIL · 1995 to 2014
$6.2M
NCRR NIH HHS P41 RR001209NCRR NIH HHS RR001209NIGMS NIH HHS GM54076NIGMS NIH HHS R01 GM054076
6 · The paper itself

Abstract

Nudaurelia capensis omega virus has a well-characterized T = 4 capsid that undergoes a pH-dependent large conformational changes (LCC) and associated auto-catalytic cleavage of the subunit. We examined previously the particle size at different pH values and showed that maturation occurred at pH 5.5. We now characterized the LCC with time-resolved small-angle x-ray scattering and showed that there were three kinetic stages initiated with an incremental drop in pH: 1), a rapid (<10 ms) collapse to an incrementally smaller particle; 2), a continuous size reduction over the next 5 s; and 3), a smaller final transition occurring in 2-3 min. Equilibrium measurements similar to those reported previously, but now more precise, showed that the particle dimension between pH 5.5 and 5 requires the autocatalytic cleavage to achieve its final compact size. A balance of electrostatic and structural forces shapes the energy landscape of the LCC with the latter requiring annealing of portions of the subunit. Equilibrium experiments showed that many intermediate states could be populated with a homogeneous ensemble of particles by carefully controlling the pH. A titration curve for the LCC was generated that showed that the virtual pK(a) (i.e., the composite of all titratable residues that contribute to the LCC) is 5.8.

Indexed as

BiophysicsCapsidCapsid ProteinsHydrogen-Ion ConcentrationKineticsMolecular ConformationMutationNormal DistributionProtein ConformationScattering, RadiationSoftwareStatic ElectricityTime FactorsVirusesX-RaysCapsid Proteinscoat protein, Nudaurelia capensis omega virus

Identifiers

PMID20371334
PMCPMC2849064

What OpenQuestion holds

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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.