Evidence map›Paper›PMID 17531807›Full record

ArticleMolecular cell2007

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids.

Benes L Trus, William W Newcomb, Naiqian Cheng, Giovanni Cardone, Lyuben Marekov, Fred L Homa, Jay C Brown, Alasdair C Steven

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

115 citing papers in PubMed, 164 citations in OpenAlex.

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  15. Stunning symmetries involved in the self-assembly of the HSV-1 capsid.The journal of the Korean Physical Society · 2021
    Review
  16. Article
  17. Article
  18. HSV-1 Cytoplasmic Envelopment and Egress.International journal of molecular sciences · 2020
    Review
  19. Article
  20. Article

55 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

8 authors at 3 institutions in 1 country.

Benes L TrusLaboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
William W Newcomb
Naiqian Cheng
Giovanni Cardone
Lyuben Marekov
Fred L Homa
Jay C Brown
Alasdair C Steven
National Institutes of Health · USUniversity of Virginia Health System · USUniversity of Pittsburgh · US

Funding

STRUCTURAL BIOLOGY OF VIRUS ASSEMBLYZ01AR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1987 to 2008
$3.0M
ASSEMBLY OF THE HERPES SIMPLEX VIRUS CAPSIDR01AI041644 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BROWN, JAY CLARK · 1997 to 2012
$2.8M
MOLECULAR GRAPHICS, COMPUTER MODELING, AND SEQUENCE ANALYSISZ01CT000090 · CIT · COMPUTER RESEARCH AND TECHNOLOGY · PI TRUS, BENES L · 1985 to 2008
$2.1M
Herpes Simplex Virus Capsid Assembly and DNA PackagingR01AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2006 to 2010
$1.6M
Herpes Simples Virus Capsid Assembly and DNA PackagingR56AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2011 to 2011
$379k
Assembly of the Herpes Simplex Virus CapsidR56AI041644 · NIAID · UNIVERSITY OF VIRGINIA · PI BROWN, JAY C. · 2007 to 2007
$354k
Intramural NIH HHS Z01 AR027002Intramural NIH HHS Z01 CT000090Intramural NIH HHS Z99 AR999999NIAID NIH HHS AI060836NIAID NIH HHS AI41644-10NIAID NIH HHS R01 AI041644NIAID NIH HHS R01 AI060836NIAID NIH HHS R56 AI041644NIAID NIH HHS R56 AI060836
6 · The paper itself

Abstract

UL25 and UL17 are two essential minor capsid proteins of HSV-1, implicated in DNA packaging and capsid maturation. We used cryo-electron microscopy to examine their binding to capsids, whose architecture observes T = 16 icosahedral geometry. C-capsids (mature DNA-filled capsids) have an elongated two-domain molecule present at a unique, vertex-adjacent site that is not seen at other quasiequivalent sites or on unfilled capsids. Using SDS-PAGE and mass spectrometry to analyze wild-type capsids, UL25 null capsids, and denaturant-extracted capsids, we conclude that (1) the C-capsid-specific component is a heterodimer of UL25 and UL17, and (2) capsids have additional populations of UL25 and UL17 that are invisible in reconstructions because of sparsity and/or disorder. We infer that binding of the ordered population reflects structural changes induced on the outer surface as pressure builds up inside the capsid during DNA packaging. Its binding may signal that the C-capsid is ready to exit the nucleus.

Indexed as

Allosteric RegulationCapsidCapsid ProteinsCell NucleusCryoelectron MicroscopyDimerizationHerpesvirus 1, HumanImage Processing, Computer-AssistedMass SpectrometryProtein BindingProtein TransportViral ProteinsCapsid ProteinsDNA cleavage and packaging proteins, HerpesvirusViral Proteins

Identifiers

PMID17531807
PMCPMC1945812
OpenAlexW1999985873

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.