Evidence map›Paper›PMID 29622628›Full record

ArticleScience (New York, N.Y.)2018

Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.

Xinghong Dai, Z Hong Zhou

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 1 pooled it
18.2field-weighted citation impact, top 1% 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

114 citing papers in PubMed, 1 synthesis or guideline pooled it, 191 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Nociceptor neurons shape antiviral immunity.Journal of neuroinflammation · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Structure and Antigenicity of Kaposi's Sarcoma-Associated Herpesvirus Glycoprotein B.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  18. Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Xinghong DaiDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.ORCID 0000-0002-4102-3175
Z Hong ZhouDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA. hong.zhou@ucla.edu.ORCID 0000-0002-8373-4717
California NanoSystems Institute · US

Funding

Genome Structure, Transcription and Packaging of dsRNA VirusesR01AI094386 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Z Hong ZHOU · 2012 to 2026
$6.0M
High-Resolution CryoEM Reconstruction of Large ComplexesR01GM071940 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2006 to 2025
$5.0M
In situ atomic structures of the Kaposi's sarcoma-associated herpesvirus portal-terminase complex and glycoproteinsR01DE025567 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WU, TING-TING, ZHOU, Z HONG · 2016 to 2024
$4.0M
West/Midwest Consortium for High-Resolution Cryo Electron MicroscopyU24GM116792 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AGBANDJE-MCKENNA, MAVIS, DOKLAND, TERJE · 2016 to 2020
$3.0M
Therapeutic Strategies for Patients With BRAF Mutant Colorectal CancerR01CA187238 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI HONG, DAVID S., KOPETZ, SCOTT · 2014 to 2018
$1.7M
Direct Detection Device for atomic resolution cryoEM of macromolecular complexesS10OD018111 · OD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHOU, Z HONG · 2014 to 2014
$598k
NCI NIH HHS R01 CA187238NIAID NIH HHS R01 AI094386NIDCR NIH HHS R01 DE025567NIGMS NIH HHS R01 GM071940NIGMS NIH HHS U24 GM116792NIH HHS S10 OD018111
6 · The paper itself

Abstract

Herpes simplex viruses (HSVs) rely on capsid-associated tegument complex (CATC) for long-range axonal transport of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC, each containing a pUL17 monomer supporting the coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear capsid egress and axonal capsid transport. Notwithstanding newly discovered fold conservation between triplex proteins and bacteriophage λ protein gpD and the previously recognized bacteriophage HK97 gp5-like fold in VP5, HSV-1 capsid proteins exhibit extraordinary diversity in forms of domain insertion and conformational polymorphism, not only for interactions with tegument proteins but also for encapsulation of large genomes.

Indexed as

AnimalsCapsidCapsid ProteinsChlorocebus aethiopsCryoelectron MicroscopyGlycoproteinsHerpesvirus 1, HumanHumansProtein Conformation, alpha-HelicalVero CellsCapsid ProteinsGlycoproteinsgpD protein, lambda phage

Identifiers

PMID29622628
PMCPMC5959011
OpenAlexW2796156307

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.