Evidence map›Paper›PMID 28057257›Full record

ReviewAdvances in virus research2017

Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.

J M Bigalke, E E Heldwein

Abstract readReview
In one paragraph

Review in Advances in virus research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
29.9field-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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Research progress on the mechanism of exosome-mediated virus infection.Frontiers in cellular and infection microbiology · 2024
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. HSV-1 Cytoplasmic Envelopment and Egress.International journal of molecular sciences · 2020
    Review
  16. Review
  17. Article
  18. Article
  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

2 authors at 1 institution in 1 country.

J M BigalkeTufts University School of Medicine, Boston, MA, United States.
E E HeldweinTufts University School of Medicine, Boston, MA, United States. Electronic address: katya.heldwein@tufts.edu.
Tufts University · US

Funding

Structural mechanism of membrane remodeling during herpesvirus nuclear egressR01GM111795 · NIGMS · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2014 to 2017
$1.3M
Structural mechanism of herpesvirus nuclear egressR21AI097573 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2012 to 2013
$441k
NIAID NIH HHS R21 AI097573NIGMS NIH HHS R01 GM111795
6 · The paper itself

Abstract

Herpesviruses are unusual among enveloped viruses because they bud twice yet acquire a single envelope. Furthermore, unlike other DNA viruses that replicate in the nucleus, herpesviruses do not exit it by passing through the nuclear pores or by rupturing the nuclear envelope. Instead, herpesviruses have a complex mechanism of nuclear escape whereby nascent capsids bud at the inner nuclear membrane to form perinuclear virions that subsequently fuse with the outer nuclear membrane, releasing capsids into the cytosol. This makes them some of the very few known viruses that bud into the nuclear envelope. The envelope acquired during nuclear budding does not end up in the mature viral particle but instead allows the capsid to translocate from the nucleus into the cytosol. The viral nuclear egress complex (NEC) is a critical player in the nuclear egress, yet its function and mechanism have remained enigmatic. Recent studies have demonstrated that the NEC buds membranes without the help of other proteins by forming a honeycomb coat, which established the NEC as the first virally encoded budding machine that operates at the nuclear, as opposed to cytoplasmic, membrane. This review discusses our current understanding of the NEC budding mechanism, with the emphasis on studies that illuminated the structure of the NEC coat and its role in capsid budding during herpesvirus nuclear escape.

Indexed as

Virus ReleaseAnimalsCapsidCell NucleusHerpesviridaeHerpesviridae InfectionsHumansNuclear EnvelopeViral ProteinsViral ProteinsBuddingCoatDeenvelopmentEnvelopmentHerpesvirusesHexagonalHoneycombLatticeNECNuclear egressScissionStructureUL31UL34

Identifiers

PMID28057257
PMCPMC5367388
OpenAlexW2510256757

What OpenQuestion holds

Textmetadata
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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.