Evidence map›Paper›PMID 32371601›Full record

ArticlemBio2020

Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein.

Claire M Metrick, Andrea L Koenigsberg, Ekaterina E Heldwein

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. An interchangeable prion-like domain is required for Ty1 retrotransposition.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
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 at 1 institution in 1 country.

Claire M MetrickDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, USA.ORCID 0000-0001-8660-5665
Andrea L KoenigsbergDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, USA.
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts, USA katya.heldwein@tufts.edu.ORCID 0000-0003-3113-6958
Tufts University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
MOLECULAR ANALYSIS OF MICROBIAL PATHOGENST32AI007422 · NIAID · TUFTS UNIVERSITY BOSTON · PI Ralph R. Isberg · 1992 to 2026
$5.7M
Structural mechanism of membrane remodeling during herpesvirus nuclear egressR01GM111795 · NIGMS · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2014 to 2017
$1.3M
Structural and biochemical insights into multiple functions of HSV-1 UL21 in viral life cycleF31GM115121 · NIGMS · TUFTS UNIVERSITY BOSTON · PI METRICK, CLAIRE · 2015 to 2016
$78k
Howard Hughes Medical Institute 55108533NIAID NIH HHS T32 AI007422NIGMS NIH HHS F31 GM115121NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM111795
6 · The paper itself

Abstract

A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we do not yet understand their individual functions or how the tegument is assembled and organized. UL11, the smallest tegument protein, is important for several distinct processes in replication, including efficient virion morphogenesis and cell-cell spread. However, the mechanistic understanding of its role in these and other processes is limited in part by the scant knowledge of its biochemical and structural properties. Here, we report that UL11 from herpes simplex virus 1 (HSV-1) is an intrinsically disordered, conformationally dynamic protein that undergoes liquid-liquid phase separation (LLPS)

Indexed as

CrystallographyHerpesvirus 1, HumanProtein BindingRNA-Binding ProteinsViral Structural ProteinsRNA-Binding ProteinsUL11 protein, herpesviridaeViral Structural Proteinsbiomolecular condensateconformational flexibilityherpesvirusintrinsically disordered protein (IDP)liquid-liquid phase separation (LLPS)RNA-binding proteinsmall‐angle X‐ray scattering (SAXS)structural modeltegumentviral assemblyviral protein

Identifiers

PMID32371601
PMCPMC7403781
OpenAlexW3023625205

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.