Evidence map›Paper›PMID 36298770›Full record

ReviewViruses2022

Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.

Ravi K Lokareddy, Chun-Feng David Hou, Fenglin Li, Ruoyu Yang, Gino Cingolani

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Treatment ofViruses · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Structural basis for DNA recognition by a viral genome-packaging machine.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Nucleic Acid Packaging in Viruses.Sub-cellular biochemistry · 2024
    Review
  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

5 authors at 1 institution in 1 country.

Ravi K LokareddyDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0002-5357-1857
Chun-Feng David HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0002-1820-9588
Fenglin LiDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0001-7932-0071
Ruoyu YangDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Gino CingolaniDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Thomas Jefferson University · US

Funding

Mechanism of Viral Genome Delivery into CellsR35GM140733 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI CINGOLANI, GINO · 2021 to 2025
$2.8M
Multisubunit viral ATPases that couple ATP-hydrolysis to genome translocationR01GM100888 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2012 to 2020
$2.5M
NIGMS NIH HHS R35 GM140733NIH HHS R01 GM100888NIH HHS R35 GM140733
6 · The paper itself

Abstract

The genome packaging motor of bacteriophages and herpesviruses is built by two terminase subunits, known as large (TerL) and small (TerS), both essential for viral genome packaging. TerL structure, composition, and assembly to an empty capsid, as well as the mechanisms of ATP-dependent DNA packaging, have been studied in depth, shedding light on the chemo-mechanical coupling between ATP hydrolysis and DNA translocation. Instead, significantly less is known about the small terminase subunit, TerS, which is dispensable or even inhibitory in vitro, but essential in vivo. By taking advantage of the recent revolution in cryo-electron microscopy (cryo-EM) and building upon a wealth of crystallographic structures of phage TerSs, in this review, we take an inventory of known TerSs studied to date. Our analysis suggests that TerS evolved and diversified into a flexible molecular framework that can conserve biological function with minimal sequence and quaternary structure conservation to fit different packaging strategies and environmental conditions.

Indexed as

BacteriophagesVirus AssemblyAdenosine TriphosphateCryoelectron MicroscopyDNA PackagingDNA, ViralEndodeoxyribonucleasesViral ProteinsAdenosine TriphosphateDNA, ViralEndodeoxyribonucleasesterminaseViral Proteinsbacteriophagescryo-EMherpesvirusesterminase subunitsTerSviral genome packagingX-ray crystallography

Identifiers

PMID36298770
PMCPMC9611059
OpenAlexW4304788898

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.