Evidence map›Paper›PMID 36202211›Full record

ArticleThe Journal of biological chemistry2022

Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation.

Christopher R Carlson, Armin N Adly, Maxine Bi, Conor J Howard, Adam Frost, Yifan Cheng, David O Morgan

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.6field-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

47 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Mapping SARS-CoV-2 Nucleocapsid Function with Nanobodies.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Christopher R CarlsonDepartment of Physiology, University of California, San Francisco, California, USA.
Armin N AdlyDepartment of Physiology, University of California, San Francisco, California, USA.
Maxine BiDepartment of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
Conor J HowardDepartment of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
Adam FrostDepartment of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
Yifan ChengDepartment of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
David O MorganDepartment of Physiology, University of California, San Francisco, California, USA. Electronic address: David.Morgan@ucsf.edu.
University of California, San Francisco · US

Funding

Regulatory Enzymes and Systems in Cell Cycle ControlR35GM118053 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVID Owen MORGAN · 2016 to 2026
$10.3M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM118053NIGMS NIH HHS T32 GM008284
6 · The paper itself

Abstract

The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35 to 40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined in vitro with short fragments of the viral genome, forms 15-nm particles similar to the vRNP structures observed within virions. These vRNPs depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine region weakens these interactions to generate less compact vRNPs. We propose that unmodified N protein binds structurally diverse regions in genomic RNA to form compact vRNPs within the nucleocapsid, while phosphorylation alters vRNP structure to support other N protein functions in viral transcription.

Indexed as

COVID-19SARS-CoV-2GenomicsHumansNucleocapsid ProteinsPhosphorylationRibonucleoproteinsRNA, ViralNucleocapsid ProteinsRibonucleoproteinsRNA, ViralN proteinnucleocapsidnucleosomephosphorylationplus-stranded RNA virusRNA binding proteinRNA virusSARS-CoV-2

Identifiers

PMID36202211
PMCPMC9529352
OpenAlexW4300717212

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.