Evidence map›Paper›PMID 15731220›Full record

ArticleJournal of virology2005

Functional interaction of heterogeneous nuclear ribonucleoprotein C with poliovirus RNA synthesis initiation complexes.

Jo Ellen Brunner, Joseph H C Nguyen, Holger H Roehl, Tri V Ho, Kristine M Swiderek, Bert L Semler

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Seneca Valley Virus 3CFrontiers in microbiology · 2022
    Article
  14. A single mutation in theEmerging microbes & infections · 2021
    Article
  15. Seneca Valley virus 3CVirulence · 2021
    Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Review

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

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

6 authors at 2 institutions in 1 country.

Jo Ellen BrunnerDepartment of Microbiology and Molecular Genetics, College of Medicine, University of California, Med. Sci. B240, Irvine, CA 92697, USA.
Joseph H C Nguyen
Holger H Roehl
Tri V Ho
Kristine M Swiderek
Bert L Semler
University of California, Irvine · USBeckman Research Institute

Funding

Transgenic Mouse FacilityP30CA033572 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI STANLEY R. HAMILTON · 1985 to 2026
$86.3M
POLIOVIRUS GENE FUNCTION AND REGULATIONR01AI022693 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI SEMLER, BERT L · 1985 to 2015
$4.6M
SYNTHESIS AND STRUCTURE OF BIOLOGICAL MACROMOLECULEST32GM007311 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI OSBORNE, TIMOTHY F · 1985 to 2004
$1.6M
NCI NIH HHS CA33572NCI NIH HHS P30 CA033572NIAID NIH HHS AI 22693NIAID NIH HHS R01 AI022693NIGMS NIH HHS GM07311NIGMS NIH HHS T32 GM007311
6 · The paper itself

Abstract

We had previously demonstrated that a cellular protein specifically interacts with the 3' end of poliovirus negative-strand RNA. We now report the identity of this protein as heterogeneous nuclear ribonucleoprotein (hnRNP) C1/C2. Formation of an RNP complex with poliovirus RNA was severely impaired by substitution of a lysine, highly conserved among vertebrates, with glutamine in the RNA recognition motif (RRM) of recombinant hnRNP C1, suggesting that the binding is mediated by the RRM in the protein. We have also shown that in a glutathione S-transferase (GST) pull-down assay, GST/hnRNP C1 binds to poliovirus polypeptide 3CD, a precursor to the viral RNA-dependent RNA polymerase, 3D(pol), as well as to P2 and P3, precursors to the nonstructural proteins. Truncation of the auxiliary domain in hnRNP C1 (C1DeltaC) diminished these protein-protein interactions. When GST/hnRNP C1DeltaC was added to in vitro replication reactions, a significant reduction in RNA synthesis was observed in contrast to reactions supplemented with wild-type fusion protein. Indirect functional depletion of hnRNP C from in vitro replication reactions, using poliovirus negative-strand cloverleaf RNA, led to a decrease in RNA synthesis. The addition of GST/hnRNP C1 to the reactions rescued RNA synthesis to near mock-depleted levels. Furthermore, we demonstrated that poliovirus positive-strand and negative-strand RNA present in cytoplasmic extracts prepared from infected HeLa cells coimmunoprecipitated with hnRNP C1/C2. Our findings suggest that hnRNP C1 has a role in positive-strand RNA synthesis in poliovirus-infected cells, possibly at the level of initiation.

Indexed as

3C Viral ProteasesAmino Acid SubstitutionCysteine EndopeptidasesHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group CHumansPoliovirusProtein BindingRNA, ViralSequence DeletionViral Nonstructural ProteinsViral Proteins3C Viral ProteasesCysteine EndopeptidasesHeterogeneous-Nuclear Ribonucleoprotein Group CRNA, ViralViral Nonstructural ProteinsViral Proteins

Identifiers

PMID15731220
PMCPMC1075716
OpenAlexW2112147369

What OpenQuestion holds

Textmetadata
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.