Evidence map›Paper›PMID 11032824›Full record

ArticleThe EMBO journal2000

A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.

S Nanduri, F Rahman, B R Williams, J Qin

Abstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
–field-weighted citation impact
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

81 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. SARS-CoV-2 nsp14 induces the mCommunications biology · 2025
    Article
  5. Article
  6. Article
  7. RNA recognition by PKR during DNA virus infection.Journal of medical virology · 2024
    Review
  8. Review
  9. Review
  10. dsRNA-induced condensation of antiviral proteins modulates PKR activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Regulation of PKR activation and apoptosis during oxidative stress by TRBP phosphorylation.The international journal of biochemistry & cell biology · 2021
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Inhibition of PKR by Viruses.Frontiers in microbiology · 2021
    Review
  19. Article
  20. Review

21 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

4 authors.

S NanduriStructural Biology Program and Department of Cancer Biology, Lerner Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA.
F Rahman
B R Williams
J Qin

Funding

STRUCTURES AND MECHANISMS OF ANK REPEAT BEARING PROTEINSR01HL058758 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI JUN QIN · 1999 to 2026
$9.0M
REGULATION OF INTERFERON-INDUCED DSRNA-ACTIVATED KINASER01AI034039 · NIAID · MONASH UNIVERSITY · PI WILLIAMS, BRYAN R. G. · 1993 to 2008
$2.5M
INTERFERON-REGULATED DS RNA-ACTIVATED KINASE, PKRR21AI034039 · NIAID · CLEVELAND CLINIC FOUNDATION · PI WILLIAMS, BRYAN R. G. · 1998 to 1998
–
NHLBI NIH HHS HL58758NHLBI NIH HHS R01 HL058758NIAID NIH HHS AI34039NIAID NIH HHS R01 AI034039
6 · The paper itself

Abstract

A key step in the activation of interferon-inducible antiviral kinase PKR involves differential binding of viral double-stranded RNA (dsRNA) to its two structurally similar N-terminal dsRNA binding motifs, dsRBM1 and dsRBM2. We show here, using NMR spectroscopy, that dsRBM1 with higher RNA binding activity exhibits significant motional flexibility on a millisecond timescale as compared with dsRBM2 with lower RNA binding activity. We further show that dsRBM2, but not dsRBM1, specifically interacts with the C-terminal kinase domain. These results suggest a dynamically tuned dsRNA binding mechanism for PKR activation, where motionally more flexible dsRBM1 anchors to dsRNA, thereby inducing a cooperative RNA binding for dsRBM2 to expose the kinase domain.

Indexed as

Amino Acid SequenceAnimalseIF-2 KinaseEnzyme ActivationMagnetic Resonance SpectroscopyModels, BiologicalModels, MolecularMolecular Sequence DataMotionNitrogen IsotopesPliabilityProtein Structure, SecondaryProtein Structure, TertiaryRNA-Binding ProteinsRNA, Double-StrandedRNA, ViraleIF-2 KinaseNitrogen IsotopesRNA-Binding ProteinsRNA, Double-StrandedRNA, Viral

Identifiers

PMID11032824
PMCPMC314023

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.