Evidence map›Paper›PMID 11175897›Full record

ReviewNature structural biology2001

A new twist on RNA helicases: DExH/D box proteins as RNPases.

B Schwer

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature structural biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Article
  3. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

1 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

1 author at 1 institution in 1 country.

B SchwerDepartment of Microbiology & Immunology, Weill Medical College of Cornell University, New York, New York 10021, USA. bschwer@mail.med.cornell.edu
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DExH/D box proteins are required for the major transactions of RNA, including mRNA synthesis, pre-mRNA splicing, ribosome biogenesis, translation and RNA decay. In the popular imagination, DExH/D box proteins have become synonymous with 'RNA helicases', which are enzymes that unwind duplex RNAs in concert with the hydrolysis of nucleoside triphosphates (NTPs). But all DExH/D box proteins may not be RNA helicases and the energy of NTP hydrolysis by DExH/D box proteins may be harnessed for other purposes. Cellular RNAs are associated with proteins, often in large ribonucleoprotein (RNP) complexes. This review focuses on recent progress suggesting a role for DExH/D box proteins as 'RNPases' that use chemical energy to remodel the interactions of RNA and proteins.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAnimalsBase SequenceRibonucleoproteinsRNARNA-Binding ProteinsRNA HelicasesRNA SplicingSpliceosomesAdenosine TriphosphatasesRibonucleoproteinsRNARNA-Binding ProteinsRNA Helicases

Identifiers

PMID11175897
OpenAlexW1576289065

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.