Evidence map›Paper›PMID 8756671›Full record

ArticleMolecular and cellular biology1996

A DEAD-box-family protein is required for nucleocytoplasmic transport of yeast mRNA.

S Liang, M Hitomi, Y H Hu, Y Liu, A M Tartakoff

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.5field-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

56 citing papers in PubMed, 100 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  9. Article
  10. Article
  11. RNA helicases in RNA decay.Biochemical Society transactions · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Ribonucleoprotein complexes that control circadian clocks.International journal of molecular sciences · 2013
    Review
  19. Article
  20. Review
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.

S LiangInstitute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
M Hitomi
Y H Hu
Y Liu
A M Tartakoff
Case Western Reserve University · US

Funding

Translational Research in Cystic FibrosisP30DK027651 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI DRUMM, MITCHELL L · 1986 to 2014
$15.6M
MRNA EXPORT FROM THE NUCLEUS OF SACCHAROMYCES CEREVISIAER01GM046569 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI TARTAKOFF, ALAN MICHAEL · 1991 to 1993
–
NIDDK NIH HHS DK27651NIGMS NIH HHS GM46569
6 · The paper itself

Abstract

An enormous variety of primary and secondary mRNA structures are compatible with export from the nucleus to the cytoplasm. Therefore, there seems to be a mechanism for RNA export which is independent of sequence recognition. There nevertheless is likely to be some relatively uniform mechanism which allows transcripts to be packaged as ribonucleoprotein particles, to gain access to the periphery of the nucleus and ultimately to translocate across nuclear pores. To study these events, we and others have generated temperature-sensitive recessive mRNA transport (mtr) mutants of Saccharomyces cerevisiae which accumulate poly(A)+ RNA in the nucleus at 37 degrees C. Several of the corresponding genes have been cloned. Upon depletion of one of these proteins, Mtr4p, conspicuous amounts of nuclear poly(A)+ RNA accumulate in association with the nucleolus. Corresponding dense material is also seen by electron microscopy. MTR4 is essential for growth and encodes a novel nuclear protein with a size of approximately 120 kDa. Mtr4p shares characteristic motifs with DEAD-box RNA helicases and associates with RNA. It therefore may well affect RNA conformation. It shows extensive homology to a human predicted gene product and the yeast antiviral protein Ski2p. Critical residues of Mtr4p, including the mtr4-1 point mutation, have been identified. Mtr4p may serve as a chaperone which translocates or normalizes the structure of mRNAs in preparation for export.

Indexed as

Regulatory Sequences, Nucleic AcidRNA HelicasesSaccharomyces cerevisiae ProteinsAmino Acid SequenceBiological TransportCell NucleusCloning, MolecularCytoplasmDEAD-box RNA HelicasesHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular Sequence DataNuclear ProteinsNucleic Acid ConformationRibonucleoproteinsRNA-Binding ProteinsDEAD-box RNA HelicasesHeterogeneous-Nuclear RibonucleoproteinsMTR4 protein, S cerevisiaeNuclear ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA HelicasesRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID8756671
PMCPMC231514
OpenAlexW2164006415

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.