Evidence map›Paper›PMID 9023105›Full record

ArticleNucleic acids research1997

Xp54, the Xenopus homologue of human RNA helicase p54, is an integral component of stored mRNP particles in oocytes.

M Ladomery, E Wade, J Sommerville

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

53 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
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  4. P-body-like condensates in the germline.Seminars in cell & developmental biology · 2024
    Review
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  19. New insights into the regulation of RNP granule assembly in oocytes.International review of cell and molecular biology · 2012
    Review
  20. Article
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

3 authors at 1 institution in 1 country.

M LadomerySchool of Biological and Medical Sciences, Bute Buildings, University of St Andrews, St Andrews, Fife KY16 9TS, UK.
E Wade
J Sommerville
University of St Andrews · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

In investigating the composition of stored (maternal) mRNP particles in Xenopus oocytes, attention has focussed primarily on the phosphoproteins pp60/56, which are Y-box proteins involved in a general packaging of mRNA. We now identify a third, abundant, integral component of stored mRNP particles, Xp54, which belongs to the family of DEAD-box RNA helicases. Xp54 was first detected by its ability to photocrosslink ATP. Subsequent sequence analysis identifies Xp54 as a member of a helicase subfamily which includes: human p54, encoded at a chromosomal breakpoint in the B-cell lymphoma cell line, RC-K8; Drosophila ME31B, encoded by a maternally-expressed gene, and Saccharomyces pombe Ste13, cloned by complementation of the sterility mutant ste13. Expression studies reveal that the gene encoding Xp54 is transcribed maximally at early oogenesis: no transcripts are detected in adult tissues, other than ovary. Using a monospecific antibody raised against native Xp54, its presence in mRNP particles is confirmed by immunoblotting fractions bound to oligo(dT)-cellulose and separated by rate sedimentation and buoyant density. On isolating Xp54 from mRNP particles, it is shown to possess an ATP-dependent RNA helicase activity. Possible functions of Xp54 are discussed in relation to the assembly and utilization of mRNP particles.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCells, CulturedCentrifugation, Density GradientCloning, MolecularDNA, ComplementaryEmbryo, NonmammalianFemaleHumansMolecular Sequence DataOocytesPolymerase Chain ReactionProtein ConformationRecombinant Fusion ProteinsRibonucleoproteinsDNA, Complementarymessenger ribonucleoproteinRecombinant Fusion ProteinsRibonucleoproteinsRNA HelicasesRNA, MessengerRNA Nucleotidyltransferases

Identifiers

PMID9023105
PMCPMC146530
OpenAlexW2098228905

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.