Evidence map›Paper›PMID 9774689›Full record

ArticleMolecular and cellular biology1998

The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein.

T Achsel, K Ahrens, H Brahms, S Teigelkamp, R Lührmann

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In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

73 citing papers in PubMed, 150 citations in OpenAlex.

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  12. RNAs as Regulators of Cellular Matchmaking.Frontiers in molecular biosciences · 2021
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13 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

5 authors at 1 institution in 1 country.

T AchselInstitut für Molekularbiologie und Tumorforschung, Philipps-Universität Marburg, 35037 Marburg, Germany.
K Ahrens
H Brahms
S Teigelkamp
R Lührmann
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human small nuclear ribonucleoprotein (snRNP) U5 is biochemically the most complex of the snRNP particles, containing not only the Sm core proteins but also 10 particle-specific proteins. Several of these proteins have sequence motifs which suggest that they participate in conformational changes of RNA and protein. Together, the specific proteins comprise 85% of the mass of the U5 snRNP particle. Therefore, protein-protein interactions should be highly important for both the architecture and the function of this particle. We investigated protein-protein interactions using both native and recombinant U5-specific proteins. Native U5 proteins were obtained by dissociation of U5 snRNP particles with the chaotropic salt sodium thiocyanate. A stable, RNA-free complex containing the 116-kDa EF-2 homologue (116kD), the 200kD RNA unwindase, the 220kD protein, which is the orthologue of the yeast Prp8p protein, and the U5-40kD protein was detected by sedimentation analysis of the dissociated proteins. By cDNA cloning, we show that the 40kD protein is a novel WD-40 repeat protein and is thus likely to mediate regulated protein-protein interactions. Additional biochemical analyses demonstrated that the 220kD protein binds simultaneously to the 40- and the 116kD proteins and probably also to the 200kD protein. Since the 220kD protein is also known to contact both the pre-mRNA and the U5 snRNA, it is in a position to relay the functional state of the spliceosome to the other proteins in the complex and thus modulate their activity.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBlotting, WesternCarrier ProteinsCloning, MolecularFungal ProteinsHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationPeptide Elongation Factor 2Peptide Elongation FactorsProtein BindingRecombinant ProteinsRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearCarrier ProteinsFungal ProteinsPeptide Elongation Factor 2Peptide Elongation FactorsPRP8 protein, S cerevisiaePRPF8 protein, humanRecombinant ProteinsRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA-Binding ProteinsSaccharomyces cerevisiae Proteinssodium thiocyanateThiocyanates

Identifiers

PMID9774689
PMCPMC109259
OpenAlexW2158118253

What OpenQuestion holds

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Registered trials

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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.