Evidence map›Paper›PMID 15175653›Full record

ArticleThe EMBO journal2004

A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing.

Olga V Makarova, Evgeny M Makarov, Henning Urlaub, Cindy L Will, Marc Gentzel, Matthias Wilm, Reinhard Lührmann

Abstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

106 citing papers in PubMed.

  1. Microbiology (Reading, England) · 2026
    Review
  2. Article
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  15. Article
  16. Article
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  18. Article
  19. Article
  20. Structural Insights into Nuclear pre-mRNA Splicing in Higher Eukaryotes.Cold Spring Harbor perspectives in biology · 2019
    Review

46 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

7 authors.

Olga V MakarovaDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Evgeny M Makarov
Henning Urlaub
Cindy L Will
Marc Gentzel
Matthias Wilm
Reinhard Lührmann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During catalytic activation of the spliceosome, snRNP remodeling events occur, leading to the formation of a 35S U5 snRNP that contains a large group of proteins, including Prp19 and CDC5, not found in 20S U5 snRNPs. To investigate the function of 35S U5 proteins, we immunoaffinity purified human spliceosomes that had not yet undergone catalytic activation (designated BDeltaU1), which contained U2, U4, U5, and U6, but lacked U1 snRNA. Comparison of the protein compositions of BDeltaU1 and activated B* spliceosomes revealed that, whereas U4/U6 snRNP proteins are stably associated with BDeltaU1 spliceosomes, 35S U5-associated proteins (which are present in B*) are largely absent, suggesting that they are dispensable for complex B formation. Indeed, immunodepletion/complementation experiments demonstrated that a subset of 35S U5 proteins including Prp19, which form a stable heteromeric complex, are required prior to catalytic step 1 of splicing, but not for stable integration of U4/U6.U5 tri-snRNPs. Thus, comparison of the proteomes of spliceosomal complexes at defined stages can provide information as to which proteins function as a group at a particular step of splicing.

Indexed as

Carrier ProteinsCatalysisDNA Repair EnzymesHeLa CellsHumansNuclear ProteinsRNA SplicingRNA Splicing FactorsCarrier ProteinsDNA Repair EnzymesNuclear ProteinsPRPF19 protein, humanRNA Splicing Factors

Identifiers

PMID15175653
PMCPMC423283

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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.