Evidence map›Paper›PMID 21536652›Full record

ArticleMolecular and cellular biology2011

Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis method.

Dmitry E Agafonov, Jochen Deckert, Elmar Wolf, Peter Odenwälder, Sergey Bessonov, Cindy L Will, Henning Urlaub, Reinhard Lührmann

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

124 citing papers in PubMed, 230 citations in OpenAlex.

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  8. C-terminal frameshift variants in GPKOW are associated with a multisystemic X-linked disorder.Genetics in medicine : official journal of the American College of Medical Genetics · 2025
    Article
  9. Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly.Nature structural & molecular biology · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Structure of the human 20S U5 snRNP.Nature structural & molecular biology · 2024
    Article
  18. Article
  19. Article
  20. Dysfunction of Gpl1-Gih35-Wdr83 Complex inInternational journal of molecular sciences · 2024
    Article

64 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

8 authors at 1 institution in 1 country.

Dmitry E AgafonovDept. of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Jochen Deckert
Elmar Wolf
Peter Odenwälder
Sergey Bessonov
Cindy L Will
Henning Urlaub
Reinhard Lührmann
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

More than 200 proteins associate with human spliceosomes, but little is known about their relative abundances in a given spliceosomal complex. Here we describe a novel two-dimensional (2D) electrophoresis method that allows separation of high-molecular-mass proteins without in-gel precipitation and thus without loss of protein. Using this system coupled with mass spectrometry, we identified 171 proteins altogether on 2D maps of stage-specific spliceosomal complexes. By staining with a fluorescent dye with a wide linear intensity range, we could quantitate and categorize proteins as present in high, moderate, or low abundance. Affinity-purified human B, B(act), and C complexes contained 69, 63, and 72 highly/moderately abundant proteins, respectively. The recruitment and release of spliceosomal proteins were followed based on their abundances in A, B, B(act), and C spliceosomal complexes. Staining with a phospho-specific dye revealed that approximately one-third of the proteins detected in human spliceosomal complexes by 2D gel analyses are phosphorylated. The 2D gel electrophoresis system described here allows for the first time an objective view of the relative abundances of proteins present in a particular spliceosomal complex and also sheds additional light on the spliceosome's compositional dynamics and the phosphorylation status of spliceosomal proteins at specific stages of splicing.

Indexed as

Electrophoresis, Gel, Two-DimensionalHeLa CellsHumansProteinsProteomicsSpliceosomesProteins

Identifiers

PMID21536652
PMCPMC3133382
OpenAlexW2168915479

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.