Evidence map›Paper›PMID 22199231›Full record

ArticleMolecular & cellular proteomics : MCP2012

Proteomic analysis of mitotic RNA polymerase II reveals novel interactors and association with proteins dysfunctional in disease.

André Möller, Sheila Q Xie, Fabian Hosp, Benjamin Lang, Hemali P Phatnani, Sonya James, Francisco Ramirez, Gayle B Collin, Jürgen K Naggert, M Madan Babu and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Maintaining Transcriptional Specificity Through Mitosis.Annual review of genomics and human genetics · 2022
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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

13 authors at 6 institutions in 3 countries.

André MöllerMRC Clinical Sciences Centre, Imperial College School of Medicine, Hammersmith Hospital Campus, London W12 0NN, United Kingdom. andre.moeller.rnapii@gmail.com
Sheila Q Xie
Fabian Hosp
Benjamin Lang
Hemali P Phatnani
Sonya James
Francisco Ramirez
Gayle B Collin
Jürgen K Naggert
M Madan Babu
Arno L Greenleaf
Matthias Selbach
Ana Pombo
Hammersmith Hospital · GBDuke University · USJackson Laboratory · USMax Delbrück Center · DEMRC Laboratory of Molecular Biology · GBSouth West Thames Institute for Renal Research · GB

Funding

TRANSCRIPTASE KINASES FROM YEAST AND DROSOPHILAR01GM040505 · NIGMS · DUKE UNIVERSITY · PI GREENLEAF, ARNO L. · 1988 to 2014
$5.1M
MOLECULAR GENETIC CHARACTERIZATION OF ALSTROM SYNDROMER01HD036878 · NICHD · JACKSON LABORATORY · PI NAGGERT, JUERGEN K. · 1998 to 2011
$4.2M
Medical Research Council MC_U105185859Medical Research Council MC_U120061476NICHD NIH HHS HD036878NICHD NIH HHS R01 HD036878NIGMS NIH HHS R01 GM040505
6 · The paper itself

Abstract

RNA polymerase II (RNAPII) transcribes protein-coding genes in eukaryotes and interacts with factors involved in chromatin remodeling, transcriptional activation, elongation, and RNA processing. Here, we present the isolation of native RNAPII complexes using mild extraction conditions and immunoaffinity purification. RNAPII complexes were extracted from mitotic cells, where they exist dissociated from chromatin. The proteomic content of native complexes in total and size-fractionated extracts was determined using highly sensitive LC-MS/MS. Protein associations with RNAPII were validated by high-resolution immunolocalization experiments in both mitotic cells and in interphase nuclei. Functional assays of transcriptional activity were performed after siRNA-mediated knockdown. We identify >400 RNAPII associated proteins in mitosis, among these previously uncharacterized proteins for which we show roles in transcriptional elongation. We also identify, as novel functional RNAPII interactors, two proteins involved in human disease, ALMS1 and TFG, emphasizing the importance of gene regulation for normal development and physiology.

Indexed as

MitosisChromatography, GelDiseaseGene Knockdown TechniquesHeLa CellsHumansImmunoprecipitationInterphaseNuclear ProteinsProtein Interaction MappingProtein SubunitsProteomeProteomicsRibonucleoproteinsRibosomal ProteinsRNA InterferenceNuclear ProteinsProtein SubunitsProteomeRibonucleoproteinsRibosomal ProteinsRNA Polymerase II

Identifiers

PMID22199231
PMCPMC3433901
OpenAlexW2123008529

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.