Evidence map›Paper›PMID 11248041›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF.

K Kamada, J De Angelis, R G Roeder, S K Burley

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structural characterization of human general transcription factor TFIIF in solution.Protein science : a publication of the Protein Society · 2008
    Article
  13. Article
  14. Article
  15. NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  16. Article
  17. 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

4 authors at 2 institutions in 1 country.

K KamadaLaboratories of Molecular Biophysics and Biochemistry and Molecular Biology, and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
J De Angelis
R G Roeder
S K Burley
Howard Hughes Medical Institute · USRockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-A resolution. The alpha/beta structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3gamma (HNF-3gamma), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3gamma and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the beta subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

Indexed as

Saccharomyces cerevisiae ProteinsTranscription Factors, TFIIAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataPeptide MappingPhosphoprotein PhosphatasesProtein Phosphatase 2Protein Phosphatase 2CProtein Structure, TertiarySequence Homology, Amino AcidTranscription Factorscarboxy-terminal domain phosphatasePhosphoprotein PhosphatasesProtein Phosphatase 2Protein Phosphatase 2CPTC1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTranscription Factors, TFIItranscription factor TFIIEtranscription factor TFIIFZinc

Identifiers

PMID11248041
PMCPMC30616
OpenAlexW2058921861

What OpenQuestion holds

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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.