Evidence map›Paper›PMID 9153318›Full record

ArticleNucleic acids research1997

CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues.

M Bellorini, D K Lee, J C Dantonel, K Zemzoumi, R G Roeder, L Tora, R Mantovani

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 128 citations in OpenAlex.

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  12. Transcriptional regulation of the human neutral ceramidase gene.Archives of biochemistry and biophysics · 2011
    Article
  13. AP-1 binding transcriptionally regulates human neutral ceramidase.Archives of biochemistry and biophysics · 2011
    Article
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  15. Article
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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 at 1 institution in 1 country.

M BelloriniDipartimento di Genetica e Biologia dei Microrganismi, Università di Milano, Via Celoria 26, 20133 Milano, Italy.
D K Lee
J C Dantonel
K Zemzoumi
R G Roeder
L Tora
R Mantovani
University of Milan · IT

Funding

FUNCTIONAL STUDIES OF THE C-FOS ENHANCER BINDING PROTEINF32CA008648 · NCI · ROCKEFELLER UNIVERSITY · PI ROWLAND-GAGNE, ELIZABETH A · 1988 to 1990
–
NCI NIH HHS F32 CA08648PHPPO CDC HHS PHSCA 42567
6 · The paper itself

Abstract

Both the TATA and CCAAT boxes are widespread promoter elements and their binding proteins, TBP and NF-Y, are extremely conserved in evolution. NF-Y is composed of three subunits, NF-YA, NF-YB and NF-YC, all necessary for DNA binding. NF-YB and NF-YC contain a putative histone-like motif, a domain also present in TBP-associated factors (TAFIIs) and in the subunits of the transcriptional repressor NC2. Immunopurification of holo-TFIID with anti-TBP and anti-TAFII100 antibodies indicates that a fraction of NF-YB associates with TFIID in the absence of NF-YA. Sedimentation velocity centrifugation experiments confirm that two pools of NF-YB, and most likely NF-YC, exist: one associated with NF-YA and binding to the CCAAT box; another involved in high molecular weight complexes. We started to dissect NF-Y-TFIID interactions by showing that: (i) NF-YB and NF-YC interact with TBP in solution, both separately and once bound to each other; (ii) short stretches of both NF-YB and NF-YC located within the evolutionary conserved domains, adjacent to the putative histone fold motifs, are necessary for TBP binding; (iii) TBP single amino acid mutants in the HS2 helix, previously shown to be defective in NC2 binding, are also unable to bind NF-YB and NF-YC.

Indexed as

HistonesProtein FoldingTATA BoxAmino Acid SequenceAnimalsBinding SitesCCAAT-Binding FactorCCAAT-Enhancer-Binding ProteinsCentrifugation, Density GradientDNA-Binding ProteinsEscherichia coliHumansMiceMolecular Sequence DataMolecular WeightRatsCCAAT-Binding FactorCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsHistonesNfyc protein, ratTATA-Box Binding ProteinTranscription FactorsTranscription Factors, TFIITranscription Factor TFIID

Identifiers

PMID9153318
PMCPMC146709
OpenAlexW2021345333

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.