Evidence map›Paper›PMID 18212061›Full record

ArticleMolecular and cellular biology2008

The histone-like NF-Y is a bifunctional transcription factor.

Michele Ceribelli, Diletta Dolfini, Daniele Merico, Raffaella Gatta, Alessandra M Viganò, Giulio Pavesi, Roberto Mantovani

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

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  11. The Plant NF-Y DNA MatrixPlants (Basel, Switzerland) · 2019
    Article
  12. Transcriptional regulation of the porcine miR-17-92 cluster.Molecular genetics and genomics : MGG · 2019
    Article
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  18. Article
  19. Article
  20. TXNIP regulates myocardial fatty acid oxidation via miR-33a signaling.American journal of physiology. Heart and circulatory physiology · 2016
    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

7 authors.

Michele CeribelliDipartimento di Scienze Biomolecolari e Biotecnologie, Università di Milano, Via Celoria 26, 20133 Milano, Italy.
Diletta Dolfini
Daniele Merico
Raffaella Gatta
Alessandra M Viganò
Giulio Pavesi
Roberto Mantovani

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NF-Y is a trimeric transcription factor containing H2A/H2B-like subunits, which specifically binds to the CCAAT box, a common eukaryotic promoter element. To gain insights into NF-Y-dependent transcriptional regulation, we assessed its relationships with positive histone marks by chromatin immunoprecipitation-on-chip and correlative-profiling studies. Unbiased identification of binding sites shows that the majority of genes are bound by NF-Y in the promoter and/or within the coding region. Parallel analysis of H3K9-14ac and H3K4me3 sites indicates that NF-Y loci can be divided in two distinct clusters: (i) a large cohort contains H3K9-14ac and H3K4me3 marks and correlates with expression and (ii) a sizeable group is devoid of these marks and is found on transcriptionally silent genes. Within this class, we find that NF-Y binding is associated with negative histone marks, such as H4K20me3 and H3K27me3. NF-Y removal by a dominant negative NF-YA leads to a decrease in the transcription of expressed genes associated with H3K4me3 and H3K9-14ac, while increasing the levels of many inactive genes. These data indicate that NF-Y is embedded in positive as well as in negative methyl histone marks, serving a dual function in transcriptional regulation, as an activator or as a repressor.

Indexed as

AcetylationBinding SitesCCAAT-Binding FactorCell LineChromatin ImmunoprecipitationChromosomes, Human, Pair 21Enhancer Elements, GeneticGene Expression ProfilingHistonesHumansMethylationProtein Processing, Post-TranslationalProtein SubunitsRecombinant Fusion ProteinsRepressor ProteinsTrans-ActivatorsCCAAT-Binding FactorHistonesNfya protein, mouseProtein SubunitsRecombinant Fusion ProteinsRepressor ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID18212061
PMCPMC2268390

What OpenQuestion holds

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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.