Evidence map›Paper›PMID 11884585›Full record

ArticleMolecular and cellular biology2002

The PHD type zinc finger is an integral part of the CBP acetyltransferase domain.

Eric Kalkhoven, Hans Teunissen, Ada Houweling, C Peter Verrijzer, Alt Zantema

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In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 102 citations in OpenAlex.

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  15. Article
  16. Nuclear phosphoinositide regulation of chromatin.Journal of cellular physiology · 2018
    Review
  17. Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
  20. Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

5 authors at 1 institution in 1 country.

Eric KalkhovenDepartment of Molecular Cell Biology, MGC Center for Biomedical Genetics, Leiden University Medical Center, 2300 RA Leiden, The Netherlands. E.Kalkhoven@lumc.nl
Hans Teunissen
Ada Houweling
C Peter Verrijzer
Alt Zantema
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone acetyltransferases (HATs) such as CBP and p300 are regarded as key regulators of RNA polymerase II-mediated transcription, but the critical structural features of their HAT modules remain ill defined. The HAT domains of CBP and p300 are characterized by the presence of a highly conserved putative plant homeodomain (PHD) (C4HC3) type zinc finger, which is part of the functionally uncharacterized cysteine-histidine-rich region 2 (CH2). Here we show that this region conforms to the PHD type zinc finger consensus and that it is essential for in vitro acetylation of core histones and the basal transcription factor TFIIE34 as well as for CBP autoacetylation. PHD finger mutations also reduced the transcriptional activity of the full-length CBP protein when tested on transfected reporter genes. Importantly, similar results were obtained on integrated reporters, which reflect a more natural chromatinized state. Taken together, our results indicate that the PHD finger forms an integral part of the enzymatic core of the HAT domain of CBP.

Indexed as

Saccharomyces cerevisiae ProteinsZinc FingersAcetylationAcetyltransferasesAmino Acid SequenceAnimalsCell LineConserved SequenceCREB-Binding ProteinCyclic AMP Response Element-Binding ProteinDrosophilaHistone AcetyltransferasesHistonesHumansMolecular Sequence DataMutationAcetyltransferasesCREB-Binding ProteinCREBBP protein, humanCyclic AMP Response Element-Binding ProteinHistone AcetyltransferasesHistonesNuclear ProteinsSaccharomyces cerevisiae ProteinsTrans-Activators

Identifiers

PMID11884585
PMCPMC133676
OpenAlexW2171849558

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.