Evidence map›Paper›PMID 17142463›Full record

ArticleThe Journal of biological chemistry2007

Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.

Xiaobing Shi, Ioulia Kachirskaia, Kay L Walter, Jen-Hao A Kuo, Aimee Lake, Foteini Davrazou, Steve M Chan, David G E Martin, Ian M Fingerman, Scott D Briggs and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

155 citing papers in PubMed, 254 citations in OpenAlex.

  1. Article
  2. Article
  3. A PHD-zinc finger-mediated mechanism for PHF21B recognition of H3K36me3.Genomic psychiatry : advancing science from genes to society · 2026
    Article
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  6. Review
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  17. Article
  18. Cells · 2022
    Article
  19. Article
  20. Article

95 more citing papers are in PubMed but not listed here.

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

16 authors at 6 institutions in 2 countries.

Xiaobing ShiDepartment of Biological Sciences, Stanford University, Stanford, California 94305, USA.
Ioulia Kachirskaia
Kay L Walter
Jen-Hao A Kuo
Aimee Lake
Foteini Davrazou
Steve M Chan
David G E Martin
Ian M Fingerman
Scott D Briggs
LeAnn Howe
Paul J Utz
Tatiana G Kutateladze
Alexey A Lugovskoy
Mark T Bedford
Or Gozani
Purdue University West Lafayette · USStanford University · USThe University of Texas MD Anderson Cancer Center · USUniversity of British Columbia · CAUniversity of Colorado Hospital · USStanford Medicine · US

Funding

Role of Set1-mediated methylation in chromatin functionR01GM074183 · NIGMS · PURDUE UNIVERSITY · PI BRIGGS, SCOTT D · 2006 to 2010
$1.4M
NIGMS NIH HHS R01 GM074183
6 · The paper itself

Abstract

The PHD finger motif is a signature chromatin-associated motif that is found throughout eukaryotic proteomes. Here we have determined the histone methyl-lysine binding activity of the PHD fingers present within the Saccharomyces cerevisiae proteome. We provide evidence on the genomic scale that PHD fingers constitute a general class of effector modules for histone H3 trimethylated at lysine 4 (H3K4me3) and histone H3 trimethylated at lysine 36 (H3K36me3). Structural modeling of PHD fingers demonstrates a conserved mechanism for recognizing the trimethyl moiety and provides insight into the molecular basis of affinity for the different methyl-histone ligands. Together, our study suggests that a common function for PHD fingers is to transduce methyl-lysine events and sheds light on how a single histone modification can be linked to multiple biological outcomes.

Indexed as

Homeodomain ProteinsSaccharomyces cerevisiae ProteinsAmino Acid MotifsAmino Acid SequenceDNA-Binding ProteinsHistonesLysineMethylationMolecular Sequence DataProtein BindingProtein Structure, TertiaryProteomeSaccharomyces cerevisiaeDNA-Binding ProteinsHistonesHomeodomain ProteinsLysineProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID17142463
PMCPMC2735445
OpenAlexW2054150044

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.