Evidence map›Paper›PMID 22334692›Full record

ArticleThe Journal of biological chemistry2012

Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins.

Simone Culurgioni, Inés G Muñoz, Alberto Moreno, Alicia Palacios, Maider Villate, Ignacio Palmero, Guillermo Montoya, Francisco J Blanco

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

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  15. ING1 and ING2: multifaceted tumor suppressor genes.Cellular and molecular life sciences : CMLS · 2013
    Review
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

8 authors at 3 institutions in 2 countries.

Simone CulurgioniStructural Biology Unit, CIC bioGUNE, E-48160 Derio, Spain.
Inés G Muñoz
Alberto Moreno
Alicia Palacios
Maider Villate
Ignacio Palmero
Guillermo Montoya
Francisco J Blanco
Consejo Superior de Investigaciones Científicas · ESUniversidad Autónoma de Madrid · ESCIC bioGUNE · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein ING4 binds to histone H3 trimethylated at Lys-4 (H3K4me3) through its C-terminal plant homeodomain, thus recruiting the HBO1 histone acetyltransferase complex to target promoters. The structure of the plant homeodomain finger bound to an H3K4me3 peptide has been described, as well as the disorder and flexibility in the ING4 central region. We report the crystal structure of the ING4 N-terminal domain, which shows an antiparallel coiled-coil homodimer with each protomer folded into a helix-loop-helix structure. This arrangement suggests that ING4 can bind simultaneously two histone tails on the same or different nucleosomes. Dimerization has a direct impact on ING4 tumor suppressor activity because monomeric mutants lose the ability to induce apoptosis after genotoxic stress. Homology modeling based on the ING4 structure suggests that other ING dimers may also exist.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsApoptosisCell Cycle ProteinsCell LineCell ProliferationChromatinCrystallography, X-RayHistone AcetyltransferasesHomeodomain ProteinsHumansMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedCell Cycle ProteinsChromatinHistone AcetyltransferasesHomeodomain ProteinsING4 protein, humanKAT7 protein, humanTumor Suppressor Proteins

Identifiers

PMID22334692
PMCPMC3322854
OpenAlexW1991596856

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.