Evidence map›Paper›PMID 35234136›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Structural and functional analysis of the SET3 histone deacetylase complex.

Alexis A Reyes, Susan Fishbain, Yuan He

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Alexis A ReyesMolecular Biosciences, Northwestern University, Evanston, Illinois, USA.
Susan FishbainMolecular Biosciences, Northwestern University, Evanston, Illinois, USA.
Yuan HeMolecular Biosciences, Northwestern University, Evanston, Illinois, USA.

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Spatio-Temporal Organization of Chromatin and Information Transfer in CancerU54CA193419 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BACKMAN, VADIM · 2015 to 2020
$10.4M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Structure and Mechanism of Non-Homologous End JoiningR01GM135651 · NIGMS · NORTHWESTERN UNIVERSITY · PI HE, YUAN · 2020 to 2024
$1.8M
Acquisition of Amersham Typhoon 5 Variable-mode ImagerS10OD026963 · OD · NORTHWESTERN UNIVERSITY · PI GRIGORESCU, ARABELA A · 2019 to 2019
$143k
NCI NIH HHS P01 CA092584NCI NIH HHS P30 CA060553NCI NIH HHS U54 CA193419NIGMS NIH HHS R01 GM129325NIGMS NIH HHS R01 GM135651NIGMS NIH HHS T32 GM008382NIH HHS 1S10OD026963-01NIH HHS P01-CA092584NIH HHS R01-GM135651NIH HHS S10 OD026963
6 · The paper itself

Abstract

The SET3 complex (SET3C) is a seven-subunit histone deacetylase complex that is capable of transcriptional regulation. Methylated histone 3 marks recruit SET3C to the nucleosome, and the SET3C catalytic subunits deacetylate the histone 3 and 4 tails. There is very limited structural knowledge of the SET3C subunits, with most subunits having unknown structures or functions. Here, a catalytically active SET3 complex was endogenously purified from Saccharomyces cerevisiae and utilized for negative-stain electron microscopy (EM) to determine an apo model for the holo complex. The negative-stain EM 3D model revealed a three-lobe architecture, with each lobe extending from a central point.

Indexed as

Histone DeacetylasesSaccharomyces cerevisiae ProteinsCrystallography, X-RayStructure-Activity RelationshipTranscription, GeneticHistone DeacetylasesSaccharomyces cerevisiae ProteinsSet3 protein, S cerevisiaeelectron microscopyhistone deacetylationSET3 complex

Identifiers

PMID35234136
PMCPMC8900736

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.