Evidence map›Paper›PMID 32467258›Full record

ArticleMolecular & cellular proteomics : MCP2020

Differential Complex Formation via Paralogs in the Human Sin3 Protein Interaction Network.

Mark K Adams, Charles A S Banks, Janet L Thornton, Cassandra G Kempf, Ying Zhang, Sayem Miah, Yan Hao, Mihaela E Sardiu, Maxime Killer, Gaye L Hattem and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

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  14. Structure of a SIN3-HDAC complex from budding yeast.Nature structural & molecular biology · 2023
    Article
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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

14 authors at 1 institution in 1 country.

Mark K AdamsStowers Institute for Medical Research, Kansas City, Missouri, USA.
Charles A S BanksStowers Institute for Medical Research, Kansas City, Missouri, USA.
Janet L ThorntonStowers Institute for Medical Research, Kansas City, Missouri, USA.
Cassandra G KempfStowers Institute for Medical Research, Kansas City, Missouri, USA.
Ying ZhangStowers Institute for Medical Research, Kansas City, Missouri, USA.
Sayem MiahStowers Institute for Medical Research, Kansas City, Missouri, USA.
Yan HaoStowers Institute for Medical Research, Kansas City, Missouri, USA.
Mihaela E SardiuStowers Institute for Medical Research, Kansas City, Missouri, USA.
Maxime KillerStowers Institute for Medical Research, Kansas City, Missouri, USA.
Gaye L HattemStowers Institute for Medical Research, Kansas City, Missouri, USA.
Alexis MurrayStowers Institute for Medical Research, Kansas City, Missouri, USA.
Maria L KattStowers Institute for Medical Research, Kansas City, Missouri, USA.
Laurence FlorensStowers Institute for Medical Research, Kansas City, Missouri, USA.
Michael P WashburnStowers Institute for Medical Research, Kansas City, Missouri, USA; Department of Pathology & Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA. Electronic address: mpw@stowers.org.
Stowers Institute for Medical Research · US

Funding

Inhibitor Reprogramming of a Human Histone Deacetylase Protein Interaction NetworkR01GM112639 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI FLORENS, LAURENCE ALEXANDRA · 2016 to 2020
$1.6M
Characterization of the SIN3A and SIN3B HDAC complexesF32GM122215 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI ADAMS, MARK K · 2017 to 2018
$116k
Deciphering the Paralogue Specific Interactions within the Sin3 Protein Interaction NetworkF31GM131536 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI KEMPF, CASSANDRA G · 2019 to 2020
$51k
NIGMS NIH HHS F31 GM131536NIGMS NIH HHS F32 GM122215NIGMS NIH HHS R01 GM112639
6 · The paper itself

Abstract

Despite the continued analysis of HDAC inhibitors in clinical trials, the heterogeneous nature of the protein complexes they target limits our understanding of the beneficial and off-target effects associated with their application. Among the many HDAC protein complexes found within the cell, Sin3 complexes are conserved from yeast to humans and likely play important roles as regulators of transcriptional activity. The presence of two Sin3 paralogs in humans, SIN3A and SIN3B, may result in a heterogeneous population of Sin3 complexes and contributes to our poor understanding of the functional attributes of these complexes. Here, we profile the interaction networks of SIN3A and SIN3B to gain insight into complex composition and organization. In accordance with existing data, we show that Sin3 paralog identity influences complex composition. Additionally, chemical cross-linking MS identifies domains that mediate interactions between Sin3 proteins and binding partners. The characterization of rare SIN3B proteoforms provides additional evidence for the existence of conserved and divergent elements within human Sin3 proteins. Together, these findings shed light on both the shared and divergent properties of human Sin3 proteins and highlight the heterogeneous nature of the complexes they organize.

Indexed as

Protein Interaction MapsAmino Acid SequenceCell LineCell NucleusChromatography, LiquidHistone Deacetylase 1HumansMultigene FamilyNuclear Localization SignalsProtein BindingProtein DomainsProtein IsoformsProteomicsRecombinant ProteinsRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexHDAC1 protein, humanHistone Deacetylase 1Nuclear Localization SignalsProtein IsoformsRecombinant ProteinsRepressor ProteinsSIN3A transcription factorSIN3B protein, humanSin3 Histone Deacetylase and Corepressor ComplexChromatin function or biologycross linkingDSSOepigeneticshistone deacetylasenuclear translocationpathway analysisprotein complex analysisprotein-protein interactions*SIN3subcellular analysissystems biology*

Identifiers

PMID32467258
PMCPMC8143632
OpenAlexW3029333022

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.