Evidence map›Paper›PMID 32294434›Full record

ArticleCell reports2020

Integrative Modeling of a Sin3/HDAC Complex Sub-structure.

Charles A S Banks, Ying Zhang, Sayem Miah, Yan Hao, Mark K Adams, Zhihui Wen, Janet L Thornton, Laurence Florens, Michael P Washburn

Abstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. SIN3B Loss Heats up Cold Tumor Microenvironment to Boost Immunotherapy in Pancreatic Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

9 authors.

Charles A S BanksStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Ying ZhangStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Sayem MiahStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Yan HaoStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Mark K AdamsStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Zhihui WenStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Janet L ThorntonStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Laurence FlorensStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Michael P WashburnStowers Institute for Medical Research, Kansas City, MO 64110, USA; Department of Pathology & Laboratory Medicine, University of Kansas Medical Center, Kansas City, KS 66160, USA. Electronic address: mpw@stowers.org.

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
NIGMS NIH HHS F32 GM122215NIGMS NIH HHS R01 GM112639
6 · The paper itself

Abstract

Sin3/HDAC complexes function by deacetylating histones, condensing chromatin, and modulating gene expression. Although components used to build these complexes have been well defined, we still have only a limited understanding of the structure of the Sin3/HDAC subunits assembled around the scaffolding protein SIN3A. To characterize the spatial arrangement of Sin3 subunits, we combined Halo affinity capture, chemical crosslinking, and high-resolution mass spectrometry (XL-MS) to determine intersubunit distance constraints, identifying 66 interprotein and 63 self-crosslinks for 13 Sin3 subunits. Having assessed crosslink authenticity by mapping self-crosslinks onto existing structures, we used distance restraints from interprotein crosslinks to guide assembly of a Sin3 complex substructure. We identified the relative positions of subunits SAP30L, HDAC1, SUDS3, HDAC2, and ING1 around the SIN3A scaffold. The architecture of this subassembly suggests that multiple factors have space to assemble to collectively influence the behavior of the catalytic subunit HDAC1.

Indexed as

HEK293 CellsHistone Deacetylase 1Histone Deacetylase 2Histone DeacetylasesHumansMass SpectrometryRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexHDAC1 protein, humanHDAC2 protein, humanHistone Deacetylase 1Histone Deacetylase 2Histone DeacetylasesRepressor ProteinsSin3 Histone Deacetylase and Corepressor Complexchromatincrosslinkingdistance restraintsDSSOHDACprotein dockingproteomicsSin3structural modelingXL-MS

Identifiers

PMID32294434
PMCPMC7217224

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.