Evidence map›Paper›PMID 21357515›Full record

ArticleMolecular & cellular proteomics : MCP2011

Proteome dynamics and proteome function of cardiac 19S proteasomes.

Ding Wang, Chenggong Zong, Myong-chul Koag, Yueju Wang, Oliver Drews, Caiyun Fang, Sarah B Scruggs, Peipei Ping

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Slow-twitch skeletal muscle defects accompany cardiac dysfunction in transgenic mice with a mutation in the myosin regulatory light chain.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. The ubiquitin proteasome system in human cardiomyopathies and heart failure.American journal of physiology. Heart and circulatory physiology · 2013
    Review
  9. Article
  10. Article
  11. The ubiquitin proteasome system and myocardial ischemia.American journal of physiology. Heart and circulatory physiology · 2013
    Review
  12. Post-translational modification of cardiac proteasomes: functional delineation enabled by proteomics.American journal of physiology. Heart and circulatory physiology · 2012
    Review
  13. The ubiquitin-proteasome system and cardiovascular disease.Progress in molecular biology and translational science · 2012
    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 1 institution in 1 country.

Ding WangDepartment of Physiology and Medicine, Division of Cardiology, University of California at Los Angeles, UCLA School of Medicine, Los Angeles, California 90095, USA.
Chenggong Zong
Myong-chul Koag
Yueju Wang
Oliver Drews
Caiyun Fang
Sarah B Scruggs
Peipei Ping
University of California, Los Angeles · US

Funding

Revealing Cardiovascular Stress Regulation beyond the Diffraction LimitR01HL088640 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI STEFANI, ENRICO · 2007 to 2011
$5.3M
Novel Signaling Mechanisms and Molecular Targets in the Stressed MyocardiumR01HL098954 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PING, PEIPEI, WANG, YIBIN · 2010 to 2013
$3.0M
NHLBI NIH HHS HHSN268201000035CNHLBI NIH HHS HL088640NHLBI NIH HHS R01 HL088640NHLBI NIH HHS R01 HL098954
6 · The paper itself

Abstract

Myocardial proteasomes are comprised of 20S core particles and 19S regulatory particles, which together carry out targeted degradation of cardiac proteins. The 19S complex is unique among the regulators of proteasomes in that it affects both the capacity and specificity of protein degradation. However, a comprehensive molecular characterization of cardiac 19S complexes is lacking. In this investigation, we tailored a multidimensional chromatography-based purification strategy to isolate structurally intact and functionally viable 19S complexes from murine hearts. Two distinct subpopulations of 19S complexes were isolated based upon (1) potency of activating 20S proteolytic activity, and (2) molecular composition using a combination of immuno-detection, two-dimensional-differential gel electrophoresis, and MS-based approaches. Heat shock protein 90 (Hsp90) was identified to be characteristic to 19S subpopulation I. The physical interaction of Hsp90 with 19S complexes was demonstrated via multiple approaches. Inhibition of Hsp90 activity using geldanamycin or BIIB021 potentiated the ability of subpopulation I to activate 20S proteasomes in the murine heart, thus demonstrating functional specificity of Hsp90 in subpopulation I. This investigation has advanced our understanding of the molecular heterogeneity of cardiac proteasomes by identifying molecularly and functionally distinct cardiac 19S complexes. The preferential association of Hsp90 with 19S subpopulation I unveils novel targets for designing proteasome-based therapeutic interventions for combating cardiac disease.

Indexed as

Amino Acid SequenceAnimalsChromatography, LiquidEnzyme ActivationHSP90 Heat-Shock ProteinsMaleMiceMice, Inbred ICRMolecular Sequence DataMyocardiumProteasome Endopeptidase ComplexProteomeTandem Mass Spectrometry26S proteasome non-ATPase regulatory subunit 13HSP90 Heat-Shock ProteinsProteasome Endopeptidase ComplexProteome

Identifiers

PMID21357515
PMCPMC3098593
OpenAlexW2067495244

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.