Evidence map›Paper›PMID 22523251›Full record

ReviewAmerican journal of physiology. Heart and circulatory physiology2012

Post-translational modification of cardiac proteasomes: functional delineation enabled by proteomics.

Sarah B Scruggs, Nobel C Zong, Ding Wang, Enrico Stefani, Peipei Ping

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Heart and circulatory physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Protein homeostasis in the aged and diseased heart.The journal of cardiovascular aging · 2023
    Article
  3. Article
  4. Review
  5. Quantitative proteomic and phosphoproteomic profiling of ischemic myocardial stunning in swine.American journal of physiology. Heart and circulatory physiology · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Proteasomal and lysosomal protein degradation and heart disease.Journal of molecular and cellular cardiology · 2014
    Review
  17. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond.Journal of molecular and cellular cardiology · 2014
    Review
  18. Article
  19. Article
  20. The ubiquitin proteasome system and myocardial ischemia.American journal of physiology. Heart and circulatory physiology · 2013
    Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sarah B ScruggsDivision of Cardiology, Department of Physiology, University of California, Los Angeles, USA.
Nobel C Zong
Ding Wang
Enrico Stefani
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
Acute and Chronic Regulation of 20S Proteasome Function by cAMP-Dependent KinaseF32HL099029 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SCRUGGS, SARAH · 2010 to 2012
$153k
NHLBI NIH HHS F32 HL099029NHLBI NIH HHS F32-HL-099029NHLBI NIH HHS HHSN268201000035CNHLBI NIH HHS R01 HL088640NHLBI NIH HHS R01-HL-088640NHLBI NIH HHS R01 HL098954NHLBI NIH HHS R01-HL-098954
6 · The paper itself

Abstract

Proteasomes are ubiquitously expressed multicatalytic complexes that serve as key regulators of protein homeostasis. There are several lines of evidence indicating that proteasomes exist in heterogeneous subpopulations in cardiac muscle, differentiated, in part, by post-translational modifications (PTMs). PTMs regulate numerous facets of proteasome function, including catalytic activities, complex assembly, interactions with associating partners, subcellular localization, substrate preference, and complex turnover. Classical technologies used to identify PTMs on proteasomes have lacked the ability to determine site specificity, quantify stoichiometry, and perform large-scale, multi-PTM analysis. Recent advancements in proteomic technologies have largely overcome these limitations. We present here a discussion on the importance of PTMs in modulating proteasome function in cardiac physiology and pathophysiology, followed by the presentation of a state-of-the-art proteomic workflow for identifying and quantifying PTMs of cardiac proteasomes.

Indexed as

ProteomicsAnimalsComputational BiologyHeartHumansMolecular Sequence DataMyocardiumMyocytes, CardiacProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalSignal TransductionSubcellular FractionsProteasome Endopeptidase Complex

Identifiers

PMID22523251
PMCPMC3404648
OpenAlexW2151374195

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.