Evidence map›Paper›PMID 34869605›Full record

ReviewFrontiers in molecular biosciences2021

SUMO-specific Isopeptidases Tuning Cardiac SUMOylation in Health and Disease.

Paul W Hotz, Stefan Müller, Luca Mendler

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
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  3. Review
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  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. ERα promotesGland surgery · 2023
    Article
  15. Function and regulation of ubiquitin-like SUMO system in heart.Frontiers in cell and developmental biology · 2023
    Review
  16. Article
  17. Article
  18. 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

3 authors.

Paul W HotzInstitute of Biochemistry II, Gustav Embden Zentrum, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany.
Stefan MüllerInstitute of Biochemistry II, Gustav Embden Zentrum, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany.
Luca MendlerInstitute of Biochemistry II, Gustav Embden Zentrum, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation is a transient posttranslational modification with small-ubiquitin like modifiers (SUMO1, SUMO2 and SUMO3) covalently attached to their target-proteins via a multi-step enzymatic cascade. SUMOylation modifies protein-protein interactions, enzymatic-activity or chromatin binding in a multitude of key cellular processes, acting as a highly dynamic molecular switch. To guarantee the rapid kinetics, SUMO target-proteins are kept in a tightly controlled equilibrium of SUMOylation and deSUMOylation. DeSUMOylation is maintained by the SUMO-specific proteases, predominantly of the SENP family. SENP1 and SENP2 represent family members tuning SUMOylation status of all three SUMO isoforms, while SENP3 and SENP5 are dedicated to detach mainly SUMO2/3 from its substrates. SENP6 and SENP7 cleave polySUMO2/3 chains thereby countering the SUMO-targeted-Ubiquitin-Ligase (StUbL) pathway. Several biochemical studies pinpoint towards the SENPs as critical enzymes to control balanced SUMOylation/deSUMOylation in cardiovascular health and disease. This study aims to review the current knowledge about the SUMO-specific proteases in the heart and provides an integrated view of cardiac functions of the deSUMOylating enzymes under physiological and pathological conditions.

Indexed as

heartheart failureischemia reperfusion (I/R) injurySENPSUMO

Identifiers

PMID34869605
PMCPMC8641784

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Registered trials

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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.