Evidence map›Paper›PMID 40810167›Full record

ArticleACS pharmacology & translational science2025

Impact of Post-Translational Succination on Small Ubiquitin-Like Modifier 1 Structure: A Dual Approach Combining Gas Phase and Solution Studies.

Louis Groignet, David Dellemme, Quentin Duez, Afaf Fizazi, Jean-Marie Colet, Patrick Brocorens, Mathieu Surin, Pascal Gerbaux, Julien De Winter

Abstract read
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In one paragraph

Article in ACS pharmacology & translational science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Louis GroignetOrganic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0009-0003-0235-1795
David DellemmeLaboratory for Chemistry of Novel Materials, Department of Chemistry, Materials Research Institute, University of Mons, Place du Parc 23, Mons B-7000, Belgium.
Quentin DuezOrganic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0000-0002-9067-7917
Afaf FizaziHuman Biology and Toxicology Laboratory, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0009-0004-2599-4168
Jean-Marie ColetHuman Biology and Toxicology Laboratory, University of Mons, Place du Parc 23, Mons B-7000, Belgium.
Patrick BrocorensLaboratory for Chemistry of Novel Materials, Department of Chemistry, Materials Research Institute, University of Mons, Place du Parc 23, Mons B-7000, Belgium.
Mathieu SurinLaboratory for Chemistry of Novel Materials, Department of Chemistry, Materials Research Institute, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0000-0001-8950-3437
Pascal GerbauxOrganic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0000-0001-5114-4352
Julien De WinterOrganic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, Mons B-7000, Belgium.ORCID https://orcid.org/0000-0003-3429-5911

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO1 (small ubiquitin-like modifier 1) is a key protein involved in the post-translational modification of a wide range of substrate proteins. SUMOylation plays a pivotal role in regulating various cellular processes such as protein localization, functional modulation, and complex formation. Notably, SUMO1 contains a cysteine residue in its sequence, making it susceptible to succination, i.e., a Michael addition of cysteine onto fumarate, forming a succinated cysteine. This could occur under conditions of elevated intracellular fumarate concentration, a hallmark of metabolic dysregulation. To investigate this hypothesis, we employ a multidisciplinary approach integrating advanced analytical techniques such as mass spectrometry (including liquid chromatography, ion mobility spectrometry, and hydrogen-deuterium exchange experiments), circular dichroism spectroscopy, and molecular dynamics simulations. We demonstrate that SUMO1 undergoes succination

Indexed as

circular dichroismmass spectrometrymolecular dynamicssuccinationSUMO1SUMOylation

Identifiers

PMID40810167
PMCPMC12340649

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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.