Evidence map›Paper›PMID 31230944›Full record

ArticleStructure (London, England : 1993)2019

Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination.

Anna K L Liess, Alena Kucerova, Kristian Schweimer, Lu Yu, Theodoros I Roumeliotis, Mathias Diebold, Olexandr Dybkov, Christoph Sotriffer, Henning Urlaub, Jyoti S Choudhary and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. From seeds to trees: how E2 enzymes grow ubiquitin chains.Biochemical Society transactions · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. International journal of molecular sciences · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Anna K L LiessRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany.
Alena KucerovaCell Cycle, Biotechnology Center, Technische Universität Dresden, 01307 Dresden, Germany.
Kristian SchweimerBiopolymers, University of Bayreuth, 95447 Bayreuth, Germany.
Lu YuFunctional Proteomics Group, The Institute of Cancer Research, London SW3 6JB, UK.
Theodoros I RoumeliotisFunctional Proteomics Group, The Institute of Cancer Research, London SW3 6JB, UK.
Mathias DieboldInstitute of Pharmacy and Food Chemistry, University of Würzburg, 97074 Würzburg, Germany.
Olexandr DybkovDepartment for Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, 37077 Göttingen, Germany.
Christoph SotrifferInstitute of Pharmacy and Food Chemistry, University of Würzburg, 97074 Würzburg, Germany.
Henning UrlaubGroup for Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, Göttingen, 37077 Göttingen, Germany; Proteomics Service Facility, Georg-August-Universität, Göttingen, 37077 Göttingen, Germany.
Jyoti S ChoudharyFunctional Proteomics Group, The Institute of Cancer Research, London SW3 6JB, UK.
Jörg MansfeldCell Cycle, Biotechnology Center, Technische Universität Dresden, 01307 Dresden, Germany. Electronic address: joerg.mansfeld@tu-dresden.de.
Sonja LorenzRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080 Würzburg, Germany. Electronic address: sonja.lorenz@virchow.uni-wuerzburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-conjugating enzymes (E2s) govern key aspects of ubiquitin signaling. Emerging evidence suggests that the activities of E2s are modulated by posttranslational modifications; the structural underpinnings, however, are largely unclear. Here, we unravel the structural basis and mechanistic consequences of a conserved autoubiquitination event near the catalytic center of E2s, using the human anaphase-promoting complex/cyclosome-associated UBE2S as a model system. Crystal structures we determined of the catalytic ubiquitin carrier protein domain combined with MD simulations reveal that the active-site region is malleable, which permits an adjacent ubiquitin acceptor site, Lys

Indexed as

Catalytic DomainCell LineCrystallography, X-RayCysteineGene Expression RegulationHeLa CellsHomeostasisHumansLysineMitosisMolecular Dynamics SimulationUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesCysteineLysineUbe2S protein, humanUbiquitinUbiquitin-Conjugating Enzymescell cycleE2 enzymeenzyme mechanismK11 chainmass spectrometrymitosismolecular dynamicsNMRubiquitinX-ray crystallography

Identifiers

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.