Evidence map›Paper›PMID 26726734›Full record

ArticleACS chemical biology2016

Synthesis of a Bis-thio-acetone (BTA) Analogue of the Lysine Isopeptide Bond and its Application to Investigate the Effects of Ubiquitination and SUMOylation on α-Synuclein Aggregation and Toxicity.

Yuka E Lewis, Tharindumala Abeywardana, Yu Hsuan Lin, Ana Galesic, Matthew R Pratt

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. The chemical biology of ubiquitin.Biochimica et biophysica acta. General subjects · 2022
    Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Chemical Protein Ubiquitylation with Preservation of the Native Cysteine Residues.Chembiochem : a European journal of chemical biology · 2016
    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

5 authors.

Yuka E LewisDepartments of Chemistry and ‡Molecular and Computational Biology, University of Southern California , Los Angeles, California 90089, United States.
Tharindumala AbeywardanaDepartments of Chemistry and ‡Molecular and Computational Biology, University of Southern California , Los Angeles, California 90089, United States.
Yu Hsuan LinDepartments of Chemistry and ‡Molecular and Computational Biology, University of Southern California , Los Angeles, California 90089, United States.
Ana GalesicDepartments of Chemistry and ‡Molecular and Computational Biology, University of Southern California , Los Angeles, California 90089, United States.
Matthew R PrattDepartments of Chemistry and ‡Molecular and Computational Biology, University of Southern California , Los Angeles, California 90089, United States.

Funding

USC/NORRIS COMPREHENSIVE CANCER CENTER (CORE) SUPPORTP30CA014089 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Fumito Ito · 1985 to 2026
$181.4M
NCI NIH HHS P30 CA014089NCI NIH HHS P30CA014089
6 · The paper itself

Abstract

The reversible modification of protein by the small protein ubiquitin and other ubiquitin-like modifiers plays important roles in virtually every key biological process in eukaryotic cells. The establishment of a range of chemical methods for the preparation of ubiquitinated proteins has enabled the site-specific interrogation of the consequences of these modifications. However, many of these techniques require significant levels of synthetic expertise, somewhat limiting their widespread application by the biological community. To overcome this issue, the creation of structural analogues of the ubiquitin-protein linkage that can be readily prepared with commercially available reagents and buffers is an important goal. Here we present the development of conditions for the facile synthesis of bis-thio-acetone (BTA) linkages of ubiquitinated proteins in high yields. Additionally, we apply this technique to the preparation of the aggregation prone protein α-synuclein bearing either ubiquitin or the small ubiquitin-like modifier (SUMO). With these proteins, we demonstrate that the BTA linkage recapitulates the previously published effects of either of these proteins on α-synuclein, suggesting that it is a good structural mimic. Notably, the BTA linkage is chemically and enzymatically stable, enabling us to study the consequences of site-specific ubiquitination and SUMOylation on the toxicity of α-synuclein in cell culture, which revealed modification and site-specific differences.

Indexed as

Acetonealpha-SynucleinLysinePeptidesSumoylationUbiquitinationAcetonealpha-SynucleinLysinePeptides

Identifiers

PMID26726734
PMCPMC6300141

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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.