Evidence map›Paper›PMID 28710279›Full record

ArticleThe Journal of biological chemistry2017

UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN.

Sungjin Park, Peter K Foote, David T Krist, Sarah E Rice, Alexander V Statsyuk

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  2. Capturing the catalytic intermediates of parkin ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
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  5. Acta pharmaceutica Sinica. B · 2022
    Article
  6. Article
  7. Miro proteins and their role in mitochondrial transfer in cancer and beyond.Frontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Building and decoding ubiquitin chains for mitophagy.Nature reviews. Molecular cell biology · 2018
    Review
  16. Review
  17. Review
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 at 1 institution in 1 country.

Sungjin ParkFrom the Department of Cell and Molecular Biology, Northwestern University, Chicago, Illinois 60611.
Peter K Footethe Chemistry of Life Processes Institute, Department of Chemistry, Northwestern University, Evanston, Illinois 60208, and.
David T Kristthe Chemistry of Life Processes Institute, Department of Chemistry, Northwestern University, Evanston, Illinois 60208, and.
Sarah E RiceFrom the Department of Cell and Molecular Biology, Northwestern University, Chicago, Illinois 60611.
Alexander V Statsyukthe Chemistry of Life Processes Institute, Department of Chemistry, Northwestern University, Evanston, Illinois 60208, and avstatsy@central.uh.edu.ORCID 0000-0001-9954-8049
Northwestern University · US

Funding

Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
The Mechanism of Kinesin Self-RegulationR01GM072656 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI RICE, SARAH E. · 2005 to 2014
$2.5M
Pharmacological Inhibitors of Nedd4 ubiquitin ligase as anticancer therapeuticsR01GM115632 · NIGMS · UNIVERSITY OF HOUSTON · PI STATSYUK, ALEXANDER V · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM072656NIGMS NIH HHS R01 GM115632NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

Ring-between-ring (RBR) E3 ligases have been implicated in autoimmune disorders and neurodegenerative diseases. The functions of many RBR E3s are poorly defined, and their regulation is complex, involving post-translational modifications and allosteric regulation with other protein partners. The functional complexity of RBRs, coupled with the complexity of the native ubiquitination reaction that requires ATP and E1 and E2 enzymes, makes it difficult to study these ligases for basic research and therapeutic purposes. To address this challenge, we developed novel chemical probes, ubiquitin C-terminal fluorescein thioesters UbMES and UbFluor, to qualitatively and quantitatively assess the activity of the RBR E3 ligase PARKIN in a simple experimental setup and in real time using fluorescence polarization. First, we confirmed that PARKIN does not require an E2 enzyme for substrate ubiquitination, lysine selection, and polyubiquitin chain formation. Second, we confirmed that UbFluor quantitatively detects naturally occurring activation states of PARKIN caused by Ser

Indexed as

UbiquitinationAllosteric RegulationAnimalsFluorescence PolarizationHumansMolecular ProbesMutationPolyubiquitinUbiquitin-Protein LigasesMolecular Probesparkin proteinPolyubiquitinUbiquitin-Protein Ligasesenzymeenzyme mechanismparkinParkinson diseaseUbFluorubiquitin

Identifiers

PMID28710279
PMCPMC5633118
OpenAlexW2735492962

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.