Evidence map›Paper›PMID 39221915›Full record

ArticleeLife2024

Additional feedforward mechanism of Parkin activation via binding of phospho-UBL and RING0 in

Dipti Ranjan Lenka, Shakti Virendra Dahe, Odetta Antico, Pritiranjan Sahoo, Alan R Prescott, Miratul M K Muqit, Atul Kumar

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Ubiquitin Proteasome System Components, RAD23A and USP13, Modulate TDP-43 Solubility and Neuronal Toxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  3. Review
  4. Targeting mitophagy in neurodegenerative diseases.Nature reviews. Drug discovery · 2025
    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

7 authors.

Dipti Ranjan LenkaDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, India.ORCID https://orcid.org/0009-0009-8890-8331
Shakti Virendra DaheDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, India.ORCID https://orcid.org/0009-0009-8909-240X
Odetta AnticoMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Pritiranjan SahooDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, India.
Alan R PrescottDivision of Cell Signalling and Immunology, Dundee Imaging Facility, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID https://orcid.org/0000-0002-0747-7317
Miratul M K MuqitMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID https://orcid.org/0000-0001-9733-2404
Atul KumarDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal, India.ORCID https://orcid.org/0000-0003-4675-6623

Funding

IISER Bhopal AKInnovative Young Biotechnologist Award DBT/12/IYBAl2019/03Michael J Fox Foundation M.M.K.M.PMRF 0403018Ramalingaswami Re-entry Fellowship DBT/RLF/Re-entry/42/2019SERB SERB/F/6520/2019-2020Wellcome TrustWellcome Trust Senior Research Fellowship in Clinical Science 10.35802/210753
6 · The paper itself

Abstract

Loss-of-function Parkin mutations lead to early-onset of Parkinson's disease. Parkin is an auto-inhibited ubiquitin E3 ligase activated by dual phosphorylation of its ubiquitin-like (Ubl) domain and ubiquitin by the PINK1 kinase. Herein, we demonstrate a competitive binding of the phospho-Ubl and RING2 domains towards the RING0 domain, which regulates Parkin activity. We show that phosphorylated Parkin can complex with native Parkin, leading to the activation of autoinhibited native Parkin in

Indexed as

Protein BindingUbiquitin-Protein LigasesCrystallography, X-RayHumansKineticsModels, MolecularPhosphorylationUbiquitinparkin proteinUbiquitinUbiquitin-Protein LigasesE. colimolecular biophysicsParkin E3 ligaseParkinson's diseasestructural biologystructureUbiquitin

Identifiers

PMID39221915
PMCPMC11368401

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.