Evidence map›Paper›PMID 22527713›Full record

ReviewCellular and molecular life sciences : CMLS2012

Regulation of Parkin E3 ubiquitin ligase activity.

Helen Walden, R Julio Martinez-Torres

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
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  9. PICK1 inhibits the E3 ubiquitin ligase activity of Parkin and reduces its neuronal protective effect.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  19. Article
  20. Specificity and disease in the ubiquitin system.Biochemical Society transactions · 2016
    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

2 authors at 2 institutions in 1 country.

Helen WaldenProtein Structure and Function Laboratory, London Research Institute of Cancer Research UK, Lincoln's Inn Fields Laboratories, London, UK. Helen.Walden@cancer.org.uk
R Julio Martinez-Torres
Cancer Research UK · GBInstitute of Cancer Research · GB

Funding

Cancer Research UK
6 · The paper itself

Abstract

Parkin is an E3 ubiquitin ligase mutated in autosomal recessive juvenile Parkinson's disease. In addition, it is a putative tumour suppressor, and has roles outside its enzymatic activity. It is critical for mitochondrial clearance through mitophagy, and is an essential protein in most eukaryotes. As such, it is a tightly controlled protein, regulated through an array of external interactions with multiple proteins, posttranslational modifications including phosphorylation and S-nitrosylation, and self-regulation through internal associations. In this review, we highlight some of the recent studies into Parkin regulation and discuss future challenges for gaining a full molecular understanding of the regulation of Parkin E3 ligase activity.

Indexed as

HumansMitochondriaParkinson DiseaseParkinsonian DisordersProtein KinasesProtein Processing, Post-TranslationalPTEN-Induced Putative KinaseUbiquitin-Protein Ligasesparkin proteinProtein KinasesPTEN-Induced Putative KinaseUbiquitin-Protein Ligases

Identifiers

PMID22527713
PMCPMC11115052
OpenAlexW2074269616

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.