Evidence map›Paper›PMID 26740872›Full record

ReviewTranslational neurodegeneration2016

Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment.

Lih-Shen Chin, Lian Li

Open access · goldAbstract readReview
In one paragraph

Review in Translational neurodegeneration, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Mitochondrial dysfunction in Parkinson's disease.Translational neurodegeneration · 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 1 institution in 1 country.

Lih-Shen ChinDepartment of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322 USA.
Lian LiDepartment of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322 USA.
Emory University · US

Funding

Udall Parkinson's Disease Center at Emory University: Circuitry to TherapyP50NS071669 · NINDS · EMORY UNIVERSITY · PI WICHMANN, THOMAS · 2010 to 2015
$6.8M
SIMPLE-regulated trafficking and peripheral neuropathyR01NS092343 · NINDS · EMORY UNIVERSITY · PI LI, LIAN · 2015 to 2019
$1.7M
Function and mechanism of a novel SUMO proteaseR01GM103613 · NIGMS · EMORY UNIVERSITY · PI LI, LIAN · 2013 to 2016
$1.2M
Molecular Analysis of TorsinA Function and DysfunctionR21NS093550 · NINDS · EMORY UNIVERSITY · PI CHIN, LIH-SHEN · 2015 to 2016
$424k
NIGMS NIH HHS R01 GM103613NINDS NIH HHS P50 NS071669NINDS NIH HHS R01 NS092343NINDS NIH HHS R21 NS093550
6 · The paper itself

Abstract

Parkinson's disease (PD) is the most common neurodegenerative movement disorder, characterized primarily by the loss of dopaminergic neurons in substantia nigra. The pathogenic mechanisms of PD remain unclear, and no effective therapy currently exists to stop neurodegeneration in this debilitating disease. The identification of mutations in mitochondrial serine/threonine kinase PINK1 or E3 ubiquitin-protein ligase parkin as the cause of autosomal recessive PD opens up new avenues for uncovering neuroprotective pathways and PD pathogenic mechanisms. Recent studies reveal that PINK1 translocates to the outer mitochondrial membrane in response to mitochondrial depolarization and phosphorylates ubiquitin at the residue Ser65. The phosphorylated ubiquitin serves as a signal for activating parkin and recruiting autophagy receptors to promote clearance of damaged mitochondria via mitophagy. Emerging evidence has begun to indicate a link between impaired ubiquitin phosphorylation-dependent mitophagy and PD pathogenesis and supports the potential of Ser65-phosphorylated ubiquitin as a biomarker for PD. The new mechanistic insights and phenotypic screens have identified multiple potential therapeutic targets for PD drug discovery. This review highlights recent advances in understanding ubiquitin phosphorylation in mitochondrial quality control and PD pathogenesis and discusses how these findings can be translated into novel approaches for PD diagnostic and therapeutic development.

Indexed as

Mitochondrial quality controlMitophagyParkinParkinson’s diseasePINK1Ubiquitin phosphorylationUbiquitin-protein ligase

Identifiers

PMID26740872
PMCPMC4702311
OpenAlexW2231953990

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.