Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 218,276,776 papers from all fields of science
Search
Sign In
Create Free Account
PARK2 protein, human
Known as:
Parkinson disease (autosomal recessive, juvenile) 2, parkin, human
, E3 Ubiquitin-Protein Ligase Parkin
, Parkinson Disease Protein 2
Expand
E3 ubiquitin-protein ligase parkin (465 aa, ~52 kDa) is encoded by the human PARK2 gene. This protein may play a role in the ubiquitination of…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
11 relations
Cell Death
Enzyme Gene
Homo sapiens
Ligase Gene
Expand
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2017
Highly Cited
2017
Mitochondrial E3 ligase MARCH5 regulates FUNDC1 to fine‐tune hypoxic mitophagy
Ziheng Chen
,
Lei Liu
,
+10 authors
Quan Chen
EMBO Reports
2017
Corpus ID: 160127
Mitophagy is an essential process for mitochondrial quality control and turnover. It is activated by two distinct pathways, one…
Expand
Highly Cited
2015
Highly Cited
2015
Mechanism of phospho-ubiquitin induced PARKIN activation
T. Wauer
,
M. Šimíček
,
A. Schubert
,
D. Komander
Nature
2015
Corpus ID: 3726607
The E3 ubiquitin ligase PARKIN (encoded by PARK2) and the protein kinase PINK1 (encoded by PARK6) are mutated in autosomal…
Expand
Highly Cited
2015
Highly Cited
2015
A Ubl/ubiquitin switch in the activation of Parkin
V. Sauvé
,
A. Lilov
,
+7 authors
K. Gehring
EMBO Journal
2015
Corpus ID: 1319203
Mutations in Parkin and PINK1 cause an inherited early‐onset form of Parkinson's disease. The two proteins function together in a…
Expand
Highly Cited
2015
Highly Cited
2015
Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains.
Xuan Ye
,
Xiaqin Sun
,
V. Starovoytov
,
Qian Cai
Human Molecular Genetics
2015
Corpus ID: 16081984
Accumulation of dysfunctional mitochondria is one of the hallmarks in Alzheimer's disease (AD). Mitophagy, a selective autophagy…
Expand
Highly Cited
2012
Highly Cited
2012
PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
K. Okatsu
,
T. Oka
,
+17 authors
N. Matsuda
Nature Communications
2012
Corpus ID: 16808052
Dysfunction of PINK1, a mitochondrial Ser/Thr kinase, causes familial Parkinson's disease (PD). Recent studies have revealed that…
Expand
Highly Cited
2011
Highly Cited
2011
PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Xinnan Wang
,
Dominic Winter
,
+7 authors
T. Schwarz
Cell
2011
Corpus ID: 18785232
Highly Cited
2010
Highly Cited
2010
Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells
D. Suen
,
Derek P. Narendra
,
Atsushi Tanaka
,
G. Manfredi
,
R. Youle
Proceedings of the National Academy of Sciences…
2010
Corpus ID: 12719308
Mitochondrial genomes with deleterious mutations can replicate in cells along with wild-type genomes in a state of heteroplasmy…
Expand
Highly Cited
2010
Highly Cited
2010
The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations
Sven Geisler
,
Kira M. Holmström
,
+5 authors
W. Springer
Autophagy
2010
Corpus ID: 34708826
Mitochondrial dysfunction is an early sign of many neurodegenerative diseases. Very recently, two Parkinson disease (PD…
Expand
Highly Cited
2008
Highly Cited
2008
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation.
YongSung Kim
,
Jeehye Park
,
+6 authors
Jongkyeong Chung
Biochemical and Biophysical Research…
2008
Corpus ID: 5169969
Highly Cited
2005
Highly Cited
2005
Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function.
Cheng Wang
,
H. Ko
,
+11 authors
K. Lim
Human Molecular Genetics
2005
Corpus ID: 25220711
Mutations in parkin are currently recognized as the most common cause of familial Parkinsonism. Emerging evidence also suggests…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE