Results 21 to 30 of about 15,787 (93)

HUWE1 E3 ligase promotes PINK1/PARKINindependent mitophagy by regulating AMBRA1 activation via IKKa [PDF]

open access: yes, 2018
The selective removal of undesired or damaged mitochondria by autophagy, known as mitophagy, is crucial for cellular homoeostasis, and prevents tumour diffusion, neurodegeneration and ageing.
A Criollo   +70 more
core   +4 more sources

PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control [PDF]

open access: yesCell Death & Disease, 2016
AbstractMitochondrial dysfunction has been linked to the pathogenesis of a large number of inherited diseases in humans, including Parkinson’s disease, the second most common neurodegenerative disorder. The Parkinson’s disease genes pink1 and parkin, which encode a mitochondrially targeted protein kinase, and an E3 ubiquitin ligase, respectively ...
Zhuang, Na   +3 more
openaire   +2 more sources

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking [PDF]

open access: yesJournal of Neurochemistry, 2011
Intramembrane proteolysis is a conserved mechanism that regulates a variety of cellular processes ranging from transcription control to signaling. In mitochondria, the inner membrane rhomboid protease PARL has been implicated in the control of life span and apoptosis by a so far uncharacterized mechanism.
Cathrin Meissner   +4 more
openaire   +3 more sources

Primary skin fibroblasts as a model of Parkinson's disease [PDF]

open access: yes, 2012
Parkinson's disease is the second most frequent neurodegenerative disorder. While most cases occur sporadic mutations in a growing number of genes including Parkin (PARK2) and PINK1 (PARK6) have been associated with the disease.
A Grunewald   +84 more
core   +1 more source

PINK1 phosphorylates ubiquitin predominantly in astrocytes [PDF]

open access: yesnpj Parkinson's Disease, 2019
AbstractLoss-of-function mutations in PINK1 are causally linked to recessively inherited Parkinson’s disease (PD), with marked loss of dopaminergic neurons in the substantia nigra that are required for normal movement. PINK1 is a nuclear-encoded mitochondrial-targeted kinase that phosphorylates a conserved serine at amino acid 65 (pS65) in ubiquitin as
Sandeep K. Barodia   +5 more
openaire   +2 more sources

Parkin function in Parkinson's disease [PDF]

open access: yes, 2018
Parkinson's disease (PD) is the second most common neurodegenerative disease, and is characterized by involuntary shaking, muscle rigidity, and the progressive loss of dopaminergic neurons.
Arkinson, Connor, Walden, Helen
core   +1 more source

Parkin interacts with Ambra1 to induce mitophagy [PDF]

open access: yes, 2011
Mutations in the gene encoding Parkin are a major cause of recessive Parkinson's disease. Recent work has shown that Parkin translocates from the cytosol to depolarized mitochondria and induces their autophagic removal (mitophagy). However, the molecular
Cornelissen, Tom   +6 more
core   +2 more sources

The PINK1/Parkin pathway: a mitochondrial quality control system? [PDF]

open access: yes, 2009
Significant insight into the mechanisms that contribute to dopaminergic neurodegeneration in Parkinson disease has been gained from the analysis of genes linked to rare heritable forms of parkinsonism such as PINK1 and parkin, loss-of-function mutations ...
Pallanck, L.J., Whitworth, A.J.
core   +1 more source

Proteinopathy, oxidative stress and mitochondrial dysfunction: cross talk in alzheimer’s disease and parkinson’s disease [PDF]

open access: yes, 2017
Alzheimer's disease and Parkinson's disease are two common neurodegenerative diseases of the elderly people that have devastating effects in terms of morbidity and mortality.
Chakrabarti, S.   +3 more
core   +3 more sources

Depletion of mitochondria in mammalian cells through enforced mitophagy [PDF]

open access: yes, 2016
Mitochondria are not only the 'powerhouse' of the cell; they are also involved in a multitude of processes that include calcium storage, the cell cycle and cell death.
Correia-Melo, Clara   +3 more
core   +1 more source

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