Characterization of PINK1 (PTEN-induced Putative Kinase 1) Mutations Associated with Parkinson Disease in Mammalian Cells andDrosophila
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Characterization of PINK1 (PTEN-induced Putative Kinase 1) Mutations Associated with Parkinson Disease in Mammalian Cells andDrosophila
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 8, Pages 5660-5672
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-01-10
DOI
10.1074/jbc.m112.430801
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
- (2012) Andrew W Greene et al. EMBO REPORTS
- Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode
- (2012) Dorothea Becker et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Silent Information Regulator 2 (Sir2) and Forkhead Box O (FOXO) Complement Mitochondrial Dysfunction and Dopaminergic Neuron Loss inDrosophilaPTEN-induced Kinase 1 (PINK1) Null Mutant
- (2012) Hyongjong Koh et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Microtubule Affinity-regulating Kinase 2 (MARK2) Turns on Phosphatase and Tensin Homolog (PTEN)-induced Kinase 1 (PINK1) at Thr-313, a Mutation Site in Parkinson Disease
- (2012) Dorthe Matenia et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- PINK1 as a molecular checkpoint in the maintenance of mitochondrial function and integrity
- (2012) Hyongjong Koh et al. MOLECULES AND CELLS
- PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
- (2012) Kei Okatsu et al. Nature Communications
- PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
- (2012) C. Kondapalli et al. Open Biology
- Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria
- (2012) Song Liu et al. PLoS Genetics
- PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
- (2011) Xinnan Wang et al. CELL
- Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
- (2011) Nickie C. Chan et al. HUMAN MOLECULAR GENETICS
- Phylogenetic and in silico structural analysis of the Parkinson disease-related kinase PINK1
- (2011) Fernando Cardona et al. HUMAN MUTATION
- Parkin Mediates Proteasome-dependent Protein Degradation and Rupture of the Outer Mitochondrial Membrane
- (2011) Saori R. Yoshii et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
- (2011) Cathrin Meissner et al. JOURNAL OF NEUROCHEMISTRY
- Mitochondrial Parkin Recruitment Is Impaired in Neurons Derived from Mutant PINK1 Induced Pluripotent Stem Cells
- (2011) P. Seibler et al. JOURNAL OF NEUROSCIENCE
- Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations
- (2011) H. I. Woodroof et al. Open Biology
- PINK1 cleavage at position A103 by the mitochondrial protease PARL
- (2010) Emma Deas et al. HUMAN MOLECULAR GENETICS
- Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
- (2010) Karen Nuytemans et al. HUMAN MUTATION
- A New Cytosolic Pathway from a Parkinson Disease-associated Kinase, BRPK/PINK1
- (2010) Hitoshi Murata et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
- (2010) Atsushi Tanaka et al. JOURNAL OF CELL BIOLOGY
- Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
- (2010) Seok Min Jin et al. JOURNAL OF CELL BIOLOGY
- PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
- (2010) Sven Geisler et al. NATURE CELL BIOLOGY
- PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
- (2010) Derek P. Narendra et al. PLOS BIOLOGY
- The Loss of PGAM5 Suppresses the Mitochondrial Degeneration Caused by Inactivation of PINK1 in Drosophila
- (2010) Yuzuru Imai et al. PLoS Genetics
- Pink1 Forms a Multiprotein Complex with Miro and Milton, Linking Pink1 Function to Mitochondrial Trafficking†
- (2009) Andreas Weihofen et al. BIOCHEMISTRY
- PINK1 function in health and disease
- (2009) Emma Deas et al. EMBO Molecular Medicine
- Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF- B signaling
- (2009) D. Sha et al. HUMAN MOLECULAR GENETICS
- Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation
- (2009) A. Kathrin Lutz et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Parkin and PINK1 mutations in early-onset Parkinson's disease: comprehensive screening in publicly available cases and control
- (2009) J Brooks et al. JOURNAL OF MEDICAL GENETICS
- PINK1 Defect Causes Mitochondrial Dysfunction, Proteasomal Deficit and α-Synuclein Aggregation in Cell Culture Models of Parkinson's Disease
- (2009) Wencheng Liu et al. PLoS One
- Silencing of PINK1 Expression Affects Mitochondrial DNA and Oxidative Phosphorylation in DOPAMINERGIC Cells
- (2009) Matthew E. Gegg et al. PLoS One
- Mitochondrial Alterations in PINK1 Deficient Cells Are Influenced by Calcineurin-Dependent Dephosphorylation of Dynamin-Related Protein 1
- (2009) Anna Sandebring et al. PLoS One
- PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
- (2009) C. Vives-Bauza et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Mutation Analysis of the PINK1 Gene in 391 Patients With Parkinson Disease
- (2008) Ryuya Kumazawa et al. ARCHIVES OF NEUROLOGY
- PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
- (2008) Yongsung Kim et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process
- (2008) Jeehye Park et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin
- (2008) A. J. Whitworth et al. Disease Models & Mechanisms
- Characterization of PINK1 processing, stability, and subcellular localization
- (2008) William Lin et al. JOURNAL OF NEUROCHEMISTRY
- Clinical and molecular characterisation of a Parkinson family with a novel PINK1 mutation
- (2008) J. Prestel et al. JOURNAL OF NEUROLOGY
- Mitochondria in the aetiology and pathogenesis of Parkinson's disease
- (2008) Anthony HV Schapira LANCET NEUROLOGY
- L347P PINK1 mutant that fails to bind to Hsp90/Cdc37 chaperones is rapidly degraded in a proteasome-dependent manner
- (2008) Yasuhiro Moriwaki et al. NEUROSCIENCE RESEARCH
- PINK1 Is Necessary for Long Term Survival and Mitochondrial Function in Human Dopaminergic Neurons
- (2008) Alison Wood-Kaczmar et al. PLoS One
- The kinase domain of mitochondrial PINK1 faces the cytoplasm
- (2008) C. Zhou et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
- (2008) Y. Yang et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The PINK1/Parkin pathway regulates mitochondrial morphology
- (2008) A. C. Poole et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
- (2008) H. Deng et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now