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Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1001/archneur.61.12.1898openalex-snapshot

Analysis of the PINK1 Gene in a Large Cohort of Cases With Parkinson Disease

inferredcites →https://doi.org/10.1002/ana.10417openalex-snapshot

Clinical and subclinical dopaminergic dysfunction in PARK6‐linked parkinsonism: An 18F‐dopa PET study

inferredcites →https://doi.org/10.1002/ana.20247openalex-snapshot

Homozygous PINK1 C‐terminus mutation causing early‐onset parkinsonism

inferredcites →https://doi.org/10.1002/ana.20251openalex-snapshot

Novel PINK1 mutations in early‐onset parkinsonism

inferredcites →https://doi.org/10.1002/ana.74openalex-snapshot

Positron emission tomographic analysis of the nigrostriatal dopaminergic system in familial Parkinsonism associated with mutations in the Parkin gene

inferredcites →https://doi.org/10.1002/humu.20089openalex-snapshot

Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson disease (PARK7)

inferredcites →https://doi.org/10.1002/mds.10034openalex-snapshot

Phenotypic characterisation of autosomal recessive PARK6‐linked parkinsonism in three unrelated Italian families

inferredcites →https://doi.org/10.1002/mds.10422openalex-snapshot

Clinical features and neuroimaging of PARK7‐linked parkinsonism

inferredcites →https://doi.org/10.1016/j.neuron.2004.07.012openalex-snapshot

Mitochondria and Dopamine

inferredcites →https://doi.org/10.1016/s0304-3835(03)00443-9openalex-snapshot

BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential

inferredcites →https://doi.org/10.1016/s0896-6273(02)01166-2openalex-snapshot

Pathways to Parkinsonism

inferredcites →https://doi.org/10.1016/s0960-9822(03)00165-9openalex-snapshot

An Interference Effect of Observed Biological Movement on Action

inferredcites →https://doi.org/10.1016/s0960-9822(03)00446-9openalex-snapshot

Neurodegeneration: How Does Parkin Prevent Parkinson's Disease?

inferredcites →https://doi.org/10.1038/33416openalex-snapshot

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

inferredcites →https://doi.org/10.1038/sj.onc.1204608openalex-snapshot

Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway

inferredcites →https://doi.org/10.1046/j.1471-4159.2003.01742.xopenalex-snapshot

Co‐ordinate transcriptional regulation of dopamine synthesis genes by α‐synuclein in human neuroblastoma cell lines

inferredcites →https://doi.org/10.1073/pnas.0402959101openalex-snapshot

The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization

inferredcites →https://doi.org/10.1074/jbc.273.40.25587openalex-snapshot

Import into Mitochondria, Folding and Retrograde Movement of Fumarase in Yeast

inferredcites →https://doi.org/10.1074/jbc.m301807200openalex-snapshot

Phosphorylation Enhances Mitochondrial Targeting of GSTA4-4 through Increased Affinity for Binding to Cytoplasmic Hsp70

inferredcites →https://doi.org/10.1074/jbc.m304272200openalex-snapshot

L166P Mutant DJ-1, Causative for Recessive Parkinson's Disease, Is Degraded through the Ubiquitin-Proteasome System

inferredcites →https://doi.org/10.1074/jbc.m309204200openalex-snapshot

Differential Effects of Parkinson's Disease-associated Mutations on Stability and Folding of DJ-1

inferredcites →https://doi.org/10.1093/bioinformatics/14.6.523openalex-snapshot

Homology modeling, model and software evaluation: three related resources.

inferredcites →https://doi.org/10.1093/brain/awf237openalex-snapshot

Progression of nigrostriatal dysfunction in a parkin kindred: an [18F]dopa PET and clinical study

inferredcites →https://doi.org/10.1093/brain/awh150openalex-snapshot

Striatal and cortical pre- and postsynaptic dopaminergic dysfunction in sporadic parkin-linked parkinsonism

inferredcites →https://doi.org/10.1126/sageke.2004.48.pe42openalex-snapshot

Mitochondrial Injury: A Hot Spot for Parkinsonism and Parkinson's Disease?

inferredcites →https://doi.org/10.1126/science.1077209openalex-snapshot

Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism

inferredcites →https://doi.org/10.1126/science.1096284openalex-snapshot

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

inferredcites →https://doi.org/10.1146/annurev.biochem.66.1.863openalex-snapshot

PROTEIN IMPORT INTO MITOCHONDRIA

inferredcites →https://doi.org/10.1212/01.wnl.0000142089.38301.8eopenalex-snapshot

PINK1 (PARK6) associated Parkinson disease in Ireland

inferredcites →https://doi.org/10.1212/wnl.55.6.877openalex-snapshot

[ 18 F]-dopa PET study in patients with juvenile-onset PD and parkin gene mutations

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1001/archneur.63.3.328openalex-snapshot

Implications of Genetics on the Diagnosis and Care of Patients With Parkinson Disease

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Mitochondria in Parkinson Disease

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Juvenile-Onset Parkinsonism as a Result of the First Mutation in the Adenosine Triphosphate Orientation Domain of PINK1

inferred← citeshttps://doi.org/10.1002/9781119017127.ch11openalex-snapshot

PINK1 as a Sensor for Mitochondrial Function

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Genetics of Parkinson's disease and parkinsonism

inferred← citeshttps://doi.org/10.1002/biof.1256openalex-snapshot

Phloretin‐induced cytoprotective effects on mammalian cells: A mechanistic view and future directions

inferred← citeshttps://doi.org/10.1002/embr.201337294openalex-snapshot

Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy

inferred← citeshttps://doi.org/10.1002/emmm.200900006openalex-snapshot

Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function

inferred← citeshttps://doi.org/10.1002/glia.22475openalex-snapshot

Pink1 deficiency attenuates astrocyte proliferation through mitochondrial dysfunction, reduced akt and increased p38 mapk activation, and downregulation of egfr

inferred← citeshttps://doi.org/10.1002/humu.21444openalex-snapshot

Phylogenetic and in silico structural analysis of the Parkinson disease‐related kinase PINK1

inferred← citeshttps://doi.org/10.1002/humu.22127openalex-snapshot

Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1)

inferred← citeshttps://doi.org/10.1002/jnr.23396openalex-snapshot

PARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neurons

inferred← citeshttps://doi.org/10.1002/jnr.23535openalex-snapshot

PINK1 phosphorylates transglutaminase 2 and blocks its proteasomal degradation

inferred← citeshttps://doi.org/10.1002/mc.22495openalex-snapshot

Polyubiquitination of apurinic/apyrimidinic endonuclease 1 by Parkin

inferred← citeshttps://doi.org/10.1002/mds.20841openalex-snapshot

Recessive Parkinson's disease

inferred← citeshttps://doi.org/10.1002/mds.21960openalex-snapshot

Late onset sporadic Parkinson's disease caused by PINK1 mutations: Clinical and functional study

inferred← citeshttps://doi.org/10.1002/mds.22713openalex-snapshot

DJ‐1, PINK1, and their effects on mitochondrial pathways

inferred← citeshttps://doi.org/10.1002/pauz.200600167openalex-snapshot

Die Parkinson‐Krankheit: Molekulare Mechanismen und Genetik

inferred← citeshttps://doi.org/10.1007/978-1-61779-824-5_12openalex-snapshot

Assays for Pten-Induced Novel Kinase 1 (PINK1) and Leucine-Rich Repeat Kinase 2 (LRRK2), Kinases Associated with Parkinson’s Disease

inferred← citeshttps://doi.org/10.1007/978-3-211-45295-0_29openalex-snapshot

Genetic causes of Parkinson’s disease: extending the pathway

inferred← citeshttps://doi.org/10.1007/978-3-319-13939-5_6openalex-snapshot

Control of Autophagy in Parkinson’s Disease

inferred← citeshttps://doi.org/10.1007/s00018-012-1004-7openalex-snapshot

PINK1 stimulates interleukin-1β-mediated inflammatory signaling via the positive regulation of TRAF6 and TAK1

inferred← citeshttps://doi.org/10.1007/s00018-014-1774-1openalex-snapshot

Neural stem cells in Parkinson’s disease: a role for neurogenesis defects in onset and progression

inferred← citeshttps://doi.org/10.1007/s00018-019-03203-4openalex-snapshot

Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond

inferred← citeshttps://doi.org/10.1007/s00401-011-0902-3openalex-snapshot

Parkin, PINK1 and mitochondrial integrity: emerging concepts of mitochondrial dysfunction in Parkinson’s disease

inferred← citeshttps://doi.org/10.1007/s00418-025-02415-zopenalex-snapshot

Secreted Frizzled-related proteins in animal development

inferred← citeshttps://doi.org/10.1007/s10048-015-0449-xopenalex-snapshot

Splicing: is there an alternative contribution to Parkinson’s disease?

inferred← citeshttps://doi.org/10.1007/s10495-010-0465-0openalex-snapshot

Mitochondrial dynamics, cell death and the pathogenesis of Parkinson’s disease

inferred← citeshttps://doi.org/10.1007/s10863-009-9253-3openalex-snapshot

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

inferred← citeshttps://doi.org/10.1007/s10863-009-9256-0openalex-snapshot

The mitochondrial kinase PINK1, stress response and Parkinson’s disease

inferred← citeshttps://doi.org/10.1007/s11910-011-0187-xopenalex-snapshot

Molecular Mechanisms of PINK1-Related Neurodegeneration

inferred← citeshttps://doi.org/10.1007/s12017-008-8044-zopenalex-snapshot

Mitochondrial Medicine for Aging and Neurodegenerative Diseases

inferred← citeshttps://doi.org/10.1007/s12017-013-8259-5openalex-snapshot

SUMO and Parkinson’s Disease

inferred← citeshttps://doi.org/10.1007/s12031-011-9687-zopenalex-snapshot

PINK1 Overexpression Protects Against C2-ceramide-Induced CAD Cell Death Through the PI3K/AKT Pathway

inferred← citeshttps://doi.org/10.1007/s12031-014-0479-0openalex-snapshot

Silencing of PINK1 Inhibits Insulin-Like Growth Factor-1-Mediated Receptor Activation and Neuronal Survival

inferred← citeshttps://doi.org/10.1007/s12031-025-02457-xopenalex-snapshot

Ubiquitin-Specific Protease 20 Promotes CCCP-Induced Mitophagy Through Deubiquitination and Stabilization of Serine/Threonine Protein Kinase PINK1

inferred← citeshttps://doi.org/10.1007/s12035-011-8226-9openalex-snapshot

Synaptic Protein Alterations in Parkinson’s Disease

inferred← citeshttps://doi.org/10.1007/s12035-016-0303-7openalex-snapshot

LRRK2 Expression Is Deregulated in Fibroblasts and Neurons from Parkinson Patients with Mutations in PINK1

inferred← citeshttps://doi.org/10.1007/s13273-015-0011-9openalex-snapshot

Gene panels and primers for next generation sequencing studies on neurodegenerative disorders

inferred← citeshttps://doi.org/10.1016/b978-0-12-369420-1.00100-1openalex-snapshot

Parkinson's Disease: Genomic Perspectives

inferred← citeshttps://doi.org/10.1016/b978-0-12-374028-1.00017-8openalex-snapshot

Genetic Models of Familial Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-374028-1.00043-9openalex-snapshot

The use of cell-free systems to characterize parkinson's disease-related gene products

inferred← citeshttps://doi.org/10.1016/b978-0-12-374105-9.00502-5openalex-snapshot

PARK6, PINK1

inferred← citeshttps://doi.org/10.1016/b978-0-12-374934-5.00054-4openalex-snapshot

Genetics and Genomics of Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-384878-9.00012-1openalex-snapshot

Genetic Mouse Models of Neurodegenerative Diseases

inferred← citeshttps://doi.org/10.1016/b978-0-12-385883-2.00005-9openalex-snapshot

Biology of Mitochondria in Neurodegenerative Diseases

inferred← citeshttps://doi.org/10.1016/b978-0-12-385883-2.00011-4openalex-snapshot

Molecular Insights into Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-802206-1.00042-8openalex-snapshot

Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-805120-7.00007-5openalex-snapshot

Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-815950-7.00011-4openalex-snapshot

Subcellular-specific alpha-synuclein in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/b978-0-443-15540-6.00002-1openalex-snapshot

The genetic basis of neurodegenerative disorders: Implications in Alzheimer's disease

inferred← citeshttps://doi.org/10.1016/b978-1-4160-6641-5.00002-7openalex-snapshot

Genetics of Parkinson's Disease—An Overview

inferred← citeshttps://doi.org/10.1016/b978-1-4160-6641-5.00005-2openalex-snapshot

PINK1 (PARK6) and Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/bs.irmvd.2021.08.003openalex-snapshot

PINK1: Multiple mechanisms of neuroprotection

inferred← citeshttps://doi.org/10.1016/j.bbadis.2009.01.012openalex-snapshot

A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.bbadis.2009.06.012openalex-snapshot

Tickled PINK1: Mitochondrial homeostasis and autophagy in recessive Parkinsonism

inferred← citeshttps://doi.org/10.1016/j.bbadis.2009.08.013openalex-snapshot

Mitochondrial dysfunction in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.bbadis.2010.07.014openalex-snapshot

New insights into the role of mitochondrial dysfunction and protein aggregation in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.bbadis.2011.03.007openalex-snapshot

PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.011openalex-snapshot

Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.05.002openalex-snapshot

Recent advances into the understanding of mitochondrial fission

inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.09.178openalex-snapshot

Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y

inferred← citeshttps://doi.org/10.1016/j.bbrc.2007.07.115openalex-snapshot

Corrigendum to “Identification of a novel PP2C-type mitochondrial phosphatase” [Biochem. Biophys. Res. Commun. 356 (2007) 38–44]

inferred← citeshttps://doi.org/10.1016/j.bbrc.2008.10.104openalex-snapshot

PINK1 controls mitochondrial localization of Parkin through direct phosphorylation

inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.02.090openalex-snapshot

Formation of parkin aggregates and enhanced PINK1 accumulation during the pathogenesis of Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.06.049openalex-snapshot

Assessing the prevalence of PINK1 genetic variants in South African patients diagnosed with early- and late-onset Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.05.041openalex-snapshot

A novel PGC-1α isoform in brain localizes to mitochondria and associates with PINK1 and VDAC

inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.10.086openalex-snapshot

The BAG2 protein stabilises PINK1 by decreasing its ubiquitination

inferred← citeshttps://doi.org/10.1016/j.biocel.2009.02.018openalex-snapshot

The role of PTEN-induced kinase 1 in mitochondrial dysfunction and dynamics

inferred← citeshttps://doi.org/10.1016/j.biocel.2020.105720openalex-snapshot

Bcl-xL inhibits PINK1/Parkin-dependent mitophagy by preventing mitochondrial Parkin accumulation

inferred← citeshttps://doi.org/10.1016/j.brainres.2007.09.056openalex-snapshot

Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.brainres.2010.06.005openalex-snapshot

R492X mutation in PTEN-induced putative kinase 1 induced cellular mitochondrial dysfunction and oxidative stress

inferred← citeshttps://doi.org/10.1016/j.canlet.2021.07.019openalex-snapshot

LACTB2 renders radioresistance by activating PINK1/Parkin-dependent mitophagy in nasopharyngeal carcinoma

inferred← citeshttps://doi.org/10.1016/j.cell.2013.07.030openalex-snapshot

A Neo-Substrate that Amplifies Catalytic Activity of Parkinson’s-Disease-Related Kinase PINK1

inferred← citeshttps://doi.org/10.1016/j.cellsig.2011.05.021openalex-snapshot

The regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery

inferred← citeshttps://doi.org/10.1016/j.celrep.2017.06.022openalex-snapshot

The Ubiquitination of PINK1 Is Restricted to Its Mature 52-kDa Form

inferred← citeshttps://doi.org/10.1016/j.celrep.2018.02.051openalex-snapshot

An Essential Role for ECSIT in Mitochondrial Complex I Assembly and Mitophagy in Macrophages

inferred← citeshttps://doi.org/10.1016/j.celrep.2021.109729openalex-snapshot

UQCRC1 Engages Cytochrome C for Neuronal Apoptotic Cell Death

inferred← citeshttps://doi.org/10.1016/j.celrep.2023.113260openalex-snapshot

A PINK1 input threshold arises from positive feedback in the PINK1/Parkin mitophagy decision circuit

inferred← citeshttps://doi.org/10.1016/j.conb.2007.04.010openalex-snapshot

Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.cub.2022.04.053openalex-snapshot

Myotubularin-related phosphatase 5 is a critical determinant of autophagy in neurons

inferred← citeshttps://doi.org/10.1016/j.ddmec.2005.11.015openalex-snapshot

Recent advances in our understanding of Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.devcel.2011.12.014openalex-snapshot

Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin

inferred← citeshttps://doi.org/10.1016/j.expneurol.2009.03.019openalex-snapshot

Mitochondrial dynamics in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.expneurol.2009.10.018openalex-snapshot

PINK1 mutations and differential effects on mitochondrial function

inferred← citeshttps://doi.org/10.1016/j.febslet.2010.02.016openalex-snapshot

PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy

inferred← citeshttps://doi.org/10.1016/j.febslet.2015.10.021openalex-snapshot

Understanding the susceptibility of dopamine neurons to mitochondrial stressors in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2008.02.008openalex-snapshot

Role of reactive oxygen species in the neurotoxicity of environmental agents implicated in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2012.12.008openalex-snapshot

Increase of oxidative stress by a novel PINK1 mutation, P209A

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2013.12.015openalex-snapshot

Mutant PINK1 upregulates tyrosine hydroxylase and dopamine levels, leading to vulnerability of dopaminergic neurons

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2025.03.010openalex-snapshot

5-Methoxytryptophan attenuates oxidative stress-induced downregulation of PINK1 and mitigates mitochondrial damage and apoptosis in cardiac myocytes

inferred← citeshttps://doi.org/10.1016/j.gene.2017.05.041openalex-snapshot

Structural annotation of Beta-1,4- N -acetyl galactosaminyltransferase 1 (B4GALNT1) causing Hereditary Spastic Paraplegia 26

inferred← citeshttps://doi.org/10.1016/j.gene.2023.147183openalex-snapshot

Analysis of the structural dynamics of the mutations in the kinase domain of PINK1 protein associated with Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.jchemneu.2010.11.004openalex-snapshot

Expression of PINK1 in the brain, eye and ear of mouse during embryonic development

inferred← citeshttps://doi.org/10.1016/j.jmb.2023.168090openalex-snapshot

Structural Mechanisms of Mitochondrial Quality Control Mediated by PINK1 and Parkin

inferred← citeshttps://doi.org/10.1016/j.mcn.2008.12.010openalex-snapshot

Molecular interaction between parkin and PINK1 in mammalian neuronal cells

inferred← citeshttps://doi.org/10.1016/j.mito.2009.06.001openalex-snapshot

Mitochondrial kinases in Parkinson’s disease: Converging insights from neurotoxin and genetic models

inferred← citeshttps://doi.org/10.1016/j.mito.2014.09.005openalex-snapshot

Potential roles of PINK1 for increased PGC-1α-mediated mitochondrial fatty acid oxidation and their associations with Alzheimer disease and diabetes

inferred← citeshttps://doi.org/10.1016/j.molcel.2017.09.022openalex-snapshot

Mitophagy Controls the Activities of Tumor Suppressor p53 to Regulate Hepatic Cancer Stem Cells

inferred← citeshttps://doi.org/10.1016/j.molmed.2006.09.007openalex-snapshot

Understanding the molecular causes of Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.molmed.2009.11.004openalex-snapshot

Pathogenesis of Parkinson's disease: emerging role of molecular chaperones

inferred← citeshttps://doi.org/10.1016/j.molmed.2010.11.002openalex-snapshot

Mitophagy: the latest problem for Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.mrrev.2013.09.001openalex-snapshot

Mutations that affect mitochondrial functions and their association with neurodegenerative diseases

inferred← citeshttps://doi.org/10.1016/j.nbd.2006.04.001openalex-snapshot

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

inferred← citeshttps://doi.org/10.1016/j.nbd.2007.07.010openalex-snapshot

PINK1 mutants associated with recessive Parkinson’s disease are defective in inhibiting mitochondrial release of cytochrome c

inferred← citeshttps://doi.org/10.1016/j.nbd.2011.08.034openalex-snapshot

PINK1 enhances insulin-like growth factor-1-dependent Akt signaling and protection against apoptosis

inferred← citeshttps://doi.org/10.1016/j.nbd.2013.10.021openalex-snapshot

Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression

inferred← citeshttps://doi.org/10.1016/j.nbd.2014.03.019openalex-snapshot

System-based approaches to decode the molecular links in Parkinson's disease and diabetes

inferred← citeshttps://doi.org/10.1016/j.nbd.2020.104948openalex-snapshot

Sequential screening nominates the Parkinson's disease associated kinase LRRK2 as a regulator of Clathrin-mediated endocytosis

inferred← citeshttps://doi.org/10.1016/j.nbd.2022.105721openalex-snapshot

Convergence of signalling pathways in innate immune responses and genetic forms of Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.neuint.2012.01.031openalex-snapshot

Targeting phosphatases as the next generation of disease modifying therapeutics for Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.neuint.2012.12.016openalex-snapshot

Neuroinflammation and oxidative stress: Co-conspirators in the pathology of Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/j.neulet.2006.09.080openalex-snapshot

A common A340T variant in PINK1 gene associated with late-onset Parkinson's disease in Chinese

inferred← citeshttps://doi.org/10.1016/j.neulet.2007.10.019openalex-snapshot

Cytoplasmic localization and proteasomal degradation of N-terminally cleaved form of PINK1

inferred← citeshttps://doi.org/10.1016/j.neulet.2009.02.016openalex-snapshot

Molecular hydrogen is protective against 6-hydroxydopamine-induced nigrostriatal degeneration in a rat model of Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.neulet.2015.08.021openalex-snapshot

Novel P-TEN-induced putative kinase 1 (PINK1) variant in Indian Parkinson’s disease patient

inferred← citeshttps://doi.org/10.1016/j.neures.2008.01.006openalex-snapshot

L347P PINK1 mutant that fails to bind to Hsp90/Cdc37 chaperones is rapidly degraded in a proteasome-dependent manner

inferred← citeshttps://doi.org/10.1016/j.neures.2020.03.009openalex-snapshot

Two sides of a coin: Physiological significance and molecular mechanisms for damage-induced mitochondrial localization of PINK1 and Parkin

inferred← citeshttps://doi.org/10.1016/j.neuroscience.2009.12.068openalex-snapshot

Enhanced vulnerability of PARK6 patient skin fibroblasts to apoptosis induced by proteasomal stress

inferred← citeshttps://doi.org/10.1016/j.parkreldis.2006.08.009openalex-snapshot

Novel features in a patient homozygous for the L347P mutation in the PINK1 gene

inferred← citeshttps://doi.org/10.1016/j.pep.2016.08.010openalex-snapshot

Expression and purification of the kinase domain of PINK1 in Pichia pastoris

inferred← citeshttps://doi.org/10.1016/j.pharmr.2026.100128openalex-snapshot

Targeting of kinases to treat neurodegenerative diseases

inferred← citeshttps://doi.org/10.1016/j.pneurobio.2011.03.005openalex-snapshot

Gene–environment interactions: Key to unraveling the mystery of Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.pnpbp.2017.12.006openalex-snapshot

Kinases in synaptic development and neurological diseases

inferred← citeshttps://doi.org/10.1016/j.scib.2019.04.033openalex-snapshot

Miro2 supplies a platform for Parkin translocation to damaged mitochondria

inferred← citeshttps://doi.org/10.1016/j.tins.2007.03.009openalex-snapshot

Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.tins.2014.03.004openalex-snapshot

Parkin and PINK1: much more than mitophagy

inferred← citeshttps://doi.org/10.1016/j.tips.2011.06.001openalex-snapshot

Genetic mutations and functions of PINK1

inferred← citeshttps://doi.org/10.1016/j.ydbio.2016.08.028openalex-snapshot

PINK1 is required for timely cell-type specific mitochondrial clearance during Drosophila midgut metamorphosis

inferred← citeshttps://doi.org/10.1016/j.ymeth.2025.08.014openalex-snapshot

AI-augmented prediction of high-risk PINK1 variants associated with Parkinson’s disease: integrating multilayered bioinformatics, MD simulation, and deep learning

inferred← citeshttps://doi.org/10.1016/j.ymthe.2025.03.030openalex-snapshot

Recent developments in gene therapy for Parkinson’s disease

inferred← citeshttps://doi.org/10.1016/s0079-6123(10)83003-1openalex-snapshot

Unravelling the role of defective genes

inferred← citeshttps://doi.org/10.1016/s0140-6736(06)68970-8openalex-snapshot

Mitochondrial disease

inferred← citeshttps://doi.org/10.1016/s1474-4422(07)70174-6openalex-snapshot

Deciphering the role of heterozygous mutations in genes associated with parkinsonism

inferred← citeshttps://doi.org/10.1016/s1474-4422(07)70327-7openalex-snapshot

Mitochondria in the aetiology and pathogenesis of Parkinson's disease

inferred← citeshttps://doi.org/10.1017/cbo9781139087711.007openalex-snapshot

Parkinsonism

inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00818openalex-snapshot

Hippocampal Proteomic Alteration in Triple Transgenic Mouse Model of Alzheimer’s Disease and Implication of PINK 1 Regulation in Donepezil Treatment

inferred← citeshttps://doi.org/10.1021/bi8019178openalex-snapshot

Pink1 Forms a Multiprotein Complex with Miro and Milton, Linking Pink1 Function to Mitochondrial Trafficking

inferred← citeshttps://doi.org/10.1021/cr800536yopenalex-snapshot

Manganese-Induced Dopaminergic Neurodegeneration: Insights into Mechanisms and Genetics Shared with Parkinson’s Disease

inferred← citeshttps://doi.org/10.1038/cddis.2016.396openalex-snapshot

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

inferred← citeshttps://doi.org/10.1038/cddis.2017.427openalex-snapshot

Pink1 interacts with α-synuclein and abrogates α-synuclein-induced neurotoxicity by activating autophagy

inferred← citeshttps://doi.org/10.1038/ejhg.2008.162openalex-snapshot

PTEN hamartoma tumor syndromes

inferred← citeshttps://doi.org/10.1038/mp.a003826.01openalex-snapshot

Pink1

inferred← citeshttps://doi.org/10.1038/ncb1644openalex-snapshot

The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1

inferred← citeshttps://doi.org/10.1038/ncb2012openalex-snapshot

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

inferred← citeshttps://doi.org/10.1038/ncomms2016openalex-snapshot

PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria

inferred← citeshttps://doi.org/10.1038/ncomms5514openalex-snapshot

PINK1 deficiency sustains cell proliferation by reprogramming glucose metabolism through HIF1

inferred← citeshttps://doi.org/10.1038/ncpneuro0126openalex-snapshot

The genetics of Parkinson disease: implications for neurological care

inferred← citeshttps://doi.org/10.1038/nrg1831openalex-snapshot

Genetics of Parkinson disease: paradigm shifts and future prospects

inferred← citeshttps://doi.org/10.1038/nrn1868openalex-snapshot

Expanding insights of mitochondrial dysfunction in Parkinson's disease

inferred← citeshttps://doi.org/10.1038/onc.2014.81openalex-snapshot

The Parkinson’s gene PINK1 regulates cell cycle progression and promotes cancer-associated phenotypes

inferred← citeshttps://doi.org/10.1038/s41388-024-03157-3openalex-snapshot

The tumor suppressor Parkin exerts anticancer effects through regulating mitochondrial GAPDH activity

inferred← citeshttps://doi.org/10.1038/s41392-025-02179-xopenalex-snapshot

Protein kinases in neurodegenerative diseases: current understandings and implications for drug discovery

inferred← citeshttps://doi.org/10.1038/s41418-018-0206-4openalex-snapshot

The circular RNA ACR attenuates myocardial ischemia/reperfusion injury by suppressing autophagy via modulation of the Pink1/ FAM65B pathway

inferred← citeshttps://doi.org/10.1038/s41419-018-1022-yopenalex-snapshot

Distinct multilevel misregulations of Parkin and PINK1 revealed in cell and animal models of TDP-43 proteinopathy

inferred← citeshttps://doi.org/10.1038/s41467-024-47623-8openalex-snapshot

Cdk8/CDK19 promotes mitochondrial fission through Drp1 phosphorylation and can phenotypically suppress pink1 deficiency in Drosophila

inferred← citeshttps://doi.org/10.1038/s41531-021-00258-8openalex-snapshot

Systematic analysis of PINK1 variants of unknown significance shows intact mitophagy function for most variants

inferred← citeshttps://doi.org/10.1038/s41598-018-26394-5openalex-snapshot

Mitophagy is required for brown adipose tissue mitochondrial homeostasis during cold challenge

inferred← citeshttps://doi.org/10.1038/s41598-020-58315-wopenalex-snapshot

Gemcitabine induces Parkin-independent mitophagy through mitochondrial-resident E3 ligase MUL1-mediated stabilization of PINK1

inferred← citeshttps://doi.org/10.1038/s44318-026-00789-xopenalex-snapshot

Transmembrane domain switching controls PINK1 import and fate in mitochondria

inferred← citeshttps://doi.org/10.1038/sj.cdd.4402160openalex-snapshot

Mitochondrial dysfunction in Parkinson's disease

inferred← citeshttps://doi.org/10.1038/sj.cdd.4402291openalex-snapshot

The mitochondrial serine protease HtrA2/Omi: an overview

inferred← citeshttps://doi.org/10.1038/srep01002openalex-snapshot

PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy

inferred← citeshttps://doi.org/10.1039/bk9781849731843-00113openalex-snapshot

Animal Models and the Pathogenesis of Parkinson's Disease

inferred← citeshttps://doi.org/10.1042/bj20080295openalex-snapshot

Protein stability and aggregation in Parkinson's disease

inferred← citeshttps://doi.org/10.1042/bj20141025openalex-snapshot

DJ1 represses glycolysis and cell proliferation by transcriptionally up-regulatingpink1

inferred← citeshttps://doi.org/10.1049/syb2.12043openalex-snapshot

Disrupted myelination network in the cingulate cortex of Parkinson's disease

inferred← citeshttps://doi.org/10.1073/pnas.0602493103openalex-snapshot

Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin

inferred← citeshttps://doi.org/10.1073/pnas.0604661103openalex-snapshot

Antioxidants protect PINK1 -dependent dopaminergic neurons in Drosophila

inferred← citeshttps://doi.org/10.1073/pnas.0705363105openalex-snapshot

Cytoplasmic Pink1 activity protects neurons from dopaminergic neurotoxin MPTP

inferred← citeshttps://doi.org/10.1073/pnas.0709336105openalex-snapshot

The PINK1/Parkin pathway regulates mitochondrial morphology

inferred← citeshttps://doi.org/10.1073/pnas.0802076105openalex-snapshot

Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress

inferred← citeshttps://doi.org/10.1073/pnas.0802814105openalex-snapshot

The kinase domain of mitochondrial PINK1 faces the cytoplasm

inferred← citeshttps://doi.org/10.1073/pnas.0803998105openalex-snapshot

The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila

inferred← citeshttps://doi.org/10.1073/pnas.0911187107openalex-snapshot

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

inferred← citeshttps://doi.org/10.1073/pnas.1216844110openalex-snapshot

RETRACTED: PINK1 regulates histone H3 trimethylation and gene expression by interaction with the polycomb protein EED/WAIT1

inferred← citeshttps://doi.org/10.1073/pnas.2534066123openalex-snapshot

ATP13A2 restrains macrophage NLRP3 inflammasome activation to repress neurodegeneration via modulating mitochondrial homeostasis

inferred← citeshttps://doi.org/10.1074/jbc.c114.580944openalex-snapshot

Lysine 63-linked Polyubiquitination Is Dispensable for Parkin-mediated Mitophagy

inferred← citeshttps://doi.org/10.1074/jbc.m109.066662openalex-snapshot

Perturbations in Mitochondrial Dynamics Induced by Human Mutant PINK1 Can Be Rescued by the Mitochondrial Division Inhibitor mdivi-1

inferred← citeshttps://doi.org/10.1074/jbc.m110.179390openalex-snapshot

A New Cytosolic Pathway from a Parkinson Disease-associated Kinase, BRPK/PINK1

inferred← citeshttps://doi.org/10.1074/jbc.m111.262287openalex-snapshot

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

inferred← citeshttps://doi.org/10.1074/jbc.m112.365700openalex-snapshot

Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode

inferred← citeshttps://doi.org/10.1074/jbc.m112.430801openalex-snapshot

Characterization of PINK1 (PTEN-induced Putative Kinase 1) Mutations Associated with Parkinson Disease in Mammalian Cells and Drosophila*

inferred← citeshttps://doi.org/10.1074/jbc.m113.467530openalex-snapshot

Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation

inferred← citeshttps://doi.org/10.1074/jbc.m113.509653openalex-snapshot

A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment

inferred← citeshttps://doi.org/10.1074/jbc.m114.620906openalex-snapshot

PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402

inferred← citeshttps://doi.org/10.1074/jbc.m114.624767openalex-snapshot

Nitric Oxide Induction of Parkin Translocation in PTEN-induced Putative Kinase 1 (PINK1) Deficiency

inferred← citeshttps://doi.org/10.1074/jbc.m117.787739openalex-snapshot

Reactive oxygen species trigger Parkin/PINK1 pathway–dependent mitophagy by inducing mitochondrial recruitment of Parkin

inferred← citeshttps://doi.org/10.1074/jbc.m117.803890openalex-snapshot

The ubiquitin E3 ligase CHIP promotes proteasomal degradation of the serine/threonine protein kinase PINK1 during staurosporine-induced cell death

inferred← citeshttps://doi.org/10.1074/jbc.m607216200openalex-snapshot

GTPase Activity of Mycobacterial FtsZ Is Impaired Due to Its Transphosphorylation by the Eukaryotic-type Ser/Thr Kinase, PknA

inferred← citeshttps://doi.org/10.1074/jbc.m808255200openalex-snapshot

Caenorhabditits elegans LRK-1 and PINK-1 Act Antagonistically in Stress Response and Neurite Outgrowth

inferred← citeshttps://doi.org/10.1074/jbc.m808515200openalex-snapshot

Loss of PINK1 Function Promotes Mitophagy through Effects on Oxidative Stress and Mitochondrial Fission

inferred← citeshttps://doi.org/10.1074/jbc.ra119.010474openalex-snapshot

Chronic treatment with the complex I inhibitor MPP+ depletes endogenous PTEN-induced kinase 1 (PINK1) via up-regulation of Bcl-2–associated athanogene 6 (BAG6)

inferred← citeshttps://doi.org/10.1080/00207454.2018.1557168openalex-snapshot

Protective mechanism of Wnt4 gene on Parkinson’s disease (PD) transgenic Drosophila

inferred← citeshttps://doi.org/10.1080/10409238.2018.1491525openalex-snapshot

New insights into the structure of PINK1 and the mechanism of ubiquitin phosphorylation

inferred← citeshttps://doi.org/10.1080/15548627.2016.1147667openalex-snapshot

Cytosolic PINK1 promotes the targeting of ubiquitinated proteins to the aggresome-autophagy pathway during proteasomal stress

inferred← citeshttps://doi.org/10.1080/15548627.2016.1277309openalex-snapshot

PINK1 and BECN1 relocalize at mitochondria-associated membranes during mitophagy and promote ER-mitochondria tethering and autophagosome formation

inferred← citeshttps://doi.org/10.1080/15548627.2024.2383145openalex-snapshot

Spautin-1 promotes PINK1-PRKN-dependent mitophagy and improves associative learning capability in an alzheimer disease animal model

inferred← citeshttps://doi.org/10.1083/jcb.200910140openalex-snapshot

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

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