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Journal of Neurochemistry, ISSN 0022-3042, 08/2011, Volume 118, Issue 4, pp. 636 - 645
J. Neurochem. (2011) 118, 636–645. Mutations in the parkin gene cause early‐onset, autosomal recessive Parkinson’s disease. Parkin functions as an E3 ubiquitin... 
Mfn1 | mitophagy | parkin | ubiquitination | mitochondria | Parkinson’s disease | Parkinson's disease | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN LIGASE | PATHOLOGY | NEUROSCIENCES | DROSOPHILA | DEGENERATION | PINK1 | MUTANTS | PATHWAY | PROTEASOME | MORPHOLOGY | Cell Fractionation | Immunoprecipitation | Humans | Membrane Transport Proteins - drug effects | Mitochondrial Proteins - genetics | Ubiquitin-Protein Ligases - physiology | Mitochondrial Proteins - drug effects | Mitochondrial Membrane Transport Proteins | Mutation - physiology | Proteasome Endopeptidase Complex - drug effects | Ubiquitination - drug effects | Membrane Transport Proteins - genetics | Mitochondrial Proteins - metabolism | Plasmids - genetics | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Parkinson Disease - genetics | Mutation - genetics | Blotting, Western | GTP Phosphohydrolases - drug effects | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Cell Line, Tumor | Membrane Proteins - drug effects | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | Ubiquitination - genetics | Ubiquitin | Mitochondrial DNA | Ligases | Analysis | Neurochemistry | Mitochondria | Autophagy | Substrates | Parkinsons disease
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 4, p. e18568
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene cause late-onset, autosomal dominant familial Parkinson's disease (PD) and also contribute to... 
DISEASE-ASSOCIATED MUTATIONS | KINASE-ACTIVITY | R1441C MUTATION | LOCALIZATION | GENE LRRK2 | MODELS | MULTIDISCIPLINARY SCIENCES | NEURODEGENERATION | ALPHA-SYNUCLEIN | GTP-BINDING | PARKINSONS-DISEASE | Mesencephalon - metabolism | Humans | Mice, Transgenic | Mutant Proteins - metabolism | Chromatography, High Pressure Liquid | Motor Activity | Autophagy | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Protein Transport | Behavior, Animal | Neurites - pathology | Animals | Neurites - ultrastructure | Amino Acid Substitution - genetics | Mice | Dopamine - metabolism | Organ Culture Techniques | Protein-Serine-Threonine Kinases - metabolism | Mesencephalon - pathology | Mesencephalon - ultrastructure | Neurons | Genetic aspects | Neurosciences | Parkinson's disease | Parkinsons disease | Biology | Leucine | Kinases | Complexity | Engineering | Mitochondria | Neurodegeneration | Transgenic animals | Rodents | Genetics | Life sciences | Degeneration | LRRK2 protein | Age | Movement disorders | Dopamine receptors | Medical research | Dopamine | Neurodegenerative diseases | Research & development--R&D | Abnormalities | Transgenic mice | Gene expression | Mutants | Medicine | Neurology | Pathology | Brain research | Microscopy | Stem cells | Mutation | Alzheimers disease | Neurotransmission | Cancer | Research & development | R&D
Journal Article
Neuron, ISSN 0896-6273, 01/2015, Volume 85, Issue 1, pp. 76 - 87
Parkinson’s disease (PD) is a common neurodegenerative disorder. Functional interactions between some PD genes, like and , have been identified, but whether... 
Parkinson's disease | Yeast | Disease | Neurodegenerative diseases | Genomics | Genes | Transgenic mice | Synuclein | Experiments | Proteins | Neurodegeneration | Protein folding | PTEN-induced putative kinase | Parkin protein | Mutation | Movement disorders
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 04/2012, Volume 21, Issue 8, pp. 1725 - 1743
Mutations in the ATP13A2 gene (PARK9, OMIM 610513) cause autosomal recessive, juvenile-onset Kufor-Rakeb syndrome and early-onset parkinsonism. ATP13A2 is an... 
CELLS | DEMENTIA | PROTEIN | CHAPERONE-MEDIATED AUTOPHAGY | P-TYPE ATPASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | PYRAMIDAL DEGENERATION | KUFOR-RAKEB SYNDROME | ALPHA-SYNUCLEIN | MUTATIONS | PARKINSONS-DISEASE | Lewy Bodies - ultrastructure | Pyramidal Cells - metabolism | Neurites - physiology | Proton-Translocating ATPases - immunology | Substantia Nigra - pathology | Calcium - metabolism | Humans | Substantia Nigra - metabolism | Adenosine Triphosphatases - immunology | Autophagy | Mitochondria - ultrastructure | Brain - metabolism | Proton-Translocating ATPases - metabolism | Neurons - ultrastructure | RNA Interference | Neurites - ultrastructure | Dopaminergic Neurons - metabolism | Cytoplasmic Vesicles - metabolism | Neurons - physiology | Dopaminergic Neurons - physiology | Membrane Proteins - metabolism | Neurons - metabolism | Parkinson Disease - metabolism | Parkinson Disease - pathology | Cells, Cultured | Adenosine Triphosphatases - metabolism | Rats | Membrane Proteins - immunology | Animals | Brain - pathology | Mice | Hydrogen-Ion Concentration | Brain | Cadmium | Neuroprotection | Basal ganglia | Calcium (intracellular) | Dopamine | Mesencephalon | Neurodegenerative diseases | Axonogenesis | Neurons | Substantia nigra | Adenosinetriphosphatase | Cortex | pH effects | Lewy bodies | Mitochondria | Pyramidal cells | Kinetics | Movement disorders
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2012, Volume 7, Issue 6, p. e39942
Mutations in the ATP13A2 gene (PARK9) cause autosomal recessive, juvenile-onset Kufor-Rakeb syndrome (KRS), a neurodegenerative disease characterized by... 
CELLS | HOMEOSTASIS | TRANSPORT | MULTIDISCIPLINARY SCIENCES | DISEASE | DEGRADATION | KUFOR-RAKEB SYNDROME | ALPHA-SYNUCLEIN | PROTEINS | Intracellular Membranes - enzymology | Humans | Cerebral Cortex - pathology | Protein Transport - drug effects | Endosomes - metabolism | Mutation, Missense - genetics | Proteolysis - drug effects | Lysosomes - metabolism | Proteasome Endopeptidase Complex - drug effects | Proton-Translocating ATPases - genetics | Endoplasmic Reticulum - drug effects | Endosomes - drug effects | HEK293 Cells | Female | Parkinsonian Disorders - genetics | Cerebral Cortex - drug effects | Neurites - drug effects | Endoplasmic Reticulum - enzymology | Lysosomes - drug effects | Rats | Parkinsonian Disorders - enzymology | Neurites - metabolism | Rats, Sprague-Dawley | Homozygote | Animals | Metals, Heavy - toxicity | Protein Stability - drug effects | Age of Onset | Cell Line, Tumor | Intracellular Membranes - drug effects | Proteasome Endopeptidase Complex - metabolism | Proteins | Brain | Nervous system diseases | Parkinson's disease | Analysis | Genetic aspects | Heavy metals | Adenosine triphosphatase | Oxidative stress | Membranes | Basal ganglia | Laboratories | Toxicity | Neurotoxicity | Missense mutation | Bioenergetics | Transgenic animals | Rodents | Life sciences | Localization | Age | Movement disorders | Sensitizing | Cadmium | Stability | Neurons | Axonogenesis | Cortex | Central nervous system diseases | Mutants | Brain research | Morphology | Nickel | Mutation | Endoplasmic reticulum | Viability
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e47784
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are a common cause of autosomal dominant familial Parkinson's disease (PD). LRRK2 encodes a... 
DISEASE-ASSOCIATED MUTATIONS | KINASE-ACTIVITY | ACTIVATION | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | LINK | GTP-BINDING | DOPAMINERGIC NEURON | PARKINSONS-DISEASE | Phosphorylation | Humans | Male | Phosphoproteins - metabolism | Brain - metabolism | Multiprotein Complexes - metabolism | HEK293 Cells | Aged, 80 and over | Female | Mammals - metabolism | Parkinson Disease - pathology | Protein-Serine-Threonine Kinases - genetics | Rats | Mutation - genetics | Subcellular Fractions - metabolism | Phosphothreonine - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Animals | Carrier Proteins - metabolism | Parkinson Disease - enzymology | Brain - pathology | Aged | Mice | Protein Processing, Post-Translational | Adaptor Proteins, Signal Transducing - metabolism | Brain | Usage | Parkinson's disease | Gene mutations | Leucine zipper | Genetic aspects | Research | Complex formation | Toxicity | Parkinsons disease | Leucine | Kinases | Mammalian cells | Proteins | Neurotoxicity | Enzymatic activity | Neurodegeneration | Rodents | Animal tissues | Post-translation | Physiology | Life sciences | LRRK2 protein | Localization | Coordination compounds | Movement disorders | Neurodegenerative diseases | Drosophila | Transgenic mice | Mammals | Substrates | Neurology | Insects | Mutation | Initiation factor eIF-4E | Guanosinetriphosphatase
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 04/2014, Volume 23, Issue 8, pp. 2055 - 2077
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 2014, Volume 23, Issue 18, pp. 4887 - 4905
Journal Article