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1. Full Text Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson's disease
by Burbulla, LF and Song, PP and Mazzulli, JR and Zampese, E and Wong, YC and Jeon, S and Santos, DP and Blanz, J and Obermaier, CD and Strojny, C and Savas, JN and Kiskinis, E and Zhuang, XX and Kruger, R and Surmeier, DJ and Krainc, D
SCIENCE, ISSN 0036-8075, 09/2017, Volume 357, Issue 6357, pp. 1255 - 1255
Mitochondrial and lysosomal dysfunction have been implicated in substantia nigra dopaminergic neurodegeneration in Parkinson's disease (PD), but how these... 
GLUCOCEREBROSIDASE | PACEMAKING | DJ-1 | ALPHA-SYNUCLEIN | SUBSTANTIA-NIGRA | MULTIDISCIPLINARY SCIENCES | Mitochondria - enzymology | Mesencephalon - metabolism | Humans | Protein Deglycase DJ-1 - genetics | Substantia Nigra - metabolism | Melanins - metabolism | Glucosylceramidase - deficiency | Lysosomes - metabolism | Dopaminergic Neurons - metabolism | Tacrolimus - pharmacology | Parkinson Disease - metabolism | Dopamine - metabolism | Disease Models, Animal | Substantia Nigra - enzymology | Cell Line | Calcineurin Inhibitors - pharmacology | Oxidation-Reduction | Mesencephalon - enzymology | Mitochondria - metabolism | Antioxidants - pharmacology | Mitochondria - drug effects | Parkinson Disease - genetics | Mice, Knockout | Animals | Parkinson Disease - enzymology | Mice | Oxidative Stress - drug effects | alpha-Synuclein - metabolism | Oxidation-reduction reaction | Development and progression | Mitochondria | Dopamine | Parkinson's disease | Health aspects | Brain | Energy metabolism | Animal models | Target recognition | Mesencephalon | Pathogenesis | Substantia nigra | Parkinsons disease | Lysosomes | Synuclein | Accumulation | Pathways | Enzymatic activity | Neurodegeneration | Rodents | Oxidation | Degeneration | Species | Movement disorders | Dopamine receptors | Neurodegenerative diseases | Neurons | Medical treatment | Metabolism | Patients | Glucosylceramidase | Index Medicus
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2. Full Text Defects in trafficking bridge Parkinson's disease pathology and genetics
by Abeliovich, Asa and Gitler, Aaron D
Nature, ISSN 0028-0836, 11/2016, Volume 539, Issue 7628, pp. 207 - 216
Parkinson's disease is a debilitating, age-associated movement disorder. A central aspect of the pathophysiology of Parkinson's disease is the progressive... 
INTELLECTUAL DISABILITY | DOPAMINE NEURONS | MEDIATED AUTOPHAGY | NEUROTRANSMITTER RELEASE | LYSOSOMAL DYSFUNCTION | SYNUCLEIN ACTIVATES MICROGLIA | MULTIDISCIPLINARY SCIENCES | DAMAGED MITOCHONDRIA | ALPHA-SYNUCLEIN | GENOME-WIDE ASSOCIATION | GAUCHER-DISEASE | Parkinson Disease - therapy | Inflammation - pathology | Neurons - pathology | Prions - metabolism | Glucosylceramidase - genetics | Parkinson Disease - pathology | Synaptic Vesicles - metabolism | Humans | Glucosylceramidase - metabolism | Parkinson Disease - genetics | Molecular Targeted Therapy | Endocytosis | Inflammation - metabolism | Animals | Lysosomes - metabolism | Models, Biological | Biological Transport - genetics | Neurons - metabolism | Parkinson Disease - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 - metabolism | alpha-Synuclein - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 - genetics | Development and progression | Genetic aspects | Parkinson's disease | Proteins | Pathology | Dopamine | Pathogenesis | Neurons | Genes | Parkinsons disease | Genetics | Genomes | Mutation | Kinases
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3. Full Text Characterization of Gaucher disease bone marrow mesenchymal stromal cells reveals an altered inflammatory secretome
by Campeau, Philippe M and Rafei, Moutih and Boivin, Marie-Noëlle and Sun, Ying and Grabowski, Gregory A and Galipeau, Jacques
Blood, ISSN 0006-4971, 2009, Volume 114, Issue 15, pp. 3181 - 3190
Gaucher disease causes pathologic skeletal changes that are not fully explained. Considering the important role of mesenchymal stromal cells (MSCs) in bone... 
STEM-CELLS | PLASMA | TARTRATE-RESISTANT | STORAGE DISEASES | MYELOMA CELLS | LIPID RAFTS | CHEMOKINE RECEPTOR | GENE-EXPRESSION | RESISTANT ACID-PHOSPHATASE | MICE | HEMATOLOGY | Interleukin-8 - genetics | Glucosylceramidase - genetics | Dinoprostone - biosynthesis | Stromal Cells - pathology | Humans | Middle Aged | Male | Gaucher Disease - pathology | Mutation, Missense | Cholesterol - genetics | Cyclooxygenase 2 - biosynthesis | Lysosomes - metabolism | Cyclooxygenase 2 - genetics | Inflammation Mediators - metabolism | Female | Lysosomes - pathology | Chemokine CCL2 - metabolism | Interleukin-8 - metabolism | Glucosylceramides - genetics | Inositol - pharmacology | Gaucher Disease - metabolism | Osteocytes - metabolism | Dinoprostone - genetics | Interleukin-8 - biosynthesis | Stromal Cells - metabolism | Bone Marrow Cells - pathology | Cells, Cultured | Enzyme Inhibitors - pharmacology | Chemokine CCL2 - genetics | Up-Regulation - genetics | Glucosylceramidase - metabolism | Cholesterol - metabolism | Inositol - analogs & derivatives | Adipocytes - pathology | Glucosylceramidase - antagonists & inhibitors | Dinoprostone - metabolism | Up-Regulation - drug effects | Gaucher Disease - genetics | Cell Differentiation - drug effects | Adipocytes - metabolism | Cyclooxygenase 2 - metabolism | Chemokine CCL2 - biosynthesis | Osteocytes - pathology | Glucosylceramides - metabolism | Bone Marrow Cells - metabolism | Amino Acid Substitution | Hematopoiesis and Stem Cells
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4. Full Text LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase
by Reczek, David and Schwake, Michael and Schröder, Jenny and Hughes, Heather and Blanz, Judith and Jin, Xiaoying and Brondyk, William and Van Patten, Scott and Edmunds, Tim and Saftig, Paul
Cell, ISSN 0092-8674, 2007, Volume 131, Issue 4, pp. 770 - 783
β-glucocerebrosidase, the enzyme defective in Gaucher disease, is targeted to the lysosome independently of the mannose-6-phosphate receptor.... 
CELLBIO | HUMDISEASE | CYTOPLASMIC TAIL | CELLS | IN-VITRO | PROTEIN | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | MANNOSE 6-PHOSPHATE RECEPTOR | BINDING | MOTIF | FIBROBLASTS | GAUCHER-DISEASE | CELL BIOLOGY | Glucosylceramidase - genetics | CD36 Antigens - genetics | Mannosephosphates - genetics | Humans | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Lysosomes - metabolism | CD36 Antigens - metabolism | Fibroblasts - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Cell Line | Lysosome-Associated Membrane Glycoproteins - metabolism | Gaucher Disease - metabolism | Protein Structure, Secondary | Glucosylceramidase - metabolism | Recombinant Proteins - genetics | Macrophages - cytology | Protein Transport | Macrophages - metabolism | Sequence Alignment | Animals | Mannosephosphates - metabolism | Lysosome-Associated Membrane Glycoproteins - genetics | Protein Binding | Fibroblasts - cytology | Mice
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5. Full Text Gaucher Disease Glucocerebrosidase and α-Synuclein Form a Bidirectional Pathogenic Loop in Synucleinopathies
by Mazzulli, Joseph R and Xu, You-Hai and Sun, Ying and Knight, Adam L and McLean, Pamela J and Caldwell, Guy A and Sidransky, Ellen and Grabowski, Gregory A and Krainc, Dimitri
Cell, ISSN 0092-8674, 2011, Volume 146, Issue 1, pp. 37 - 52
Parkinson's disease (PD), an adult neurodegenerative disorder, has been clinically linked to the lysosomal storage disorder Gaucher disease (GD), but the... 
CATECHOLS | ENZYME | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATIONS | MOUSE MODELS | DEFICIENCY | OLIGOMERS | PARKINSONS-DISEASE | CELL BIOLOGY | Gaucher Disease - metabolism | Humans | Cells, Cultured | Glucosylceramidase - metabolism | Gaucher Disease - pathology | Brain - metabolism | Feedback, Physiological | Animals | Lysosomes - metabolism | Mice | Neurons - metabolism | Glucosylceramides - metabolism | alpha-Synuclein - metabolism | Disease Models, Animal | Index Medicus
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6. Full Text Neuronal accumulation of glucosylceramide in a mouse model of neuronopathic gaucher disease leads to neurodegeneration
by Farfel-Becker, Tamar and Vitner, Einat B and Kelly, Samuel L and Bame, Jessica R and Duan, Jingjing and Shinder, Vera and Merrill Jr, Alfred H and Dobrenis, Kostantin and Futerman, Anthony H
Human Molecular Genetics, ISSN 0964-6906, 02/2014, Volume 23, Issue 4, pp. 843 - 854
Gaucher disease has recently received wide attention due to the unexpected discovery that it is a genetic risk factor for Parkinsons disease. Gaucher disease... 
FINE STRUCTURE | METABOLISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | STORAGE DISORDERS | NEUROPATHOLOGY | SPHINGOLIPIDS | INFANTILE | GLUCOSYLSPHINGOSINE ACCUMULATION | GLUCOCEREBROSIDASE MUTATIONS | TYPE-2 | PARKINSONS-DISEASE | Neurons - pathology | Glucosylceramidase - genetics | Sphingomyelins - metabolism | Gaucher Disease - metabolism | Humans | Psychosine - metabolism | Lactosylceramides - metabolism | Gaucher Disease - pathology | Nerve Degeneration - metabolism | Mice, Knockout | Brain - metabolism | Animals | Glucosylceramidase - deficiency | Brain - pathology | Mice | Neurons - metabolism | Glucosylceramides - metabolism | Animal models
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7. Full Text Intercellular Skin Barrier Lipid Composition and Organization in Netherton Syndrome Patients
by van Smeden, Jeroen and Janssens, Michelle and Boiten, Walter A and van Drongelen, Vincent and Furio, Laetitia and Vreeken, Rob J and Hovnanian, Alain and Bouwstra, Joke A
Journal of Investigative Dermatology, ISSN 0022-202X, 05/2014, Volume 134, Issue 5, pp. 1238 - 1245
Netherton syndrome (NTS) is a rare genetic skin disease caused by mutations in the serine protease inhibitor Kazal-type 5 gene, which encodes the... 
ATOPIC-DERMATITIS | ACID | EPIDERMAL PERMEABILITY BARRIER | PHASE-BEHAVIOR | CERAMIDES | SPINK5 | LEKTI | INFANTILE ERYTHRODERMAS | STRATUM-CORNEUM LIPIDS | EXPRESSION | DERMATOLOGY | Epidermis - metabolism | Epidermis - pathology | Ceramides - metabolism | Netherton Syndrome - metabolism | Humans | Male | Dermatitis, Atopic - pathology | Glucosylceramidase - metabolism | Netherton Syndrome - pathology | Fatty Acids, Unsaturated - metabolism | Young Adult | Body Water - metabolism | Fatty Acids, Nonesterified - metabolism | Glucosyltransferases - metabolism | Sphingomyelin Phosphodiesterase - metabolism | Adolescent | Adult | Female | Child | Dermatitis, Atopic - metabolism | Fatty Acids - metabolism
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8. Full Text Activation of beta-Glucocerebrosidase Reduces Pathological alpha-Synuclein and Restores Lysosomal Function in Parkinson's Patient Midbrain Neurons
by Mazzulli, JR and Zunke, F and Tsunemi, T and Toker, NJ and Jeon, S and Burbulla, LF and Patnaik, S and Sidransky, E and Marugan, JJ and Sue, CM and Krainc, D
JOURNAL OF NEUROSCIENCE, ISSN 0270-6474, 07/2016, Volume 36, Issue 29, pp. 7693 - 7706
Parkinson's disease (PD) is characterized by the accumulation of alpha-synuclein (alpha-syn) within Lewy body inclusions in the nervous system. There are... 
synucleinopathy | CELLS | DEFECTS | Parkinson's disease | PARK9 | alpha-synuclein | NEUROSCIENCES | glucocerebrosidase | INHIBITION | ENZYME | MOUSE MODEL | DISEASE | induced pluripotent stem cells | lysosomes | DYSFUNCTION | MUTATIONS | AGGREGATION | Neurodegenerative Diseases - etiology | Humans | Dopaminergic Neurons - ultrastructure | Subcellular Fractions - pathology | Proton-Translocating ATPases - metabolism | Cell Differentiation - genetics | Lysosomes - metabolism | Dopaminergic Neurons - metabolism | Dopaminergic Neurons - drug effects | Neuroblastoma - pathology | Mesencephalon - pathology | Synaptophysin - metabolism | Parkinson Disease - pathology | Neurodegenerative Diseases - pathology | Gene Expression Regulation - genetics | Enzyme Inhibitors - pharmacology | Glucosylceramidase - metabolism | Neurodegenerative Diseases - metabolism | Mutation - genetics | Subcellular Fractions - metabolism | Gene Expression Regulation - drug effects | Cell Differentiation - drug effects | Cell Line, Tumor | Induced Pluripotent Stem Cells | alpha-Synuclein - metabolism | Lysosomal-Associated Membrane Protein 2 - metabolism | α-synuclein
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9. Full Text A shortcut to the lysosome: The mannose-6-phosphate-independent pathway
by Coutinho, Maria Francisca and Prata, Maria João and Alves, Sandra
Molecular Genetics and Metabolism, ISSN 1096-7192, 11/2012, Volume 107, Issue 3, pp. 257 - 266
Lysosomal hydrolases have long been known to be responsible for the degradation of different substrates in the cell. These acid hydrolases are synthesized in... 
Action myoclonus-renal failure syndrome (AMRF) | Mannose-6-phosphate-dependent pathway | Sortilin/neurotensin receptor-3 | Lysosomal integral membrane protein 2 (LIMP2) | MEDICINE, RESEARCH & EXPERIMENTAL | PROGRESSIVE MYOCLONUS EPILEPSY | VACUOLAR CARBOXYPEPTIDASE-Y | RENAL FAILURE SYNDROME | AMYOTROPHIC-LATERAL-SCLEROSIS | MESENCHYMAL STEM-CELLS | GAUCHER-DISEASE | DEMYELINATING PERIPHERAL NEUROPATHY | LIGAND BETA-GLUCOCEREBROSIDASE | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | 100-KDA NEUROTENSIN RECEPTOR | CORONARY-ARTERY-DISEASE | G(M2) Activator Protein - metabolism | Humans | Adaptor Proteins, Vesicular Transport - deficiency | Adaptor Proteins, Vesicular Transport - genetics | Lysosomal Storage Diseases - genetics | Receptors, Scavenger - deficiency | Glucosylceramidase - metabolism | Lysosomal Storage Diseases - pathology | Receptor, IGF Type 2 - metabolism | Neurotensin - metabolism | Protein Transport | Saposins - metabolism | trans-Golgi Network - metabolism | Carrier Proteins - metabolism | Lysosomes - metabolism | Mannosephosphates - metabolism | Receptors, Scavenger - genetics | Cathepsins - metabolism | Sphingomyelin Phosphodiesterase - metabolism | Lysosomal Storage Diseases - metabolism | Lysosome-Associated Membrane Glycoproteins - genetics | Lysosome-Associated Membrane Glycoproteins - deficiency | Lysosomes - pathology | Phosphates | Aquaporins | Cathepsins | Lipids | Neuropeptides | Neurotensin | Cells | Sugars | Monosaccharides
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10. Full Text N370S‐GBA1 mutation causes lysosomal cholesterol accumulation in Parkinson's disease
by García‐Sanz, Patricia and Orgaz, Lorena and Bueno‐Gil, Guillermo and Espadas, Isabel and Rodríguez‐Traver, Eva and Kulisevsky, Jaime and Gutierrez, Antonia and Dávila, José C and González‐Polo, Rosa A and Fuentes, José M and Mir, Pablo and Vicario, Carlos and Moratalla, Rosario
Movement Disorders, ISSN 0885-3185, 10/2017, Volume 32, Issue 10, pp. 1409 - 1422
Background Heterozygous mutations in the GBA1 gene, which encodes the lysosomal enzyme β‐glucocerebrosidase‐1, increase the risk of developing Parkinson's... 
multilamellar bodies | ER stress | cell death | autophagic vesicles | mitochondria | CANCER-CELLS | BETA-GLUCOCEREBROSIDASE | ENDOCYTIC PATHWAY | ALPHA-SYNUCLEIN | AUTOPHAGIC VACUOLES | FIBROBLASTS | CLINICAL NEUROLOGY | GAUCHER-DISEASE | ENDOPLASMIC-RETICULUM | DYSFUNCTION | GLUCOCEREBROSIDASE ACTIVITY | Glucosylceramidase - genetics | TOR Serine-Threonine Kinases - metabolism | Humans | Endoplasmic Reticulum - metabolism | Male | Fibroblasts - ultrastructure | Endoplasmic Reticulum - ultrastructure | Lysosomes - metabolism | Female | Parkinson Disease - metabolism | Autophagy - genetics | Calnexin - metabolism | Golgi Apparatus - ultrastructure | Asparagine - genetics | Parkinson Disease - pathology | Oxidative Stress - genetics | Serine - genetics | Parkinson Disease - genetics | Cholesterol - metabolism | Fibroblasts - pathology | Mutation - genetics | Lysosomes - ultrastructure | Models, Biological | Golgi Apparatus - metabolism | Lysosomal-Associated Membrane Protein 1 - metabolism | Beclin-1 - metabolism | Transcription Factor CHOP - metabolism | Calnexin - ultrastructure | Enzymes | Genetic aspects | Analysis | Cholesterol | Flow cytometry | Reactive oxygen species | Parkinson's disease | Parkinsons disease | Homeostasis | Lysosomes | mRNA | Autophagy | Mitochondria | Protein folding | Fibroblasts | Membrane potential | Protein transport | Movement disorders | Neurodegenerative diseases | Electron microscopy | Golgi apparatus | Storage diseases | Cell death | Glucosylceramidase | Mutation | Immunofluorescence | Endoplasmic reticulum | Phagocytosis | Apoptosis
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11. Full Text Mitochondria and quality control defects in a mouse model of gaucher disease - Links to parkinson's disease
by Osellame, Laura D and Rahim, Ahad A and Hargreaves, Iain P and Gegg, Matthew E and Richard-Londt, Angela and Brandner, Sebastian and Waddington, Simon N and Schapira, Anthony H.V and Duchen, Michael R
Cell Metabolism, ISSN 1550-4131, 06/2013, Volume 17, Issue 6, pp. 941 - 953
Mutations in the glucocerebrosidase (gba) gene cause Gaucher disease (GD), the most common lysosomal storage disorder, and increase susceptibility to... 
OXIDATIVE STRESS | PINK1 | INHIBITION | GENE | ENDOCRINOLOGY & METABOLISM | LYSOSOMAL STORAGE DISEASES | ALPHA-SYNUCLEIN | AUTOPHAGY | DYSFUNCTION | GLUCOCEREBROSIDASE MUTATIONS | COMPLEX-I DEFICIENCY | CELL BIOLOGY | Astrocytes - cytology | Mitochondrial Diseases - genetics | Electron Transport | Glucosylceramidase - genetics | Gaucher Disease - metabolism | Sequestosome-1 Protein | Heat-Shock Proteins - metabolism | Humans | Lysosomes - genetics | Cells, Cultured | Neurons - cytology | Mitochondria - metabolism | Parkinson Disease - genetics | Mice, Knockout | Animals | Gaucher Disease - genetics | Lysosomes - metabolism | Mitochondria - genetics | Mice | Parkinson Disease - metabolism | Autophagy - genetics | Adaptor Proteins, Signal Transducing - metabolism | alpha-Synuclein - metabolism | Disease Models, Animal | Proteins | High technology industry | Neurosciences | Developmental biology | Analysis | Quality control | Mitochondrial DNA
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12. Full Text Atp13a2 expression in the periaqueductal gray is decreased in the Pink1 -/- rat model of Parkinson disease
by Kelm-Nelson, Cynthia A and Stevenson, Sharon A and Ciucci, Michelle R
Neuroscience Letters, ISSN 0304-3940, 05/2016, Volume 621, pp. 75 - 82
Vocal communication deficits are common in Parkinson disease (PD). Widespread alpha-synuclein pathology is a common link between familial and sporadic PD, and... 
Ultrasonic vocalization | Periaqueductal gray | Pink1 | Alpha synuclein | Rat | Gad1 | Parkinson disease | Atp13a2 | SQUIRREL-MONKEY | MOUSE PUPS | ALPHA-SYNUCLEIN | DOPAMINERGIC-NEURONS | SUBSTANTIA-NIGRA | NEUROSCIENCES | DEFICIENCY | P-TYPE ATPASE | NUCLEUS | ULTRASONIC VOCALIZATIONS | DYSFUNCTION | Biomarkers - metabolism | Tyrosine 3-Monooxygenase - metabolism | Protein Kinases - genetics | Rats, Long-Evans | Rats | Glucosylceramidase - metabolism | Parkinson Disease - genetics | Gene Knockout Techniques | Receptors, Dopamine D2 - metabolism | Periaqueductal Gray - metabolism | Receptors, Dopamine D1 - metabolism | Proton-Translocating ATPases - metabolism | Animals | Glutamate Decarboxylase - metabolism | Parkinson Disease - metabolism | Receptors, GABA-A - metabolism | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | alpha-Synuclein - metabolism | Apoptosis | Gene expression | Parkinson's disease | Neurosciences | RNA | Genes | GABA | Glutamate decarboxylase | Glutamate
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