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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
Journal Article
Journal Article
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
Journal Article
Journal Article
JOURNAL OF NEUROSCIENCE, ISSN 0270-6474, 07/2016, Volume 36, Issue 29, pp. 7693 - 7706
Journal Article
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
Journal Article
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
Journal Article
Journal Article