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1. Full Text Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease
by Burbulla, Lena F and Song, Pingping and Mazzulli, Joseph R and Zampese, Enrico and Wong, Yvette C and Jeon, Sohee and Santos, David P and Blanz, Judith and Obermaier, Carolin D and Strojny, Chelsee and Savas, Jeffrey N and Kiskinis, Evangelos and Zhuang, Xiaoxi and Krüger, Rejko and Surmeier, D. James and Krainc, Dimitri
Science (American Association for the Advancement of Science), ISSN 0036-8075, 09/2017, Volume 357, Issue 6357, pp. 1255 - 1261
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 (London), ISSN 0028-0836, 11/2016, Volume 539, Issue 7628, pp. 207 - 216
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | Index Medicus
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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
Life Sciences & Biomedicine | Hematology | Science & Technology | Hematologic and hematopoietic diseases | Errors of metabolism | Biological and medical sciences | Metabolic diseases | Medical sciences | Lipids (lysosomal enzyme disorders, storage diseases) | 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 | Index Medicus | Abridged Index Medicus | Hematopoiesis and Stem Cells
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4. Full Text Activation of β-glucocerebrosidase reduces pathological α-synuclein and restores lysosomal function in Parkinson’s patient midbrain neurons
by Mazzulli, Joseph R and Zunke, Friederike and Tsunemi, Taiji and Toker, Nicholas J and Jeon, Sohee and Burbulla, Lena F and Patnaik, Samarjit and Sidransky, Ellen and Marugan, Juan J and Sue, Carolyn M and Krainc, Dimitri
The Journal of neuroscience, ISSN 0270-6474, 07/2016, Volume 36, Issue 29, pp. 7693 - 7706
Lysosomes | Glucocerebrosidase | Induced pluripotent stem cells | Synucleinopathy | Parkinson’s disease | α-synuclein | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus | synucleinopathy | induced pluripotent stem cells | lysosomes | Parkinson's disease | glucocerebrosidase
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5. Full Text ER Stress and Autophagic Perturbations Lead to Elevated Extracellular α-Synuclein in GBA-N370S Parkinson's iPSC-Derived Dopamine Neurons
by Fernandes, Hugo J.R and Hartfield, Elizabeth M and Christian, Helen C and Emmanoulidou, Evangelia and Zheng, Ying and Booth, Heather and Bogetofte, Helle and Lang, Charmaine and Ryan, Brent J and Sardi, S. Pablo and Badger, Jennifer and Vowles, Jane and Evetts, Samuel and Tofaris, George K and Vekrellis, Kostas and Talbot, Kevin and Hu, Michele T and James, William and Cowley, Sally A and Wade-Martins, Richard
Stem cell reports, ISSN 2213-6711, 03/2016, Volume 6, Issue 3, pp. 342 - 356
Exosomes - metabolism | Cell Line | Glucosylceramidase - genetics | Parkinson Disease - pathology | Humans | Cells, Cultured | Mutation, Missense | Parkinson Disease - genetics | Autophagy | Neurogenesis | Dopaminergic Neurons - cytology | Animals | Lysosomes - metabolism | Dopaminergic Neurons - metabolism | Endoplasmic Reticulum Stress | Mice | Parkinson Disease - metabolism | Induced Pluripotent Stem Cells - cytology | alpha-Synuclein - metabolism | Induced Pluripotent Stem Cells - metabolism | Index Medicus
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6. 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
Life Sciences & Biomedicine | Dermatology | Science & Technology | 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 | Index Medicus
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7. 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 (Cambridge), ISSN 0092-8674, 2007, Volume 131, Issue 4, pp. 770 - 783
CELLBIO | HUMDISEASE | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus
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8. Full Text Finding pathogenic commonalities between Niemann-Pick type C and other lysosomal storage disorders: Opportunities for shared therapeutic interventions
by Yañez, M.J and Marín, T and Balboa, E and Klein, A.D and Alvarez, A.R and Zanlungo, S
Biochimica et biophysica acta. Molecular basis of disease, ISSN 0925-4439, 10/2020, Volume 1866, Issue 10, pp. 165875 - 165875
Gaucher | Lysosome | c-Abl | Sphingolipids | Lysosomal storage disease | Cholesterol | Niemann-Pick | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Neurons - pathology | Glucosylceramidase - genetics | Vesicular Transport Proteins - metabolism | Humans | Neurons - cytology | Intracellular Signaling Peptides and Proteins - metabolism | Gaucher Disease - pathology | Niemann-Pick Disease, Type C - pathology | Niemann-Pick Disease, Type C - metabolism | Brain - metabolism | Lysosomes - metabolism | Lipid Metabolism - genetics | Lysosomes - pathology | Neurons - metabolism | Niemann-Pick Disease, Type A - genetics | Intracellular Signaling Peptides and Proteins - genetics | Brain - cytology | Gaucher Disease - metabolism | Vesicular Transport Proteins - genetics | Sphingolipids - metabolism | Glucosylceramidase - metabolism | Signal Transduction - genetics | Cholesterol - metabolism | Gaucher Disease - genetics | Niemann-Pick Disease, Type A - metabolism | Brain - pathology | Niemann-Pick Disease, Type A - pathology | Mutation | Niemann-Pick Disease, Type C - genetics | Index Medicus
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