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1. Full Text Identification and Characterization of Ambroxol as an Enzyme Enhancement Agent for Gaucher Disease
by Gustavo H. B. Maegawa and Michael B. Tropak and Justin D. Buttner and Brigitte A. Rigat and Maria Fuller and Deepangi Pandit and Liangiie Tang and Gregory J. Kornhaber and Yoshitomo Hamuro and Joe T. R. Clarke and Don J. Mahuran
The Journal of biological chemistry, ISSN 0021-9258, 08/2009, Volume 284, Issue 35, pp. 23502 - 23516
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Ambroxol - pharmacology | Amino Acid Sequence | Glucosylceramidase - chemistry | Catalytic Domain | Fibroblasts - enzymology | Glucosylceramidase - genetics | Humans | Molecular Conformation | Cells, Cultured | Enzyme Inhibitors - pharmacology | Enzyme Stability | Molecular Sequence Data | Glucosylceramidase - metabolism | Glucosylceramidase - antagonists & inhibitors | Ambroxol - chemistry | Enzyme Inhibitors - chemistry | Fibroblasts - drug effects | Drug Evaluation, Preclinical | Binding Sites | Gaucher Disease - drug therapy | Gaucher Disease - enzymology | Index Medicus | Protein Structure and Folding
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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 The biochemical basis of interactions between Glucocerebrosidase and alpha‐synuclein in GBA1 mutation carriers
by Toffoli, Marco and Smith, Laura and Schapira, Anthony H. V
Journal of neurochemistry, ISSN 0022-3042, 07/2020, Volume 154, Issue 1, pp. 11 - 24
Parkinson disease | alpha‐synuclein | GBA1 | Gaucher disease | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Glucosylceramidase - chemistry | Genetic Predisposition to Disease - genetics | Glucosylceramidase - genetics | Humans | Protein Structure, Quaternary | Heterozygote | Glucosylceramidase - metabolism | Parkinson Disease - metabolism | Mutation | Parkinson Disease - genetics | alpha-Synuclein - metabolism | Parkinson's disease | Neurodegenerative diseases | Therapeutic applications | Genes | Parkinsons disease | Glucosylceramidase | Synuclein | Movement disorders | Index Medicus
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4. Full Text Glucocerebrosidase modulates cognitive and motor activities in murine models of Parkinson's disease
by Rockenstein, Edward and Clarke, Jennifer and Viel, Catherine and Panarello, Nicholas and Treleaven, Christopher M and Kim, Changyoun and Spencer, Brian and Adame, Anthony and Park, Hyejung and Dodge, James C and Cheng, Seng H and Shihabuddin, Lamya S and Masliah, E and Sardi, S. Pablo
Human molecular genetics, ISSN 0964-6906, 2016, Volume 25, Issue 13, pp. 2645 - 2660
Biochemistry & Molecular Biology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Gene Expression | Glucosylceramidase - genetics | Dopamine | Humans | Motor Activity - drug effects | Glucosylceramidase - metabolism | Parkinson Disease - drug therapy | Parkinson Disease - genetics | Cognition - drug effects | Animals | Gaucher Disease - genetics | alpha-Synuclein - cerebrospinal fluid | Glucosylceramidase - therapeutic use | Glucosylceramidase - physiology | Mice | Mutation | alpha-Synuclein - metabolism | Disease Models, Animal | Index Medicus
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5. Full Text Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease
by Murphy, Karen E and Gysbers, Amanda M and Abbott, Sarah K and Tayebi, Nahid and Kim, Woojin S and Sidransky, Ellen and Cooper, Antony and Garner, Brett and Halliday, Glenda M
Brain (London, England : 1878), ISSN 0006-8950, 2014, Volume 137, Issue 3, pp. 834 - 848
ceramide | chaperone-mediated autophagy | Parkinson's disease | glucocerebrosidase | α-synuclein | Neurosciences | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Neurology | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | Headache. Facial pains. Syncopes. Epilepsia. Intracranial hypertension. Brain oedema. Cerebral palsy | Biological and medical sciences | Nervous system as a whole | Medical sciences | Nervous system (semeiology, syndromes) | Glucosylceramidase - genetics | Parkinson Disease - pathology | Humans | Brain - enzymology | Lysosomes - enzymology | Male | Autophagy - physiology | Glucosylceramidase - metabolism | Mutation - genetics | Molecular Chaperones - physiology | Case-Control Studies | Glucosylceramidase - antagonists & inhibitors | Brain - metabolism | alpha-Synuclein - biosynthesis | Parkinson Disease - enzymology | Up-Regulation - physiology | Aged, 80 and over | Brain - pathology | Female | Aged | Parkinson Disease - metabolism | alpha-Synuclein - metabolism | Cohort Studies | Index Medicus | Abridged Index Medicus | Ceramide | Original | Parkinson’s disease
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6. Full Text The production of human β-glucocerebrosidase in nicotiana benthamiana root culture
by Naphatsamon, Uthailak and Ohashi, Takao and Misaki, Ryo and Fujiyama, Kazuhito
International journal of molecular sciences, ISSN 1661-6596, 07/2018, Volume 19, Issue 7, p. 1972
Plant-made pharmaceutical | Root culture | Human glucocerebrosidase | Nicotiana benthamiana | Recombinant protein | Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Multidisciplinary | Science & Technology | Glucosylceramidase - chemistry | Glucosylceramidase - genetics | Plants, Genetically Modified - genetics | Humans | Plants, Genetically Modified - enzymology | Recombinant Proteins - chemistry | Plant Roots - cytology | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Plant Roots - drug effects | Glucosylceramidase - biosynthesis | Recombinant Proteins - isolation & purification | Time Factors | Concanavalin A - chemistry | Indoleacetic Acids - pharmacology | Tobacco - genetics | Plant Roots - enzymology | Culture Media - chemistry | Tobacco - enzymology | Gaucher Disease - enzymology | Glucosylceramidase - isolation & purification | Cell culture | Enzymes | Enzyme activity | Roots | Concanavalin A | Transgenic plants | Contamination | Glycan | Mammalian cells | Proteins | Enzymatic activity | Indoleacetic acid | Glucosylceramidase | Acetic acid | Gaucher's disease | Index Medicus | human glucocerebrosidase | plant-made pharmaceutical | root culture | recombinant protein
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7. Full Text Glucosylsphingosine promotes α-synuclein pathology in mutant GBA-associated parkinson’s disease
by Taguchi, Yumiko V and Liu, Jun and Ruan, Jiapeng and Pacheco, Joshua and Zhang, Xiaokui and Abbasi, Justin and Keutzer, Joan and Mistry, Pramod K and Chandra, Sreeganga S
The Journal of neuroscience, ISSN 0270-6474, 10/2017, Volume 37, Issue 40, pp. 9617 - 9631
Glucosylsphingosine | α-synuclein | GBA | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Glucosylceramidase - genetics | Parkinson Disease - pathology | Humans | Male | Mice, Transgenic | Parkinson Disease - genetics | Psychosine - biosynthesis | Psychosine - analogs & derivatives | Brain - metabolism | Glucosylceramidase - biosynthesis | Mutation - physiology | Animals | alpha-Synuclein - biosynthesis | HEK293 Cells | Brain - pathology | Female | Psychosine - genetics | Mice | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Brain | Parkinson's disease | Neurodegenerative diseases | Parkinsons disease | Health risks | Agglomeration | Sphingolipids | Synuclein | Risk analysis | Neurogenesis | Risk factors | Sphingosine 1-phosphate | Pathology | Glucosylceramidase | Mutation | Movement disorders | Gaucher's disease | Index Medicus | glucosylsphingosine
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