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1. Full Text The role of glucocerebrosidase in Parkinson disease pathogenesis
by Gegg, Matthew E and Schapira, Anthony H. V
The FEBS journal, ISSN 1742-464X, 10/2018, Volume 285, Issue 19, pp. 3591 - 3603
Parkinson disease | unfolded protein response | autophagy | α‐synuclein | glucocerebrosidase | α-synuclein | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Gene Expression Regulation, Enzymologic | Inflammation - complications | Glucosylceramidase - genetics | Parkinson Disease - pathology | Animals | Glucosylceramidase - deficiency | Humans | Mitochondria - pathology | Mutation | Parkinson Disease - etiology | Physiological aspects | Enzymes | Hydrolases | Development and progression | Parkinson's disease | Animal models | Accounting | Pathogenesis | Parkinsons disease | Synuclein | Autophagy | Accumulation | Risk factors | Proteins | Mitochondria | Protein folding | Mathematical models | Lipid metabolism | Movement disorders | Neurodegenerative diseases | Health risks | Inflammation | Metabolism | Risk analysis | Substrates | Lewy bodies | Glucosylceramidase | Endoplasmic reticulum | Phagocytosis
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2. Full Text Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains
by Gegg, Matthew E and Burke, Derek and Heales, Simon J. R and Cooper, J. Mark and Hardy, John and Wood, Nicholas W and Schapira, Anthony H. V
Annals of neurology, ISSN 0364-5134, 09/2012, Volume 72, Issue 3, pp. 455 - 463
Neurosciences | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Neurology | Biological and medical sciences | Medical sciences | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | Mitochondria - enzymology | RNA, Small Interfering - genetics | Glucosylceramidase - genetics | Immunoprecipitation | Substantia Nigra - pathology | Humans | Middle Aged | Male | Gaucher Disease - pathology | Neuroblastoma | Aged, 80 and over | Female | Protein Kinases - deficiency | Substantia Nigra - enzymology | Parkinson Disease - complications | Parkinson Disease - pathology | Glucosylceramidase - metabolism | Gaucher Disease - complications | Gaucher Disease - genetics | Gene Expression Regulation, Enzymologic - genetics | Cell Line, Tumor | Heterozygote | Aged | Mutation | alpha-Synuclein - metabolism | RNA, Small Interfering - metabolism | Proteins | Protein expression | Kinases | Parkinsons disease | Index Medicus | Original
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3. 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
Endocrinology & Metabolism | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus
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4. Full Text Mitochondrial and lysosomal biogenesis are activated following PINK1/parkin‐mediated mitophagy
by Ivankovic, Davor and Chau, Kai‐Yin and Schapira, Anthony H. V and Gegg, Matthew E
Journal of neurochemistry, ISSN 0022-3042, 01/2016, Volume 136, Issue 2, pp. 388 - 402
TFEB | mitophagy | PINK1 | lysosomes | Parkinson's disease | Nrf2 | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Protein Kinases - metabolism | Sequestosome-1 Protein | Humans | Cytosol - drug effects | Mitochondrial Degradation - genetics | Heat-Shock Proteins - genetics | Tubulin - metabolism | Lysosomes - metabolism | Transfection | Time Factors | Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology | Cell Nucleolus - metabolism | Cell Nucleolus - drug effects | Proton Ionophores - pharmacology | Membrane Transport Proteins - metabolism | Gene Expression Regulation, Neoplastic - drug effects | Neuroblastoma - pathology | Lysosomes - drug effects | Heat-Shock Proteins - metabolism | RNA, Small Interfering - pharmacology | Ubiquitin-Protein Ligases - metabolism | Receptors, Cell Surface - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Gene Expression Regulation - drug effects | Neuroblastoma - ultrastructure | Mitochondrial Degradation - drug effects | Cell Line, Tumor | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | Cytosol - metabolism | Ubiquitin | Biosynthesis | Mitochondrial DNA | RNA | Protein binding | Proteins | Mitochondria | Transcription factors | Autophagy | Index Medicus | ORIGINAL ARTICLES | Original
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5. Full Text No evidence for substrate accumulation in Parkinson brains with GBA mutations
by Gegg, Matthew E and Sweet, Lindsay and Wang, Bing H and Shihabuddin, Lamya S and Sardi, Sergio Pablo and Schapira, Anthony H.V
Movement disorders, ISSN 0885-3185, 07/2015, Volume 30, Issue 8, pp. 1085 - 1089
lysosomes | Parkinson's disease | sphingolipids | glucocerebrosidase | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Tissue Banks | Putamen - pathology | beta-Glucosidase - genetics | Cerebellum - metabolism | Humans | Glucosylceramidase - metabolism | Mutation | Cerebellum - pathology | Putamen - metabolism | Brain | Enzymes | Analysis | Hydrolases | Lipids | Genetic aspects | Gangliosides | Index Medicus
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6. Full Text PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: Implications for Parkinson disease pathogenesis
by Gegg, Matthew E and Schapira, Anthony H.V
Autophagy, ISSN 1554-8627, 02/2011, Volume 7, Issue 2, pp. 243 - 245
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | Mitochondria | PINK1 | Mitofusin | Neurodegeneration | Parkinson disease | Mitophagy | Parkin | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Protein Kinases - metabolism | Parkinson Disease - pathology | Humans | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Mitochondria - metabolism | Adenosine Triphosphate - biosynthesis | Autophagy | Ubiquitination | Mitochondrial Proteins - metabolism | Parkinson Disease - enzymology | Fluorescent Antibody Technique | Parkinson Disease - etiology | Index Medicus | mitophagy | parkin | mitochondria | neurodegeneration | mitofusin
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7. Full Text The role of DJ-1 complexes and catecholamine metabolism: relevance for familial and idiopathic Parkinson's disease
by Piston, Dominik and Gegg, Matthew
Neural regeneration research, ISSN 1673-5374, 5/2018, Volume 13, Issue 5, pp. 815 - 816
Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Catecholamines | Care and treatment | Parkinson's disease | Research | Genetic transcription | Noradrenaline | Proteins | Brain | Oxidative stress | Dopamine | Neurodegeneration | Parkinsons disease | Neuroblastoma | Mutation | Metabolism | Autophagy | Molecular weight | Cancer
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8. Full Text Mitochondria: Key Organelle in Parkinson's Disease
by Rubén Gómez-Sánchez and José M. Bravo-San Pedro and Matthew E. Gegg and Rosa A. González-Polo and José M. Fuentes
Parkinson's disease, ISSN 2042-0080, 12/2016, Volume 2016, pp. 6230370 - 2
Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology
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9. Full Text Glucocerebrosidase in the pathogenesis and treatment of Parkinson disease
by Anthony H. V. Schapira and Matthew E. Gegg
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 2/2013, Volume 110, Issue 9, pp. 3214 - 3215
Pathology | COMMENTARIES | Gaucher disease | Histone deacetylase inhibitors | Pathogenesis | Drug interactions | Medical treatment | Parkinson disease | Lysosomes | Genetic mutation | Lewy bodies | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Animals | Parkinsonian Disorders - drug therapy | Humans | Brain - enzymology | Parkinsonian Disorders - enzymology | Glucosylceramidase - metabolism | alpha-Synuclein - metabolism | Gaucher Disease - drug therapy | Gaucher Disease - enzymology | Index Medicus | Biological Sciences | Commentaries
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10. Full Text Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in DOPAMINERGIC cells
by Gegg, Matthew E and Cooper, J. Mark and Schapira, Anthony H.V and Taanman, Jan-Willem
PloS one, ISSN 1932-6203, 03/2009, Volume 4, Issue 3, pp. e4756 - e4756
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Kinases - metabolism | Protein Kinases - genetics | DNA, Mitochondrial - metabolism | Cell Survival | Glutathione - metabolism | Humans | RNA, Small Interfering - pharmacology | Gene Silencing | Oxidative Phosphorylation | Protein Kinases - chemistry | Mitochondria - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Mitochondrial Membranes - metabolism |