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1. Contempt of court
by Miller, C. J. (Christopher J.)
2000, 3rd ed., ISBN 0198256973, cx, 769
Contempt of court
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2. Contempt of court
by Miller, C. J. (Christopher J.)
1976, ISBN 9780236310876, xl, 279
Contempt of court
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3. Contempt of court
by Miller, C. J. (Christopher J.)
1989, 2nd ed. --, ISBN 9780198254782, lix, 492
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4. Full Text Noise constraints effecting optimal propeller designs
by Miller, C. J. (Christopher J.) and Sullivan, John P and United States. National Aeronautics and Space Administration
1985, NASA technical memorandum, Volume 86967.
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5. Full Text Loss of c-Jun N-terminal kinase-interacting protein-1 does not affect axonal transport of the amyloid precursor protein or Aβ production
by Vagnoni, Alessio and Glennon, Elizabeth B.C and Perkinton, Michael S and Gray, Emma H and Noble, Wendy and Miller, Christopher C.J
Human Molecular Genetics, ISSN 0964-6906, 11/2013, Volume 22, Issue 22, pp. 4646 - 4652
Disruption to axonal transport is an early pathological feature in Alzheimer's disease. The amyloid precursor protein (APP) is a key axonal transport cargo in... 
Axonal Transport | Humans | Middle Aged | Axons - metabolism | Rats | Male | Embryo, Mammalian - metabolism | Gene Knockdown Techniques | Brain - metabolism | Animals | Adaptor Proteins, Signal Transducing - genetics | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Amyloid beta-Protein Precursor - metabolism | Aged, 80 and over | Female | Aged | Neurons - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Alzheimer Disease - genetics
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6. Full Text Role of axonal transport in neurodegenerative diseases
by De Vos, Kurt J and Grierson, Andrew J and Ackerley, Steven and Miller, Christopher C. J
Annual Review of Neuroscience, ISSN 0147-006X, 2008, Volume 31, Issue 1, pp. 151 - 173
Many major human neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS), display axonal... 
Amyotrophic lateral sclerosis | Parkinson's disease | Huntington's disease | Alzheimer's disease | Charcot-Marie-tooth disease | Motor neuron disease | motor neuron disease | MARIE-TOOTH-DISEASE | ACTIVATED PROTEIN-KINASE | HEREDITARY SPASTIC PARAPLEGIA | GLYCOGEN-SYNTHASE KINASE-3 | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | MUTANT SUPEROXIDE-DISMUTASE | amyotrophic lateral sclerosis | HUNTINGTIN-ASSOCIATED PROTEIN-1 | NEUROSCIENCES | Charcot-Marie-Tooth disease | NUCLEOTIDE EXCHANGE FACTOR | CYCLIN-DEPENDENT KINASE-5 | Axonal Transport - genetics | Central Nervous System - metabolism | Humans | Central Nervous System - pathology | Charcot-Marie-Tooth Disease - genetics | Motor Neuron Disease - metabolism | Motor Neuron Disease - genetics | Parkinson Disease - metabolism | Motor Neuron Disease - physiopathology | Charcot-Marie-Tooth Disease - metabolism | Huntington Disease - physiopathology | Alzheimer Disease - physiopathology | Axons - metabolism | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - metabolism | Parkinson Disease - genetics | Parkinson Disease - physiopathology | Huntington Disease - metabolism | Animals | Neurodegenerative Diseases - physiopathology | Axons - pathology | Alzheimer Disease - metabolism | Huntington Disease - genetics | Central Nervous System - physiopathology | Charcot-Marie-Tooth Disease - physiopathology | Alzheimer Disease - genetics | Nervous system | Degeneration | Axonal transport | Analysis
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7. Full Text [alpha]-Synuclein binds to the ER-mitochondria tethering protein VAPB to disrupt Ca^sup 2+^ homeostasis and mitochondrial ATP production
by Sébastien Paillusson and Patricia Gomez-Suaga and Radu Stoica and Daniel Little and Paul Gissen and Michael J Devine and Wendy Noble and Diane P Hanger and Christopher C J Miller
Acta Neuropathologica, ISSN 0001-6322, 07/2017, Volume 134, Issue 1, p. 129
[alpha]-Synuclein is strongly linked to Parkinson's disease but the molecular targets for its toxicity are not fully clear. However, many neuronal functions... 
Tyrosine | Parkinson's disease | Neurodegenerative diseases | Neurons | Toxicity | Parkinsons disease | Homeostasis | Protein B | Synuclein | Organelles | Membrane proteins | Calcium signalling | Proteins | Mitochondria | Neurotoxicity | Stem cells | Endoplasmic reticulum | Pluripotency | Adenosine triphosphatase | Movement disorders | Protein-tyrosine-phosphatase
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8. Full Text ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43
by Stoica, Radu and De Vos, Kurt J and Paillusson, Sébastien and Mueller, Sarah and Sancho, Rosa M and Lau, Kwok-Fai and Vizcay-Barrena, Gema and Lin, Wen-Lang and Xu, Ya-Fei and Lewis, Jada and Dickson, Dennis W and Petrucelli, Leonard and Mitchell, Jacqueline C and Shaw, Christopher E and Miller, Christopher C. J
Nature Communications, ISSN 2041-1723, 06/2014, Volume 5, Issue 1, p. 3996
Mitochondria and the endoplasmic reticulum (ER) form tight structural associations and these facilitate a number of cellular functions. However, the mechanisms... 
MOTOR-NEURONS | CALCIUM HOMEOSTASIS | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | PROTEIN TDP-43 | ENDOPLASMIC-RETICULUM | AXONAL-TRANSPORT | AMYOTROPHIC-LATERAL-SCLEROSIS | ALPHA-SYNUCLEIN | FRONTOTEMPORAL LOBAR DEGENERATION | TRANSGENIC MICE | Cell Line | Calcium - metabolism | Vesicular Transport Proteins - metabolism | Humans | Endoplasmic Reticulum - metabolism | Glycogen Synthase Kinase 3 beta | Protein Tyrosine Phosphatases - metabolism | Mitochondria - metabolism | Glycogen Synthase Kinase 3 - metabolism | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Animals | Mitochondrial Proteins - metabolism | Amyotrophic Lateral Sclerosis - metabolism | HEK293 Cells | Membrane Proteins - metabolism | Mice
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9. Full Text Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion
by Mitchell, Jacqueline C and McGoldrick, Philip and Vance, Caroline and Hortobagyi, Tibor and Sreedharan, Jemeen and Rogelj, Boris and Tudor, Elizabeth L and Smith, Bradley N and Klasen, Christian and Miller, Christopher C. J and Cooper, Jonathan D and Greensmith, Linda and Shaw, Christopher E
Acta Neuropathologica, ISSN 0001-6322, 2/2013, Volume 125, Issue 2, pp. 273 - 288
Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) are relentlessly progressive neurodegenerative disorders with overlapping... 
Medicine & Public Health | Pathology | Neurosciences | LOCALIZATION | PROTEIN | SPLICING REGULATION | INCLUSIONS | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | NEUROSCIENCES | CLINICAL NEUROLOGY | TDP-43 | FUS/TLS | MUTATIONS | Immunohistochemistry | Motor Neurons - physiology | Cell Survival | Gene Expression Regulation - genetics | Humans | Mice, Inbred C57BL | RNA-Binding Protein FUS - genetics | Cytoplasm - metabolism | Mice, Transgenic | Gene Dosage | Paralysis - genetics | Paralysis - pathology | Blotting, Western | Motor Neuron Disease - pathology | Animals | Aging - physiology | Motor Neuron Disease - genetics | Spinal Cord - pathology | Inclusion Bodies - pathology | RNA-Binding Protein FUS - physiology | Mice | Isometric Contraction - physiology | Muscle Fibers, Skeletal - physiology | Ubiquitin | Nervous system diseases | Tremor | Sarcoma | RNA | Neurons | DNA | Amyotrophic lateral sclerosis | Paralysis | Protein binding | Brain | Limbs | Motor neurons | tremor | Animal models | Spinal cord | Neurodegenerative diseases | Transgenic mice | FUS gene | Atrophy | FUS protein | RNA-binding protein | DNA-binding protein | Inclusion bodies | Frontotemporal dementia | Denervation | Original Paper
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10. Full Text There's Something Wrong with my MAM; the ER–Mitochondria Axis and Neurodegenerative Diseases
by Paillusson, Sebastien and Stoica, Radu and Gomez-Suaga, Patricia and Lau, Dawn H.W and Mueller, Sarah and Miller, Tanya and Miller, Christopher C.J
Trends in Neurosciences, ISSN 0166-2236, 2016, Volume 39, Issue 3, pp. 146 - 157
Alzheimer's disease (AD), Parkinson's disease (PD), and amyotrophic lateral sclerosis with associated frontotemporal dementia (ALS/FTD) are major... 
Neurology | amyotrophic lateral sclerosis/fronto-temporal dementia | Parkinson's disease | Alzheimer's disease | mitochondria associated ER membranes | mitochondria | endoplasmic reticulum | Amyotrophic lateral sclerosis/fronto-temporal dementia | Mitochondria | Endoplasmic reticulum | Mitochondria associated ER membranes | TAU PHOSPHORYLATION | CONTACT SITES | VAPB INTERACTS | MOTOR-NEURON DEGENERATION | ALZHEIMERS-DISEASE | CALCIUM HOMEOSTASIS | ENDOPLASMIC-RETICULUM | AXONAL-TRANSPORT | ALPHA-SYNUCLEIN | NEUROSCIENCES | PARKINSONS-DISEASE | Animals | Neurodegenerative Diseases - pathology | Humans | Endoplasmic Reticulum - metabolism | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - therapy | Mitochondria - metabolism | Neurodegenerative Diseases - metabolism | Mitochondria - ultrastructure | Endoplasmic Reticulum - ultrastructure | Nervous system diseases | Mitochondrial DNA | fronto-temporal dementia | Review | amyotrophic lateral sclerosis
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11. Full Text Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations
by Godena, Vinay K and Brookes-Hocking, Nicholas and Moller, Annekathrin and Shaw, Gary and Oswald, Matthew and Sancho, Rosa M and Miller, Christopher C. J and Whitworth, Alexander J and De Vos, Kurt J
Nature Communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, p. 5245
Leucine-rich repeat kinase 2 (LRRK2) mutations are the most common genetic cause of Parkinson's disease. LRRK2 is a multifunctional protein affecting many... 
DISEASE-ASSOCIATED MUTATIONS | GENE | REPEAT KINASE 2 | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | MOUSE MODEL | MITOCHONDRIA | DOPAMINERGIC-NEURONS | INHIBITORS | HDAC6 | DEGENERATION | Protein Structure, Tertiary | Axons - enzymology | Drosophila | Humans | Protein-Serine-Threonine Kinases - genetics | Rats | Drosophila Proteins - chemistry | Parkinson Disease - genetics | Drosophila Proteins - metabolism | Parkinson Disease - physiopathology | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Microtubules - metabolism | Animals | Biological Transport | Neurons - enzymology | Parkinson Disease - enzymology | Protein-Serine-Threonine Kinases - chemistry | Acetylation | Drosophila Proteins - genetics | Mutation | Protein-Serine-Threonine Kinases - metabolism | Cell Movement
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12. Full Text The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy
by Gomez-Suaga, Patricia and Paillusson, Sebastien and Stoica, Radu and Noble, Wendy and Hanger, Diane P and Miller, Christopher C.J
Current Biology, ISSN 0960-9822, 02/2017, Volume 27, Issue 3, pp. 371 - 385
Mitochondria form close physical associations with the endoplasmic reticulum (ER) that regulate a number of physiological functions. One mechanism by which... 
autophagy | calcium | Alzheimer’s disease | VAPB | mitochondria | MAM | PTPIP51 | amyotrophic lateral sclerosis | endoplasmic reticulum | Parkinson’s disease | Parkinson's disease | Alzheimer's disease | CONTACT SITES | HOMEOSTASIS | ASSOCIATIONS | MITOFUSIN 2 | INS(1,4,5)P-3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE | MEMBRANES | RECEPTOR | ENDOPLASMIC-RETICULUM | MEDIATED APOPTOSIS | CELL BIOLOGY | Neurosciences | Protein binding
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13. Full Text VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
by De vos, Kurt J and Mórotz, Gábor M and Stoica, Radu and Tudor, Elizabeth L and Lau, Kwok-Fai and Ackerley, Steven and Warley, Alice and Shaw, Christopher E and Miller, Christopher C.J
Human Molecular Genetics, ISSN 0964-6906, 03/2012, Volume 21, Issue 6, pp. 1299 - 1311
A proline to serine substitution at position 56 in the gene encoding vesicle-associated membrane protein-associated protein B (VAPB) causes some dominantly... 
MOTOR-NEURONS | WILD-TYPE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | LINKED SOD1 MUTANTS | MEMBRANE-PROTEIN | ENDOPLASMIC-RETICULUM | AXONAL-TRANSPORT | MEDIATED TRANSPORT | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | TRANSGENIC MICE | Immunoprecipitation | Calcium - metabolism | Vesicular Transport Proteins - metabolism | Humans | Cercopithecus aethiops | Endoplasmic Reticulum - metabolism | Protein Tyrosine Phosphatases - metabolism | Mitochondrial Proteins - genetics | Immunoenzyme Techniques | Protein Tyrosine Phosphatases - genetics | Mitochondrial Proteins - metabolism | Motor Neurons - cytology | Vesicular Transport Proteins - immunology | Rabbits | Vesicular Transport Proteins - genetics | Cells, Cultured | Rats | Mitochondria - metabolism | Blotting, Western | Motor Neurons - metabolism | Two-Hybrid System Techniques | Amyotrophic Lateral Sclerosis - pathology | Animals | Homeostasis - physiology | Amyotrophic Lateral Sclerosis - metabolism | Tyrosine | Calcium (intracellular) | Serine | Mam protein | Motor neuron disease | Proline | Amyotrophic lateral sclerosis | Cytosol | Organelles | Calcium influx | Membrane proteins | Mitochondria | protein B | Endoplasmic reticulum | Calcium homeostasis
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