[go: up one dir, main page]

Dyment et al., 2015 - Google Patents

Homozygous nonsense mutation in SYNJ1 associated with intractable epilepsy and tau pathology

Dyment et al., 2015

Document ID
9057123659828238198
Author
Dyment D
Smith A
Humphreys P
Schwartzentruber J
Beaulieu C
Bulman D
Majewski J
Woulfe J
Michaud J
Boycott K
FORGE Canada Consortium
et al.
Publication year
Publication venue
Neurobiology of aging

External Links

Snippet

The tauopathies are a heterogeneous group of neurodegenerative disorders characterized by the shared presence of tau aggregates and neurofibrillary tangles within the central nervous system. Here, we present a child with a severe neurodegenerative disorder …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
    • G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2800/00—Detection or diagnosis of diseases
    • G01N2800/28—Neurological disorders
    • G01N2800/2814—Dementia; Cognitive disorders
    • G01N2800/2821—Alzheimer
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
    • C12Q1/6876—Hybridisation probes
    • C12Q1/6883—Hybridisation probes for diseases caused by alterations of genetic material
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2800/00—Detection or diagnosis of diseases
    • G01N2800/28—Neurological disorders
    • G01N2800/2835—Movement disorders, e.g. Parkinson, Huntington, Tourette

Similar Documents

Publication Publication Date Title
Dyment et al. Homozygous nonsense mutation in SYNJ1 associated with intractable epilepsy and tau pathology
Combs et al. Tau and axonal transport misregulation in tauopathies
Nakashima et al. Chronic lithium treatment decreases tau lesions by promoting ubiquitination in a mouse model of tauopathies
Smith et al. Mutations in the vesicular trafficking protein annexin A11 are associated with amyotrophic lateral sclerosis
Stöhr et al. Insulin receptor signaling mediates APP processing and β-amyloid accumulation without altering survival in a transgenic mouse model of Alzheimer’s disease
Zhou et al. Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer's disease
Stroo et al. Cellular regulation of amyloid formation in aging and disease
Zempel et al. Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
Wen et al. VPS35 haploinsufficiency increases Alzheimer’s disease neuropathology
Reddy Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
Schraen-Maschke et al. Tau as a biomarker of neurodegenerative diseases
Valles‐Ortega et al. Neurodegeneration and functional impairments associated with glycogen synthase accumulation in a mouse model of Lafora disease
Braunewell The visinin-like proteins VILIP-1 and VILIP-3 in Alzheimer's disease—old wine in new bottles
Maurel et al. A role for SUMOylation in the formation and cellular localization of TDP-43 aggregates in amyotrophic lateral sclerosis
Connell et al. Quantitative analysis of tau isoform transcripts in sporadic tauopathies
Stopschinski et al. Anatomic survey of seeding in Alzheimer’s disease brains reveals unexpected patterns
Iovino et al. The novel MAPT mutation K298E: mechanisms of mutant tau toxicity, brain pathology and tau expression in induced fibroblast-derived neurons
Tuz et al. The Joubert syndrome-associated missense mutation (V443D) in the Abelson-helper integration site 1 (AHI1) protein alters its localization and protein-protein interactions
Deramecourt et al. Clinical, neuropathological, and biochemical characterization of the novel tau mutation P332S
Trease et al. Hyperphosphorylated human tau accumulates at the synapse, localizing on synaptic mitochondrial outer membranes and disrupting respiration in a mouse model of tauopathy
Iqbal et al. Effect of sodium selenate on hippocampal proteome of 3× Tg-AD mice—exploring the antioxidant dogma of selenium against Alzheimer’s disease
Chu et al. The influence of 5-lipoxygenase on Alzheimer’s disease-related tau pathology: in vivo and in vitro evidence
Houben et al. Tau pathology and adult hippocampal neurogenesis: What tau mouse models tell us?
Chu et al. 5-Lipoxygenase pharmacological blockade decreases tau phosphorylation in vivo: involvement of the cyclin-dependent kinase-5
Renoux et al. Fragile X mental retardation protein expression in Alzheimer’s disease