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Nature Neuroscience, ISSN 1097-6256, 11/2012, Volume 15, Issue 11, pp. 1488 - 1497
FUS/TLS (fused in sarcoma/translocated in liposarcoma) and TDP-43 are integrally involved in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia.... 
NEURODEGENERATIVE DISEASE | GENE | AMYOTROPHIC-LATERAL-SCLEROSIS | FAMILY PROTEINS | FUS PATHOLOGY | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | BINDING | NEUROSCIENCES | BRAIN | NASCENT TRANSCRIPTION | RNA, Small Interfering - genetics | Protein Binding - genetics | Oligonucleotide Array Sequence Analysis | Humans | tau Proteins - metabolism | Gene Expression Profiling | RNA, Messenger - metabolism | Kv Channel-Interacting Proteins - metabolism | Brain - metabolism | Frontotemporal Dementia - metabolism | RNA Splicing - genetics | Frontotemporal Dementia - genetics | RNA-Binding Protein FUS - deficiency | Amyotrophic Lateral Sclerosis - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | RNA-Binding Protein FUS - genetics | Mice, Knockout | Motor Neurons - metabolism | Amyotrophic Lateral Sclerosis - pathology | Shal Potassium Channels - metabolism | Brain - pathology | Mice | Neurofilament Proteins - metabolism | RNA, Small Interfering - metabolism | Immunoprecipitation | Spinal Cord - metabolism | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | tau Proteins - genetics | Cell Cycle Proteins - genetics | Female | RNA Precursors - metabolism | Excitatory Amino Acid Transporter 2 - genetics | Membrane Proteins - metabolism | Frontotemporal Dementia - pathology | Gene Expression Regulation - genetics | Mice, Inbred C57BL | RNA, Messenger - genetics | RNA Precursors - genetics | Protein Structure, Tertiary - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | Excitatory Amino Acid Transporter 2 - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Neural Cell Adhesion Molecules - metabolism | Neural Stem Cells - metabolism | Cell Line, Transformed | Amyotrophic lateral sclerosis | Development and progression | Genetic aspects | Messenger RNA | Health aspects
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
Neuron, ISSN 0896-6273, 08/2012, Volume 75, Issue 4, pp. 618 - 632
Mitochondrial abnormalities have been documented in Alzheimer’s disease and related neurodegenerative disorders, but the causal relationship between... 
ALZHEIMERS-DISEASE BRAIN | DOMINANT OPTIC ATROPHY | MITOCHONDRIAL-FUNCTION | MOUSE MODEL | LIGHT-CHAIN | FRONTOTEMPORAL DEMENTIA | AXONAL-TRANSPORT | NEUROSCIENCES | DYNAMIN-RELATED PROTEIN | PHOSPHORYLATION SITES | TRANSGENIC MICE | Neurons - pathology | Microtubule-Associated Proteins - genetics | Tauopathies - genetics | Cytoskeletal Proteins - genetics | Gelsolin - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Actins - metabolism | Tauopathies - pathology | Cytoplasm - metabolism | MicroRNAs - metabolism | Green Fluorescent Proteins - genetics | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | GTP-Binding Proteins - genetics | Nerve Degeneration - metabolism | Neurons - ultrastructure | tau Proteins - genetics | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | ATP Synthetase Complexes - metabolism | Cell Cycle Proteins - genetics | Tauopathies - complications | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Cytoplasm - genetics | RNA Interference - physiology | Disease Models, Animal | In Situ Nick-End Labeling | Green Fluorescent Proteins - metabolism | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | Cell Cycle Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Animals | GTP Phosphohydrolases - metabolism | Analysis of Variance | GTP Phosphohydrolases - genetics | Gelsolin - genetics | Mice | Drosophila Proteins - genetics | Nerve Degeneration - etiology | Voltage-Dependent Anion Channels - metabolism | GTP-Binding Proteins - metabolism | Nervous system diseases | Actin | Neurons | Utrophin | Myosin | Mitochondrial DNA | Alzheimer's disease | Proteins | Phosphorylation | Mitochondria | Neurotoxicity | Insects | Microscopy | Neurodegeneration | Pathogenesis | Morphology | Mutation | Defects | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2687 - 2700
The microtubule-associated protein tau forms insoluble, amyloid-type aggregates in various dementias, most notably Alzheimer's disease. Cellular chaperone... 
HEAT-SHOCK PROTEINS | NEUROFIBRILLARY TANGLES | OXIDATIVE STRESS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FRONTOTEMPORAL DEMENTIA | PAIRED HELICAL FILAMENTS | ALPHA-B-CRYSTALLIN | PLASTICITY DEFICITS | BETA-STRUCTURE | AGGREGATION | HSP27 Heat-Shock Proteins - chemistry | HSC70 Heat-Shock Proteins - metabolism | Humans | tau Proteins - metabolism | Amyloid - chemistry | Amyloid - ultrastructure | HSC70 Heat-Shock Proteins - ultrastructure | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | HSP27 Heat-Shock Proteins - genetics | HSP27 Heat-Shock Proteins - ultrastructure | Protein Isoforms - metabolism | tau Proteins - genetics | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Protein Isoforms - chemistry | Amyloid - drug effects | Protein Interaction Domains and Motifs | Dimerization | Heparin - pharmacology | tau Proteins - ultrastructure | HSC70 Heat-Shock Proteins - genetics | Solubility | Models, Molecular | Recombinant Fusion Proteins - chemistry | Down-Regulation - drug effects | Amino Acid Motifs | Cryoelectron Microscopy | HSC70 Heat-Shock Proteins - chemistry | Anticoagulants - pharmacology | HSP27 Heat-Shock Proteins - metabolism | Kinetics | Mutation | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Protein Structure and Folding | amyloid | chaperone | 70 kilodalton heat shock protein (Hsp70) | tau | aggregation | small heat shock protein (sHsp)
Journal Article
Protein Science, ISSN 0961-8368, 11/2017, Volume 26, Issue 11, pp. 2126 - 2150
The role of microtubule‐associated protein Tau in neurodegeneration has been extensively investigated since the discovery of Tau amyloid aggregates in the... 
tauopathies | Tau protein | amyloidogenesis | Alzheimer's disease | protein aggregation | FULL-LENGTH TAU | UBIQUITIN-PROTEASOME SYSTEM | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FIBRILLIZATION IN-VITRO | WILD-TYPE TAU | NEURODEGENERATIVE DISEASES | PAIRED HELICAL FILAMENTS | PROLYL ISOMERASE PIN1 | CREUTZFELDT-JAKOB-DISEASE | AMYLOID FIBRIL FORMATION | Neurons - pathology | Humans | tau Proteins - metabolism | Amyloid - ultrastructure | Prion Proteins - metabolism | tau Proteins - chemistry | Alzheimer Disease - pathology | tau Proteins - genetics | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Amyloidosis - genetics | Protein Domains | Neurons - metabolism | Prion Proteins - chemistry | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Amyloidosis - pathology | Neurons - chemistry | Protein Structure, Secondary | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | Protein Processing, Post-Translational | Alzheimer Disease - genetics | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Intrinsically Disordered Proteins - metabolism | Nervous system diseases | Amyloidosis | Prions | Amyloidogenesis | Self assembly | Brain | Seeds | Peptides | Molecular structure | Agglomeration | Monomers | Proteins | Literature reviews | Fibrillogenesis | Neurodegeneration | Post-translation | Prion protein | Neurodegenerative diseases | Pathological effects | Neurological diseases | Self-assembly | Aggregates | β-Amyloid | Mutation | Alzheimers disease | Protein interaction | Reviews | Review
Journal Article
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
Bridging integrator 1 (bin1) gene is a genetic determinant of Alzheimer's disease (AD) and has been reported to modulate Alzheimer's pathogenesis through... 
SH3 domain | nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | BIN1 | Alzheimer's disease | ALZHEIMERS-DISEASE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOLOGY | MODEL | IDENTIFIES VARIANTS | AMPHIPHYSIN | MEMBRANE CURVATURE | protein-protein interaction | BINDING | EXPRESSION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Humans | Peptides - genetics | tau Proteins - metabolism | tau Proteins - chemistry | Peptides - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Protein Isoforms - chemistry | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Neurons - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Neurons - chemistry | Peptides - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Nuclear Proteins - chemistry | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Nuclear magnetic resonance spectroscopy | Neurons | Protein-protein interactions | Spectroscopy | Clathrin | Nuclear magnetic resonance--NMR | Peptides | Neurodegenerative diseases | Pathogenesis | Complexity | Proteins | Magnetic resonance spectroscopy | Tau protein | Spectrum analysis | Isoforms | Alzheimers disease | Binding sites | tau Proteins/metabolism | Nuclear Proteins/chemistry | Protein Isoforms/chemistry | Protein Isoforms/genetics | Adaptor Proteins, Signal Transducing/genetics | Recombinant Proteins/metabolism | Peptides/metabolism | Life Sciences | Recombinant Proteins/chemistry | Adaptor Proteins, Signal Transducing/chemistry | Nuclear Proteins/metabolism | Tumor Suppressor Proteins/chemistry | Nuclear Proteins/genetics | Tumor Suppressor Proteins/metabolism | Protein Isoforms/metabolism | Peptides/chemistry | Recombinant Proteins/genetics | Biochemistry, Molecular Biology | Escherichia coli/genetics | Escherichia coli/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Neurons/chemistry | Tumor Suppressor Proteins/genetics | tau Proteins/genetics | Neurons/metabolism | Peptides/genetics | tau Proteins/chemistry
Journal Article
Neuron, ISSN 0896-6273, 02/2013, Volume 77, Issue 3, pp. 472 - 484
Major outputs of the neocortex are conveyed by corticothalamic axons (CTAs), which form reciprocal connections with thalamocortical axons, and... 
MUTANT MICE | CORTICAL AXONS | THALAMOCORTICAL AXONS | GROWTH | SEMAPHORIN 3E | CENTRAL-NERVOUS-SYSTEM | GUIDANCE | CHICK HINDLIMB | CAJAL-RETZIUS CELLS | NEUROSCIENCES | CEREBRAL-CORTEX | Thyroid Nuclear Factor 1 | Age Factors | Embryo, Mammalian | Leukocyte L1 Antigen Complex - metabolism | Gene Expression Regulation, Developmental - genetics | Axons - physiology | Cerebral Cortex - cytology | Neural Pathways - physiology | DNA-Binding Proteins - metabolism | POU Domain Factors - genetics | tau Proteins - genetics | Thalamus - physiology | Contactin 2 - metabolism | Repressor Proteins - metabolism | Glycoproteins - genetics | Tumor Suppressor Proteins - metabolism | Wnt3A Protein - genetics | Membrane Proteins - genetics | Mice, Inbred C57BL | Mice, Transgenic | Nuclear Proteins - metabolism | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Membrane Glycoproteins - genetics | Nerve Tissue Proteins - metabolism | S100 Calcium Binding Protein G - metabolism | Transcription Factors - metabolism | Animals | Calbindin 2 | Thalamus - cytology | Cerebral Cortex - physiology | Luminescent Proteins - genetics | Mice | Body Patterning - genetics | Luminescent Proteins - metabolism | Developmental biology | Neurons | Studies | Laboratories | Experiments | Repressor Proteins | Cerebral Cortex | Cellular Biology | Neural Pathways | tau Proteins | Life Sciences | Contactin 2 | Gene Expression Regulation, Developmental | Body Patterning | Thalamus | Membrane Glycoproteins | Luminescent Proteins | DNA-Binding Proteins | POU Domain Factors | Calcium-Binding Protein, Vitamin D-Dependent | Glycoproteins | Nerve Tissue Proteins | Nuclear Proteins | Membrane Proteins | Axons | Homeodomain Proteins | Leukocyte L1 Antigen Complex | Transcription Factors | Wnt3A Protein | Tumor Suppressor Proteins | reciprocal connections | handshake | waiting period | PlexinD1 | axon guidance | Sema3E | thalamocortical | corticothalamic
Journal Article
EMBO reports, ISSN 1469-221X, 11/2017, Volume 18, Issue 11, pp. 2051 - 2066
Endocytic processes are facilitated by both curvature‐generating BAR‐domain proteins and the coordinated polymerization of actin filaments. Under physiological... 
tau | N‐BAR protein Bin1 | Alzheimer's disease | actin binding | genetic risk factor | N-BAR protein Bin1 | PROTEIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | FILAMENT TURNOVER | TAU PATHOLOGY | CELL BIOLOGY | SKELETAL-MUSCLE | STRUCTURAL BASIS | SYNAPTIC VESICLE ENDOCYTOSIS | MEMBRANE CURVATURE | SH3 DOMAIN | Tauopathies - genetics | Humans | Actins - metabolism | Tauopathies - pathology | tau Proteins - metabolism | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Actin Cytoskeleton - genetics | Disease Models, Animal | Recombinant Proteins - metabolism | Gene Expression | Tumor Suppressor Proteins - metabolism | Actin Cytoskeleton - metabolism | Genetic Vectors - chemistry | Gene Expression Regulation | Genetic Vectors - metabolism | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Transcription Factors - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Tauopathies - metabolism | Animals | Carrier Proteins - metabolism | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Membranes | Neurodegenerative diseases | Drosophila | Health risks | Polymerization | Rods | Bundles | Risk factors | Membrane proteins | Bundling | Proteins | Depolymerization | Insects | Tau protein | Filaments | Neurodegeneration | Actin | Isoforms | BAR protein | Cytoskeleton | Alzheimers disease | Curvature | Neuroscience | Cell Adhesion, Polarity & Cytoskeleton
Journal Article