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Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
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
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 EMBO Journal, ISSN 0261-4189, 11/2017, Volume 36, Issue 21, pp. 3120 - 3138
The cause of protein accumulation in neurodegenerative disease is incompletely understood. In Alzheimer's disease (AD), the axonally enriched protein Tau forms... 
amyloid‐β | protein synthesis | microtubule‐associated protein Tau | Src kinase Fyn | proximity ligation assay | amyloid-β | microtubule-associated protein Tau | S6 PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CEREBROSPINAL-FLUID | SYNAPTIC PLASTICITY | MOUSE MODELS | CELL BIOLOGY | amyloid-beta | COGNITIVE IMPAIRMENTS | PRION PROTEIN | MESSENGER-RNA | T-CELLS | AMYLOID-BETA OLIGOMERS | TRANSGENIC MICE | Neurons - pathology | Protein Biosynthesis | Ribosomal Protein S6 Kinases - metabolism | Embryo, Mammalian | Humans | Injections, Intraventricular | tau Proteins - metabolism | Male | Alzheimer Disease - pathology | MAP Kinase Signaling System | Proto-Oncogene Proteins c-fyn - genetics | Neurons - ultrastructure | tau Proteins - genetics | Amyloid beta-Protein Precursor - metabolism | HEK293 Cells | Puromycin - pharmacology | Neurons - metabolism | Amyloid beta-Peptides - administration & dosage | Mice, Inbred C57BL | Peptide Fragments - administration & dosage | Gene Expression Regulation | Hippocampus - pathology | Mice, Knockout | Stereotaxic Techniques | Hippocampus - metabolism | Amyloid beta-Protein Precursor - genetics | Animals | Proto-Oncogene Proteins c-fyn - metabolism | Alzheimer Disease - metabolism | Mice | Alzheimer Disease - genetics | Ribosomal Protein S6 Kinases - genetics | Phosphorylation | Translation | Neurodegenerative diseases | Extracellular signal-regulated kinase | Protein biosynthesis | Activation | Pharmacology | Agglomeration | Kinases | Accumulation | Proteins | Signal transduction | Signaling | Detachment | Clonal deletion | Tau protein | Protein synthesis | Microtubules | Deletion | β-Amyloid | Transduction | Alzheimers disease | Alzheimer's disease | Fyn protein | Neuroscience | Protein Biosynthesis & Quality Control
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
The FEBS Journal, ISSN 1742-464X, 05/2017, Volume 284, Issue 9, pp. 1279 - 1295
The ubiquitous eukaryotic 14‐3‐3 proteins coordinate multiple cellular processes due to their well‐known regulatory function, which is based on specific... 
hydrophobicity | signal transduction | dimer interface | aggregation | oligomeric structure | neurodegenerative disorders | chaperones | phosphorylation | 14‐3‐3 proteins | dimer–monomer equilibrium | 14-3-3 proteins | TAU-PROTEIN | FUNCTIONAL INTERACTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOFORM-SPECIFIC MANNER | SUBCELLULAR-LOCALIZATION | ALPHA-CRYSTALLIN | RAT-LIVER CYTOSOL | PRECURSOR PROTEINS | dimer-monomer equilibrium | MOLECULAR CHAPERONE | C-TERMINAL EXTENSION | MITOCHONDRIAL IMPORT | Phosphorylation | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Protein Refolding | Models, Molecular | Molecular Chaperones - chemistry | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Animals | Hydrophobic and Hydrophilic Interactions | 14-3-3 Proteins - chemistry | Protein Conformation | Protein Interaction Domains and Motifs | Protein Processing, Post-Translational | Binding Sites | Dimerization | Molecular Chaperones - agonists | Heat shock proteins | Control systems | Nervous system diseases | Prions | Huntingtin | Aggresomes | Neurodegenerative diseases | Hydrophobicity | Chaperones | Small heat shock proteins | Synuclein | Proteins | 14-3-3 protein | Eukaryotes | Molecular modelling | Tau protein | Protein folding | Quality control | Proteasomes | Molecular biology | Prion protein
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, p. e0178933
Abundant regulatory 14-3-3 proteins have an extremely wide interactome and coordinate multiple cellular events via interaction with specifically phosphorylated... 
Exoribonucleases - genetics | Phosphorylation | Humans | tau Proteins - metabolism | Protein Interaction Maps | Cyclic AMP-Dependent Protein Kinases - genetics | Protein Isoforms - metabolism | tau Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Parkinson Disease - metabolism | Exoribonucleases - analysis | 14-3-3 Proteins - genetics | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Expression | Biomarkers, Tumor - analysis | Protein Isoforms - analysis | 14-3-3 Proteins - metabolism | Cyclic AMP-Dependent Protein Kinases - analysis | 14-3-3 Proteins - analysis | Escherichia coli - genetics | Alzheimer Disease - metabolism | Biomarkers, Tumor - genetics | tau Proteins - analysis | Exoribonucleases - metabolism | Protein Isoforms - genetics | Research | Protein kinases | Protein-protein interactions | Protein kinase A | Stoichiometry | Residues | Identification methods | Disorders | Displays | Biochemistry | Biology | Kinases | Proteins | Signal transduction | Functional anatomy | E coli | Rodents | Bacteria | Physiology | Binding | Neurodegenerative diseases | Fetuses | Cloning | Diseases | Studies | Neurological diseases | 14-3-3 protein | Tau protein | Protein kinase | Plasmids | Isoforms | Protein expression | Regulation | Alzheimers disease | In vitro methods and tests | Binding sites | Apoptosis
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