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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
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
.... 1H, 15N spectra showed that the C‐terminal SH3 domain of BIN1 isoform 1 (BIN1Iso1) is not mobile in solution but locked with the core of the protein... 
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
PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, p. e0180905
Proteins associated with neurodegenerative diseases are highly pleiomorphic and may adopt an all-a-helical fold in one environment, assemble into all-beta-sheet or collapse into a coil in another... 
ALPHA-SYNUCLEIN OLIGOMERS | ATOMIC-FORCE MICROSCOPY | SOLID-STATE NMR | SODIUM DODECYL-SULFATE | MULTIDISCIPLINARY SCIENCES | PARTIALLY FOLDED STRUCTURE | PAIRED HELICAL FILAMENTS | AMYLOID-BETA-PROTEIN | C-TERMINAL THREONINE | INDUCED CONFORMATIONAL-CHANGES | HUMAN PRION PROTEIN | Protein Aggregates | Protein Structure, Secondary | Humans | Protein Multimerization | Models, Molecular | tau Proteins - metabolism | PrPSc Proteins - chemistry | Protein Folding | tau Proteins - chemistry | PrPSc Proteins - genetics | alpha-Synuclein - chemistry | PrPSc Proteins - metabolism | Animals | tau Proteins - genetics | Amyloid beta-Peptides - genetics | Amyloid beta-Peptides - metabolism | Protein Domains | alpha-Synuclein - genetics | Amyloid beta-Peptides - chemistry | Protein Stability | alpha-Synuclein - metabolism | Electrons | Hydrogen-Ion Concentration | Protein folding | Physiological aspects | Nervous system | Development and progression | Degeneration | Genetic aspects | Research | Coils | Amyloidogenesis | Backbone | Rate constants | Agglomeration | Synuclein | pH effects | Neuromodulation | Modulators | Proteins | Oligomers | Fibrillogenesis | Pathways | Chirality | Chemical bonds | Catalysis | Prion protein | Dimerization | Folding | Linkages | Polypeptides | Incubation | Neurodegenerative diseases | Tertiary structure | Polymerization | Shielding | Secondary structure | Density distribution | Neurological diseases | Chemistry | Tensors | Propagation (polymerization) | Aggregates | Tau protein | Prions | Morphology | β-Amyloid | Dimers | Mutation | Protein structure
Journal Article
Nature neuroscience, ISSN 1546-1726, 2012, Volume 15, Issue 11, pp. 1488 - 1497
... and that encode proteins that are essential... 
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
PloS one, ISSN 1932-6203, 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 partner proteins... 
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
The Journal of biological chemistry, ISSN 0021-9258, 2013, Volume 288, Issue 3, pp. 1856 - 1870
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 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... 
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