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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
Molecular biology of the cell, ISSN 1939-4586, 2009, Volume 20, Issue 3, pp. 870 - 881
Using a bioinformatic approach, we identified a TP53INP1-related gene encoding a protein with 30... 
GATE-16 | MOLECULAR MACHINERY | GENE | MEMBRANE-TRANSPORT MODULATOR | PANCREATITIS | INHIBITORS | EXPRESSION | CONJUGATION SYSTEM | GABARAP | SUBUNIT | CELL BIOLOGY | Gene Silencing - drug effects | Microtubule-Associated Proteins - metabolism | Humans | Molecular Sequence Data | Protein Transport - drug effects | Luminescent Measurements | Phylogeny | Autophagy - drug effects | Protein Binding - drug effects | Cloning, Molecular | Conserved Sequence | Carrier Proteins - chemistry | Membrane Proteins - metabolism | Phagosomes - drug effects | Beclin-1 | Amino Acid Sequence | Cell Line | Heat-Shock Proteins - metabolism | Phagosomes - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Sirolimus - pharmacology | Apoptosis Regulatory Proteins - metabolism | Animals | Carrier Proteins - metabolism | Mice | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - chemistry | Heat-Shock Proteins: chemistry,metabolism | Membrane Proteins: metabolism | Protein Binding: drug effects | Gene Silencing: drug effects | Adaptor Proteins, Signal Transducing: metabolism | Life Sciences | Phagosomes: drug effects,metabolism | Apoptosis Regulatory Proteins: metabolism | Nuclear Proteins: chemistry,metabolism | Autophagy: drug effects | Protein Transport: drug effects | Microtubule-Associated Proteins: metabolism | Sirolimus: pharmacology | Carrier Proteins: chemistry,metabolism | Other
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, 2017, Volume 12, Issue 7, p. e0177962
.... We performed comparative analyses in terms of gene and protein expression as well as functional characterizations... 
PROGENITOR CELLS | MESENCHYMAL STROMAL CELLS | STEM-CELLS | TRUNK | MULTIDISCIPLINARY SCIENCES | PERIODONTAL-LIGAMENT | ONTOGENY | GENERATION | SKIN-DERIVED PRECURSORS | DIFFERENTIATION | MELANOCYTES | RNA-Binding Proteins - genetics | Humans | Adipose Tissue - cytology | Melanocytes - metabolism | Neurons - cytology | Receptors, Nerve Growth Factor - metabolism | Neural Stem Cells - cytology | Schwann Cells - cytology | Neural Crest - metabolism | Adipose Tissue - metabolism | Mesenchymal Stromal Cells - cytology | Snail Family Transcription Factors - genetics | Melanocytes - cytology | Nestin - genetics | Adult | Female | Cell Differentiation | Neurons - metabolism | Dermis - cytology | Nuclear Proteins - genetics | Biomarkers - metabolism | SOX9 Transcription Factor - metabolism | Gene Expression | Neural Crest - cytology | Dermis - metabolism | Snail Family Transcription Factors - metabolism | Microinjections | Bone Marrow Cells - cytology | Neural Crest - growth & development | Mesenchymal Stromal Cells - metabolism | Nuclear Proteins - metabolism | Schwann Cells - metabolism | Transcription Factor Brn-3A - metabolism | Chick Embryo | Nerve Tissue Proteins - genetics | Receptors, Nerve Growth Factor - genetics | Nerve Tissue Proteins - metabolism | Nestin - metabolism | Animals | Transcription Factor Brn-3A - genetics | Twist-Related Protein 1 - genetics | Twist-Related Protein 1 - metabolism | Neural Stem Cells - metabolism | SOX9 Transcription Factor - genetics | Bone Marrow Cells - metabolism | Mesenchymal Stem Cell Transplantation | RNA-Binding Proteins - metabolism | Adipose tissues | Comparative analysis | Skin | Neurosciences | Nestin | Adipose tissue | Leukocyte migration | Laboratories | Sox9 protein | Dermis | Melanocytes | Nervous system | Human tissues | Regeneration (physiology) | Cell adhesion & migration | Msi1 protein | Plasticity (neural) | Ethics | Immunology | Pathways | Surgery | Bone marrow | Hair | Hematology | Neurons | Tissue engineering | Schwann cells | Brn-3 protein | Gene expression | Embryos | Neural crest | Medicine | Regeneration | Human performance | Stromal cells | Stem cells | Cell migration | Dental pulp
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 489, Issue 7415, pp. 313 - 317
Cornelia de Lange syndrome (CdLS) is a dominantly inherited congenital malformation disorder, caused by mutations in the cohesin-loading protein NIPBL1,2 for nearly 60... 
SISTER-CHROMATID COHESION | NIPPED-B | COMPLEX | NIPBL | HUMAN GENOME | RNA-SEQ | MULTIDISCIPLINARY SCIENCES | X-CHROMOSOME-INACTIVATION | S-PHASE | PROTEINS | BINDING | Chromatin - metabolism | Chondroitin Sulfate Proteoglycans - chemistry | Humans | Crystallography, X-Ray | Male | Phosphoproteins - metabolism | Cell Cycle Proteins - chemistry | Chromatin Immunoprecipitation | Repressor Proteins - deficiency | De Lange Syndrome - metabolism | Fibroblasts | Female | Transcription, Genetic | Acetylation | Binding Sites | Repressor Proteins - metabolism | De Lange Syndrome - genetics | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histone Deacetylases - genetics | Cell Cycle Proteins - metabolism | Chondroitin Sulfate Proteoglycans - metabolism | Histone Deacetylases - chemistry | Histone Deacetylases - deficiency | Mutant Proteins - genetics | Prophase | Models, Molecular | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Mutation - genetics | Proteins - genetics | Mutant Proteins - chemistry | Protein Conformation | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Anaphase | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Genetics | De Lange syndrome | Genetic aspects | Research | Mutation (Biology) | Proteins | Cell culture | Genes | Cell cycle | Mutation | Females | Chromosomes | Crystal structure | Chromatin | Repressor Proteins | Life Sciences | Phosphoproteins | Chromosomal Proteins, Non-Histone | Histone Deacetylases | De Lange Syndrome | Chondroitin Sulfate Proteoglycans | Nuclear Proteins | Mutant Proteins | Adaptor Proteins, Signal Transducing | Development Biology | Cell Cycle Proteins
Journal Article
Nature Immunology, ISSN 1529-2908, 12/2013, Volume 14, Issue 12, pp. 1247 - 1255
The inflammasome adaptor ASC contributes to innate immunity through the activation of caspase-1. Here we found that signaling pathways dependent on the kinases... 
LISTERIA-MONOCYTOGENES | AIM2 INFLAMMASOME | PROTEIN | INNATE IMMUNE-RESPONSES | MACROPHAGES | KINASE | HOST-DEFENSE | NLRP3 INFLAMMASOME | IMMUNOLOGY | CASPASE-1 ACTIVATION | VIRAL-INFECTION | Interleukin-18 - immunology | Inflammasomes - metabolism | Cytoskeletal Proteins - genetics | NLR Family, Pyrin Domain-Containing 3 Protein | Protein-Tyrosine Kinases - metabolism | Dendritic Cells - immunology | Humans | JNK Mitogen-Activated Protein Kinases - immunology | Caspase 1 - metabolism | Immunoblotting | Intracellular Signaling Peptides and Proteins - metabolism | RNA Interference | Bone Marrow Cells - immunology | Phosphorylation - immunology | JNK Mitogen-Activated Protein Kinases - genetics | Intracellular Signaling Peptides and Proteins - genetics | Syk Kinase | Carrier Proteins - immunology | DNA-Binding Proteins | Tyrosine - immunology | Mice, Knockout | Macrophages - metabolism | Tyrosine - metabolism | Lipopolysaccharides - pharmacology | Mice | Interleukin-18 - metabolism | Intracellular Signaling Peptides and Proteins - immunology | JNK Mitogen-Activated Protein Kinases - metabolism | Caspase 1 - immunology | Protein-Tyrosine Kinases - immunology | Protein-Tyrosine Kinases - genetics | HEK293 Cells | Cytoskeletal Proteins - metabolism | Female | Nuclear Proteins - genetics | Dendritic Cells - metabolism | Macrophages - immunology | Mice, Inbred C57BL | Cells, Cultured | Nuclear Proteins - metabolism | Nuclear Proteins - immunology | Inflammasomes - genetics | Carrier Proteins - genetics | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | Cytoskeletal Proteins - immunology | CARD Signaling Adaptor Proteins | Inflammasomes - immunology | Macrophages - drug effects | Nigericin - pharmacology | Bone Marrow Cells - metabolism | Tyrosine - genetics | Cellular signal transduction | Inflammation | Genetic aspects | Research | Properties | Phosphotransferases
Journal Article
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
eLife, ISSN 2050-084X, 2015, Volume 4, Issue 4, pp. 1 - 44
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family... 
N-Ethylmaleimide-Sensitive Proteins - metabolism | Mad2 Proteins - metabolism | Molecular Chaperones - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Crystallography, X-Ray | Phylogeny | N-Ethylmaleimide-Sensitive Proteins - genetics | Amino Acid Sequence | Gene Expression | Caenorhabditis elegans - genetics | Cell Cycle Proteins - metabolism | Molecular Chaperones - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - chemistry | Caenorhabditis elegans - classification | Escherichia coli - genetics | Adenosine Triphosphatases - genetics | Escherichia coli Proteins - chemistry | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Adaptor Proteins, Signal Transducing - chemistry | Endopeptidase Clp - chemistry | M Phase Cell Cycle Checkpoints | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Molecular Chaperones - chemistry | Cell Cycle Proteins - chemistry | Spindle Apparatus - genetics | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | N-Ethylmaleimide-Sensitive Proteins - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | ATPases Associated with Diverse Cellular Activities | Endopeptidase Clp - genetics | Escherichia coli Proteins - metabolism | Nuclear Proteins - metabolism | Endopeptidase Clp - metabolism | Mad2 Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Mad2 Proteins - genetics | Escherichia coli Proteins - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Spindle Apparatus - enzymology | Proteins | Medical research | Recombination | Software | Meiosis | Mammals | Chromosomes | DNA repair | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | BASIC BIOLOGICAL SCIENCES
Journal Article