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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
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
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase
Journal Article
Oncogene, ISSN 0950-9232, 01/2016, Volume 35, Issue 1, pp. 12 - 21
Journal Article
Neuron, ISSN 0896-6273, 2005, Volume 47, Issue 6, pp. 817 - 831
The molecular mechanisms controlling the differentiation of neural progenitors into distinct subtypes of neurons during neocortical development are unknown.... 
AREA IDENTITY | MIGRATION | CELL FATE SPECIFICATION | IN-VIVO | MOUSE | CENTRAL-NERVOUS-SYSTEM | ZINC-FINGER GENE | SUBVENTRICULAR ZONE | EXPRESSION | NEUROSCIENCES | CEREBRAL-CORTEX | Membrane Glycoproteins - metabolism | Embryo, Mammalian | Homeodomain Proteins - metabolism | Nerve Tissue Proteins - deficiency | S100 Proteins - genetics | POU Domain Factors - genetics | Forkhead Transcription Factors - metabolism | In Situ Hybridization - methods | Repressor Proteins - metabolism | Gene Expression Regulation, Developmental - physiology | POU Domain Factors - metabolism | Animals, Newborn | DNA-Binding Proteins - physiology | Motor Neurons - physiology | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cell Cycle Proteins - metabolism | S100 Proteins - metabolism | In Situ Nick-End Labeling - methods | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Immunohistochemistry - methods | Annexin A2 - genetics | Cell Death - physiology | Green Fluorescent Proteins - biosynthesis | Mice | Annexin A2 - metabolism | Age Factors | Phosphopyruvate Hydratase - metabolism | Cell Movement - physiology | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | Amino Acids - metabolism | Motor Neurons - cytology | Tumor Suppressor Proteins - genetics | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Bromodeoxyuridine - metabolism | Cell Differentiation - physiology | Pyramidal Tracts - physiology | Nerve Tissue Proteins - physiology | Neocortex - growth & development | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Dopamine and cAMP-Regulated Phosphoprotein 32 - metabolism | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Membrane Glycoproteins - genetics | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Cell Count - methods | Neocortex - cytology | Receptors, Antigen, T-Cell, alpha-beta - metabolism | Neurosciences | Neurons | Developmental biology | Stem cells | Studies | Brain | Ultrasonic imaging | Transcription factors | Hybridization | Neurogenesis
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
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 37, pp. 15287 - 15300
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates... 
CONSERVED CYSTEINE | HUMAN PTS1 RECEPTOR | DOCKING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYCLING RECEPTOR | MACHINERY | MEMBRANE-PROTEIN | II SECRETION SYSTEM | AAA PEROXINS | TARGETING SIGNAL RECEPTOR | IMPORT RECEPTOR | Humans | Protein Multimerization | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Biological Transport | Gene Deletion | Receptors, Cytoplasmic and Nuclear - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Solubility | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Fusion Proteins - chemistry | Peroxisomes - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Models, Biological | Peroxisome-Targeting Signal 1 Receptor | Endopeptidase K - metabolism | Mutation | Intracellular Membranes - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Receptors, Cytoplasmic and Nuclear - metabolism | ubiquitylation (ubiquitination) | docking | PEX5 | peroxisome | translocation module | protein import | protein sorting | receptor recycling | PEX14 | Cell Biology
Journal Article
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2010, Volume 39, Issue 6, pp. 963 - 974
... a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive... 
NECDIN GENE | EMERGING ROLES | MELANOMA | KAP1 | CANCER/TESTIS ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MDM2 INTERACTION | HOMOLOGOUS RECOMBINATION | CANCER-IMMUNOTHERAPY | CELL-LINES | EXPRESSION | CELL BIOLOGY | Melanoma-Specific Antigens - chemistry | Protein Interaction Domains and Motifs - physiology | Humans | Crystallography, X-Ray | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | RING Finger Domains | Tripartite Motif-Containing Protein 28 | Ubiquitination | Cell Nucleus - metabolism | Transfection | Protein Structure, Quaternary | Antigens, Neoplasm - metabolism | Carrier Proteins - chemistry | Neoplasm Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Antigens, Neoplasm - genetics | Cell Line | Biocatalysis | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Recombinant Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Melanoma-Specific Antigens - metabolism | Cell Line, Tumor | Ubiquitin-Protein Ligases - genetics | Melanoma-Specific Antigens - genetics | Protein Binding - physiology | Ubiquitin | Antigens | Ligases | Crystals | Melanoma | Structure | Tumor proteins | Protein binding
Journal Article
The Journal of clinical investigation, ISSN 0021-9738, 2009, Volume 119, Issue 12, pp. 3626 - 3636
The polycomb group protein B lymphoma Mo-MLV insertion region 1 homolog (Bmi-1) is dysregulated in various cancers, and its upregulation strongly correlates... 
MEDICINE, RESEARCH & EXPERIMENTAL | BREAST-CANCER CELLS |