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Nature, ISSN 0028-0836, 09/2012, 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... 
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
Oncogene, ISSN 0950-9232, 01/2016, Volume 35, Issue 1, pp. 12 - 21
Journal Article
PLoS Pathogens, ISSN 1553-7366, 11/2013, Volume 9, Issue 11, p. e1003773
Interferons (IFNs) are a group of cytokines with a well-established antiviral function. They can be induced by viral infection, are secreted and bind to... 
CELLS | DEFENSE | VIRUS-INFECTION | DISTINCT | RIG-I | MICROBIOLOGY | IRF-7 | ANTIVIRAL RESPONSE | VIROLOGY | GENE | SIGNALING PATHWAY | ADAPTER PROTEIN | PARASITOLOGY | Epithelial Cells - metabolism | Influenza A virus - genetics | Respiratory Mucosa - virology | Interferon Regulatory Factor-7 - genetics | Interferon Type I - immunology | Interferon Regulatory Factor-3 - genetics | Interleukins - metabolism | Orthomyxoviridae Infections - genetics | Respiratory Mucosa - pathology | Interleukins - genetics | Interleukins - immunology | Respiratory Mucosa - immunology | Adaptor Proteins, Signal Transducing - immunology | Interferon Type I - metabolism | Influenza A virus - immunology | Membrane Proteins - metabolism | Interferon Regulatory Factor-3 - immunology | Nerve Tissue Proteins - immunology | Membrane Proteins - genetics | Orthomyxoviridae Infections - metabolism | Epithelial Cells - pathology | Membrane Proteins - immunology | Interferon Regulatory Factor-7 - immunology | Interferon Regulatory Factor-7 - metabolism | Nerve Tissue Proteins - genetics | Mice, Knockout | Nerve Tissue Proteins - metabolism | Animals | Influenza A virus - metabolism | Epithelial Cells - immunology | Epithelial Cells - virology | Adaptor Proteins, Signal Transducing - genetics | Interferon Regulatory Factor-3 - metabolism | Interferon Type I - genetics | Mice | Respiratory Mucosa - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Orthomyxoviridae Infections - immunology | Epithelial cells | Influenza | Physiological aspects | Host-parasite relationships | Interferon | Genetic aspects | Genetic transcription | Research | Health aspects | Airway (Medicine) | Interleukins/metabolism | Nerve Tissue Proteins/immunology | Orthomyxoviridae Infections/genetics | Orthomyxoviridae Infections/metabolism | Membrane Proteins/genetics | Adaptor Proteins, Signal Transducing/genetics | Interferon Regulatory Factor-7/genetics | Interleukins/immunology | Membrane Proteins/immunology | Life Sciences | Orthomyxoviridae Infections/immunology | Influenza A virus/genetics | Nerve Tissue Proteins/metabolism | Respiratory Mucosa/immunology | Immunology | Interferon Type I/immunology | Epithelial Cells/immunology | Epithelial Cells/virology | Interferon Regulatory Factor-7/immunology | Epithelial Cells/metabolism | Interferon Regulatory Factor-3/immunology | Respiratory Mucosa/pathology | Influenza A virus/immunology | Interleukins/genetics | Interferon Regulatory Factor-3/genetics | Influenza A virus/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Epithelial Cells/pathology | Adaptor Proteins, Signal Transducing/immunology | Interferon Type I/genetics | Interferon Regulatory Factor-3/metabolism | Membrane Proteins/metabolism | Nerve Tissue Proteins/genetics | Interferon Regulatory Factor-7/metabolism | Interferon Type I/metabolism | Respiratory Mucosa/metabolism | Respiratory Mucosa/virology | Cytokines | Genes | Rodents | Genomics | Genomes | Kinases | Experiments | Viral infections
Journal Article
Journal Article
Developmental Cell, ISSN 1534-5807, 07/2016, Volume 38, Issue 1, pp. 86 - 99
Journal Article
Journal of Molecular Recognition, ISSN 0952-3499, 03/2010, Volume 23, Issue 2, pp. 105 - 116
Recognition requires protein flexibility because it facilitates conformational rearrangements and induced‐fit mechanisms upon target binding. Intrinsic... 
disorder‐to‐order transition | NMR | Sic1 | polyelectrostatic effect | dynamic complex | protein dynamics | disordered complex | conformational disorder | Dynamic complex | Disordered complex | Polyelectrostatic effect | Protein dynamics | Conformational disorder | Disorder-to-order transition | SIDE-CHAIN DYNAMICS | DEUTERIUM SPIN PROBES | BIOCHEMISTRY & MOLECULAR BIOLOGY | disorder-to-order transition | INTRINSICALLY UNSTRUCTURED PROTEINS | UBIQUITIN LIGASES | SUBSTRATE RECOGNITION | BIOPHYSICS | HUB PROTEINS | RECEPTOR ZETA-CHAIN | STRUCTURAL DISORDER | ORDER PARAMETERS | INTERACTION NETWORKS | Adaptor Proteins, Signal Transducing - chemistry | Receptors, Antigen, T-Cell - chemistry | Phosphorylation | Receptors, Antigen, T-Cell - metabolism | F-Box Proteins - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Cyclin-Dependent Kinase Inhibitor Proteins - metabolism | Ubiquitin-Protein Ligases - chemistry | Protein Folding | Cell Cycle Proteins - chemistry | Thermodynamics | Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Cyclin-Dependent Kinase Inhibitor Proteins - chemistry | Protein Binding | Protein Conformation | Proteins - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Binding | Proteins | Dynamics | Evolutionary | Disorders | Charge | Order disorder | Recognition
Journal Article
Nature Medicine, ISSN 1078-8956, 2011, Volume 17, Issue 6, pp. 720 - 725
Myotonic dystrophy is the most common muscular dystrophy in adults and the first recognized example of an RNA-mediated disease. Congenital myotonic dystrophy... 
MEDICINE, RESEARCH & EXPERIMENTAL | CTG REPEAT | CENTRONUCLEAR MYOPATHY | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MYOTUBULAR MYOPATHY | CELL BIOLOGY | SKELETAL-MUSCLE | MESSENGER-RNA | GENE | CHLORIDE CHANNEL | AMPHIPHYSIN-2 BIN1 | MUTATIONS | Cell Line | RNA-Binding Proteins - physiology | Humans | Alternative Splicing - physiology | Exons - genetics | Muscle Weakness - genetics | Protein Isoforms - physiology | Tumor Suppressor Proteins - physiology | Adaptor Proteins, Signal Transducing - physiology | Myotonic Dystrophy - physiopathology | Animals | Tumor Suppressor Proteins - genetics | Adaptor Proteins, Signal Transducing - genetics | Myotonic Dystrophy - genetics | Mice | Nuclear Proteins - physiology | Muscle Weakness - physiopathology | Nuclear Proteins - genetics | Muscle Fibers, Skeletal - physiology | RNA-Binding Proteins - metabolism | Protein Isoforms - genetics | Muscle weakness | Myotonic dystrophy | RNA | Physiological aspects | Genetic aspects | Research | Risk factors | Musculoskeletal diseases | Musculoskeletal system | Biosynthesis | Protein synthesis | Muscular dystrophy | Alternative Splicing | Exons | Myotonic Dystrophy | RNA-Binding Proteins | Nuclear Proteins | Life Sciences | Adaptor Proteins, Signal Transducing | Muscle Fibers, Skeletal | Protein Isoforms | Muscle Weakness | Tumor Suppressor Proteins | Cancer | Naturvetenskap | Natural Sciences
Journal Article
Molecular Cell, ISSN 1097-2765, 2009, Volume 35, Issue 5, pp. 563 - 573
The target of rapamycin complex 1 (TORC1) is a central regulator of eukaryotic cell growth that is activated by a variety of hormones (e.g., insulin) and... 
CELLBIO | PROTEINS | SIGNALING | YEAST SACCHAROMYCES-CEREVISIAE | CELL-GROWTH CONTROL | SIGNALING PATHWAYS | FUNCTIONAL HOMOLOG | RAG GTPASES | VACUOLE FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMINO-ACID PERMEASE | COMPONENT | GTP-BINDING PROTEINS | GAP1 PERMEASE | CELL BIOLOGY | Vacuoles - enzymology | Intracellular Membranes - enzymology | Saccharomyces cerevisiae - genetics | Multiprotein Complexes | Adaptor Proteins, Vesicular Transport - genetics | Saccharomyces cerevisiae - drug effects | Guanosine Triphosphate - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Vacuoles - drug effects | DNA-Binding Proteins - metabolism | Amino Acids - metabolism | Time Factors | Guanine Nucleotide Exchange Factors - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Guanosine Diphosphate - metabolism | Protein Synthesis Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - metabolism | Guanine Nucleotide Exchange Factors - genetics | Signal Transduction | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Monomeric GTP-Binding Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Amino Acid Transport Systems - metabolism | Sirolimus - pharmacology | Cycloheximide - pharmacology | Protein Transport | Transcription Factors - metabolism | Monomeric GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Endosomes - enzymology | Intracellular Membranes - drug effects | Mutation | Saccharomyces cerevisiae - growth & development | Proteins | Purines | Amino acids | Gross domestic product | Guanosine
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
Neuron, ISSN 0896-6273, 09/2013, Volume 79, Issue 6, pp. 1169 - 1182
The gene is located in a chromosomal region linked to various neurological disorders, including intellectual disability, autism, and schizophrenia. CYFIP1... 
MAMMALIAN TARGET | LOCAL PROTEIN-SYNTHESIS | AUTISM | FMRP | MOUSE MODEL | FRAGILE-X-SYNDROME | MECHANISMS | RAC1 | SYNAPTIC PLASTICITY | NEUROSCIENCES | CRITICAL REGION | Humans | Male | Fragile X Mental Retardation Protein - metabolism | Green Fluorescent Proteins - genetics | RNA, Messenger - metabolism | Mental Disorders - genetics | Brain-Derived Neurotrophic Factor - pharmacology | Neurons - ultrastructure | Time Factors | Chromatography, Liquid | Nerve Tissue Proteins - ultrastructure | Enzyme Inhibitors - pharmacology | Mice, Transgenic | Pyrimidines - pharmacology | Synaptosomes - ultrastructure | Analysis of Variance | Indole Alkaloids - pharmacology | Protein Biosynthesis - drug effects | Mice | Carbazoles - pharmacology | Adaptor Proteins, Signal Transducing - chemistry | Synaptosomes - drug effects | Meta-Analysis as Topic | Immunoprecipitation | Age Factors | Synaptosomes - metabolism | Cerebral Cortex - cytology | Microscopy, Immunoelectron | DNA-Binding Proteins - metabolism | Tandem Mass Spectrometry | Nerve Tissue Proteins - chemistry | Transfection | Dendritic Spines - drug effects | Protein Biosynthesis - genetics | Neurons - drug effects | Aminoquinolines - pharmacology | Green Fluorescent Proteins - metabolism | Gene Expression Regulation - genetics | Mice, Inbred C57BL | Cells, Cultured | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Animals | Adaptor Proteins, Signal Transducing - genetics | Fragile X Mental Retardation Protein - ultrastructure | Dendritic Spines - genetics | Fragile X Mental Retardation Protein - genetics | Adaptor Proteins, Signal Transducing - metabolism | In Vitro Techniques | Dendritic Spines - ultrastructure | Luminescent Proteins - metabolism | Nervous system diseases | Neurosciences | Neurons | Oncology, Experimental | Genes | Polymerization | Schizophrenia | Protein biosynthesis | Research | Genetic translation | Messenger RNA | Actin | Cancer | Proteins | Brain-derived neurotrophic factor | Protein synthesis | Crystal structure
Journal Article