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Nature (London), ISSN 1476-4687, 2013, Volume 499, Issue 7456, pp. 50 - 54
...DNA double-strand breaks (DSBs) elicit a cascade of protein recruitment on the chromatin surrounding DNA lesions that regulates DNA damage repair... 
CRB2 | RECRUITMENT | FISSION YEAST | METHYLATION | CHROMATIN | DEPENDENT RESPONSE | RESECTION | MULTIDISCIPLINARY SCIENCES | SITES | DOUBLE-STRAND BREAKS | CLASS-SWITCH RECOMBINATION | Schizosaccharomyces pombe Proteins - chemistry | Histones - chemistry | Nucleosomes - chemistry | Humans | Ubiquitin - metabolism | Molecular Sequence Data | Male | Intracellular Signaling Peptides and Proteins - metabolism | DNA Breaks, Double-Stranded | DNA-Binding Proteins - deficiency | Cell Cycle Proteins - chemistry | Intracellular Signaling Peptides and Proteins - deficiency | Ubiquitination | Schizosaccharomyces pombe Proteins - metabolism | Female | Lysine - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Schizosaccharomyces | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Signal Transduction | Cell Cycle Proteins - metabolism | Nucleosomes - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Chromosomal Proteins, Non-Histone - deficiency | Amino Acid Motifs | Chromosomal Proteins, Non-Histone - genetics | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Mutant Proteins - chemistry | Protein Binding | Mice | DNA Damage | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Chromosomal Proteins, Non-Histone - chemistry | Ubiquitin | Research | Properties | DNA repair | DNA damage | Proteins | DNA methylation | Mutation | Experiments | Recruitment
Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 20, Issue 6, pp. 939 - 949
The death-inducing signaling complex (DISC) comprising Fas, Fas-associated death domain (FADD... 
RECEPTOR SIGNALS | APOPTOSIS | INDUCED-PROXIMITY MODEL | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR STRUCTURE | DEATH-EFFECTOR DOMAIN | CASPASE ACTIVATION | CONTAINING PROTEIN | SIGNALING COMPLEX DISC | CELL-DEATH | PYRIN DOMAIN | CELL BIOLOGY | Caspase 8 | Humans | Multiprotein Complexes | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | fas Receptor - metabolism | Viral Proteins - metabolism | Death Domain Receptor Signaling Adaptor Proteins | Caspases - metabolism | Molluscum contagiosum virus - genetics | Caspase 10 | fas Receptor - genetics | Intracellular Signaling Peptides and Proteins - genetics | Amino Acid Sequence | Caspases - genetics | Viral Proteins - chemistry | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Models, Molecular | Viral Proteins - genetics | Fas-Associated Death Domain Protein | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - chemistry | Sequence Alignment | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Molluscum contagiosum virus - chemistry | Protein Conformation | CASP8 and FADD-Like Apoptosis Regulating Protein | Apoptosis - physiology | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Proteins | Oligomers | Structure | Crystals
Journal Article
Molecular cell, ISSN 1097-2765, 2017, Volume 67, Issue 3, pp. 387 - 399.e5
... (DNAPKc, Ku70, and Ku80) and paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATRIN3... 
HEXIM1 | DNA-PK | innate immune response | herpesvirus | paraspeckles | cGAS | NEAT1 | interferon stimulatory DNA | DEFENSE | PROTEIN | INHIBITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | SENSOR | POLYMERASE-II | 7SK RNA | BINDING | GMP-AMP SYNTHASE | P-TEFB | CELL BIOLOGY | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Octamer Transcription Factors - immunology | Intracellular Signaling Peptides and Proteins - metabolism | Herpesvirus 8, Human - immunology | RNA, Long Noncoding - immunology | PTB-Associated Splicing Factor - genetics | RNA Interference | Calcium-Binding Proteins - immunology | Octamer Transcription Factors - genetics | Nucleotidyltransferases - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Signal Transduction | Membrane Proteins - genetics | RNA-Binding Proteins - immunology | PTB-Associated Splicing Factor - metabolism | Nuclear Matrix-Associated Proteins - metabolism | PTB-Associated Splicing Factor - immunology | DNA - metabolism | Host-Pathogen Interactions | Nuclear Matrix-Associated Proteins - genetics | HeLa Cells | RNA-Binding Proteins - metabolism | Calcium-Binding Proteins - genetics | RNA-Binding Proteins - genetics | Multiprotein Complexes | Human Umbilical Vein Endothelial Cells - immunology | Intracellular Signaling Peptides and Proteins - immunology | Human Umbilical Vein Endothelial Cells - virology | Interferon Regulatory Factor-3 - genetics | Ku Autoantigen - genetics | Transfection | HEK293 Cells | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Octamer Transcription Factors - metabolism | Interferon Regulatory Factor-3 - immunology | Calcium-Binding Proteins - metabolism | DNA - immunology | Nuclear Matrix-Associated Proteins - immunology | Ku Autoantigen - immunology | Membrane Proteins - immunology | Nuclear Proteins - metabolism | Ku Autoantigen - metabolism | RNA, Long Noncoding - genetics | Immunity, Innate | Nuclear Proteins - immunology | DNA - genetics | Interferon Regulatory Factor-3 - metabolism | Nucleotidyltransferases - genetics | Protein Binding | Nucleotidyltransferases - immunology | RNA, Long Noncoding - metabolism | RNA sequencing | Immune response | RNA | DNA | Genetic research | Interferon | Biological response modifiers | Mass spectrometry | Human Umbilical Vein Endothelial Cells | Nuclear Matrix-Associated Proteins | Herpesvirus 8, Human | RNA-Binding Proteins | Life Sciences | Interferon Regulatory Factor-3 | Genetics | Calcium-Binding Proteins | Intracellular Signaling Peptides and Proteins | PTB-Associated Splicing Factor | Nuclear Proteins | Membrane Proteins | Nucleotidyltransferases | Ku Autoantigen | Octamer Transcription Factors | RNA, Long Noncoding
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2011, Volume 286, Issue 9, pp. 7018 - 7026
The Hippo pathway restricts the activity of transcriptional co-activators TAZ and YAP by phosphorylating them for cytoplasmic sequestration or degradation. In... 
YES-ASSOCIATED PROTEIN | EPITHELIAL-MESENCHYMAL TRANSITION | CELL CONTACT INHIBITION | WW DOMAIN | GROWTH-CONTROL | ORGAN SIZE CONTROL | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | ONCOGENIC TRANSFORMATION | BINDING | CANCER | Adaptor Proteins, Signal Transducing - chemistry | Protein Interaction Domains and Motifs - physiology | Humans | Intercellular Signaling Peptides and Proteins - chemistry | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Intercellular Signaling Peptides and Proteins - metabolism | HEK293 Cells | Membrane Proteins - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Protein Structure, Tertiary | Membrane Proteins - genetics | Intercellular Signaling Peptides and Proteins - genetics | Phosphoproteins - genetics | Cell Division - physiology | Transcription, Genetic - physiology | Membrane Proteins - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Signal Transduction - physiology | Connective Tissue Growth Factor - genetics | Adaptor Proteins, Signal Transducing - metabolism | Connective Tissue Growth Factor - metabolism | Gene Transcription | Transcription Coactivators | Signal Transduction | AmotL1 | YAP | Transcription Factors | Serine Threonine Protein Kinase | Hippo Pathway | TAZ | Amot
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2012, Volume 149, Issue 5, pp. 1035 - 1047
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2017, Volume 12, Issue 5, p. e0177516
... successful cell-therapy for muscle disorders. Here we expanded mouse muscle stem cells and human myoblasts with Notch ligands, DLL1, DLL4, and JAG1 to activate Notch signaling in vitro and to investigate whether these cells could retain... 
PROGENITOR CELLS | SATELLITE CELL NICHE | MESENCHYMAL PROGENITORS | GENE | MYOD | MULTIDISCIPLINARY SCIENCES | EXPANSION | SELF-RENEWAL | DUCHENNE MUSCULAR-DYSTROPHY | HUMAN SKELETAL-MUSCLE | TRANSPLANTATION | Immunohistochemistry | Jagged-1 Protein - metabolism | MyoD Protein - genetics | Receptors, Notch - metabolism | PAX7 Transcription Factor - genetics | Receptors, Notch - genetics | Intracellular Signaling Peptides and Proteins - metabolism | PAX7 Transcription Factor - metabolism | Stem Cells - cytology | Stem Cells - metabolism | Cell Differentiation - genetics | Intercellular Signaling Peptides and Proteins - metabolism | Myoblasts - metabolism | Regeneration - genetics | Myoblasts - cytology | Membrane Proteins - metabolism | Cell Differentiation - physiology | Intracellular Signaling Peptides and Proteins - genetics | Real-Time Polymerase Chain Reaction | Membrane Proteins - genetics | Muscle Development - physiology | Cells, Cultured | Intercellular Signaling Peptides and Proteins - genetics | MyoD Protein - metabolism | Signal Transduction - genetics | Regeneration - physiology | Jagged-1 Protein - genetics | Muscle Cells - cytology | Animals | Muscle Development - genetics | Signal Transduction - physiology | Mice | Transplantation | Research | Health aspects | Ligands (Biochemistry) | Analysis | Stem cells | Musculoskeletal diseases | Musculoskeletal system | Cell culture | MyoD protein | Allografts | Cell number | Stem cell transplantation | Ligands | Notch protein | Gene expression | Myoblasts | Signal Transduction | Intercellular Signaling Peptides and Proteins | PAX7 Transcription Factor | Intracellular Signaling Peptides and Proteins | Cellular Biology | Stem Cells | Membrane Proteins | Life Sciences | Regeneration | Muscle Development | Receptors, Notch | Cell Differentiation | Muscle Cells | MyoD Protein | Jagged-1 Protein
Journal Article
Molecular Cell, ISSN 1097-2765, 05/2008, Volume 30, Issue 4, pp. 507 - 518
...). The crystal structures of ternary complexes between PHD, HD1, and two different H3K4me peptides reveal a unique mode of histone tail recognition... 
DNA | SIGNALING | ARMADILLO/BETA-CATENIN | TARGET GENES | BINDING MODULES | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COACTIVATOR PYGOPUS | PLANT HOMEODOMAIN | BETA-CATENIN | DNA-REPAIR | PHD-FINGER | CELL BIOLOGY | Histones - chemistry | Humans | Peptides - genetics | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | Drosophila Proteins - metabolism | Neoplasm Proteins - metabolism | Wnt Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Multiprotein Complexes - metabolism | Peptides - metabolism | Lysine - metabolism | Neoplasm Proteins - genetics | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Amino Acid Sequence | Peptides - chemistry | Models, Molecular | Neoplasm Proteins - chemistry | Drosophila Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Adaptor Proteins, Signal Transducing | Multiprotein Complexes - chemistry | Sequence Alignment | Animals | Histones - genetics | Intracellular Signaling Peptides and Proteins - chemistry | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Conformation | Signal Transduction - physiology | Drosophila Proteins - genetics | Histones - metabolism | Methylation | Drosophila melanogaster | Histones | Genetic engineering | Genetic transcription | Peptides
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2008, Volume 105, Issue 32, pp. 11212 - 11217
Genetic studies have shown that ubiquitination and endocytosis of the Drosophila ligand Delta in signal-sending cells are required for activation of Notch signaling, but how these events promote Notch... 
T lymphocytes | Molecules | Endocytosis | Receptors | Cell lines | HeLa cells | Antibodies | Ligands | Lipids | Recycling | Ubiquitination | Membrane microdomains | Transendocytosis | Membrane Microdomains - metabolism | Membrane Proteins - genetics | Drosophila | Humans | Intercellular Signaling Peptides and Proteins - genetics | Protein Transport - physiology | Intracellular Signaling Peptides and Proteins - metabolism | Receptor, Notch1 - metabolism | Recombinant Fusion Proteins - metabolism | Endocytosis - physiology | Intercellular Signaling Peptides and Proteins - metabolism | Animals | Recombinant Fusion Proteins - genetics | Signal Transduction - physiology | Membrane Proteins - metabolism | Mice | HeLa Cells | Ubiquitination - physiology | Receptor, Notch1 - genetics | Intracellular Signaling Peptides and Proteins - genetics | Membrane Microdomains - genetics | Physiological aspects | Cellular signal transduction | Genetic aspects | Ligands (Biochemistry) | Membrane Microdomains | Signal Transduction | Intercellular Signaling Peptides and Proteins | Biochemistry, Molecular Biology | Intracellular Signaling Peptides and Proteins | Recombinant Fusion Proteins | Protein Transport | Membrane Proteins | Life Sciences | Receptor, Notch1 | Molecular biology | Hela Cells | Biological Sciences | recycling | transendocytosis | membrane microdomains | ubiquitination
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 4, pp. 1273 - 1278
The COP9 (Constitutive photomorphogenesis 9) signalosome (CSN), a large multiprotein complex that resembles the 19S lid of the 26S proteasome, plays a central... 
Proteins | Molecules | Enzymes | Active sites | Ubiquitins | Crystals | Dimers | Gene expression regulation | Zinc | Crystal structure | COMPLEX | DOMAIN | JAB1/CSN5 | DROSOPHILA-MELANOGASTER | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | Rpn11 | CUL1 | MPN | NEDD8 | cullin regulation | DENEDDYLATION | PROTEASOME | DEGRADATION | protein degradation | Protein Subunits | Peptide Hydrolases - genetics | Zinc - metabolism | Humans | Protein Multimerization | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Protein Structure, Quaternary | Intracellular Signaling Peptides and Proteins - genetics | Ubiquitins - metabolism | NEDD8 Protein | Peptide Hydrolases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Mutagenesis, Site-Directed | Models, Molecular | COP9 Signalosome Complex | Recombinant Fusion Proteins - chemistry | Molecular Dynamics Simulation | Peptide Hydrolases - chemistry | Arginine - chemistry | Sequence Homology, Amino Acid | Intracellular Signaling Peptides and Proteins - chemistry | Recombinant Fusion Proteins - genetics | Enzyme Activation | Ubiquitin | Ligases | Proteases | Proteomics | Physiological aspects | Research | Health aspects | Biochemistry, Molecular Biology | Intracellular Signaling Peptides and Proteins | Cellular Biology | Recombinant Fusion Proteins | Life Sciences | Arginine | Peptide Hydrolases | Development Biology | Biological Sciences
Journal Article
Nature chemical biology, ISSN 1552-4469, 2014, Volume 10, Issue 10, pp. 853 - 860
Activation of the ERK pathway is a hallmark of cancer, and targeting of upstream signaling partners led to the development of approved drugs... 
ACTIVATION | MEK INHIBITION | DETERMINANTS | RAF | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | ACQUIRED-RESISTANCE | MAP KINASE ERK2 | BRAF | CONFORMATION | DEFICIENCY | Humans | Mitogen-Activated Protein Kinase 3 - antagonists & inhibitors | Gene Expression Regulation, Neoplastic | Intracellular Signaling Peptides and Proteins - metabolism | Piperazines - chemistry | Mitogen-Activated Protein Kinase 1 - chemistry | Enzyme Inhibitors - chemistry | Mitogen-Activated Protein Kinase 1 - genetics | Mitogen-Activated Protein Kinase 8 - genetics | Antineoplastic Agents - pharmacology | Mitogen-Activated Protein Kinase 3 - chemistry | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Gene Expression | Indazoles - chemistry | Mitogen-Activated Protein Kinase 3 - genetics | Protein Structure, Secondary | Mitogen-Activated Protein Kinase 1 - antagonists & inhibitors | Mitogen-Activated Protein Kinase 8 - chemistry | Mitogen-Activated Protein Kinase 8 - metabolism | Enzyme Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Antineoplastic Agents - chemistry | Piperazines - pharmacology | Indazoles - pharmacology | MAP Kinase Signaling System - drug effects | Mitogen-Activated Protein Kinase 3 - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Cell Line, Tumor | Protein Binding | Protein-Serine-Threonine Kinases - chemistry | Kinetics | Mitogen-Activated Protein Kinase 1 - metabolism | Signal transduction | Binding sites | Pharmaceutical sciences | Cancer
Journal Article