Oncogene, ISSN 0950-9232, 11/2016, Volume 35, Issue 47, pp. 6077 - 6086
Notch receptors have been implicated as oncogenic drivers in several cancers, the most notable example being NOTCH1 in T-cell acute lymphoblastic leukemia...
ONCOLOGY | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | REGULATORY REGION | MICE | MATURATION | NEGATIVE BREAST-CANCER | INSIGHTS | CELL BIOLOGY | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - pathology | Humans | Epitopes - immunology | Codon | Receptor, Notch3 - antagonists & inhibitors | Female | Receptor, Notch3 - genetics | Antineoplastic Agents - pharmacology | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - metabolism | Disease Models, Animal | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - drug therapy | Receptor, Notch3 - metabolism | Antibodies, Monoclonal - pharmacology | Models, Molecular | Xenograft Model Antitumor Assays | Animals | Signal Transduction - drug effects | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - genetics | Cell Line, Tumor | Protein Conformation | Epitopes - chemistry | Mice | Mutation | Amino Acid Substitution | Receptor, Notch3 - chemistry | Development and progression | Cellular signal transduction | Genetic aspects | Acute lymphocytic leukemia | Gene mutations | Health aspects | Monoclonal antibodies | Lymphomas | Inhibitor drugs | Leukemia | Cells | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | NOTCH3 | inhibitory antibody | Notch signaling | T-ALL
ONCOLOGY | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | REGULATORY REGION | MICE | MATURATION | NEGATIVE BREAST-CANCER | INSIGHTS | CELL BIOLOGY | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - pathology | Humans | Epitopes - immunology | Codon | Receptor, Notch3 - antagonists & inhibitors | Female | Receptor, Notch3 - genetics | Antineoplastic Agents - pharmacology | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - metabolism | Disease Models, Animal | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - drug therapy | Receptor, Notch3 - metabolism | Antibodies, Monoclonal - pharmacology | Models, Molecular | Xenograft Model Antitumor Assays | Animals | Signal Transduction - drug effects | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - genetics | Cell Line, Tumor | Protein Conformation | Epitopes - chemistry | Mice | Mutation | Amino Acid Substitution | Receptor, Notch3 - chemistry | Development and progression | Cellular signal transduction | Genetic aspects | Acute lymphocytic leukemia | Gene mutations | Health aspects | Monoclonal antibodies | Lymphomas | Inhibitor drugs | Leukemia | Cells | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | NOTCH3 | inhibitory antibody | Notch signaling | T-ALL
Journal Article
Nature Structural Biology, ISSN 1072-8368, 12/1995, Volume 2, Issue 12, pp. 1075 - 1082
Infection with HIV-1 is initiated by fusion of cellular and viral membranes. The gp41 subunit of the HIV-1 envelope plays a major role in this process, but the...
MEMBRANE-FUSION | HTLV-III/LAV | SOLUBLE CD4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | OLIGOMERIC STRUCTURE | ENVELOPE GLYCOPROTEIN | RECEPTOR-MEDIATED ACTIVATION | HUMAN-IMMUNODEFICIENCY-VIRUS | COILED-COIL | INFLUENZA HEMAGGLUTININ | GCN4 LEUCINE-ZIPPER | CELL BIOLOGY | Amino Acid Sequence | Giant Cells - chemistry | Molecular Weight | Peptides - chemistry | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Recombinant Proteins - chemistry | Viral Envelope Proteins - ultrastructure | HIV Envelope Protein gp120 - ultrastructure | Proline - chemistry | HIV-1 - ultrastructure | Endopeptidases - chemistry | Membrane Glycoproteins - ultrastructure | HIV-1 - chemistry | Viral Envelope Proteins - chemistry | Cloning, Molecular | Protein Conformation | HIV Envelope Protein gp120 - chemistry
MEMBRANE-FUSION | HTLV-III/LAV | SOLUBLE CD4 | BIOCHEMISTRY & MOLECULAR BIOLOGY | OLIGOMERIC STRUCTURE | ENVELOPE GLYCOPROTEIN | RECEPTOR-MEDIATED ACTIVATION | HUMAN-IMMUNODEFICIENCY-VIRUS | COILED-COIL | INFLUENZA HEMAGGLUTININ | GCN4 LEUCINE-ZIPPER | CELL BIOLOGY | Amino Acid Sequence | Giant Cells - chemistry | Molecular Weight | Peptides - chemistry | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Recombinant Proteins - chemistry | Viral Envelope Proteins - ultrastructure | HIV Envelope Protein gp120 - ultrastructure | Proline - chemistry | HIV-1 - ultrastructure | Endopeptidases - chemistry | Membrane Glycoproteins - ultrastructure | HIV-1 - chemistry | Viral Envelope Proteins - chemistry | Cloning, Molecular | Protein Conformation | HIV Envelope Protein gp120 - chemistry
Journal Article
Biochemical Society Transactions, ISSN 0300-5127, 11/2004, Volume 32, Issue 5, pp. 721 - 723
The LDLR (low-density lipoprotein receptor) is a modular protein built from several distinct structural units: LA (LDLR type-A), epidermal growth factor-like...
Ligand binding | NMR | Lipoprotein | Interdomain linkers | Structure | Conformational change | BACKBONE DYNAMICS | FAMILIAL HYPERCHOLESTEROLEMIA | DOMAIN | lipoprotein | LDL RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN APOLIPOPROTEIN-E | interdomain linkers | conformational change | structure | MODULES | CONCATEMER | NMR STRUCTURE | ligand binding | PAIR | Protein Structure, Tertiary | Humans | Receptors, LDL - metabolism | Crystallography, X-Ray | Receptors, LDL - chemistry | Animals | Models, Biological | Epidermal Growth Factor - chemistry | Protein Binding | Ligands | Cell Membrane - metabolism | Green Fluorescent Proteins - chemistry | Hydrogen-Ion Concentration
Ligand binding | NMR | Lipoprotein | Interdomain linkers | Structure | Conformational change | BACKBONE DYNAMICS | FAMILIAL HYPERCHOLESTEROLEMIA | DOMAIN | lipoprotein | LDL RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN APOLIPOPROTEIN-E | interdomain linkers | conformational change | structure | MODULES | CONCATEMER | NMR STRUCTURE | ligand binding | PAIR | Protein Structure, Tertiary | Humans | Receptors, LDL - metabolism | Crystallography, X-Ray | Receptors, LDL - chemistry | Animals | Models, Biological | Epidermal Growth Factor - chemistry | Protein Binding | Ligands | Cell Membrane - metabolism | Green Fluorescent Proteins - chemistry | Hydrogen-Ion Concentration
Journal Article
Biochemistry, ISSN 0006-2960, 11/1995, Volume 34, Issue 46, pp. 14955 - 14962
Previous attempts to define the oligomeric state of the HIV and SIV envelope glycoproteins have yielded conflicting results. We have produced in Escherichia...
Amino Acid Sequence | Peptide Fragments - metabolism | Protein Structure, Secondary | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Recombinant Proteins - chemistry | Chromatography, High Pressure Liquid | Hot Temperature | Simian Immunodeficiency Virus - chemistry | Protein Folding | Macromolecular Substances | Peptide Fragments - chemistry | Endopeptidase K | HIV - chemistry | Viral Envelope Proteins - chemistry | Retroviridae Proteins - chemistry | Serine Endopeptidases - metabolism | Circular Dichroism | Hydrogen-Ion Concentration | Simian immunodeficiency virus | Glycoproteins | Research
Amino Acid Sequence | Peptide Fragments - metabolism | Protein Structure, Secondary | Membrane Glycoproteins - chemistry | Molecular Sequence Data | Recombinant Proteins - chemistry | Chromatography, High Pressure Liquid | Hot Temperature | Simian Immunodeficiency Virus - chemistry | Protein Folding | Macromolecular Substances | Peptide Fragments - chemistry | Endopeptidase K | HIV - chemistry | Viral Envelope Proteins - chemistry | Retroviridae Proteins - chemistry | Serine Endopeptidases - metabolism | Circular Dichroism | Hydrogen-Ion Concentration | Simian immunodeficiency virus | Glycoproteins | Research
Journal Article
Biochemistry, ISSN 0006-2960, 10/2001, Volume 40, Issue 43, pp. 12801 - 12807
To investigate how three disulfide bonds and coordination of a calcium ion cooperate to specify the structure of an LDL-A module, we studied the...
3-DIMENSIONAL STRUCTURE | FAMILIAL HYPERCHOLESTEROLEMIA | NMR SOLUTION STRUCTURE | CYSTEINE-RICH REPEAT | MOLTEN GLOBULE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING DOMAIN | INTERMEDIATE | PANCREATIC TRYPSIN-INHIBITOR | DENSITY-LIPOPROTEIN RECEPTOR | Amino Acid Sequence | Mutagenesis, Site-Directed | Magnetic Resonance Spectroscopy | Peptides - chemistry | Protein Structure, Secondary | Models, Molecular | Molecular Sequence Data | Chromatography, High Pressure Liquid | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Receptors, LDL - chemistry | Protein Folding | Dose-Response Relationship, Drug | Sequence Homology, Amino Acid | Time Factors | Disulfides - chemistry | Escherichia coli - metabolism | Protein Binding | Ligands | Protein Conformation | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Research | Calcium-binding proteins | Protein folding | Analysis | Low density lipoproteins | Structure-activity relationships (Biochemistry)
3-DIMENSIONAL STRUCTURE | FAMILIAL HYPERCHOLESTEROLEMIA | NMR SOLUTION STRUCTURE | CYSTEINE-RICH REPEAT | MOLTEN GLOBULE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING DOMAIN | INTERMEDIATE | PANCREATIC TRYPSIN-INHIBITOR | DENSITY-LIPOPROTEIN RECEPTOR | Amino Acid Sequence | Mutagenesis, Site-Directed | Magnetic Resonance Spectroscopy | Peptides - chemistry | Protein Structure, Secondary | Models, Molecular | Molecular Sequence Data | Chromatography, High Pressure Liquid | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Receptors, LDL - chemistry | Protein Folding | Dose-Response Relationship, Drug | Sequence Homology, Amino Acid | Time Factors | Disulfides - chemistry | Escherichia coli - metabolism | Protein Binding | Ligands | Protein Conformation | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Research | Calcium-binding proteins | Protein folding | Analysis | Low density lipoproteins | Structure-activity relationships (Biochemistry)
Journal Article
Journal of Virology, ISSN 0022-538X, 04/2001, Volume 75, Issue 8, pp. 3520 - 3526
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
APOPTOSIS | CYTOTOXIC LIGAND TRAIL | VIROLOGY | CELL-SURFACE RECEPTOR | SUPERINFECTION | MURINE LEUKEMIA VIRUSES | DEATH RECEPTOR-5 | GLYCOPROTEIN | SARCOMA-VIRUSES | IDENTIFICATION | VIRAL ENTRY | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Avian Leukosis Virus - pathogenicity | Receptors, Virus - metabolism | Humans | Cytopathogenic Effect, Viral | Molecular Sequence Data | Substrate Specificity | Avian Leukosis Virus - metabolism | Glycosylation | Receptors, Virus - genetics | Precipitin Tests | Cysteine - genetics | Flow Cytometry | Receptors, Virus - chemistry | Transfection | Models, Biological | Avian Leukosis Virus - genetics | Cysteine - metabolism | Receptors, Virus - antagonists & inhibitors | Superinfection - virology | Avian Leukosis Virus - classification | Virus-Cell Interactions
APOPTOSIS | CYTOTOXIC LIGAND TRAIL | VIROLOGY | CELL-SURFACE RECEPTOR | SUPERINFECTION | MURINE LEUKEMIA VIRUSES | DEATH RECEPTOR-5 | GLYCOPROTEIN | SARCOMA-VIRUSES | IDENTIFICATION | VIRAL ENTRY | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Avian Leukosis Virus - pathogenicity | Receptors, Virus - metabolism | Humans | Cytopathogenic Effect, Viral | Molecular Sequence Data | Substrate Specificity | Avian Leukosis Virus - metabolism | Glycosylation | Receptors, Virus - genetics | Precipitin Tests | Cysteine - genetics | Flow Cytometry | Receptors, Virus - chemistry | Transfection | Models, Biological | Avian Leukosis Virus - genetics | Cysteine - metabolism | Receptors, Virus - antagonists & inhibitors | Superinfection - virology | Avian Leukosis Virus - classification | Virus-Cell Interactions
Journal Article
Nature Structural Biology, ISSN 1072-8368, 09/1996, Volume 3, Issue 9, pp. 758 - 762
3-DIMENSIONAL STRUCTURE | DOMAIN | CYSTEINE-RICH REPEAT | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE-PROTEIN | GLYCOPROTEIN | EPIDERMAL GROWTH-FACTOR | EXPRESSION | DENSITY-LIPOPROTEIN RECEPTOR | APOLIPOPROTEIN-E | CELL BIOLOGY | Hyperlipoproteinemia Type II - metabolism | Amino Acid Sequence | Point Mutation | Receptors, LDL - genetics | Calcium - metabolism | Humans | Molecular Sequence Data | Receptors, LDL - metabolism | Receptors, LDL - chemistry | Protein Folding | Hyperlipoproteinemia Type II - genetics
Journal Article
Analytical Biochemistry, ISSN 0003-2697, 10/2001, Volume 297, Issue 1, pp. 60 - 70
The study of the early events in translation would be greatly facilitated by reconstitution with easily purified components. Here, Escherichia coli...
reconstitution | epsilon | enhancer | peptide | tRNA | elongation factor | biotin | translation | ribosome | unnatural amino acid | E. coli | initiation factor | Initiation factor | Translation | Ribosome | Enhancer | Unnatural amino acid | TRNA | Epsilon | Elongation factor | Biotin | Reconstitution | Peptide | CHEMISTRY, ANALYTICAL | PROTEIN | ESCHERICHIA-COLI | TRANSLATION INITIATION | IN-VITRO SYNTHESIS | ELONGATION-FACTOR-TU | BETA-GALACTOSIDASE | GENE-EXPRESSION | FACTOR-II | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | INITIATION-FACTOR IF3 | DOWNSTREAM BOX | Peptide Elongation Factors - metabolism | Amino Acids - chemistry | Ribosomes - metabolism | Chromatography, High Pressure Liquid | Histidine - metabolism | RNA, Messenger - metabolism | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | Amino Acids - metabolism | Peptide Biosynthesis | Peptides - metabolism | Time Factors | Base Sequence | Escherichia coli - metabolism | Lysine - metabolism | Lysine - analogs & derivatives | Peptide Chain Initiation, Translational - genetics | Bacteriophage T7 - genetics | Peptides - chemistry | RNA, Messenger - genetics | Valine - analogs & derivatives | Mutation - genetics | Regulatory Sequences, Nucleic Acid - genetics | Threonine - analogs & derivatives | Peptide Initiation Factors - metabolism | Valine - metabolism | Escherichia coli - genetics
reconstitution | epsilon | enhancer | peptide | tRNA | elongation factor | biotin | translation | ribosome | unnatural amino acid | E. coli | initiation factor | Initiation factor | Translation | Ribosome | Enhancer | Unnatural amino acid | TRNA | Epsilon | Elongation factor | Biotin | Reconstitution | Peptide | CHEMISTRY, ANALYTICAL | PROTEIN | ESCHERICHIA-COLI | TRANSLATION INITIATION | IN-VITRO SYNTHESIS | ELONGATION-FACTOR-TU | BETA-GALACTOSIDASE | GENE-EXPRESSION | FACTOR-II | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | INITIATION-FACTOR IF3 | DOWNSTREAM BOX | Peptide Elongation Factors - metabolism | Amino Acids - chemistry | Ribosomes - metabolism | Chromatography, High Pressure Liquid | Histidine - metabolism | RNA, Messenger - metabolism | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | Amino Acids - metabolism | Peptide Biosynthesis | Peptides - metabolism | Time Factors | Base Sequence | Escherichia coli - metabolism | Lysine - metabolism | Lysine - analogs & derivatives | Peptide Chain Initiation, Translational - genetics | Bacteriophage T7 - genetics | Peptides - chemistry | RNA, Messenger - genetics | Valine - analogs & derivatives | Mutation - genetics | Regulatory Sequences, Nucleic Acid - genetics | Threonine - analogs & derivatives | Peptide Initiation Factors - metabolism | Valine - metabolism | Escherichia coli - genetics
Journal Article
Biochemistry, ISSN 0006-2960, 03/2001, Volume 40, Issue 9, pp. 2808 - 2815
The ligand-binding domain of the LDL receptor consists of seven contiguous LDL-A modules. The fifth of these ligand-binding modules is absolutely required for...
3-DIMENSIONAL STRUCTURE | CYSTEINE-RICH REPEAT | NMR SOLUTION STRUCTURE | DIFFERENT PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILIAL HYPERCHOLESTEROLEMIA MUTATIONS | CALCIUM-BINDING | GENE FAMILY | MONOCLONAL-ANTIBODIES | DENSITY-LIPOPROTEIN RECEPTOR | VLDL RECEPTOR | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | Humans | Molecular Sequence Data | Receptors, LDL - metabolism | Nitrogen Isotopes | Receptors, LDL - chemistry | Amino Acid Motifs | Thermodynamics | Peptide Fragments - chemistry | Repetitive Sequences, Amino Acid | Solutions | Nuclear Magnetic Resonance, Biomolecular | Ligands | Protein Conformation | Lipoproteins | Biochemistry | Research
3-DIMENSIONAL STRUCTURE | CYSTEINE-RICH REPEAT | NMR SOLUTION STRUCTURE | DIFFERENT PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILIAL HYPERCHOLESTEROLEMIA MUTATIONS | CALCIUM-BINDING | GENE FAMILY | MONOCLONAL-ANTIBODIES | DENSITY-LIPOPROTEIN RECEPTOR | VLDL RECEPTOR | Protein Structure, Tertiary | Amino Acid Sequence | Peptide Fragments - metabolism | Humans | Molecular Sequence Data | Receptors, LDL - metabolism | Nitrogen Isotopes | Receptors, LDL - chemistry | Amino Acid Motifs | Thermodynamics | Peptide Fragments - chemistry | Repetitive Sequences, Amino Acid | Solutions | Nuclear Magnetic Resonance, Biomolecular | Ligands | Protein Conformation | Lipoproteins | Biochemistry | Research
Journal Article
Biochemistry, ISSN 0006-2960, 10/2000, Volume 39, Issue 43, pp. 13127 - 13135
Mutations at conserved sites within the ligand-binding LDL-A modules of the LDL receptor cause the genetic disease familial hypercholesterolemia (FH), and...
EGF-LIKE DOMAIN | DIFFERENT PROTEINS | STRUCTURAL INTEGRITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MARFAN-SYNDROME | FACTOR-LIKE DOMAINS | CALCIUM-BINDING | GROWTH-FACTOR PRECURSOR | CULTURED HUMAN FIBROBLASTS | DENSITY-LIPOPROTEIN RECEPTOR | CYSTEINE-RICH | Calcium-Binding Proteins - metabolism | Amino Acid Sequence | Receptors, LDL - genetics | Mutagenesis, Site-Directed | Calcium - metabolism | Humans | Molecular Sequence Data | Receptors, LDL - metabolism | Spectrometry, Fluorescence | Protein Folding | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Amino Acid Motifs - genetics | Calcium-Binding Proteins - genetics | Hyperlipoproteinemia Type II - genetics | Lipoproteins | Gene mutations | Physiological aspects | Amino acids | Ligands | Biochemistry | Research | Membrane proteins
EGF-LIKE DOMAIN | DIFFERENT PROTEINS | STRUCTURAL INTEGRITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MARFAN-SYNDROME | FACTOR-LIKE DOMAINS | CALCIUM-BINDING | GROWTH-FACTOR PRECURSOR | CULTURED HUMAN FIBROBLASTS | DENSITY-LIPOPROTEIN RECEPTOR | CYSTEINE-RICH | Calcium-Binding Proteins - metabolism | Amino Acid Sequence | Receptors, LDL - genetics | Mutagenesis, Site-Directed | Calcium - metabolism | Humans | Molecular Sequence Data | Receptors, LDL - metabolism | Spectrometry, Fluorescence | Protein Folding | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Amino Acid Motifs - genetics | Calcium-Binding Proteins - genetics | Hyperlipoproteinemia Type II - genetics | Lipoproteins | Gene mutations | Physiological aspects | Amino acids | Ligands | Biochemistry | Research | Membrane proteins
Journal Article
Journal of the American Medical Association, ISSN 0098-7484, 12/1993, Volume 270, Issue 23, pp. 2819 - 2822
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/1990, Volume 87, Issue 2, pp. 696 - 700
How easy is it to improve the catalytic power of an enzyme? To address this question, the gene encoding a sluggish mutant triose-phosphate isomerase...
Phosphates | Enzymes | Mutagenesis | Active sites | Plasmids | Oligonucleotides | Amino acids | Catalytic activity | Biochemistry | Genetic mutation | Evolution | triase-phosphate isomerase | Pseudorevertants | Spiked oligonucleotides | Triose-phosphate isomerase | MULTIDISCIPLINARY SCIENCES | Genes, Bacterial | Oligonucleotide Probes | Escherichia coli - enzymology | Models, Molecular | Aspartic Acid | Glutamic Acid | Triose-Phosphate Isomerase - genetics | Escherichia coli - genetics | Triose-Phosphate Isomerase - metabolism | Protein Conformation | Kinetics | Mutation | Glutamates | Carbohydrate Epimerases - genetics
Phosphates | Enzymes | Mutagenesis | Active sites | Plasmids | Oligonucleotides | Amino acids | Catalytic activity | Biochemistry | Genetic mutation | Evolution | triase-phosphate isomerase | Pseudorevertants | Spiked oligonucleotides | Triose-phosphate isomerase | MULTIDISCIPLINARY SCIENCES | Genes, Bacterial | Oligonucleotide Probes | Escherichia coli - enzymology | Models, Molecular | Aspartic Acid | Glutamic Acid | Triose-Phosphate Isomerase - genetics | Escherichia coli - genetics | Triose-Phosphate Isomerase - metabolism | Protein Conformation | Kinetics | Mutation | Glutamates | Carbohydrate Epimerases - genetics
Journal Article
Gene, ISSN 0378-1119, 1989, Volume 84, Issue 1, pp. 143 - 151
A new procedure for the production of a defined library of random mutants is described. Long spiked oligodeoxyribonucleotides (oligos), in which a...
incorporation of mismatching bases | pseudorevertants | on-line mixing | automated DNA synthesis | Recombinant DNA | triosephosphate isomerase | phagemid vectors | GENETICS & HEREDITY | Gene Library | Escherichia coli - genetics | Plasmids | Base Sequence | Cloning, Molecular | Molecular Sequence Data | Templates, Genetic | Mutation | Oligonucleotide Probes - chemical synthesis
incorporation of mismatching bases | pseudorevertants | on-line mixing | automated DNA synthesis | Recombinant DNA | triosephosphate isomerase | phagemid vectors | GENETICS & HEREDITY | Gene Library | Escherichia coli - genetics | Plasmids | Base Sequence | Cloning, Molecular | Molecular Sequence Data | Templates, Genetic | Mutation | Oligonucleotide Probes - chemical synthesis
Journal Article
Cold Spring Harbor Symposia on Quantitative Biology, ISSN 0091-7451, 1987, Volume 52, pp. 597 - 602
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 11/2010, Volume 17, Issue 11, pp. 1312 - 1317
Ligand-induced proteolysis of Notch produces an intracellular effector domain that transduces essential signals by regulating the transcription of target...
PRESENILIN | ACTIVATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DROSOPHILA | CELL BIOLOGY | BIOPHYSICS | DNA | ACUTE LYMPHOBLASTIC-LEUKEMIA | GENES | LIGAND | CSL | MASTERMIND | Transcription Factor HES-1 | Transcription Factors - chemistry | Homeodomain Proteins - metabolism | Humans | Receptor, Notch1 - chemistry | Molecular Sequence Data | Crystallography, X-Ray | DNA-Binding Proteins - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | Base Sequence | Conserved Sequence | Binding Sites | Dimerization | Immunoglobulin J Recombination Signal Sequence-Binding Protein - chemistry | Protein Structure, Tertiary | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Promoter Regions, Genetic | Repressor Proteins - chemistry | Models, Molecular | Receptor, Notch1 - metabolism | Homeodomain Proteins - chemistry | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Animals | Mice | Basic Helix-Loop-Helix Transcription Factors - chemistry | Promoters (Genetics) | Physiological aspects | Cellular signal transduction | Genetic aspects | Research | Genetic transcription | Membrane proteins | Signal transduction | Molecular structure | Molecular biology | Deoxyribonucleic acid--DNA | Binding sites
PRESENILIN | ACTIVATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DROSOPHILA | CELL BIOLOGY | BIOPHYSICS | DNA | ACUTE LYMPHOBLASTIC-LEUKEMIA | GENES | LIGAND | CSL | MASTERMIND | Transcription Factor HES-1 | Transcription Factors - chemistry | Homeodomain Proteins - metabolism | Humans | Receptor, Notch1 - chemistry | Molecular Sequence Data | Crystallography, X-Ray | DNA-Binding Proteins - metabolism | Basic Helix-Loop-Helix Transcription Factors - metabolism | Base Sequence | Conserved Sequence | Binding Sites | Dimerization | Immunoglobulin J Recombination Signal Sequence-Binding Protein - chemistry | Protein Structure, Tertiary | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Promoter Regions, Genetic | Repressor Proteins - chemistry | Models, Molecular | Receptor, Notch1 - metabolism | Homeodomain Proteins - chemistry | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Animals | Mice | Basic Helix-Loop-Helix Transcription Factors - chemistry | Promoters (Genetics) | Physiological aspects | Cellular signal transduction | Genetic aspects | Research | Genetic transcription | Membrane proteins | Signal transduction | Molecular structure | Molecular biology | Deoxyribonucleic acid--DNA | Binding sites
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 04/2007, Volume 14, Issue 4, pp. 295 - 300
Notch receptors transmit signals between adjacent cells. Signaling is initiated when ligand binding induces metalloprotease cleavage of Notch within an...
UBIQUITIN LIGASE | DELTA | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEOLYTIC ACTIVATION | MIND-BOMB | SEA DOMAIN | DROSOPHILA | CELL BIOLOGY | SIGNAL-TRANSDUCTION | LIGAND ENDOCYTOSIS | CAENORHABDITIS-ELEGANS | BIOPHYSICS | IN-VIVO | Protein Structure, Tertiary | Receptor, Notch2 - antagonists & inhibitors | Protein Structure, Secondary | Humans | Models, Molecular | Protein Binding | Crystallography, X-Ray | Structure-Activity Relationship | Receptor, Notch2 - chemistry | Genes, Reporter | Cell receptors | Control | Physiological aspects | Cellular signal transduction | Glycoproteins | Research | Structure | Molecular biology | Leukemia | Mutation
UBIQUITIN LIGASE | DELTA | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEOLYTIC ACTIVATION | MIND-BOMB | SEA DOMAIN | DROSOPHILA | CELL BIOLOGY | SIGNAL-TRANSDUCTION | LIGAND ENDOCYTOSIS | CAENORHABDITIS-ELEGANS | BIOPHYSICS | IN-VIVO | Protein Structure, Tertiary | Receptor, Notch2 - antagonists & inhibitors | Protein Structure, Secondary | Humans | Models, Molecular | Protein Binding | Crystallography, X-Ray | Structure-Activity Relationship | Receptor, Notch2 - chemistry | Genes, Reporter | Cell receptors | Control | Physiological aspects | Cellular signal transduction | Glycoproteins | Research | Structure | Molecular biology | Leukemia | Mutation
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 11/2014, Volume 111, Issue 46, pp. E4946 - E4953
Notch is needed for T-cell development and is a common oncogenic driver in T-cell acute lymphoblastic leukemia. The protooncogene c-Myc (Myc) is a critical...
Chromatin | Enhancer | Transcription | Gene regulation | Brd4 | TARGET | enhancer | transcription | MULTIDISCIPLINARY SCIENCES | COMPLEXES | C-MYC | chromatin | GENOME | SUPER-ENHANCERS | gene regulation | ACUTE LYMPHOBLASTIC-LEUKEMIA | MARGINAL ZONE LYMPHOMA | EXPRESSION | Humans | Molecular Sequence Data | Genes, myc | Neoplasm Proteins - metabolism | Promoter Regions, Genetic - genetics | Gene Expression Regulation, Leukemic - genetics | Chromatin Immunoprecipitation | Base Sequence | Transcription, Genetic | Neoplasm Proteins - genetics | Genes, Reporter | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - metabolism | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Genome-Wide Association Study | Models, Molecular | Transcription Factors - antagonists & inhibitors | Receptor, Notch1 - metabolism | Sequence Homology, Nucleic Acid | Sequence Alignment | Animals | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - genetics | Nuclear Proteins - antagonists & inhibitors | Cell Line, Tumor | Protein Conformation | Enhancer Elements, Genetic - genetics | Histones - metabolism | Receptor, Notch1 - antagonists & inhibitors | Biological Sciences | PNAS Plus
Chromatin | Enhancer | Transcription | Gene regulation | Brd4 | TARGET | enhancer | transcription | MULTIDISCIPLINARY SCIENCES | COMPLEXES | C-MYC | chromatin | GENOME | SUPER-ENHANCERS | gene regulation | ACUTE LYMPHOBLASTIC-LEUKEMIA | MARGINAL ZONE LYMPHOMA | EXPRESSION | Humans | Molecular Sequence Data | Genes, myc | Neoplasm Proteins - metabolism | Promoter Regions, Genetic - genetics | Gene Expression Regulation, Leukemic - genetics | Chromatin Immunoprecipitation | Base Sequence | Transcription, Genetic | Neoplasm Proteins - genetics | Genes, Reporter | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - metabolism | Immunoglobulin J Recombination Signal Sequence-Binding Protein - metabolism | Genome-Wide Association Study | Models, Molecular | Transcription Factors - antagonists & inhibitors | Receptor, Notch1 - metabolism | Sequence Homology, Nucleic Acid | Sequence Alignment | Animals | Precursor T-Cell Lymphoblastic Leukemia-Lymphoma - genetics | Nuclear Proteins - antagonists & inhibitors | Cell Line, Tumor | Protein Conformation | Enhancer Elements, Genetic - genetics | Histones - metabolism | Receptor, Notch1 - antagonists & inhibitors | Biological Sciences | PNAS Plus
Journal Article
Nature Structural Biology, ISSN 1072-8368, 04/2002, Volume 9, Issue 4, pp. 282 - 287
Cysteine-rich repeats in the integrin β subunit stalk region relay activation signals to the ligand-binding headpiece. The NMR solution structure and disulfide...
DOMAIN | LIGAND-BINDING | LDL RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | CRYSTALLOGRAPHY | CELL BIOLOGY | PROTEIN STRUCTURES | NMR | EPITOPE | BIOPHYSICS | CALCIUM | INFLUENZA HEMAGGLUTININ | Disulfides - metabolism | Amino Acid Sequence | Protein Subunits | Epitopes - metabolism | Humans | Models, Molecular | Molecular Sequence Data | CD18 Antigens - chemistry | Structure-Activity Relationship | Amino Acid Motifs | CD18 Antigens - metabolism | Repetitive Sequences, Amino Acid | Sequence Alignment | Models, Biological | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Cysteine - metabolism | Epitopes - chemistry | Physiological aspects | Cysteine | Genetic aspects | Research | Gene expression | Integrins
DOMAIN | LIGAND-BINDING | LDL RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | CRYSTALLOGRAPHY | CELL BIOLOGY | PROTEIN STRUCTURES | NMR | EPITOPE | BIOPHYSICS | CALCIUM | INFLUENZA HEMAGGLUTININ | Disulfides - metabolism | Amino Acid Sequence | Protein Subunits | Epitopes - metabolism | Humans | Models, Molecular | Molecular Sequence Data | CD18 Antigens - chemistry | Structure-Activity Relationship | Amino Acid Motifs | CD18 Antigens - metabolism | Repetitive Sequences, Amino Acid | Sequence Alignment | Models, Biological | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Cysteine - metabolism | Epitopes - chemistry | Physiological aspects | Cysteine | Genetic aspects | Research | Gene expression | Integrins
Journal Article