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Publication Date2017, CABI biotechnology series, ISBN 1780647697, Volume 5, x, 213 pages
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Cancer Letters, ISSN 0304-3835, 2015, Volume 368, Issue 1, pp. 88 - 96
Highlights • xCT is highly expressed in CRC. • SSZ promotes substantial accumulation of ROS in CRC. • SSZ and CDDP cause more than additive ROS accumulation in...
Hematology, Oncology and Palliative Medicine | xCT | Sulfasalazine | Chemosensitization | Cisplatin | Colorectal cancer | ROS | XCT | BETA-PHENYLETHYL ISOTHIOCYANATE | DRUG | 1ST-LINE TREATMENT | POTENTIAL USE | OVARIAN-CANCER | CELL-LINES | BREAST-CANCER | THERAPY | ONCOLOGY | GLUTATHIONE | RESISTANCE | Reactive Oxygen Species - metabolism | Glutathione - metabolism | HCT116 Cells | Humans | Sulfasalazine - pharmacology | Antioxidants - pharmacology | Cisplatin - pharmacology | Antineoplastic Combined Chemotherapy Protocols - pharmacology | Dose-Response Relationship, Drug | HT29 Cells | Amino Acid Transport System y+ - metabolism | Amino Acid Transport System y+ - antagonists & inhibitors | Cell Proliferation - drug effects | Histones - metabolism | Oxidative Stress - drug effects | Colorectal Neoplasms - pathology | Colorectal Neoplasms - metabolism | Drug Resistance, Neoplasm - drug effects | Reactive oxygen species | Cysteine | Toxicity | Epithelial cells | Colorectal carcinoma | DNA damage | Acetylcysteine | Cytotoxicity | Cancer therapies | Anticancer properties | Cystine | Antioxidants | Synthesis | Platinum | Inhibition | Colon | Deoxyribonucleic acid--DNA | Glutathione | Enzymes | Mortality | Detoxification | Inflammation | FDA approval | Tumor cell lines | Studies | Inflammatory bowel disease | Chemotherapy | Cell lines | N-Acetyl-L-cysteine | Intracellular | Synergistic effect | Transporter | Apoptosis | Cancer | Index Medicus
Hematology, Oncology and Palliative Medicine | xCT | Sulfasalazine | Chemosensitization | Cisplatin | Colorectal cancer | ROS | XCT | BETA-PHENYLETHYL ISOTHIOCYANATE | DRUG | 1ST-LINE TREATMENT | POTENTIAL USE | OVARIAN-CANCER | CELL-LINES | BREAST-CANCER | THERAPY | ONCOLOGY | GLUTATHIONE | RESISTANCE | Reactive Oxygen Species - metabolism | Glutathione - metabolism | HCT116 Cells | Humans | Sulfasalazine - pharmacology | Antioxidants - pharmacology | Cisplatin - pharmacology | Antineoplastic Combined Chemotherapy Protocols - pharmacology | Dose-Response Relationship, Drug | HT29 Cells | Amino Acid Transport System y+ - metabolism | Amino Acid Transport System y+ - antagonists & inhibitors | Cell Proliferation - drug effects | Histones - metabolism | Oxidative Stress - drug effects | Colorectal Neoplasms - pathology | Colorectal Neoplasms - metabolism | Drug Resistance, Neoplasm - drug effects | Reactive oxygen species | Cysteine | Toxicity | Epithelial cells | Colorectal carcinoma | DNA damage | Acetylcysteine | Cytotoxicity | Cancer therapies | Anticancer properties | Cystine | Antioxidants | Synthesis | Platinum | Inhibition | Colon | Deoxyribonucleic acid--DNA | Glutathione | Enzymes | Mortality | Detoxification | Inflammation | FDA approval | Tumor cell lines | Studies | Inflammatory bowel disease | Chemotherapy | Cell lines | N-Acetyl-L-cysteine | Intracellular | Synergistic effect | Transporter | Apoptosis | Cancer | Index Medicus
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Loading RightsCatalysis Today, ISSN 0920-5861, 08/2010, Volume 153, Issue 3-4, pp. 70 - 76
Selective catalytic reduction (SCR) of NO with NH over Mn substituted iron titanate catalyst (Fe Mn TiO ) was fully investigated using in situ diffuse...
inhibition effect | SCR mechanism | Mn substitution | Ammonium nitrate | O/SO | Iron titanate catalyst | Selective catalytic reduction | MIXED OXIDES | AMMONIA | MNOX CATALYSTS | CHEMISTRY, PHYSICAL | FT-IR | TRANSIENT REACTION ANALYSIS | ADSORPTION | OXIDE CATALYSTS | LOW-TEMPERATURE SCR | ENGINEERING, CHEMICAL | NITRIC-OXIDE | NITROGEN-OXIDES | CHEMISTRY, APPLIED | H2O/SO2 inhibition effect
inhibition effect | SCR mechanism | Mn substitution | Ammonium nitrate | O/SO | Iron titanate catalyst | Selective catalytic reduction | MIXED OXIDES | AMMONIA | MNOX CATALYSTS | CHEMISTRY, PHYSICAL | FT-IR | TRANSIENT REACTION ANALYSIS | ADSORPTION | OXIDE CATALYSTS | LOW-TEMPERATURE SCR | ENGINEERING, CHEMICAL | NITRIC-OXIDE | NITROGEN-OXIDES | CHEMISTRY, APPLIED | H2O/SO2 inhibition effect
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Loading RightsMolecular Cell, ISSN 1097-2765, 10/2013, Volume 52, Issue 2, pp. 248 - 254
HipA of is a eukaryote-like serine-threonine kinase that inhibits cell growth and induces persistence (multidrug tolerance). Previously, it was proposed that...
TOXIN-ANTITOXIN | REPLICATION | INHIBITION | GROWTH ARREST | MULTIDRUG TOLERANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI K-12 | TRANSCRIPTION | TRANSLATION | TRANSFER-RNA-SYNTHETASE | CONTROLLED EXPRESSION | CELL BIOLOGY | Aminoacylation | Phosphorylation | Protein Biosynthesis | Escherichia coli - drug effects | Ribosomes - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Peptide Elongation Factor Tu - genetics | Glutamate-tRNA Ligase - chemistry | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Drug Tolerance | Protein-Serine-Threonine Kinases - genetics | Models, Molecular | Serine - genetics | Escherichia coli Proteins - metabolism | Binding Sites - genetics | Serine - chemistry | RNA, Transfer, Glu - genetics | Serine - metabolism | Peptide Elongation Factor Tu - metabolism | Glutamate-tRNA Ligase - metabolism | Ribosomes - genetics | Escherichia coli - genetics | RNA, Transfer, Glu - metabolism | Escherichia coli Proteins - genetics | Anti-Bacterial Agents - pharmacology | Models, Genetic | Mutation | Glutamate-tRNA Ligase - genetics | Guanosine Pentaphosphate - metabolism | Biological products | Ligases | Cells | Transfer RNA | Index Medicus
TOXIN-ANTITOXIN | REPLICATION | INHIBITION | GROWTH ARREST | MULTIDRUG TOLERANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI K-12 | TRANSCRIPTION | TRANSLATION | TRANSFER-RNA-SYNTHETASE | CONTROLLED EXPRESSION | CELL BIOLOGY | Aminoacylation | Phosphorylation | Protein Biosynthesis | Escherichia coli - drug effects | Ribosomes - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Peptide Elongation Factor Tu - genetics | Glutamate-tRNA Ligase - chemistry | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Drug Tolerance | Protein-Serine-Threonine Kinases - genetics | Models, Molecular | Serine - genetics | Escherichia coli Proteins - metabolism | Binding Sites - genetics | Serine - chemistry | RNA, Transfer, Glu - genetics | Serine - metabolism | Peptide Elongation Factor Tu - metabolism | Glutamate-tRNA Ligase - metabolism | Ribosomes - genetics | Escherichia coli - genetics | RNA, Transfer, Glu - metabolism | Escherichia coli Proteins - genetics | Anti-Bacterial Agents - pharmacology | Models, Genetic | Mutation | Glutamate-tRNA Ligase - genetics | Guanosine Pentaphosphate - metabolism | Biological products | Ligases | Cells | Transfer RNA | Index Medicus
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Loading RightsNature Communications, ISSN 2041-1723, 2013, Volume 4, Issue 1, pp. 2613 - 2613
Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An...
ARABIDOPSIS-THALIANA | SIGNALING PATHWAYS | INHIBITION | MULTIDISCIPLINARY SCIENCES | GIBBERELLIN | CRYSTAL-STRUCTURES | GERMINATION | PLANT HORMONE | MAX2 | F-BOX PROTEIN | RICE | Hydrolases - genetics | Oryza - metabolism | Crystallography, X-Ray | 4-Butyrolactone - metabolism | Plant Growth Regulators - chemistry | Oryza - genetics | Gibberellins - metabolism | Plant Proteins - chemistry | Plants, Genetically Modified | Escherichia coli - metabolism | Gene Expression Regulation, Plant | 4-Butyrolactone - chemistry | Plant Proteins - metabolism | Hydrolases - metabolism | Recombinant Proteins - metabolism | Signal Transduction | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Gibberellins - chemistry | Plant Proteins - genetics | Rhizosphere | Two-Hybrid System Techniques | Escherichia coli - genetics | Hydrolases - chemistry | 4-Butyrolactone - analogs & derivatives | Plant Growth Regulators - metabolism | Index Medicus
ARABIDOPSIS-THALIANA | SIGNALING PATHWAYS | INHIBITION | MULTIDISCIPLINARY SCIENCES | GIBBERELLIN | CRYSTAL-STRUCTURES | GERMINATION | PLANT HORMONE | MAX2 | F-BOX PROTEIN | RICE | Hydrolases - genetics | Oryza - metabolism | Crystallography, X-Ray | 4-Butyrolactone - metabolism | Plant Growth Regulators - chemistry | Oryza - genetics | Gibberellins - metabolism | Plant Proteins - chemistry | Plants, Genetically Modified | Escherichia coli - metabolism | Gene Expression Regulation, Plant | 4-Butyrolactone - chemistry | Plant Proteins - metabolism | Hydrolases - metabolism | Recombinant Proteins - metabolism | Signal Transduction | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Gibberellins - chemistry | Plant Proteins - genetics | Rhizosphere | Two-Hybrid System Techniques | Escherichia coli - genetics | Hydrolases - chemistry | 4-Butyrolactone - analogs & derivatives | Plant Growth Regulators - metabolism | Index Medicus
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Loading RightsThe Journal of Allergy and Clinical Immunology, ISSN 0091-6749, 05/2018, Volume 141, Issue 5, pp. 1677 - 1689.e8
T 2 cell–released IL-31 is a critical mediator in patients with atopic dermatitis (AD), a prevalent and debilitating chronic skin disorder. Brain-derived...
pruritus | dendritic cells | pruritogens | soluble N-ethylmaleimide–sensitive factor activating protein receptors | Atopic dermatitis | dorsal root ganglion | skin | keratinocytes | brain-derived natriuretic peptide | IMMUNOLOGY | ANTI-INTERLEUKIN-31 RECEPTOR | SENSORY NEURONS | IL-31 | ITCH | ALLERGY | INFLAMMATORY PAIN | soluble N-ethylmaleimide-sensitive factor activating protein receptors | MURINE MODELS | EXPRESSION | T-CELLS | Dendritic cells | Analysis | Immunohistochemistry | Neuroimaging | Brain | Animal models | Spinal cord | Endothelin | Peptides | Neuropeptides | Lymphocytes T | Pruritus | Kinases | Dermatitis | Gene sequencing | Rodents | Inhibition | Ethylmaleimide | Brain natriuretic peptide | Cytokines | Neurons | House dust | Transgenic mice | Calcium imaging | Pharmacology | Inflammation | Endothelin 1 | Oncostatin M | Gene expression | Ribonucleic acid--RNA | Patients | Histamine | Communications systems | Signaling | Mice | Skin | Calcium ions | N-Ethylmaleimide
pruritus | dendritic cells | pruritogens | soluble N-ethylmaleimide–sensitive factor activating protein receptors | Atopic dermatitis | dorsal root ganglion | skin | keratinocytes | brain-derived natriuretic peptide | IMMUNOLOGY | ANTI-INTERLEUKIN-31 RECEPTOR | SENSORY NEURONS | IL-31 | ITCH | ALLERGY | INFLAMMATORY PAIN | soluble N-ethylmaleimide-sensitive factor activating protein receptors | MURINE MODELS | EXPRESSION | T-CELLS | Dendritic cells | Analysis | Immunohistochemistry | Neuroimaging | Brain | Animal models | Spinal cord | Endothelin | Peptides | Neuropeptides | Lymphocytes T | Pruritus | Kinases | Dermatitis | Gene sequencing | Rodents | Inhibition | Ethylmaleimide | Brain natriuretic peptide | Cytokines | Neurons | House dust | Transgenic mice | Calcium imaging | Pharmacology | Inflammation | Endothelin 1 | Oncostatin M | Gene expression | Ribonucleic acid--RNA | Patients | Histamine | Communications systems | Signaling | Mice | Skin | Calcium ions | N-Ethylmaleimide
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Loading RightsChemBioChem, ISSN 1439-4227, 11/2007, Volume 8, Issue 17, pp. 2152 - 2161
The initial transition of amyloid beta (1-42) (A beta 42) soluble monomers/small oligomers from unordered/alpha-helix to a beta-sheet-rich conformation...
Amyloid β (1-42) peptide | Mechanism of inhibition | Alzheimer's disease | Circular dichroism | Conformational transition | FIBRIL FORMATION | OXIDATIVE STRESS | CHEMISTRY, MEDICINAL | amyloid beta (1-42) peptide | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-DIFFRACTION | circular dichroism | THIOFLAVINE-T INTERACTION | mechanism of inhibition | IN-VITRO | ATOMIC-FORCE MICROSCOPY | conformational transition | BETA-PROTEIN FIBRILLOGENESIS | A-BETA | SHEET BREAKERS | Peptide Fragments - metabolism | Reproducibility of Results | Sodium Chloride | Temperature | Protein Structure, Quaternary - drug effects | Amyloid beta-Peptides - antagonists & inhibitors | Peptide Fragments - chemistry | Peptide Fragments - antagonists & inhibitors | Protein Binding - drug effects | Amyloid beta-Peptides - metabolism | Amyloid beta-Peptides - chemistry | Kinetics | Circular Dichroism | Index Medicus
Amyloid β (1-42) peptide | Mechanism of inhibition | Alzheimer's disease | Circular dichroism | Conformational transition | FIBRIL FORMATION | OXIDATIVE STRESS | CHEMISTRY, MEDICINAL | amyloid beta (1-42) peptide | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-DIFFRACTION | circular dichroism | THIOFLAVINE-T INTERACTION | mechanism of inhibition | IN-VITRO | ATOMIC-FORCE MICROSCOPY | conformational transition | BETA-PROTEIN FIBRILLOGENESIS | A-BETA | SHEET BREAKERS | Peptide Fragments - metabolism | Reproducibility of Results | Sodium Chloride | Temperature | Protein Structure, Quaternary - drug effects | Amyloid beta-Peptides - antagonists & inhibitors | Peptide Fragments - chemistry | Peptide Fragments - antagonists & inhibitors | Protein Binding - drug effects | Amyloid beta-Peptides - metabolism | Amyloid beta-Peptides - chemistry | Kinetics | Circular Dichroism | Index Medicus
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Loading RightsCell, ISSN 0092-8674, 2007, Volume 128, Issue 3, pp. 533 - 546
Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown...
CELLBIO | CELLIMMUNO | PROGRAMMED CELL-DEATH | CASPASE-2 ACTIVATION | PROVIDES INSIGHTS | INHIBITION | INDUCED APOPTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | SUPERFAMILY | PIDD | MUTATIONAL ANALYSIS | CONTAINING PROTEIN | CELL BIOLOGY | CRADD Signaling Adaptor Protein - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | CRADD Signaling Adaptor Protein - metabolism | Mutagenesis, Site-Directed | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Caspase 2 - metabolism | Recombinant Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - genetics | Multiprotein Complexes - metabolism | CRADD Signaling Adaptor Protein - genetics | Protein Conformation | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Structure | Crystals | Index Medicus
CELLBIO | CELLIMMUNO | PROGRAMMED CELL-DEATH | CASPASE-2 ACTIVATION | PROVIDES INSIGHTS | INHIBITION | INDUCED APOPTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | SUPERFAMILY | PIDD | MUTATIONAL ANALYSIS | CONTAINING PROTEIN | CELL BIOLOGY | CRADD Signaling Adaptor Protein - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | CRADD Signaling Adaptor Protein - metabolism | Mutagenesis, Site-Directed | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Caspase 2 - metabolism | Recombinant Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - genetics | Multiprotein Complexes - metabolism | CRADD Signaling Adaptor Protein - genetics | Protein Conformation | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Structure | Crystals | Index Medicus
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Loading RightsInternational Journal of Cancer, ISSN 0020-7136, 09/2014, Volume 135, Issue 5, pp. 1178 - 1186
The mechanisms by which tumor‐associated neutrophils (TANs) affect tumor growth are to a large extent unknown. Regulatory T‐cells (T‐regs) are functionally...
immune avoidance | regulatory T‐cells | tumor immunology | CCL17 | tumor‐associated neutrophils | tumor-associated neutrophils | regulatory T-cells | ACTIVATION | CHEMOKINES | TOLERANCE | GRANULOCYTES | SUPPRESSION | CANCER | INHIBITION | ONCOLOGY | GROWTH | ACCUMULATION | PROGRESSION | Humans | Mice, Inbred C57BL | Neutrophils - immunology | Lymphocyte Depletion | T-Lymphocytes, Regulatory - immunology | Cell Movement - immunology | Lymphocyte Activation - immunology | Animals | Antigens, Ly - immunology | Neoplasms - immunology | Chemokine CCL17 - immunology | Cell Line, Tumor | Mice | Mice, Inbred BALB C | Antibodies, Monoclonal - immunology | Lymphocytes, Tumor-Infiltrating - immunology | Employee recruitment | Analysis | Monoclonal antibodies | Disease susceptibility | T cells | Enzyme-linked immunosorbent assay | Tumors | Medical research | Rodents | Immune system | Index Medicus
immune avoidance | regulatory T‐cells | tumor immunology | CCL17 | tumor‐associated neutrophils | tumor-associated neutrophils | regulatory T-cells | ACTIVATION | CHEMOKINES | TOLERANCE | GRANULOCYTES | SUPPRESSION | CANCER | INHIBITION | ONCOLOGY | GROWTH | ACCUMULATION | PROGRESSION | Humans | Mice, Inbred C57BL | Neutrophils - immunology | Lymphocyte Depletion | T-Lymphocytes, Regulatory - immunology | Cell Movement - immunology | Lymphocyte Activation - immunology | Animals | Antigens, Ly - immunology | Neoplasms - immunology | Chemokine CCL17 - immunology | Cell Line, Tumor | Mice | Mice, Inbred BALB C | Antibodies, Monoclonal - immunology | Lymphocytes, Tumor-Infiltrating - immunology | Employee recruitment | Analysis | Monoclonal antibodies | Disease susceptibility | T cells | Enzyme-linked immunosorbent assay | Tumors | Medical research | Rodents | Immune system | Index Medicus
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Loading RightsProceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2011, Volume 108, Issue 48, pp. 19365 - 19370
Arenaviruses cause disease in industrialized and developing nations alike. Among them, the hemorrhagic fever virus Lassa is responsible for ∼300,000—500,000...
Proteins | Head | RNA | Nucleoproteins | Viruses | Viral morphology | Lassa virus | Genetic mutation | Arenavirus | Crystal structure | Structural biology | Virology | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | LYMPHOCYTIC CHORIOMENINGITIS VIRUS | MATRIX PROTEIN-Z | REPLICATION | INHIBITION | ANOMALOUS DIFFRACTION | virology | structural biology | NUCLEOCAPSID PROTEIN | NONSPECIFIC RNA | RESPIRATORY SYNCYTIAL VIRUS | FEVER | Cell Line | Enzyme-Linked Immunosorbent Assay | Viral Proteins - chemistry | Humans | Crystallization | Models, Molecular | Lassa virus - chemistry | Protein Conformation | RNA, Viral - metabolism | Ribonucleoproteins - metabolism | Ribonucleoproteins - chemistry | Viral Proteins - metabolism | Viral proteins | Physiological aspects | Genetic aspects | Research | Arenaviruses | Protein binding | Ribonucleic acid--RNA | Genomics | Binding sites | Index Medicus | Hemorrhagic fever | Transcription | Hydrogen-deuterium exchange | Ribonucleoproteins | Genomes | Infection | scaffolds | Mutagenesis | Replication | genomics | Models | Gating | Biological Sciences
Proteins | Head | RNA | Nucleoproteins | Viruses | Viral morphology | Lassa virus | Genetic mutation | Arenavirus | Crystal structure | Structural biology | Virology | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | LYMPHOCYTIC CHORIOMENINGITIS VIRUS | MATRIX PROTEIN-Z | REPLICATION | INHIBITION | ANOMALOUS DIFFRACTION | virology | structural biology | NUCLEOCAPSID PROTEIN | NONSPECIFIC RNA | RESPIRATORY SYNCYTIAL VIRUS | FEVER | Cell Line | Enzyme-Linked Immunosorbent Assay | Viral Proteins - chemistry | Humans | Crystallization | Models, Molecular | Lassa virus - chemistry | Protein Conformation | RNA, Viral - metabolism | Ribonucleoproteins - metabolism | Ribonucleoproteins - chemistry | Viral Proteins - metabolism | Viral proteins | Physiological aspects | Genetic aspects | Research | Arenaviruses | Protein binding | Ribonucleic acid--RNA | Genomics | Binding sites | Index Medicus | Hemorrhagic fever | Transcription | Hydrogen-deuterium exchange | Ribonucleoproteins | Genomes | Infection | scaffolds | Mutagenesis | Replication | genomics | Models | Gating | Biological Sciences
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Loading RightsNature Chemical Biology, ISSN 1552-4450, 10/2011, Volume 7, Issue 10, pp. 701 - 711
Oxygen (O-2) is a prerequisite for cellular respiration in aerobic organisms but also elicits toxicity. To understand how animals cope with the ambivalent...
ZINC FINGERS | ACTIVATION | ION-CHANNEL TRPA1 | PAIN | INHIBITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | COVALENT MODIFICATION | COLD | HYPOXIA | CYSTEINES | SENSORY NEURONS
ZINC FINGERS | ACTIVATION | ION-CHANNEL TRPA1 | PAIN | INHIBITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | COVALENT MODIFICATION | COLD | HYPOXIA | CYSTEINES | SENSORY NEURONS
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Loading RightsProceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2013, Volume 110, Issue 44, pp. 17862 - 17867
Glucose transporters are required to bring glucose into cells, where it is an essential energy source and precursor in protein and lipid synthesis. These...
Active transport | Biochemical mechanisms | Facilitative glucose transport proteins | Symporters | Escherichia coli | Counterflow | Biochemistry | Cytochalasins | Crystal structure | P branes | GLUT1 | SITE | PROTEIN | GLUT | MULTIDISCIPLINARY SCIENCES | EXOFACIAL LIGAND-BINDING | ESCHERICHIA-COLI | MONOSACCHARIDE TRANSPORTERS | COLI MEMBRANE-VESICLES | FAMILY | INHIBITION | sugar transporter | solute-carrier 2A | membrane protein | major facilitator superfamily | CYTOCHALASIN-B | Cytochalasin B - pharmacology | Mutagenesis, Site-Directed | Colforsin - pharmacology | Humans | Crystallization | Staphylococcus epidermidis - chemistry | Models, Molecular | Glucose Transport Proteins, Facilitative - chemistry | Staphylococcus epidermidis - genetics | Sequence Homology | Mutagenesis | Phloretin - pharmacology | Cloning, Molecular | Protein Conformation | Biological Transport - physiology | Glucose Transport Proteins, Facilitative - genetics | Glucose Transport Proteins, Facilitative - antagonists & inhibitors | Gram-positive bacteria | Lipids | Glucose | Molecular structure | Protein synthesis | Index Medicus | Biological Sciences
Active transport | Biochemical mechanisms | Facilitative glucose transport proteins | Symporters | Escherichia coli | Counterflow | Biochemistry | Cytochalasins | Crystal structure | P branes | GLUT1 | SITE | PROTEIN | GLUT | MULTIDISCIPLINARY SCIENCES | EXOFACIAL LIGAND-BINDING | ESCHERICHIA-COLI | MONOSACCHARIDE TRANSPORTERS | COLI MEMBRANE-VESICLES | FAMILY | INHIBITION | sugar transporter | solute-carrier 2A | membrane protein | major facilitator superfamily | CYTOCHALASIN-B | Cytochalasin B - pharmacology | Mutagenesis, Site-Directed | Colforsin - pharmacology | Humans | Crystallization | Staphylococcus epidermidis - chemistry | Models, Molecular | Glucose Transport Proteins, Facilitative - chemistry | Staphylococcus epidermidis - genetics | Sequence Homology | Mutagenesis | Phloretin - pharmacology | Cloning, Molecular | Protein Conformation | Biological Transport - physiology | Glucose Transport Proteins, Facilitative - genetics | Glucose Transport Proteins, Facilitative - antagonists & inhibitors | Gram-positive bacteria | Lipids | Glucose | Molecular structure | Protein synthesis | Index Medicus | Biological Sciences
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Loading RightsFood Chemistry, ISSN 0308-8146, 01/2016, Volume 190, pp. 207 - 215
α-Glucosidase is a therapeutic target for diabetes mellitus, and α-glucosidase inhibitors play a vital role in the treatments for the disease. As a kind of...
Spectroscopy | Inhibitory kinetics | α-Glucosidase | Kaempferol | Molecular docking | Inhibition mechanism | FLUORESCENCE SPECTROSCOPY | TYROSINASE | FOOD SCIENCE & TECHNOLOGY | FLAVONOIDS | HYDROCHLORIDE | NANOPARTICLES | IN-VITRO | NUTRITION & DIETETICS | alpha-Glucosidase | SIMULATIONS | CHEMISTRY, APPLIED | BOVINE SERUM-ALBUMIN | INSIGHTS | Molecular Docking Simulation - methods | Kaempferols - chemistry | Spectrum Analysis - methods | Kinetics | Flavonoids - chemistry | alpha-Glucosidases - metabolism | alpha-Glucosidases - chemistry | Index Medicus
Spectroscopy | Inhibitory kinetics | α-Glucosidase | Kaempferol | Molecular docking | Inhibition mechanism | FLUORESCENCE SPECTROSCOPY | TYROSINASE | FOOD SCIENCE & TECHNOLOGY | FLAVONOIDS | HYDROCHLORIDE | NANOPARTICLES | IN-VITRO | NUTRITION & DIETETICS | alpha-Glucosidase | SIMULATIONS | CHEMISTRY, APPLIED | BOVINE SERUM-ALBUMIN | INSIGHTS | Molecular Docking Simulation - methods | Kaempferols - chemistry | Spectrum Analysis - methods | Kinetics | Flavonoids - chemistry | alpha-Glucosidases - metabolism | alpha-Glucosidases - chemistry | Index Medicus
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