1997, Topics in current chemistry, ISBN 3540620338, Volume 186., viii, 239
This book presents the state of the art in the synthesis very complex saccharide structures, written by leading scientists at the forefront of this rapidly...
Biochemistry, general | Biochemistry | Chemistry, Organic | Organic Chemistry
Biochemistry, general | Biochemistry | Chemistry, Organic | Organic Chemistry
Book
1997, Topics in current chemistry, ISBN 354062032X, Volume 187., viii, 321
The synthesis of very complex saccharide structures is one of the most challenging areas of modern glycoscience. This volume presents the state of the art of...
Biochemistry, general | Biochemistry | Chemistry, Organic | Organic Chemistry
Biochemistry, general | Biochemistry | Chemistry, Organic | Organic Chemistry
Book
Nature, ISSN 0028-0836, 01/2011, Volume 469, Issue 7328, pp. 58 - 64
Arbuscular mycorrhiza (AM) is a root endosymbiosis between plants and glomeromycete fungi. It is the most widespread terrestrial plant symbiosis, improving...
DIFFUSIBLE FACTOR | PROTEIN | NODULE DEVELOPMENT | RHIZOBIUM | MEDICAGO-TRUNCATULA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GENES | CHITOOLIGOSACCHARIDE NODULATION FACTORS | BACTERIAL | LEGUMES | Carbohydrate Sequence | Symbiosis | Plant Extracts - chemistry | Plant Roots - metabolism | Daucus carota - chemistry | Signal Transduction | Medicago truncatula - growth & development | Lipopolysaccharides - metabolism | Molecular Sequence Data | Daucus carota - microbiology | Chromatography, High Pressure Liquid | Medicago truncatula - chemistry | Medicago truncatula - microbiology | Medicago truncatula - metabolism | Plant Roots - microbiology | Spores, Fungal - chemistry | Plant Extracts - metabolism | Spores, Fungal - metabolism | Plant Roots - chemistry | Mycorrhizae - metabolism | Daucus carota - metabolism | Lipopolysaccharides - chemistry | Plant Roots - growth & development | Glomeromycota - metabolism | Mycorrhizas | Legumes | Beans | Physiological aspects | Roots (Botany) | Research | Oligosaccharides | Mimosaceae | Microbiology | E coli | Genes | Genetic engineering | Biological assays | Mass spectrometry | Chromatography
DIFFUSIBLE FACTOR | PROTEIN | NODULE DEVELOPMENT | RHIZOBIUM | MEDICAGO-TRUNCATULA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GENES | CHITOOLIGOSACCHARIDE NODULATION FACTORS | BACTERIAL | LEGUMES | Carbohydrate Sequence | Symbiosis | Plant Extracts - chemistry | Plant Roots - metabolism | Daucus carota - chemistry | Signal Transduction | Medicago truncatula - growth & development | Lipopolysaccharides - metabolism | Molecular Sequence Data | Daucus carota - microbiology | Chromatography, High Pressure Liquid | Medicago truncatula - chemistry | Medicago truncatula - microbiology | Medicago truncatula - metabolism | Plant Roots - microbiology | Spores, Fungal - chemistry | Plant Extracts - metabolism | Spores, Fungal - metabolism | Plant Roots - chemistry | Mycorrhizae - metabolism | Daucus carota - metabolism | Lipopolysaccharides - chemistry | Plant Roots - growth & development | Glomeromycota - metabolism | Mycorrhizas | Legumes | Beans | Physiological aspects | Roots (Botany) | Research | Oligosaccharides | Mimosaceae | Microbiology | E coli | Genes | Genetic engineering | Biological assays | Mass spectrometry | Chromatography
Journal Article
ChemBioChem, ISSN 1439-4227, 05/2001, Volume 2, Issue 5, pp. 311 - 318
Oligosaccharides in which at least one glycosidic oxygen atom is replaced with a sulfur atom can be routinely synthesized and act as competitive inhibitors of...
carbohydrates | hydrolases | protein structures | enzyme catalysis | thiooligosaccharides | Carbohydrates | Hydrolases | Enzyme catalysis | Thiooligosaccharides | Protein structures | ASPERGILLUS-NIGER | CHEMISTRY, MEDICINAL | ANALOGS | STARCH-BINDING DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLUCOAMYLASE G1 | CYCLODEXTRIN GLYCOSYLTRANSFERASE | BETA-CYCLODEXTRIN | CONFORMATIONAL-ANALYSIS | GLUCANOTRANSFERASE | OLIGOSACCHARIDE SUBSTRATE | GLYCOSYL HYDROLASES | Oligosaccharides - pharmacology | Disulfides - chemistry | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Enzyme Inhibitors - pharmacology | Protein Binding | Disulfides - pharmacology | Structure-Activity Relationship | Carbohydrate Conformation | Glycoside Hydrolases - antagonists & inhibitors
carbohydrates | hydrolases | protein structures | enzyme catalysis | thiooligosaccharides | Carbohydrates | Hydrolases | Enzyme catalysis | Thiooligosaccharides | Protein structures | ASPERGILLUS-NIGER | CHEMISTRY, MEDICINAL | ANALOGS | STARCH-BINDING DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLUCOAMYLASE G1 | CYCLODEXTRIN GLYCOSYLTRANSFERASE | BETA-CYCLODEXTRIN | CONFORMATIONAL-ANALYSIS | GLUCANOTRANSFERASE | OLIGOSACCHARIDE SUBSTRATE | GLYCOSYL HYDROLASES | Oligosaccharides - pharmacology | Disulfides - chemistry | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Enzyme Inhibitors - pharmacology | Protein Binding | Disulfides - pharmacology | Structure-Activity Relationship | Carbohydrate Conformation | Glycoside Hydrolases - antagonists & inhibitors
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 04/2016, Volume 12, Issue 4, pp. 298 - 303
Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and...
SUBSTRATE-SPECIFICITY | ACTIVATION | ENZYME | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY | COORDINATION | CONFORMATION | OXYGENASES | CELLULOSE DEGRADATION | DISCOVERY | Amino Acid Sequence | Catalytic Domain | Oxidation-Reduction | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Lentinula - enzymology | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Aspergillus oryzae - genetics | Aspergillus oryzae - enzymology | Lentinula - genetics | Oligosaccharides - chemistry | Chitin - metabolism | Copper - metabolism | Fluorescence Resonance Energy Transfer | Mixed Function Oxygenases - genetics | Binding Sites | Cellulose - metabolism | Enzymes | Biomass | Copper | Spectrum analysis | Life Sciences | Biomolecules | Quantitative Methods | Biochemistry, Molecular Biology | Chemical Engineering | Kemiteknik
SUBSTRATE-SPECIFICITY | ACTIVATION | ENZYME | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY | COORDINATION | CONFORMATION | OXYGENASES | CELLULOSE DEGRADATION | DISCOVERY | Amino Acid Sequence | Catalytic Domain | Oxidation-Reduction | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Lentinula - enzymology | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Aspergillus oryzae - genetics | Aspergillus oryzae - enzymology | Lentinula - genetics | Oligosaccharides - chemistry | Chitin - metabolism | Copper - metabolism | Fluorescence Resonance Energy Transfer | Mixed Function Oxygenases - genetics | Binding Sites | Cellulose - metabolism | Enzymes | Biomass | Copper | Spectrum analysis | Life Sciences | Biomolecules | Quantitative Methods | Biochemistry, Molecular Biology | Chemical Engineering | Kemiteknik
Journal Article
New Phytologist, ISSN 0028-646X, 11/2013, Volume 200, Issue 3, pp. 656 - 662
Rhizobial nodulation (Nod) factors activate both nodule morphogenesis and infection thread development during legume nodulation. Nod factors induce two...
Legumes | Receptors | Calcium | Hair cells | Nodulation | Infections | Root hairs | Inductive reasoning | Plants | Nodules | Rapid reports | Medicago truncatula | Nod factor | infection | nodulation | ethylene | calcium influx | Infection | Calcium influx | Ethylene | NADPH OXIDASE | CELLS | FACTOR SIGNAL-TRANSDUCTION | NODULATION FACTOR | ARBUSCULAR MYCORRHIZA | RECEPTOR | ORGANOGENESIS | PLANT SCIENCES | LOTUS-JAPONICUS | RHIZOBIUM | GENE | Symbiosis | Medicago truncatula - genetics | Root Nodules, Plant - metabolism | Calcium - metabolism | Genes, Plant | Bacterial Proteins - genetics | Medicago truncatula - microbiology | Medicago truncatula - metabolism | Sinorhizobium meliloti - metabolism | Ethylenes - metabolism | Plant Root Nodulation - genetics | Mycorrhizae - metabolism | Bacterial Proteins - metabolism | Mutation | Calcium Signaling - genetics | Beans | Health aspects | Mimosaceae | Research
Legumes | Receptors | Calcium | Hair cells | Nodulation | Infections | Root hairs | Inductive reasoning | Plants | Nodules | Rapid reports | Medicago truncatula | Nod factor | infection | nodulation | ethylene | calcium influx | Infection | Calcium influx | Ethylene | NADPH OXIDASE | CELLS | FACTOR SIGNAL-TRANSDUCTION | NODULATION FACTOR | ARBUSCULAR MYCORRHIZA | RECEPTOR | ORGANOGENESIS | PLANT SCIENCES | LOTUS-JAPONICUS | RHIZOBIUM | GENE | Symbiosis | Medicago truncatula - genetics | Root Nodules, Plant - metabolism | Calcium - metabolism | Genes, Plant | Bacterial Proteins - genetics | Medicago truncatula - microbiology | Medicago truncatula - metabolism | Sinorhizobium meliloti - metabolism | Ethylenes - metabolism | Plant Root Nodulation - genetics | Mycorrhizae - metabolism | Bacterial Proteins - metabolism | Mutation | Calcium Signaling - genetics | Beans | Health aspects | Mimosaceae | Research
Journal Article
Chemistry – A European Journal, ISSN 0947-6539, 07/2015, Volume 21, Issue 30, pp. 10903 - 10912
A fast chemoenzymatic synthesis of sialylated oligosaccharides containing C5‐modified neuraminic acids is reported. Analogues of GM3 and GM2 ganglioside...
influenza | glycomimetics | neuraminic acids | chemoenzymatic synthesis | oligosaccharides | Glycomimetics | Neuraminic acids | Oligosaccharides | Chemoenzymatic synthesis | Influenza | IN-VIVO SYNTHESIS | N-ACYL | SIALIC-ACID | CHEMISTRY, MULTIDISCIPLINARY | POLYSIALIC ACID | SCALE SYNTHESIS | INFLUENZA NEURAMINIDASE | GD3 GANGLIOSIDE | ACYL SIDE-CHAIN | MAACKIA-AMURENSIS | BINDING | Metabolic Engineering | Sialic Acids - chemical synthesis | Neuraminic Acids - chemical synthesis | Sialic Acids - metabolism | Neuraminic Acids - pharmacology | Neuraminic Acids - chemistry | Oligosaccharides - metabolism | Agglutinins - metabolism | Sialic Acids - chemistry | Hemagglutinins - metabolism | Hydrolysis | Oligosaccharides - pharmacology | Oligosaccharides - chemical synthesis | Vibrio cholerae - enzymology | Animals | Cattle | Escherichia coli - genetics | Neuraminic Acids - metabolism | Sialic Acids - pharmacology | Oligosaccharides - chemistry | Escherichia coli - metabolism | Maackia - metabolism | Neuraminidase - antagonists & inhibitors | Bacteria | Cholera toxin | Escherichia coli | Acids | Cholera | Synthesis | Viruses | Strategy | Inhibition | Vibrio | Life Sciences | Chemical Sciences
influenza | glycomimetics | neuraminic acids | chemoenzymatic synthesis | oligosaccharides | Glycomimetics | Neuraminic acids | Oligosaccharides | Chemoenzymatic synthesis | Influenza | IN-VIVO SYNTHESIS | N-ACYL | SIALIC-ACID | CHEMISTRY, MULTIDISCIPLINARY | POLYSIALIC ACID | SCALE SYNTHESIS | INFLUENZA NEURAMINIDASE | GD3 GANGLIOSIDE | ACYL SIDE-CHAIN | MAACKIA-AMURENSIS | BINDING | Metabolic Engineering | Sialic Acids - chemical synthesis | Neuraminic Acids - chemical synthesis | Sialic Acids - metabolism | Neuraminic Acids - pharmacology | Neuraminic Acids - chemistry | Oligosaccharides - metabolism | Agglutinins - metabolism | Sialic Acids - chemistry | Hemagglutinins - metabolism | Hydrolysis | Oligosaccharides - pharmacology | Oligosaccharides - chemical synthesis | Vibrio cholerae - enzymology | Animals | Cattle | Escherichia coli - genetics | Neuraminic Acids - metabolism | Sialic Acids - pharmacology | Oligosaccharides - chemistry | Escherichia coli - metabolism | Maackia - metabolism | Neuraminidase - antagonists & inhibitors | Bacteria | Cholera toxin | Escherichia coli | Acids | Cholera | Synthesis | Viruses | Strategy | Inhibition | Vibrio | Life Sciences | Chemical Sciences
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2008, Volume 283, Issue 32, pp. 21864 - 21872
Xyloglucan endo -transglycosylases (XETs) are key enzymes involved in the restructuring of plant cell walls during morphogenesis. As members of glycoside...
ENDOTRANSGLYCOSYLASE | EVOLUTION | OLIGOSACCHARIDES | ACTIVE-SITE | BACILLUS-SUBTILIS | CELL WALL COMPOSITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | LEVANSUCRASE | CRYSTAL-STRUCTURES | IDENTIFICATION | BINDING | Hydrolysis | Thermodynamics | Glycosyltransferases - metabolism | Populus - enzymology | Glycosyltransferases - chemistry | Mass Spectrometry | Oligosaccharides - chemistry | Staining and Labeling | Populus - chemistry | Glycosyltransferases - biosynthesis | Oligosaccharides - metabolism | Transglycosylases | Biokemi | Biochemistry | Plant cell walls | Xyloglucans | Biomaterials | Glycoside hydrolase family 16 | Xyloglucan | Polysaccharides | Plant cell culture | Glucosidic bonds | Biochemistry and Molecular Biology | Glycosyl acceptors | Natural Sciences | Sugars | Glycosyl donors | Key enzymes | Biological Sciences | Plants (botany) | Free energy changes | Gene transfer | Electrospray mass spectrometries | Direct observations | Free energy | Glycosyl | Chemistry | Naturvetenskap | Biokemi och molekylärbiologi | Kemi | Biologiska vetenskaper | In-vivo | Enzyme complexes | Mass spectrometry | High performance liquid chromatography
ENDOTRANSGLYCOSYLASE | EVOLUTION | OLIGOSACCHARIDES | ACTIVE-SITE | BACILLUS-SUBTILIS | CELL WALL COMPOSITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | LEVANSUCRASE | CRYSTAL-STRUCTURES | IDENTIFICATION | BINDING | Hydrolysis | Thermodynamics | Glycosyltransferases - metabolism | Populus - enzymology | Glycosyltransferases - chemistry | Mass Spectrometry | Oligosaccharides - chemistry | Staining and Labeling | Populus - chemistry | Glycosyltransferases - biosynthesis | Oligosaccharides - metabolism | Transglycosylases | Biokemi | Biochemistry | Plant cell walls | Xyloglucans | Biomaterials | Glycoside hydrolase family 16 | Xyloglucan | Polysaccharides | Plant cell culture | Glucosidic bonds | Biochemistry and Molecular Biology | Glycosyl acceptors | Natural Sciences | Sugars | Glycosyl donors | Key enzymes | Biological Sciences | Plants (botany) | Free energy changes | Gene transfer | Electrospray mass spectrometries | Direct observations | Free energy | Glycosyl | Chemistry | Naturvetenskap | Biokemi och molekylärbiologi | Kemi | Biologiska vetenskaper | In-vivo | Enzyme complexes | Mass spectrometry | High performance liquid chromatography
Journal Article
The Plant Cell, ISSN 1040-4651, 5/2002, Volume 14, Issue 5, pp. 1033 - 1052
Family 3 β-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze the hydrolytic removal of β-D-glucosyl residues from...
Enzymes | Barley | Active sites | Substrate specificity | Atoms | Amino acids | Kinetics | Enzyme substrates | Functional groups | Plant cells | CELLULOSE-BINDING DOMAIN | PATHOGEN INTERACTIONS | WALL-BOUND EXO-1,3-BETA-D-GLUCANASE | D-GLUCOSIDASE | TRICHODERMA-REESEI | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTAL-STRUCTURES | GLYCOSIDE HYDROLASE | PLANT SCIENCES | CELL BIOLOGY | BARLEY HORDEUM-VULGARE | CATALYTIC MECHANISM | SUBSITE AFFINITIES | Disaccharides - metabolism | Glucosidases - metabolism | Glycoside Hydrolases - genetics | Glucosidases - genetics | Molecular Sequence Data | Substrate Specificity | Structure-Activity Relationship | Phylogeny | Disaccharides - chemistry | beta-Glucosidase - chemistry | Plants - enzymology | Glucosidases - chemistry | Glucan Endo-1,3-beta-D-Glucosidase - chemistry | Trisaccharides - chemistry | Plants - genetics | beta-Glucosidase - genetics | Glucan Endo-1,3-beta-D-Glucosidase - metabolism | Glycoside Hydrolases - chemistry | beta-Glucosidase - metabolism | Glucans - metabolism | Catalysis | Trisaccharides - metabolism | Binding Sites | Carbohydrate Sequence | Amino Acid Sequence | Glucan Endo-1,3-beta-D-Glucosidase - genetics | Models, Molecular | Cellobiose - metabolism | Sequence Homology, Amino Acid | Cellobiose - chemistry | Protein Binding | Glucans - chemistry | Glycoside Hydrolases - metabolism
Enzymes | Barley | Active sites | Substrate specificity | Atoms | Amino acids | Kinetics | Enzyme substrates | Functional groups | Plant cells | CELLULOSE-BINDING DOMAIN | PATHOGEN INTERACTIONS | WALL-BOUND EXO-1,3-BETA-D-GLUCANASE | D-GLUCOSIDASE | TRICHODERMA-REESEI | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTAL-STRUCTURES | GLYCOSIDE HYDROLASE | PLANT SCIENCES | CELL BIOLOGY | BARLEY HORDEUM-VULGARE | CATALYTIC MECHANISM | SUBSITE AFFINITIES | Disaccharides - metabolism | Glucosidases - metabolism | Glycoside Hydrolases - genetics | Glucosidases - genetics | Molecular Sequence Data | Substrate Specificity | Structure-Activity Relationship | Phylogeny | Disaccharides - chemistry | beta-Glucosidase - chemistry | Plants - enzymology | Glucosidases - chemistry | Glucan Endo-1,3-beta-D-Glucosidase - chemistry | Trisaccharides - chemistry | Plants - genetics | beta-Glucosidase - genetics | Glucan Endo-1,3-beta-D-Glucosidase - metabolism | Glycoside Hydrolases - chemistry | beta-Glucosidase - metabolism | Glucans - metabolism | Catalysis | Trisaccharides - metabolism | Binding Sites | Carbohydrate Sequence | Amino Acid Sequence | Glucan Endo-1,3-beta-D-Glucosidase - genetics | Models, Molecular | Cellobiose - metabolism | Sequence Homology, Amino Acid | Cellobiose - chemistry | Protein Binding | Glucans - chemistry | Glycoside Hydrolases - metabolism
Journal Article
ChemBioChem, ISSN 1439-4227, 01/2014, Volume 15, Issue 2, pp. 293 - 300
We report the enzymatic synthesis of α‐D‐glucopyranosyl‐(1→4)‐α‐L‐rhamnopyranoside and α‐D‐glucopyranosyl‐(1→3)‐α‐L‐rhamnopyranoside by using a wild‐type...
carbohydrates | cis‐glycosylation | Shigella flexneri | cyclodextrin glucanotransferase | biocatalysis | cis-glycosylation | O-SPECIFIC POLYSACCHARIDE | BACILLUS-CIRCULANS STRAIN-251 | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-STRUCTURE | ENZYMATIC-SYNTHESIS | CYCLODEXTRIN GLYCOSYLTRANSFERASE | CYCLOMALTODEXTRIN GLUCANOTRANSFERASE | CHEMOENZYMATIC SYNTHESIS | ACCEPTOR SPECIFICITY | CONVERGENT SYNTHESIS | TRANSGLYCOSYLATION REACTION | Carbohydrate Sequence | Temperature | Biocatalysis | Enzyme Stability | Molecular Sequence Data | Glycosylation | Glucosyltransferases - metabolism | Haptens - chemistry | Oligosaccharides - chemical synthesis | beta-Cyclodextrins - chemistry | Bacillus - enzymology | Oligosaccharides - chemistry | Kinetics | Oxidases | Glucose metabolism | Dysentery | Cyclodextrins | Dextrins | Glucose | Dextrose | Bacteriology
carbohydrates | cis‐glycosylation | Shigella flexneri | cyclodextrin glucanotransferase | biocatalysis | cis-glycosylation | O-SPECIFIC POLYSACCHARIDE | BACILLUS-CIRCULANS STRAIN-251 | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-STRUCTURE | ENZYMATIC-SYNTHESIS | CYCLODEXTRIN GLYCOSYLTRANSFERASE | CYCLOMALTODEXTRIN GLUCANOTRANSFERASE | CHEMOENZYMATIC SYNTHESIS | ACCEPTOR SPECIFICITY | CONVERGENT SYNTHESIS | TRANSGLYCOSYLATION REACTION | Carbohydrate Sequence | Temperature | Biocatalysis | Enzyme Stability | Molecular Sequence Data | Glycosylation | Glucosyltransferases - metabolism | Haptens - chemistry | Oligosaccharides - chemical synthesis | beta-Cyclodextrins - chemistry | Bacillus - enzymology | Oligosaccharides - chemistry | Kinetics | Oxidases | Glucose metabolism | Dysentery | Cyclodextrins | Dextrins | Glucose | Dextrose | Bacteriology
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2014, Volume 9, Issue 12, p. e112635
Lipochitin oligosaccharides (LCOs) are signaling molecules required by ecologically and agronomically important bacteria and fungi to establish symbioses with...
CHITOOLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | RHIZOBIUM-LEGUMINOSARUM | HIGH-AFFINITY | ARBUSCULAR MYCORRHIZA | RECEPTOR-LIKE KINASE | NODULATION FACTORS | BINDING | ENDOTHELIAL GROWTH-FACTOR | INNATE IMMUNITY | Neovascularization, Physiologic - drug effects | Acylation - drug effects | Aorta - drug effects | Extracellular Matrix - drug effects | Humans | Rats, Inbred F344 | Extracellular Matrix - metabolism | Cell Adhesion - drug effects | Disaccharides - chemistry | Integrins - metabolism | Cell Movement - drug effects | Disaccharides - pharmacology | Soybeans - chemistry | Acetylation - drug effects | Animals | Signal Transduction - drug effects | Endothelial Cells - cytology | Lipopolysaccharides - pharmacology | Mammals - physiology | Lipopolysaccharides - chemistry | Symbiosis - drug effects | In Vitro Techniques | Aorta - physiology | Endothelial Cells - drug effects | Fibronectins | Therapeutics | Physiological aspects | Chitin | Neovascularization | Cells | Sugars | Homeopathy | Materia medica and therapeutics | Chitinase | Diabetic retinopathy | Vitronectin | Innate immunity | Biology | Kinases | Immunity | Physiological responses | Fibronectin | Mammalian cells | Plant cells | Substitutes | Proteins | Fungi | Angiogenesis | Signal transduction | Receptors | Biological effects | E coli | Agronomy | Cell adhesion | Bacteria | Physiology | Inhibition | Plant sciences | Chemical synthesis | Symbiosis | Heparan sulfate | Carbohydrates | Medical research | Legumes | Plants (botany) | Disaccharides | Blood vessels | Oligosaccharides | Nitrogen | Mammals | Gene expression | Biological activity | Endothelial cells | Medicine | Signaling | Alzheimers disease | Recognition | Chemical Sciences
CHITOOLIGOSACCHARIDES | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | RHIZOBIUM-LEGUMINOSARUM | HIGH-AFFINITY | ARBUSCULAR MYCORRHIZA | RECEPTOR-LIKE KINASE | NODULATION FACTORS | BINDING | ENDOTHELIAL GROWTH-FACTOR | INNATE IMMUNITY | Neovascularization, Physiologic - drug effects | Acylation - drug effects | Aorta - drug effects | Extracellular Matrix - drug effects | Humans | Rats, Inbred F344 | Extracellular Matrix - metabolism | Cell Adhesion - drug effects | Disaccharides - chemistry | Integrins - metabolism | Cell Movement - drug effects | Disaccharides - pharmacology | Soybeans - chemistry | Acetylation - drug effects | Animals | Signal Transduction - drug effects | Endothelial Cells - cytology | Lipopolysaccharides - pharmacology | Mammals - physiology | Lipopolysaccharides - chemistry | Symbiosis - drug effects | In Vitro Techniques | Aorta - physiology | Endothelial Cells - drug effects | Fibronectins | Therapeutics | Physiological aspects | Chitin | Neovascularization | Cells | Sugars | Homeopathy | Materia medica and therapeutics | Chitinase | Diabetic retinopathy | Vitronectin | Innate immunity | Biology | Kinases | Immunity | Physiological responses | Fibronectin | Mammalian cells | Plant cells | Substitutes | Proteins | Fungi | Angiogenesis | Signal transduction | Receptors | Biological effects | E coli | Agronomy | Cell adhesion | Bacteria | Physiology | Inhibition | Plant sciences | Chemical synthesis | Symbiosis | Heparan sulfate | Carbohydrates | Medical research | Legumes | Plants (botany) | Disaccharides | Blood vessels | Oligosaccharides | Nitrogen | Mammals | Gene expression | Biological activity | Endothelial cells | Medicine | Signaling | Alzheimers disease | Recognition | Chemical Sciences
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 03/2006, Volume 45, Issue 11, pp. 1778 - 1780
Sugar production: A microbiological method has been developed for the production of fucosyl α1,2‐linked carbohydrates from lactose. The syntheses of...
transferases | antigens | gene technology | biosynthesis | oligosaccharides | Antigens | Biosynthesis | Oligosaccharides | Gene technology | Transferases
transferases | antigens | gene technology | biosynthesis | oligosaccharides | Antigens | Biosynthesis | Oligosaccharides | Gene technology | Transferases
Journal Article
Carbohydrate Polymers, ISSN 0144-8617, 03/2012, Volume 88, Issue 1, pp. 185 - 193
Journal Article
ChemBioChem, ISSN 1439-4227, 01/2014, Volume 15, Issue 2, pp. 293 - 300
Journal Article
ChemBioChem, ISSN 1439-4227, 01/2014, Volume 15, Issue 2, pp. 293 - 300
We report the enzymatic synthesis of α-D-glucopyranosyl-(1→4)-α-L-rhamnopyranoside and α-D-glucopyranosyl-(1→3)-α-L-rhamnopyranoside by using a wild-type...
Carbohydrate Sequence | Biotechnology | Temperature | Biocatalysis | Enzyme Stability | Molecular Sequence Data | Shigella flexneri | Glycosylation | Haptens | Oligosaccharides | Chemical Sciences | Life Sciences | Organic chemistry | beta-Cyclodextrins | Bacillus | Glucosyltransferases | Kinetics | Catalysis
Carbohydrate Sequence | Biotechnology | Temperature | Biocatalysis | Enzyme Stability | Molecular Sequence Data | Shigella flexneri | Glycosylation | Haptens | Oligosaccharides | Chemical Sciences | Life Sciences | Organic chemistry | beta-Cyclodextrins | Bacillus | Glucosyltransferases | Kinetics | Catalysis
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2008, Volume 283, Issue 32, pp. 21853 - 21863
Restructuring the network of xyloglucan (XG) and cellulose during plant cell wall morphogenesis involves the action of xyloglucan endo -transglycosylases...
ENDOXYLOGLUCAN TRANSFERASE | SEEDS | NOMENCLATURE | ENDOTRANSGLYCOSYLASE | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT-CELL WALL | PURIFICATION | GLYCOSYL-ENZYME INTERMEDIATE | BINDING | ACCEPTOR | Electrophoresis, Capillary | Glycosyltransferases - metabolism | Populus - enzymology | Time Factors | Small Molecule Libraries - metabolism | Kinetics | Oligosaccharides - metabolism | Naphthalenes - metabolism | Binding Sites | nomenclature | endotransglycosylase | acceptor | glycosyl-enzyme intermediate | seeds | purification | endoxyloglucan | binding | transferase | mechanism | plant-cell wall
ENDOXYLOGLUCAN TRANSFERASE | SEEDS | NOMENCLATURE | ENDOTRANSGLYCOSYLASE | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT-CELL WALL | PURIFICATION | GLYCOSYL-ENZYME INTERMEDIATE | BINDING | ACCEPTOR | Electrophoresis, Capillary | Glycosyltransferases - metabolism | Populus - enzymology | Time Factors | Small Molecule Libraries - metabolism | Kinetics | Oligosaccharides - metabolism | Naphthalenes - metabolism | Binding Sites | nomenclature | endotransglycosylase | acceptor | glycosyl-enzyme intermediate | seeds | purification | endoxyloglucan | binding | transferase | mechanism | plant-cell wall
Journal Article