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Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14401 - 14412
Clostridium difficile is a clinically significant pathogen that causes mild-to-severe (and often recurrent) colon infections. Disease symptoms stem from the... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Epitope Mapping | Glucosyltransferases - toxicity | Enterotoxins - toxicity | Enterocytes - metabolism | Peptide Fragments - toxicity | Humans | Antibodies, Neutralizing - metabolism | Bacterial Proteins - chemistry | Bacterial Toxins - toxicity | Crystallography, X-Ray | Glucosyltransferases - metabolism | Repetitive Sequences, Amino Acid | Bacterial Proteins - toxicity | Immunoglobulin Fab Fragments - metabolism | Anti-Bacterial Agents - chemistry | Clostridium difficile - enzymology | Conserved Sequence | Bacterial Toxins - genetics | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Glucosyltransferases - genetics | Caco-2 Cells | Recombinant Proteins - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Bacterial Proteins - genetics | Antibodies, Monoclonal, Humanized - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Anti-Bacterial Agents - metabolism | Bacterial Toxins - chemistry | Bacterial Toxins - metabolism | Enterotoxins - genetics | Peptide Fragments - chemistry | Enterocytes - drug effects | Antibodies, Neutralizing - chemistry | Immunoglobulin Fab Fragments - chemistry | Glucosyltransferases - chemistry | Enterotoxins - metabolism | Recombinant Proteins - toxicity | Bacterial Proteins - metabolism | Protein Conformation | Enterotoxins - chemistry | Binding Sites, Antibody | Antibodies, Monoclonal, Humanized - chemistry | Index Medicus | BASIC BIOLOGICAL SCIENCES | SEC-MALS | Clostridium difficile | crystal structure | cell surface receptor | monoclonal antibody | bacterial toxin | electron microscopy (EM) | Microbiology
Journal Article
The FEBS journal, ISSN 1742-464X, 02/2014, Volume 281, Issue 3, pp. 778 - 786
Glycoside hydrolase (GH) family 65 contains phosphorylases acting on maltose (Glc‐α1,4‐Glc), kojibiose (Glc‐α1,2‐Glc), trehalose (Glc‐α1,α1,‐Glc), and nigerose... 
maltose phosphorylase | structure–function relationships | enzyme–substrate interactions | substrate specificity | oligosaccharide synthesis | Oligosaccharide synthesis | Maltose phosphorylase | Substrate specificity | Enzyme-substrate interactions | Structure-function relationships | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Threonine - chemistry | Disaccharides - metabolism | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Phosphates - chemistry | Substrate Specificity | Tryptophan - chemistry | Disaccharides - chemistry | Glucosyltransferases - metabolism | X-Ray Diffraction | Sulfates - chemistry | Glycoside Hydrolases - chemistry | Glucosyltransferases - genetics | Recombinant Proteins - metabolism | Catalytic Domain | Mutagenesis, Site-Directed | Sulfates - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Phosphates - metabolism | Thermoanaerobacter - enzymology | Mutant Proteins - chemistry | Glucose - chemistry | Glucosyltransferases - chemistry | Glucose - metabolism | Bacterial Proteins - metabolism | Protein Conformation | Glycoside Hydrolases - metabolism | Amino Acid Substitution | Glutamic Acid - chemistry | Phosphates | Glucose metabolism | Enzymes | Analysis | Crystals | Hydrolases | Genetic aspects | Glucose | Structure | Sulfates | Sugars | Dextrose | Mutation | Molecular biology | Substrates | Crystal structure | Index Medicus
Journal Article
Biochimica et biophysica acta. Proteins and proteomics, ISSN 1570-9639, 09/2014, Volume 1844, Issue 9, pp. 1619 - 1630
Escherichia coli C-glycosyltransferase IroB catalyzes the formation of a CC bond between enterobactin and the glucose moiety of UDP-glucose, resulting in the... 
Enterobactin | Siderophore | Salmochelin | Glycosyltransferase | UDP-glucose | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Molecular Sequence Data | Tryptophan - chemistry | Tryptophan - metabolism | Uropathogenic Escherichia coli - chemistry | Glucosyltransferases - metabolism | Enterobactin - chemistry | Enterobactin - metabolism | Glucosyltransferases - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Biocatalysis | Protein Structure, Secondary | Siderophores - metabolism | Uridine Diphosphate Glucose - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Glycosylation | Recombinant Proteins - genetics | Siderophores - chemistry | Sequence Alignment | Glucosyltransferases - chemistry | Escherichia coli Proteins - genetics | Protein Binding | Aspartic Acid - metabolism | Glutamic Acid - metabolism | Structural Homology, Protein | Aspartic Acid - chemistry | Escherichia coli Proteins - chemistry | Uropathogenic Escherichia coli - enzymology | Uridine Diphosphate Glucose - metabolism | Amino Acid Substitution | Glutamic Acid - chemistry | Glucose metabolism | Analysis | Transferases | Escherichia coli | Cellulose | Glucose | Catalysis | Dextrose
Journal Article
Molecular biology of the cell, ISSN 1059-1524, 11/2014, Volume 25, Issue 22, pp. 3630 - 3642
Journal Article