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Current Opinion in Chemical Biology, ISSN 1367-5931, 2008, Volume 12, Issue 5, pp. 539 - 555
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1874 - 11
Endoglycosidase S (EndoS) is a bacterial endo-beta-N-acetylglucosaminidase that specifically catalyzes the hydrolysis of the beta-1,4 linkage between the first... 
STREPTOCOCCUS-PYOGENES | BIOLOGICAL MACROMOLECULES | PROTEIN | SPECIFICITY | ACTIVE-SITE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | RESOLUTION | SUBSTRATE-ASSISTED CATALYSIS | ANTIBODY | GLYCOSYLATION | Antibodies, Monoclonal - biosynthesis | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Isoenzymes - chemistry | Trichoderma - enzymology | Vibrio cholerae - chemistry | Thermodynamics | Vibrio cholerae - enzymology | Isoenzymes - metabolism | Oligosaccharides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Glycoside Hydrolases - chemistry | Protein Interaction Domains and Motifs | Streptococcus pyogenes - chemistry | Antibodies, Monoclonal - chemistry | Carbohydrate Sequence | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Isoenzymes - genetics | Streptomyces - chemistry | Bacterial Proteins - genetics | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Oligosaccharides - metabolism | Amino Acid Motifs | Hydrolysis | Protein Conformation, beta-Strand | Escherichia coli - genetics | Streptococcus pyogenes - enzymology | Protein Binding | Bacterial Proteins - metabolism | Streptomyces - enzymology | Molecular Docking Simulation | Glycoside Hydrolases - metabolism | Kinetics | Trichoderma - chemistry | Bioengineering | N-Acetylglucosaminidase | N-Acetylglucosamine | Hydrolase | Immunoglobulin G | Grooves | Oligosaccharides | N-glycans | Antennae | Substrates | Molecular chains | Glycan | Polysaccharides | N-linked glycans | Substrate specificity | Monoclonal antibodies | Chemical synthesis | Binding sites | Glycoside hydrolase | Crystal structure
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 07/2012, Volume 134, Issue 29, pp. 12308 - 12318
Journal Article
The EMBO Journal, ISSN 0261-4189, 04/2006, Volume 25, Issue 7, pp. 1569 - 1578
O‐linked N‐acetylglucosamine (O‐GlcNAc) modification of specific serines/threonines on intracellular proteins in higher eukaryotes has been shown to directly... 
protein structure | glycosylation | O‐GlcNAc | PUGNAc | phosphorylation | Phosphorylation | Glycosylation | O-GlcNAc | Protein structure | NUCLEOCYTOPLASMIC GLYCOSYLATION | NUCLEAR | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBSTRATE-ASSISTED CATALYSIS | CELL BIOLOGY | D-GLUCOSAMINIDASE | BETA-N-ACETYLGLUCOSAMINIDASE | TYROSINE-PHOSPHATASE 1B | INSULIN-RESISTANCE | LINKED GLCNAC | CHITINASE | CYTOSOLIC PROTEINS | Histone Acetyltransferases - chemistry | Humans | Histone Acetyltransferases - genetics | Molecular Sequence Data | Multienzyme Complexes - metabolism | Substrate Specificity | Crystallography, X-Ray | beta-N-Acetylhexosaminidases - chemistry | Acetylglucosaminidase - genetics | Acetylglucosamine - metabolism | Acetylglucosaminidase - metabolism | Histone Acetyltransferases - metabolism | Acetylglucosamine - analogs & derivatives | Catalysis | Binding Sites | Amino Acid Sequence | Clostridium perfringens - enzymology | Phenylcarbamates - chemistry | Models, Molecular | Multienzyme Complexes - genetics | Acetylglucosamine - chemistry | Multienzyme Complexes - chemistry | Hydrolysis | Oximes - chemistry | Sequence Homology, Amino Acid | Animals | Acetylglucosaminidase - chemistry | Protein Conformation | Mice | Mutation | Streptozocin - chemistry | 3T3 Cells | Proteins | Enzymes | Eukaryotes | Molecular biology | Crystal structure
Journal Article
New Phytologist, ISSN 0028-646X, 12/2012, Volume 196, Issue 4, pp. 1122 - 1132
Journal Article
Molecular Oral Microbiology, ISSN 2041-1006, 08/2012, Volume 27, Issue 4, pp. 221 - 245
Summary Surface‐exposed proteins of pathogenic bacteria are considered as potential virulence factors through their direct contribution to host–pathogen... 
non‐classical surface proteins | three‐dimensional structure | choline‐binding proteins | surface proteins | LPXTG proteins | lipoproteins | Streptococcus pneumoniae | Lipoproteins | Three-dimensional structure | Non-classical surface proteins | Surface proteins | Choline-binding proteins | ACID PHOSPHORYLCHOLINE ESTERASE | TEICHOIC-ACID | non-classical surface proteins | BACTERIUM STREPTOCOCCUS-PNEUMONIAE | IMMUNOGLOBULIN RECEPTOR HPIGR | VIRULENCE FACTOR | MICROBIOLOGY | choline-binding proteins | BETA-N-ACETYLGLUCOSAMINIDASE | CHOLINE-BINDING-PROTEIN | STRUCTURAL BASIS | three-dimensional structure | DENTISTRY, ORAL SURGERY & MEDICINE | RAY DIFFRACTION ANALYSIS | PNEUMONIAE HYALURONATE LYASE | Adhesins, Bacterial - chemistry | Phosphogluconate Dehydrogenase - chemistry | Bacterial Proteins - chemistry | Lipoproteins - chemistry | Virulence Factors | Host-Pathogen Interactions | Endopeptidases - chemistry | Phosphoglycerate Kinase - chemistry | Streptococcus pneumoniae - chemistry | Membrane Proteins - chemistry | Phosphopyruvate Hydratase - chemistry | Protein Conformation | Serine Proteases - chemistry | Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) - chemistry | Streptococcus pneumoniae - physiology | Pathogens | Protein sorting signals | Lipoteichoic acid | Gram-positive bacteria | Cell surface | Teichoic acids | virulence factors | Host-pathogen interactions | Infection | Choline-binding protein | Antibiotics | Choline | Evolution | Cell envelopes
Journal Article