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Chemical Communications, ISSN 1359-7345, 10/2013, Volume 49, Issue 77, pp. 8629 - 8631
In this study, we developed a one-pot one-step deracemization method for the production of various enantiomerically pure amines using two opposite... 
Comamonadaceae - enzymology | Vibrio - enzymology | Stereoisomerism | Transaminases - metabolism | Neosartorya - enzymology | Phenethylamines - chemistry | Phenethylamines - metabolism | Bacteria - enzymology | Mycobacterium - enzymology | Index Medicus
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 04/2016, Volume 12, Issue 4, pp. 268 - 274
Activity-based protein profiling (ABPP) is a chemoproteomic tool for detecting active enzymes in complex biological systems. We used ABPP to identify secreted... 
SERINE HYDROLASE ACTIVITIES | PROTEIN | INTELECTIN-1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | GALACTOFURANOSE | SUPERFAMILY | MECHANISMS | PROTEOMIC ANALYSIS | IDENTIFICATION | VIBRIO-CHOLERAE | DISCOVERY | Proteins | Enzymes | Pathogens | Cholera | Proteases | Index Medicus
Journal Article
PLoS Computational Biology, ISSN 1553-734X, 12/2010, Volume 6, Issue 12, pp. e1001029 - e1001029
Chelt, a cholera-like toxin from Vibrio cholerae, and Certhrax, an anthrax-like toxin from Bacillus cereus, are among six new bacterial protein toxins we... 
STRUCTURAL BASIS | PERFRINGENS IOTA-TOXIN | CRYSTAL-STRUCTURE | BIOCHEMICAL RESEARCH METHODS | MATHEMATICAL & COMPUTATIONAL BIOLOGY | MULTIPLE SEQUENCE ALIGNMENTS | ENTEROCOCCUS-FAECALIS | RIBOSYLATING BACTERIAL TOXINS | BACILLUS-CEREUS | PHOTORHABDUS-LUMINESCENS | SACCHAROMYCES-CEREVISIAE | PROTEIN-STRUCTURE PREDICTION | Bacillus cereus - pathogenicity | Vibrio - chemistry | Vibrio cholerae - pathogenicity | Bacterial Proteins - chemistry | Molecular Sequence Data | Data Mining | Mycobacterium avium - chemistry | Structure-Activity Relationship | Bacillus cereus - enzymology | Phylogeny | Vibrio cholerae - chemistry | Vibrio cholerae - enzymology | Mycobacterium avium - pathogenicity | Photorhabdus - pathogenicity | ADP Ribose Transferases - chemistry | ADP Ribose Transferases - metabolism | Enterococcus faecalis - enzymology | Amino Acid Sequence | Enterococcus faecalis - pathogenicity | Reproducibility of Results | Enterococcus faecalis - chemistry | Computational Biology | Models, Molecular | Sequence Analysis, DNA | Bacterial Toxins - chemistry | Photorhabdus - chemistry | Bacterial Toxins - metabolism | Mycobacterium avium - enzymology | Sequence Alignment | Vibrio - enzymology | Bacillus cereus - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Vibrio - pathogenicity | Photorhabdus - enzymology | Bacterial proteins | Transferases | Physiological aspects | Adenosine diphosphate | Cholera toxin | Research | Health aspects | Index Medicus | Proteins | Medical research | Enzymes | Toxins | Microbiology
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2010, Volume 400, Issue 3, pp. 335 - 353
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 | ANTIBODY-BASED THERAPEUTICS | BIOLOGICAL MACROMOLECULES | PROTEIN | ACTIVE-SITE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | HUMAN-IGG | SUBSTRATE-ASSISTED CATALYSIS | RAY SOLUTION SCATTERING | GLYCOSYL HYDROLASES | 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 | Index Medicus
Journal Article
Glycobiology, ISSN 0959-6658, 08/2016, Volume 26, Issue 8, pp. 834 - 849
Neuraminidase-1 ( NEU1) is the predominant sialidase expressed in human airway epithelia and lung microvascular endothelia where it mediates multiple... 
lung | sialidase | PPCA | neuraminidase | NEU1 | MOLECULAR-BIOLOGY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE | NEU1 SIALIDASE | LYSOSOMAL SIALIDASE | MATRIX-METALLOPROTEINASE-9 CROSS-TALK | VIBRIO-CHOLERAE NEURAMINIDASE | MICROVASCULAR ENDOTHELIA | ELASTIN RECEPTOR | SELECTIVE INHIBITORS | Endothelium, Vascular - cytology | Fibroblasts - enzymology | Epithelial Cells - drug effects | Humans | Neuraminidase - genetics | Endothelium, Vascular - drug effects | Endothelium, Vascular - enzymology | Lung - cytology | Lung - enzymology | Flagellin - pharmacology | Cathepsin A - genetics | Isoenzymes - metabolism | Mucin-1 - chemistry | Cathepsin A - metabolism | Protein Domains | Protein Interaction Domains and Motifs | Epithelial Cells - cytology | Protein Conformation, alpha-Helical | Mucin-1 - metabolism | Isoenzymes - genetics | N-Acetylneuraminic Acid - pharmacology | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Gene Expression Regulation | Models, Molecular | Neuraminidase - metabolism | Hydrolysis | N-Acetylneuraminic Acid - chemistry | Cell Movement - drug effects | Pseudomonas aeruginosa - chemistry | Animals | Protein Conformation, beta-Strand | Endothelial Cells - cytology | Fibroblasts - drug effects | Lung - drug effects | Epithelial Cells - enzymology | Flagellin - antagonists & inhibitors | Protein Binding | Bacterial Proteins - metabolism | N-Acetylneuraminic Acid - analogs & derivatives | Neuraminidase - antagonists & inhibitors | Fibroblasts - cytology | Mice | Endothelial Cells - enzymology | Isoenzymes - antagonists & inhibitors | Endothelial Cells - drug effects | Mucin-1 - genetics | Index Medicus | Original articles
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2011, Volume 286, Issue 52, pp. 44344 - 44349
Journal Article