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index medicus (214) 214
biochemistry & molecular biology (205) 205
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enzyme inhibitors - pharmacology (148) 148
glycosyltransferases (142) 142
glycosyltransferase (122) 122
glycosyltransferases - antagonists & inhibitors (120) 120
glycosyltransferases - metabolism (109) 109
enzyme inhibitors - chemistry (94) 94
glycosylation (93) 93
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analysis (57) 57
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physiological aspects (49) 49
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article (37) 37
binding sites (37) 37
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crystal-structure (35) 35
proteins (35) 35
drug design (34) 34
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escherichia coli - enzymology (32) 32
chemistry, multidisciplinary (30) 30
gene expression (30) 30
amino acid sequence (29) 29
analogs (29) 29
glycoside hydrolases - antagonists & inhibitors (29) 29
microbial sensitivity tests (29) 29
microbiology (29) 29
bacterial proteins - metabolism (28) 28
protein binding (28) 28
anti-bacterial agents - chemistry (27) 27
binding (27) 27
inhibitor (27) 27
catalysis (26) 26
membrane proteins (26) 26
n-acetylglucosaminyltransferases - antagonists & inhibitors (26) 26
oligosaccharides (26) 26
pharmacology & pharmacy (26) 26
galactosyltransferases - antagonists & inhibitors (24) 24
rats (24) 24
antibiotics (23) 23
base sequence (23) 23
gene (23) 23
glucosyltransferases - antagonists & inhibitors (23) 23
n-acetylglucosaminyltransferases - metabolism (23) 23
oligosaccharides - chemistry (23) 23
life sciences (22) 22
magnetic resonance spectroscopy (22) 22
penicillin-binding proteins (22) 22
cell line (21) 21
ligands (21) 21
male (21) 21
mechanism (21) 21
peptidoglycan glycosyltransferase - antagonists & inhibitors (21) 21
signal transduction (21) 21
bacterial proteins - antagonists & inhibitors (20) 20
biochemistry, general (20) 20
cells (20) 20
complex (20) 20
cricetinae (20) 20
enzyme inhibitors - metabolism (20) 20
fucosyltransferases - antagonists & inhibitors (20) 20
galactosyltransferases - metabolism (20) 20
glycosyltransferase inhibitors (20) 20
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multidisciplinary sciences (20) 20
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escherichia coli - drug effects (19) 19
molecular biology (19) 19
biochemistry (18) 18
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chemistry, applied (18) 18
cho cells (18) 18
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1. Full Text A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases in Bacillus subtilis
by Hill, Norbert S and Zuke, Jason D and Buske, P.J and Chien, An-Chun and Levin, Petra Anne
BMC Microbiology, ISSN 1471-2180, 04/2018, Volume 18, Issue 1, pp. 1 - 14
Background: Changes in nutrient availability have dramatic and well-defined impacts on both transcription and translation in bacterial cells. At the same time,... 
Cell division | ClpP | Cell size | UgtP | Cell cycle | UDP-glucose | LIPOTEICHOIC ACID | ESCHERICHIA-COLI | GROWTH-RATE | CELL-SIZE | MICROBIOLOGY | PROTEOLYSIS | CHAPERONE ACTIVITY | IRON HOMEOSTASIS | MEMBRANE-DERIVED OLIGOSACCHARIDES | TRANSCRIPTION FACTOR | ADAPTER PROTEIN | Gene mutations | Bacillus subtilis | Proteases | Analysis | Glycosyltransferases | Research
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2. Full Text Regulation of the Peptidoglycan Polymerase Activity of PBP1b by Antagonist Actions of the Core Divisome Proteins FtsBLQ and FtsN
by Boes, Aien and Olatunji, Samir and Breukink, Eefjan and Terrak, Mohammed
mBio, ISSN 2161-2129, 01/2019, Volume 10, Issue 1, p. e01912-18
Peptidoglycan (PG) is an essential constituent of the bacterial cell wall. During cell division, PG synthesis localizes at midcell under the control of a... 
FtsN | divisome | peptidoglycan | FtsBLQ | PBP1b | lipid II | Peptidoglycan | Lipid II | Divisome | LOCALIZATION | COMPLEX | ESCHERICHIA-COLI | MICROBIOLOGY | GLYCOSYLTRANSFERASE ACTIVITY | CYTOKINETIC RING | TRANSPEPTIDASE | CONSTRICTION | CELL-DIVISION PROTEIN | DOMAINS | PENICILLIN-BINDING PROTEIN-1A
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3. Full Text Crystal Structure of the Membrane-Bound Bifunctional Transglycosylase PBP1b from Escherichia Coli
by Ming-Ta Sung and Yen-Ting Lai and Chia-Ying Huang and Lien-Yang Chou and Hao-Wei Shih and Wei-Chieh Cheng and Chi-Huey Wong and Che Ma
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2009, Volume 106, Issue 22, pp. 8824 - 8829
Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a... 
Proteins | Antibiotics | Molecular structure | Cell walls | Drug interactions | Escherichia coli | Crystals | Lipids | Bacteria | Crystal structure | Peptidoglycan synthesis | Membrane protein structure | Protein-protein interaction | Antibacterial development | Antibiotic resistance | ANTIBIOTICS | DESIGN | DOMAIN | LYTIC TRANSGLYCOSYLASE | PROTEIN-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MODEL | membrane protein structure | antibacterial development | REPAIR | antibiotic resistance | MOENOMYCIN | protein-protein interaction | BINDING | CELL-WALL PEPTIDOGLYCAN | peptidoglycan synthesis | Amino Acid Sequence | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - chemistry | Molecular Sequence Data | Crystallography, X-Ray | Serine-Type D-Ala-D-Ala Carboxypeptidase - chemistry | Penicillin-Binding Proteins - chemistry | Serine-Type D-Ala-D-Ala Carboxypeptidase - antagonists & inhibitors | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Protein Conformation | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Escherichia coli Proteins - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Escherichia coli Proteins - chemistry | Physiological aspects | Properties | Bacterial proteins | Membrane proteins | Ionizing radiation | Enzymatic activity | Drug resistance | Protein interaction | Antibacterial agents | penicillin-binding protein 1b | moenomycin | Biological Sciences | Physical Sciences | protein–protein interaction
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4. Full Text Multivalent inhibitors for carbohydrate-processing enzymes: Beyond the "lock-and-key" concept
by Gouin, Sébastien G
Chemistry - A European Journal, ISSN 0947-6539, 09/2014, Volume 20, Issue 37, pp. 11616 - 11628
During the last decades, tremendous chemical efforts have been dedicated to design monovalent inhibitors of carbohydrate-processing enzymes, with comparatively... 
carbohydrates | inhibitors | enzymes | drug design | GLYCOCLUSTERS | GLYCOGEN-PHOSPHORYLASE | PHARMACOLOGICAL CHAPERONES | ESCHERICHIA-COLI | INFLUENZA-VIRUS NEURAMINIDASE | CHEMISTRY, MULTIDISCIPLINARY | IMINOSUGAR CLICK CLUSTERS | GLYCOSIDASE INHIBITION | LIGANDS | HIGHLY POTENT | BINDING | Humans | alpha-Mannosidase - chemistry | alpha-Mannosidase - metabolism | Carbohydrate Metabolism | Enzyme Inhibitors - pharmacology | alpha-Mannosidase - antagonists & inhibitors | Models, Molecular | Neuraminidase - metabolism | Structure-Activity Relationship | Animals | Carbohydrates - chemistry | Enzyme Inhibitors - chemistry | Drug Design | Neuraminidase - chemistry | Glycoside Hydrolases - chemistry | Neuraminidase - antagonists & inhibitors | Glycoside Hydrolases - metabolism | Glycoside Hydrolases - antagonists & inhibitors | Lectins | Enzymes | Drugs | Carbohydrates | Inhibitors | Glycosidases | Strategy | Inhibition
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5. Full Text Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome
by Rillahan, Cory D and Antonopoulos, Aristotelis and Lefort, Craig T and Sonon, Roberto and Azadi, Parastoo and Ley, Klaus and Dell, Anne and Haslam, Stuart M and Paulson, James C
Nature Chemical Biology, ISSN 1552-4450, 2012, Volume 8, Issue 7, pp. 661 - 668
Despite the fundamental roles of sialyl- and fucosyltransferases in mammalian physiology, there are few pharmacological tools to manipulate their function in a... 
CELLS | GDP-MANNOSE | ACID | CHEMOENZYMATIC SYNTHESIS | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | E-SELECTIN | ATHEROSCLEROSIS | GLYCOSYLATION | GLYCOSYLTRANSFERASES | SIALYLTRANSFERASE | Fucose - metabolism | Fucosyltransferases - antagonists & inhibitors | Sialyltransferases - antagonists & inhibitors | Carbohydrate Metabolism | Enzyme Inhibitors - pharmacology | Enzymes | Leucocytes | Pharmacology | Cellular biology | Metabolism
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6. Full Text Structure–Activity Relationships of Novel Tryptamine-Based Inhibitors of Bacterial Transglycosylase
by Sosič, Izidor and Anderluh, Marko and Sova, Matej and Gobec, Martina and Mlinarič Raščan, Irena and Derouaux, Adeline and Amoroso, Ana and Terrak, Mohammed and Breukink, Eefjan and Gobec, Stanislav
Journal of Medicinal Chemistry, ISSN 0022-2623, 12/2015, Volume 58, Issue 24, pp. 9712 - 9721
Penicillin-binding proteins represent well-established, validated, and still very promising targets for the design and development of new antibacterial agents.... 
NISIN | TARGET | ANTIBIOTICS | CHEMISTRY, MEDICINAL | PEPTIDOGLYCAN BIOSYNTHESIS | MEMBRANE | COLI | LIPID-II | PENICILLIN-BINDING PROTEINS | DISCOVERY | Tryptamines - chemistry | Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives | Enterococcus faecium - drug effects | Tryptamines - toxicity | Escherichia coli - drug effects | Humans | Structure-Activity Relationship | Microbial Sensitivity Tests | Uridine Diphosphate N-Acetylmuramic Acid - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - antagonists & inhibitors | Tryptamines - pharmacology | Anti-Bacterial Agents - chemistry | HEK293 Cells | Protein Binding | Anti-Bacterial Agents - pharmacology | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Anti-Bacterial Agents - toxicity | Escherichia coli Proteins - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Methicillin Resistance | Staphylococcus aureus - drug effects
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7. Full Text The Stories Tryptophans Tell: Exploring Protein Dynamics of Heptosyltransferase I from Escherichia coli
by Cote, Joy M and Ramirez-Mondragon, Carlos A and Siegel, Zarek S and Czyzyk, Daniel J and Gao, Jiali and Sham, Yuk Y and Mukerji, Ishita and Taylor, Erika A
Biochemistry, ISSN 0006-2960, 02/2017, Volume 56, Issue 6, pp. 886 - 895
Heptosyltransferase I (HepI) catalyzes the addition of l-glycero-β-d-manno-heptose to Kdo2-Lipid A, as part of the biosynthesis of the core region of... 
LIPOPOLYSACCHARIDE BIOSYNTHESIS | FLUORESCENCE SPECTROSCOPY | CIRCULAR-DICHROISM | CONFORMATIONAL-CHANGES | ENZYME | WAAC | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | INHIBITORS | GLYCOSYLTRANSFERASES | Solvents - chemistry | Tryptophan - chemistry | Surface Properties | Apoenzymes - metabolism | Escherichia coli Proteins - antagonists & inhibitors | Glycosyltransferases - genetics | Binding Sites | Circular Dichroism | Lipid A - chemistry | Apoenzymes - antagonists & inhibitors | Acylation | Recombinant Proteins - metabolism | Biocatalysis | Escherichia coli - enzymology | Mutagenesis, Site-Directed | Lipid A - metabolism | Glycosyltransferases - chemistry | Enzyme Stability | Solubility | Models, Molecular | Recombinant Proteins - chemistry | Spectrometry, Fluorescence | Escherichia coli Proteins - metabolism | Molecular Dynamics Simulation | Glycosyltransferases - metabolism | Apoenzymes - genetics | Apoenzymes - chemistry | Escherichia coli Proteins - genetics | Protein Conformation | Mutation | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Glycosyltransferases - antagonists & inhibitors | Proteins | Usage | Escherichia coli | Analysis | Fluorescence | Molecular dynamics | Catalysis | Research | Circular dichroism | Index Medicus | structural rearrangement | GT-B | glycosyltransferase | protein dynamics | circular dichroism | Heptosyltransferase | tryptophan fluorescence
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8. Full Text Glycosyltransferases and glycosaminoglycans in bleomycin and transforming growth factor-β1-induced pulmonary fibrosis
by Venkatesan, Narayanan and Tsuchiya, Kimitake and Kolb, Martin and Farkas, Laszlo and Bourhim, Mustapha and Ouzzine, Mohamed and Ludwig, Mara S
American Journal of Respiratory Cell and Molecular Biology, ISSN 1044-1549, 2014, Volume 50, Issue 3, pp. 583 - 594
Glycosaminoglycan (GAG) chains of proteoglycans (PGs) play important roles in fibrosis through cell-matrix interactions and growth factor binding in the... 
Fibroblasts | Bleomycin | Glycosaminoglycans | Proteoglycans | Up-Regulation | Fibroblasts - enzymology | Chondroitin Sulfates - metabolism | Transforming Growth Factor beta1 - antagonists & inhibitors | Transforming Growth Factor beta1 - metabolism | Male | Pulmonary Fibrosis - genetics | Pentosyltransferases - metabolism | RNA, Messenger - metabolism | Lung - enzymology | Transfection | Time Factors | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Sulfotransferases - metabolism | p38 Mitogen-Activated Protein Kinases - metabolism | Glycosyltransferases - genetics | Glycosaminoglycans - genetics | Protein-Serine-Threonine Kinases - metabolism | Disease Models, Animal | Lung - pathology | Signal Transduction | Glycosaminoglycans - metabolism | Cells, Cultured | Rats | Antibodies, Neutralizing - pharmacology | Pulmonary Fibrosis - pathology | Transforming Growth Factor beta1 - genetics | Fibroblasts - pathology | Rats, Sprague-Dawley | Gene Expression Regulation, Enzymologic | Glycosyltransferases - metabolism | Animals | Receptors, Transforming Growth Factor beta - antagonists & inhibitors | Glucuronosyltransferase - metabolism | Receptors, Transforming Growth Factor beta - metabolism | Lung - drug effects | Pulmonary Fibrosis - enzymology | p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors | Pulmonary Fibrosis - prevention & control | Pulmonary Fibrosis - chemically induced | Protein Kinase Inhibitors - pharmacology | Versicans - metabolism
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9. Full Text An Efficient Approach to the Discovery of Potent Inhibitors against Glycosyltransferases
by Hosoguchi, Kensaku and Maeda, Takahiro and Furukawa, Jun-ichi and Shinohara, Yasuro and Hinou, Hiroshi and Sekiguchi, Mitsuaki and Togame, Hiroko and Takemoto, Hiroshi and Kondo, Hirosato and Nishimura, Shin-Ichiro
Journal of Medicinal Chemistry, ISSN 0022-2623, 08/2010, Volume 53, Issue 15, pp. 5607 - 5619
We describe a standardized approach for searching potent and selective inhibitors of glycosyltransferases by high throughput quantitative MALDI-TOFMS-based... 
CAMPYLOBACTER-JEJUNI | CHEMISTRY, MEDICINAL | FUCOSYL-TRANSFERASE | HUMAN ALPHA-1,3-FUCOSYL-TRANSFERASE | CLICK CHEMISTRY | STRUCTURAL-ANALYSIS | TERMINAL ALKYNES | DONOR ANALOGS | SUBSTRATE-ANALOG | SIALYLTRANSFERASE INHIBITORS | RATIONAL DESIGN | Alkynes - chemical synthesis | Recombinant Proteins - antagonists & inhibitors | Fucosyltransferases - chemistry | Fucosyltransferases - antagonists & inhibitors | Humans | Glycopeptides - chemistry | Rats | Recombinant Proteins - chemistry | Alkynes - chemistry | Structure-Activity Relationship | Azides - chemistry | Nucleotides - chemistry | Oligosaccharides - chemical synthesis | Glycopeptides - chemical synthesis | Animals | Oligosaccharides - chemistry | Sialyltransferases - antagonists & inhibitors | Sialyltransferases - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Nucleotides - chemical synthesis | Azides - chemical synthesis | Databases, Factual | Glycosyltransferases - antagonists & inhibitors
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10. Full Text Methicillin resistance in Staphylococcus aureus requires glycosylated wall teichoic acids
by Stephanie Brown and Guoqing Xia and Lyly G. Luhachack and Jennifer Campbell and Timothy C. Meredith and Calvin Chen and Volker Winstel and Cordula Gekeler and Javier E. Irazoqui and Andreas Peschel and Suzanne Walker
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2012, Volume 109, Issue 46, pp. 18909 - 18914
Staphylococcus aureus peptidoglycan (PG) is densely functionalized with anionic polymers called wall teichoic acids (WTAs). These polymers contain three... 
Bacteriophages | Phenotypes | Antibiotics | Cell division | Infections | Polymers | Staphylococcus aureus | Teichoic acids | Tailoring | Sugars | Murein | PBP2A | Beta lactam potentiation | Antibiotic resistance | WTA glycosylation | LIPOTEICHOIC ACID | murein | MULTIDISCIPLINARY SCIENCES | ENZYMATIC-SYNTHESIS | beta lactam potentiation | CELL-WALL | PEPTIDOGLYCAN | GENE | antibiotic resistance | BACILLUS-SUBTILIS | BIOSYNTHESIS | N-ACETYLGLUCOSAMINYLRIBITOL LINKAGES | BETA-LACTAM ANTIBIOTICS | D-ALANINE | Methicillin Resistance - physiology | Bacterial Proteins - antagonists & inhibitors | Teichoic Acids - genetics | Humans | Bacterial Proteins - genetics | Cell Wall - genetics | Glycosylation | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Animals | Cell Wall - metabolism | Gene Deletion | Teichoic Acids - metabolism | Bacterial Proteins - metabolism | Glycosyltransferases - genetics | Methicillin-Resistant Staphylococcus aureus - enzymology | Methicillin-Resistant Staphylococcus aureus - genetics | Glycosyltransferases - antagonists & inhibitors | Methicillin | Physiological aspects | Drug resistance in microorganisms | Health aspects | Biological Sciences
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11. Full Text High-Throughput Screen for Inhibitors of Transglycosylase and/or Transpeptidase Activities of Escherichia coli Penicillin Binding Protein 1b
by B. Chandrakala and Radha K. Shandil and Upasana Mehra and Sudha Ravishankar and Parvinder Kaur and Veeraraghavan Usha and Bina Joe and Sunita M. deSousa
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 01/2004, Volume 48, Issue 1, pp. 30 - 40
Classifications Services AAC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... 
SCINTILLATION PROXIMITY ASSAY | MEMBRANE-ASSOCIATED STEPS | K-12 | ACETYLMURAMYL-PENTAPEPTIDE | BIOSYNTHESIS | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | POLYMERIZATION | RESISTANT STAPHYLOCOCCUS-AUREUS | D-ALANINE CARBOXYPEPTIDASE | BACTERIAL PEPTIDOGLYCAN | CELL-WALL PEPTIDOGLYCAN | Escherichia coli - drug effects | Hexosyltransferases - metabolism | Muramoylpentapeptide Carboxypeptidase - metabolism | Penicillin-Binding Proteins | Ristocetin - pharmacology | Vancomycin - pharmacology | Wheat Germ Agglutinins | Transferases - antagonists & inhibitors | Muramoylpentapeptide Carboxypeptidase - antagonists & inhibitors | Peptidyl Transferases - antagonists & inhibitors | Bacterial Proteins - antagonists & inhibitors | Detergents - pharmacology | Drug Evaluation, Preclinical - methods | Bacterial Outer Membrane Proteins | Peptidyl Transferases - metabolism | Escherichia coli - enzymology | Carrier Proteins - antagonists & inhibitors | Enzyme Inhibitors - pharmacology | Hexosyltransferases - antagonists & inhibitors | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | Carrier Proteins - metabolism | N-Acetylglucosaminyltransferases - antagonists & inhibitors | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Glycosyltransferases - antagonists & inhibitors | Mechanisms of Action | Physiological Effects
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12. Full Text Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition
by Sarkar, Sujoy K and Dutta, Mouparna and Kumar, Akash and Mallik, Dhriti and Ghosh, Anindya S
PloS one, ISSN 1932-6203, 2012, Volume 7, Issue 11, p. e48598
The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the... 
SHIGELLA | SHAPE | SCREEN | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | RESISTANCE | LYSIS | TRANSPEPTIDASE | PENICILLIN-BINDING PROTEIN-1A | DELETION | Cefsulodin - pharmacology | Peptidoglycan Glycosyltransferase - metabolism | O Antigens - metabolism | Escherichia coli - drug effects | Humans | Escherichia coli - immunology | Fluorescence | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - metabolism | Mutation - genetics | Microbial Sensitivity Tests | Serine-Type D-Ala-D-Ala Carboxypeptidase - antagonists & inhibitors | Time Factors | Escherichia coli - isolation & purification | Gene Deletion | Anti-Bacterial Agents - pharmacology | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Drug Resistance, Bacterial - drug effects | Escherichia coli Proteins - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | beta-Lactamases - metabolism | Drug Evaluation, Preclinical | Sensitizing | Salmonella | Antigens | Biotechnology | Penicillin-binding protein | Laboratories | Clinical isolates | Amides | Cefsulodin | Gene deletion | Drug resistance | Pbp1b gene | Proteins | Clonal deletion | Antibiotics | E coli | Plasmids | Penicillin | Cell cycle | Deletion | Bacteria | Inhibition
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13. Full Text Chemical Approaches To Perturb, Profile, and Perceive Glycans
by Agard, Nicholas J and Bertozzi, Carolyn R
Accounts of Chemical Research, ISSN 0001-4842, 06/2009, Volume 42, Issue 6, pp. 788 - 797
Glycosylation is an essential form of post-translational modification that regulates intracellular and extracellular processes. Regrettably, conventional... 
N-ACETYLGLUCOSAMINE | LECTIN MICROARRAY | O-LINKED GLYCOSYLATION | IN-VIVO | GLCNAC-MODIFIED PROTEINS | COPPER-FREE | FREE CLICK CHEMISTRY | SIALYL-LEWIS-X | CHEMISTRY, MULTIDISCIPLINARY | SMALL-MOLECULE SWITCH | MASS-SPECTROMETRY | Glycosyltransferases - metabolism | Protein Engineering | Polysaccharides - chemistry | Glycosylation | Glycoside Hydrolases - metabolism | Green Fluorescent Proteins - chemistry | Glycoside Hydrolases - antagonists & inhibitors | Glycosyltransferases - antagonists & inhibitors | Polysaccharides - metabolism | Chemical properties | Nucleic acids | Analysis | Green fluorescent protein
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14. Full Text Chemical Glycobiology
by Carolyn R. Bertozzi and Laura L. Kiessling
Science, ISSN 0036-8075, 3/2001, Volume 291, Issue 5512, pp. 2357 - 2364
Chemical tools have proven indispensable for studies in glycobiology. Synthetic oligosaccharides and glycoconjugates provide materials for correlating... 
Enzymes | Carbohydrates | Polysaccharides | Reviews | Glycoconjugates | Ligands | Glycoproteins | Biosynthesis | Biochemistry | Oligosaccharides | Sugars | DESIGN | ACID | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | OLIGOSACCHARIDE SYNTHESIS | LIGATION | ACYL SIDE-CHAIN | INHIBITORS | GLYCOPROTEIN | SELECTIN-CARBOHYDRATE INTERACTIONS | SIALYL-LEWIS-X | Humans | Enzyme Inhibitors - pharmacology | Glycoproteins - metabolism | Glycosylation | Oligosaccharides - metabolism | Polysaccharides - metabolism | Oligosaccharides - chemical synthesis | Glycosyltransferases - metabolism | Animals | Oligosaccharides - chemistry | Polysaccharides - chemistry | Cell Membrane - metabolism | Glycoside Hydrolases - metabolism | Glycoproteins - chemistry | Binding Sites | Glycoside Hydrolases - antagonists & inhibitors | Glycoproteins - chemical synthesis | Glycosyltransferases - antagonists & inhibitors | Molecular structure | Research | Chemical processes | Methods | Molecules | Chemistry | Sugar | Cells
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15. Full Text Iminosugar C‑Glycoside Analogues of α‑d‑GlcNAc-1-Phosphate: Synthesis and Bacterial Transglycosylase Inhibition
by Hsu, Che-Hsiung and Schelwies, Mathias and Enck, Sebastian and Huang, Lin-Ya and Huang, Shih-Hsien and Chang, Yi-Fan and Cheng, Ting-Jen Rachel and Cheng, Wei-Chieh and Wong, Chi-Huey
The Journal of Organic Chemistry, ISSN 0022-3263, 09/2014, Volume 79, Issue 18, pp. 8629 - 8637
We herein describe the first synthesis of iminosugar C-glycosides of α-d-GlcNAc-1-phosphate in 10 steps starting from unprotected d-GlcNAc. A... 
RESONANCE | TRANSITION-STATE ANALOGS | CRYSTAL-STRUCTURE | CHEMISTRY, ORGANIC | GLYCOSYLTRANSFERASES | PEPTIDOGLYCAN SYNTHESIS | EFFICIENT | DERIVATIVES | Bacterial Proteins - antagonists & inhibitors | Stereoisomerism | Glycosyltransferases - chemistry | Bacterial Proteins - chemistry | Acetylglucosamine - analogs & derivatives | Glycoside Hydrolases - chemistry | Molecular Structure | Acetylglucosamine - chemistry | Glycosides - chemistry | Imino Sugars - chemical synthesis | Glycosyltransferases - antagonists & inhibitors | Imino Sugars - chemistry | Glycosides | Research | Ring formation (Chemistry) | Chemical properties | Chemical synthesis
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16. Full Text New structures, chemical functions, and inhibitors for glycosyltransferases
by Roychoudhury, Rajarshi and Pohl, Nicola LB
Current Opinion in Chemical Biology, ISSN 1367-5931, 2010, Volume 14, Issue 2, pp. 168 - 173
Glycosyltransferases are key enzymes in a range of biological processes. The last two years have seen a new appreciation for the range of structural folds that... 
CELLS | GLUCOSYLTRANSFERASE | BIOPHYSICS | GLYCOSYLATION | IDENTIFICATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | Bacterial Proteins - antagonists & inhibitors | Glycosyltransferases - chemistry | Humans | Bacterial Proteins - chemistry | Models, Molecular | Glycosyltransferases - metabolism | Animals | Plant Proteins - chemistry | Plant Proteins - antagonists & inhibitors | Bacterial Proteins - metabolism | Protein Conformation | Plant Proteins - metabolism | Glycosyltransferases - antagonists & inhibitors | Transferases
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17. Full Text Covalent inhibitors of LgtC: A blueprint for the discovery of non-substrate-like inhibitors for bacterial glycosyltransferases
by Xu, Yong and Smith, Ruth and Vivoli, Mirella and Ema, Masaki and Goos, Niina and Gehrke, Sebastian and Harmer, Nicholas J and Wagner, Gerd K
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 06/2017, Volume 25, Issue 12, pp. 3182 - 3194
Non-substrate-like inhibitors of glycosyltransferases are sought after as chemical tools and potential lead compounds for medicinal chemistry, chemical biology... 
Covalent inhibitor | Chemical tool | Enzyme | Glycosyltransferase | Virulence factor | IRREVERSIBLE INHIBITORS | COMPLEX | CHEMISTRY, MEDICINAL | PROTEIN | ANALOGS | DOCKING | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, ORGANIC | LIBRARIES | ADHESION | DRUGS | RESISTANCE | ELECTROPHILES | Catalytic Domain - drug effects | Pasteurella Infections - microbiology | Bacterial Proteins - antagonists & inhibitors | Glycosyltransferases - chemistry | Humans | Bacterial Proteins - chemistry | Enzyme Inhibitors - pharmacology | Pasteurella multocida - chemistry | Drug Discovery | Glycosyltransferases - metabolism | Animals | Cattle | Meningitis, Meningococcal - microbiology | Enzyme Inhibitors - chemistry | Neisseria meningitidis - chemistry | Pasteurella multocida - enzymology | Bacterial Proteins - metabolism | Pasteurella Infections - drug therapy | Molecular Docking Simulation | Meningitis, Meningococcal - drug therapy | Neisseria meningitidis - enzymology | Glycosyltransferases - antagonists & inhibitors | Physiological aspects | Lead compounds | Drug discovery | Catalysis | Analysis | Transferases
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