acetylglucosamine has been researched along with n-acetylglucosamine thiazoline in 19 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 9 (47.37) | 29.6817 |
| 2010's | 8 (42.11) | 24.3611 |
| 2020's | 2 (10.53) | 2.80 |
| Authors | Studies |
|---|---|
| Blackburn, NT; Clarke, AJ; Reid, CW | 1 |
| Auzanneau, FI; Blackburn, NT; Clarke, AJ; Legaree, BA; Reid, CW | 1 |
| Chin, D; Debowski, AW; Macauley, MS; Vocadlo, DJ; Whitworth, GE | 1 |
| Cherney, MM; James, MN; Lemieux, MJ; Mahuran, DJ; Mark, BL; Withers, SG | 1 |
| Black, GW; Charnock, SJ; Davies, GJ; Macauley, MS; Robinson, CE; Sheldon, WL; Taylor, EJ; Vocadlo, DJ | 1 |
| Davies, GJ; Dennis, RJ; Greig, IR; Macauley, MS; Stubbs, KA; Taylor, EJ; Vocadlo, DJ; Whitworth, GE | 1 |
| Bezouska, K; Charvátová-Pisvejcová, A; Hofbauerová, K; Kavan, D; Kren, V; Man, P; Novák, P; Plíhal, O; Pompach, P; Ryslavá, H; Sklenár, J; Weignerová, L | 1 |
| Collyer, CA; Guss, JM; Harty, DW; Hunter, N; Jacques, NA; Langley, DB | 1 |
| Alves, CN; Kanaan, N; Lameira, J; Martí, S; Moliner, V; Tuñón, I | 1 |
| Macauley, MS; Vocadlo, DJ | 1 |
| Brocks, CA; Chatham, JC; Laczy, B; Marsh, SA; Wittmann, I | 1 |
| Alves, CN; de Alencar, NA; Lameira, J; Martí, S; Moliner, V; Silva, JR; Sousa, PR | 1 |
| Bojarová, P; Cvačka, J; Ettrich, R; Kalachova, L; Krejzová, J; Křen, V; Kulik, N; Marhol, P; Pelantová, H; Simon, P; Slámová, K | 1 |
| Liu, T; Shen, X; Wang, J; Xia, M; Yang, Q; Zhang, H; Zhou, H | 1 |
| Kalachova, L; Krejzová, J; Křen, V; Pelantová, H; Šimon, P; Slámová, K | 1 |
| Chen, W; Dong, Y; Kong, H; Lu, H; Wang, D; Yang, Q; Zhang, J | 1 |
| Krejzová, J; Křen, V; Kulik, N; Slámová, K | 1 |
| Aunkham, A; Bulmer, DM; Kaewmaneewat, A; Kardkuntod, A; Meekrathok, P; Stubbs, KA; Suginta, W; van den Berg, B | 1 |
| Almanasra, A; Havranek, B; Islam, SM | 1 |
1 review(s) available for acetylglucosamine and n-acetylglucosamine thiazoline
| Article | Year |
|---|---|
Increasing O-GlcNAc levels: An overview of small-molecule inhibitors of O-GlcNAcase.
Topics: Acetylglucosamine; Acetylglucosaminidase; Animals; Catalytic Domain; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; N-Acetylglucosaminyltransferases; Oximes; Phenylcarbamates; Pyrazoles; Pyridines; Streptozocin; Thiazoles; Uridine Diphosphate N-Acetylglucosamine | 2010 |
18 other study(ies) available for acetylglucosamine and n-acetylglucosamine thiazoline
| Article | Year |
|---|---|
The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli.
Topics: Acetylglucosamine; Cell Membrane; Escherichia coli; Lipopolysaccharides; Microscopy, Phase-Contrast; Thiazoles | 2004 |
Inhibition of membrane-bound lytic transglycosylase B by NAG-thiazoline.
Topics: Acetylglucosamine; Base Sequence; DNA Primers; Enzyme Inhibitors; Glycoside Hydrolases; Glycosyltransferases; Membrane Proteins; Mutagenesis, Site-Directed; Thiazoles | 2004 |
O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors.
Topics: Acetylglucosamine; Acetylglucosaminidase; Acetyltransferases; Animals; beta-N-Acetylhexosaminidases; Catalysis; Chlorocebus aethiops; COS Cells; Enzyme Activation; Glycoconjugates; Histone Acetyltransferases; Humans; Lysosomes; Multienzyme Complexes; Substrate Specificity; Thiazoles | 2005 |
Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis.
Topics: Acetylglucosamine; Amino Acid Substitution; Arginine; Aspartic Acid; beta-N-Acetylhexosaminidases; Binding Sites; Crystallography, X-Ray; Dimerization; Gangliosidoses, GM2; Glycine; Glycosylation; Hexosaminidase A; Humans; Hydrolysis; Models, Molecular; Mutation; Protein Conformation; Protein Subunits; Tay-Sachs Disease; Thiazoles | 2006 |
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a beta-N-acetylglucosaminidase and not a hyaluronidase.
Topics: Acetylglucosamine; Acetylglucosaminidase; Amino Acid Sequence; Animals; beta-N-Acetylhexosaminidases; Catalysis; Chlorocebus aethiops; COS Cells; Escherichia coli; Histone Acetyltransferases; Humans; Hyaluronoglucosaminidase; Hydrolysis; Hymecromone; Kinetics; Molecular Sequence Data; Multienzyme Complexes; Nuclear Magnetic Resonance, Biomolecular; Sequence Homology, Amino Acid; Streptococcus pyogenes; Structure-Activity Relationship; Substrate Specificity; Thiazoles | 2006 |
Analysis of PUGNAc and NAG-thiazoline as transition state analogues for human O-GlcNAcase: mechanistic and structural insights into inhibitor selectivity and transition state poise.
Topics: Acetylglucosamine; beta-N-Acetylhexosaminidases; Catalysis; Crystallography, X-Ray; Enzyme Activation; Enzyme Inhibitors; Glycosylation; Humans; Models, Molecular; Oximes; Phenylcarbamates; Substrate Specificity; Thermodynamics; Thiazoles | 2007 |
Large propeptides of fungal beta-N-acetylhexosaminidases are novel enzyme regulators that must be intracellularly processed to control activity, dimerization, and secretion into the extracellular environment.
Topics: Acetylglucosamine; Amino Acid Sequence; beta-N-Acetylhexosaminidases; Biological Transport; Catalysis; Dimerization; Endoplasmic Reticulum; Enzyme Activation; Enzyme Precursors; Enzyme Stability; Fungi; Furin; Molecular Sequence Data; Sequence Homology, Amino Acid; Thiazoles; Transcription, Genetic | 2007 |
Structure of N-acetyl-beta-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline.
Topics: Acetylglucosamine; Acetylglucosaminidase; Binding Sites; Crystallography, X-Ray; Dimerization; Endocarditis, Bacterial; Ligands; Models, Molecular; Protein Structure, Tertiary; Streptococcus gordonii; Thiazoles | 2008 |
A quantum mechanics/molecular mechanics study of the protein-ligand interaction of two potent inhibitors of human O-GlcNAcase: PUGNAc and NAG-thiazoline.
Topics: Acetylglucosamine; beta-N-Acetylhexosaminidases; Binding Sites; Biocatalysis; Drug Design; Enzyme Inhibitors; Humans; Ligands; Models, Molecular; Molecular Conformation; Oximes; Phenylcarbamates; Protein Binding; Protons; Quantum Theory; Static Electricity; Thermodynamics; Thiazoles | 2008 |
Inhibition of O-GlcNAcase in perfused rat hearts by NAG-thiazolines at the time of reperfusion is cardioprotective in an O-GlcNAc-dependent manner.
Topics: Acetylglucosamine; Animals; beta-N-Acetylhexosaminidases; Desmin; Enzyme Inhibitors; Male; Models, Animal; Myocardial Reperfusion Injury; Myocardium; Rats; Rats, Sprague-Dawley; Thiazoles | 2010 |
Computational analysis of human OGA structure in complex with PUGNAc and NAG-thiazoline derivatives.
Topics: Acetylglucosamine; Bacterial Proteins; Bacteroides; beta-N-Acetylhexosaminidases; Binding Sites; Clostridium perfringens; Crystallography, X-Ray; Humans; Isoenzymes; Kinetics; Ligands; Molecular Docking Simulation; Oximes; Phenylcarbamates; Protein Binding; Protein Conformation; Structural Homology, Protein; Thermodynamics; Thiazoles | 2012 |
Inhibition of GlcNAc-processing glycosidases by C-6-azido-NAG-thiazoline and its derivatives.
Topics: Acetylglucosamine; beta-N-Acetylhexosaminidases; Catalytic Domain; Drug Stability; Glycoside Hydrolases; Models, Molecular; Molecular Conformation; Protein Binding; Thiazoles | 2014 |
Exploring NAG-thiazoline and its derivatives as inhibitors of chitinolytic β-acetylglucosaminidases.
Topics: Acetylglucosamine; Acetylglucosaminidase; Animals; Enzyme Inhibitors; Insect Proteins; Molecular Dynamics Simulation; Moths; Thiazoles | 2015 |
Inhibition of microbial β-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline.
Topics: Acetylglucosamine; Bacterial Proteins; Bacteroides; beta-N-Acetylhexosaminidases; Fungal Proteins; Fungi; Kinetics; Protein Binding; Streptomyces; Substrate Specificity; Thiazoles | 2014 |
Synthesis of NAG-thiazoline-derived inhibitors for β-N-acetyl-d-hexosaminidases.
Topics: Acetylglucosamine; Animals; beta-N-Acetylhexosaminidases; Chemistry Techniques, Synthetic; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; Lepidoptera; Substrate Specificity; Thiazoles | 2015 |
Expression of human β-N-acetylhexosaminidase B in yeast eases the search for selective inhibitors.
Topics: Acetylglucosamine; beta-Hexosaminidase beta Chain; Catalytic Domain; Enzyme Inhibitors; Gene Expression; Humans; Kinetics; Models, Molecular; Pichia; Recombinant Proteins; Thiazoles | 2016 |
NAG-thiazoline is a potent inhibitor of the Vibrio campbellii GH20 β-N-Acetylglucosaminidase.
Topics: Acetylglucosamine; Acetylglucosaminidase; Animals; Bacterial Infections; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Humans; Inhibitory Concentration 50; Kinetics; Models, Molecular; Oligosaccharides; Protein Domains; Substrate Specificity; Thermodynamics; Thiazoles; Vibrio | 2020 |
In-silico screening and microsecond molecular dynamics simulations to identify single point mutations that destabilize β-hexosaminidase A causing Tay-Sachs disease.
Topics: Acetylglucosamine; beta-Hexosaminidase alpha Chain; Binding Sites; Central Nervous System; G(M2) Ganglioside; Gene Expression; Humans; Hydrogen Bonding; Molecular Dynamics Simulation; Neurons; Peripheral Nervous System; Point Mutation; Polymorphism, Single Nucleotide; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Tay-Sachs Disease; Thermodynamics; Thiazoles | 2021 |