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1. Full Text HCF-1 is cleaved in the active site of O-GlcNAc transferase
by Lazarus, Michael B and Jiang, Jiaoyang and Kapuria, Vaibhav and Bhuiyan, Tanja and Janetzko, John and Zandberg, Wesley F and Vocadlo, David J and Herr, Winship and Walker, Suzanne and Brookhaven National Laboratory (BNL)
Science (American Association for the Advancement of Science), ISSN 0036-8075, 2013, Volume 342, Issue 6163, pp. 1235 - 1239
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Catalytic Domain | Humans | Models, Molecular | Crystallography, X-Ray | Glycosylation | Recombinant Fusion Proteins - chemistry | Host Cell Factor C1 - metabolism | N-Acetylglucosaminyltransferases - chemistry | Pyrrolidonecarboxylic Acid - metabolism | Recombinant Fusion Proteins - metabolism | N-Acetylglucosaminyltransferases - metabolism | Amino Acid Motifs | Uridine Diphosphate N-Acetylglucosamine - chemistry | Hydrogen Bonding | Proteolysis | Protein Conformation | Host Cell Factor C1 - chemistry | Amino Acid Substitution | Uridine Diphosphate N-Acetylglucosamine - metabolism | Proteins | Cellular control mechanisms | Glycosyltransferases | Physiological aspects | Research | Molecular biology | Enzymes | Peptides | Cell cycle | Index Medicus | Human | Residues | Progressions | Nutrients | Cleavage | Biochemistry | Diphosphates | Glutamine
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2. Full Text UDP-sugar accumulation drives hyaluronan synthesis in breast cancer
by Oikari, Sanna and Kettunen, Tiia and Tiainen, Satu and Häyrinen, Jukka and Masarwah, Amro and Sudah, Mazen and Sutela, Anna and Vanninen, Ritva and Tammi, Markku and Auvinen, Päivi
Matrix biology, ISSN 0945-053X, 04/2018, Volume 67, pp. 63 - 74
Hyaluronan | UDP-sugar | Breast cancer | UDP-N-Acetylglucosamine | Warburg effect | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Up-Regulation | Uridine Diphosphate Glucuronic Acid - metabolism | Humans | Middle Aged | Gene Expression Regulation, Neoplastic | Case-Control Studies | Breast Neoplasms - metabolism | Young Adult | Breast Neoplasms - genetics | Hyaluronan Synthases - genetics | Hyaluronic Acid - metabolism | Aged, 80 and over | Adult | Female | Aged | Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - genetics | Uridine Diphosphate N-Acetylglucosamine - metabolism | Physiological aspects | Glucose metabolism | RNA | Hyaluronic acid | Enzymes | Fructose-6-phosphate | N-Acetylglucosamine | Gene expression | Fructose | Intermediates | Metabolites | Glycolysis | Genetics | Extracellular matrix | Sugar | Tumors | Glutamine | Index Medicus
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3. Full Text From Chitin to α‐Glycosides of N‐Acetylglucosamine Using Catalytic Copper Triflate in a Heated Sealed‐Vessel Reactor
by Frem, Dany and Urban, Dominique and Norsikian, Stéphanie and Beau, Jean‐Marie
European journal of organic chemistry, ISSN 1434-193X, 09/2017, Volume 2017, Issue 34, pp. 5094 - 5101
Glycosides | Carbohydrates | Glycosylation | Copper | N‐Acetylglucosamine | Isomerization | N-Acetylglucosamine
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4. Full Text Crystal structure of UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) from Mycobacterium tuberculosis
by Eniyan, Kandasamy and Dharavath, Sudhaker and Vijayan, Ramachandran and Bajpai, Urmi and Gourinath, Samudrala
Biochimica et biophysica acta. Proteins and proteomics, ISSN 1570-9639, 03/2018, Volume 1866, Issue 3, pp. 397 - 406
NADPH | FAD | UDP-GlcNAc-EP | UDP-MurNAc | Mycobacterium tuberculosis | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Amino Acid Sequence | Catalytic Domain | Biocatalysis | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Crystallography, X-Ray | Binding Sites - genetics | NADP - chemistry | Molecular Dynamics Simulation | Uridine Diphosphate N-Acetylglucosamine - chemistry | Sequence Homology, Amino Acid | Mycobacterium tuberculosis - enzymology | Protein Binding | Protein Domains | Bacterial Proteins - metabolism | Uridine Diphosphate N-Acetylglucosamine - analogs & derivatives | NADP - metabolism | Uridine Diphosphate N-Acetylglucosamine - genetics | Mycobacterium tuberculosis - genetics | Uridine Diphosphate N-Acetylglucosamine - metabolism | Enzymes | Tuberculosis | Implants, Artificial | Prosthesis | Analysis | Crystals | Physiological aspects | Bacteria | Structure | Index Medicus
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5. Full Text Cytoplasmic steps of peptidoglycan biosynthesis
by Barreteau, Hélène and Kovač, Andreja and Boniface, Audrey and Sova, Matej and Gobec, Stanislav and Blanot, Didier
FEMS microbiology reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 168 - 207
d‐alanine | peptidoglycan | UDP‐N‐acetylglucosamine | bacterial cell wall | d‐glutamic acid | UDP‐N‐acetylmuramic acid | Peptidoglycan | UDP-N-acetylglucosamine | Bacterial cell wall | UDP-N-acetylmuramic acid | D-alanine | D-glutamic acid | Life Sciences & Biomedicine | Microbiology | Science & Technology | Bacterial Proteins - antagonists & inhibitors | Bacteria - metabolism | Uridine Diphosphate N-Acetylglucosamine - biosynthesis | Phosphoglucomutase - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Multienzyme Complexes - metabolism | Cytoplasm - metabolism | Escherichia coli Proteins - metabolism | Biosynthetic Pathways | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Bacteria - enzymology | Bacterial Proteins - metabolism | Escherichia coli Proteins - chemistry | Phosphoglucomutase - metabolism | Physiological aspects | Peptidoglycans | Index Medicus
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6. Full Text The conserved threonine-rich region of the HCF-1PRO repeat activates promiscuous OGT:UDP-GlcNAc glycosylation and proteolysis activities
by Kapuria, Vaibhav and Röhrig, Ute F and Waridel, Patrice and Lammers, Fabienne and Borodkin, Vladimir S and Van Aalten, Daan M.F and Zoete, Vincent and Herr, Winship
The Journal of biological chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 46, pp. 17754 - 17768
Index Medicus | post-translational modification (PTM) | host-cell factor-1 | O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) | O-GlcNAcylation | Glycobiology and Extracellular Matrices | enzyme mechanism | glycobiology
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7. Full Text Discovery of Novel Inhibitors Targeting Multi-UDP-hexose Pyrophosphorylases as Anticancer Agents
by Yang, Yueqin and Vankayalapati, Hariprasad and Tang, Manshu and Zheng, Yingbo and Li, Yingri and Ma, Cong and Lai, Kent
Molecules (Basel, Switzerland), ISSN 1420-3049, 02/2020, Volume 25, Issue 3, p. 645
Biochemistry & Molecular Biology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Multidisciplinary | Science & Technology | Competition | Hexose | N-Acetylglucosamine | Toxicity | Tunicamycin | Biosynthesis | Drug resistance | Cancer therapies | Optimization | Metastases | Anticancer properties | Antitumor agents | Fibroblasts | UDP-N-acetylglucosamine pyrophosphorylase | Tumorigenesis | Enzymes | Bortezomib | Hexoses | Glycoproteins | Glycosylation | siRNA | Metabolism | Gene expression | Phosphorylase | Glycan | Chemotherapy | Phosphorylases | Computer applications | Galactose | Binding sites | Cancer | Index Medicus | cancer metabolism | galactose-1 phosphate uridylyltransferase (GALT) | UDP-glucose pyrophosphorylase (UGP2) | UDP-N-acetylglucosamine pyrophosphorylase (AGX1 | polypharmacology | fragment-based screening | glycosylation | UAP1 | UDP-hexose pyrophosphorylase | multi-target approach | udp-n-acetylglucosamine pyrophosphorylase (agx1/uap1) | galactose-1 phosphate uridylyltransferase (galt) | udp-hexose pyrophosphorylase | udp-glucose pyrophosphorylase (ugp2)
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