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Structural variation of the 3-acetamido-4,5,6-trihydroxyazepane iminosugar through epimerization and C -alkylation leads to low micromolar HexAB and NagZ inhibitors

Organic & biomolecular chemistry, 2022-01, Vol.20 (3), p.619-629

2022

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HBP/O-GlcNAcylation Metabolic Axis Regulates Bone Resorption Outcome

Journal of dental research, 2023-04, Vol.102 (4), p.440-449

2023

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Axonal Transport of Lysosomes Is Unaffected in Glucocerebrosidase-Inhibited iPSC-Derived Forebrain Neurons

eNeuro, 2023-10, Vol.10 (10), p.ENEURO.0079-23.2023

2023

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Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O -GlcNAcase

Chemical science (Cambridge), 2016-01, Vol.7 (6), p.3742-3750

2016

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Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibiotics

Organic & biomolecular chemistry, 2017, Vol.15 (21), p.4609-4619

2017

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Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

Nature (London), 2001-08, Vol.412 (6849), p.835-838

2001

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HCF-1 is cleaved in the active site of O-GlcNAc transferase

Science (American Association for the Advancement of Science), 2013-12, Vol.342 (6163), p.1235-1239

2013

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Crystallographic Evidence for Substrate-assisted Catalysis in a Bacterial β-Hexosaminidase

The Journal of biological chemistry, 2001-03, Vol.276 (13), p.10330-10337

2001

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Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state

The Journal of biological chemistry, 2002-10, Vol.277 (42), p.40055-40065

2002

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Structural snapshots of the reaction coordinate for O-GlcNAc transferase

Nature chemical biology, 2012-12, Vol.8 (12), p.966-968

2012

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Streptococcus pneumoniae Endohexosaminidase D, Structural and Mechanistic Insight into Substrate-assisted Catalysis in Family 85 Glycoside Hydrolases

The Journal of biological chemistry, 2009-04, Vol.284 (17), p.11676-11689

2009

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Mechanism of Action and Identification of Asp242 as the Catalytic Nucleophile of Vibrio furnisii N-Acetyl-β-d-glucosaminidase Using 2-Acetamido-2-deoxy-5-fluoro-α-l-idopyranosyl Fluoride

Biochemistry (Easton), 2000-01, Vol.39 (1), p.117-126

2000

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Crystal Structure of β- d-Xylosidase from Thermoanaerobacterium saccharolyticum, a Family 39 Glycoside Hydrolase

Journal of molecular biology, 2004-01, Vol.335 (1), p.155-165

2004

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Structural variation of the 3-acetamido-4,5,6-trihydroxyazepane iminosugar through epimerization and -alkylation leads to low micromolar HexAB and NagZ inhibitors

Organic & biomolecular chemistry, 2022-01, Vol.2 (3), p.619-629

2022

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Characterization of the Glu and Asp Residues in the Active Site of Human β-Hexosaminidase B

Biochemistry (Easton), 2001-02, Vol.40 (7), p.2201-2209

2001

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Differential Recognition and Hydrolysis of Host Carbohydrate Antigens by Streptococcus pneumoniae Family 98 Glycoside Hydrolases

The Journal of biological chemistry, 2009-09, Vol.284 (38), p.26161-26173

2009

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Biochemical and Structural Assessment of the 1-N-Azasugar GalNAc-isofagomine as a Potent Family 20 β-N-Acetylhexosaminidase Inhibitor

The Journal of biological chemistry, 2001-11, Vol.276 (45), p.42131-42137

2001

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Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibioticsElectronic supplementary information (ESI) available: Copies of 1H, 19F and 13C spectra of all new compounds; glycosidase assays. See DOI: 10.1039/c7ob00838d

2017-05

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A Chemical Approach for Identifying O-GlcNAc-Modified Proteins in Cells

Proceedings of the National Academy of Sciences - PNAS, 2003-08, Vol.100 (16), p.9116-9121

2003

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O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors

The Journal of biological chemistry, 2005-07, Vol.280 (27), p.25313-25322

2005

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A Strategy for Functional Proteomic Analysis of Glycosidase Activity from Cell Lysates

Angewandte Chemie (International ed.), 2004-10, Vol.43 (40), p.5338-5342

2004

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Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcaseElectronic supplementary information (ESI) available: Detailed experimental procedures, NMR spectra and additional figures illustrating Ki graphs, kinetic data, pKa titration data and structural analysis data. See DOI: 10.1039/c6sc00370b

2016-05

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Detailed Comparative Analysis of the Catalytic Mechanisms of β-N-Acetylglucosaminidases from Families 3 and 20 of Glycoside Hydrolases

Biochemistry (Easton), 2005-09, Vol.44 (38), p.12809-12818

2005

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Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase† †Electronic supplementary information (ESI) available: Detailed experimental procedures, NMR spectra and additional figures illustrating Ki graphs, kinetic data, pKa titration data and structural analysis data. See DOI: 10.1039/c6sc00370b

Chemical science (Cambridge), 2016-02, Vol.7 (6), p.3742-3750

2016

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Identification of active site residues in glycosidases by use of tandem mass spectrometry

Methods in molecular biology (Clifton, N.J.), 2000, Vol.146, p.203

2000

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Structural variation of the 3-acetamido-4,5,6-trihydroxyazepane iminosugar through epimerization and C -alkylation leads to low micromolar HexAB and NagZ inhibitors

HBP/O-GlcNAcylation Metabolic Axis Regulates Bone Resorption Outcome

Axonal Transport of Lysosomes Is Unaffected in Glucocerebrosidase-Inhibited iPSC-Derived Forebrain Neurons

Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O -GlcNAcase

Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibiotics

Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate

HCF-1 is cleaved in the active site of O-GlcNAc transferase

Crystallographic Evidence for Substrate-assisted Catalysis in a Bacterial β-Hexosaminidase

Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state

Structural snapshots of the reaction coordinate for O-GlcNAc transferase

Streptococcus pneumoniae Endohexosaminidase D, Structural and Mechanistic Insight into Substrate-assisted Catalysis in Family 85 Glycoside Hydrolases

Mechanism of Action and Identification of Asp242 as the Catalytic Nucleophile of Vibrio furnisii N-Acetyl-β-d-glucosaminidase Using 2-Acetamido-2-deoxy-5-fluoro-α-l-idopyranosyl Fluoride

Crystal Structure of β- d-Xylosidase from Thermoanaerobacterium saccharolyticum, a Family 39 Glycoside Hydrolase

Structural variation of the 3-acetamido-4,5,6-trihydroxyazepane iminosugar through epimerization and -alkylation leads to low micromolar HexAB and NagZ inhibitors

Characterization of the Glu and Asp Residues in the Active Site of Human β-Hexosaminidase B

Differential Recognition and Hydrolysis of Host Carbohydrate Antigens by Streptococcus pneumoniae Family 98 Glycoside Hydrolases

Biochemical and Structural Assessment of the 1-N-Azasugar GalNAc-isofagomine as a Potent Family 20 β-N-Acetylhexosaminidase Inhibitor

Selective trihydroxylated azepane inhibitors of NagZ, a glycosidase involved in Pseudomonas aeruginosa resistance to β-lactam antibioticsElectronic supplementary information (ESI) available: Copies of 1H, 19F and 13C spectra of all new compounds; glycosidase assays. See DOI: 10.1039/c7ob00838d

A Chemical Approach for Identifying O-GlcNAc-Modified Proteins in Cells

O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors

A Strategy for Functional Proteomic Analysis of Glycosidase Activity from Cell Lysates

Detailed Comparative Analysis of the Catalytic Mechanisms of β-N-Acetylglucosaminidases from Families 3 and 20 of Glycoside Hydrolases

Identification of active site residues in glycosidases by use of tandem mass spectrometry

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