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Ablation of the Galnt3 Gene Leads to Low-Circulating Intact Fibroblast Growth Factor 23 (Fgf23) Concentrations and Hyperphosphatemia Despite Increased Fgf23 Expression

Endocrinology (Philadelphia), 2009-06, Vol.150 (6), p.2543-2550

2009

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Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family

Glycobiology (Oxford), 2012-06, Vol.22 (6), p.736-756

2012

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The Beginnings of Mucin Biosynthesis: The Crystal Structure of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-T1

Proceedings of the National Academy of Sciences - PNAS, 2004-10, Vol.101 (43), p.15307-15312

2004

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Glycopeptide-preferring Polypeptide GalNAc Transferase 10 (ppGalNAc T10), Involved in Mucin-type O-Glycosylation, Has a Unique GalNAc-O-Ser/Thr-binding Site in Its Catalytic Domain Not Found in ppGalNAc T1 or T2

The Journal of biological chemistry, 2009-07, Vol.284 (30), p.20387-20397

2009

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Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-2

The Journal of biological chemistry, 2006-03, Vol.281 (13), p.8613-8619

2006

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Identification of Common and Unique Peptide Substrate Preferences for the UDP-GalNAc:Polypeptide α-N-acetylgalactosaminyltransferases T1 and T2 Derived from Oriented Random Peptide Substrates

The Journal of biological chemistry, 2006-10, Vol.281 (43), p.32403-32416

2006

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All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

Glycobiology (Oxford), 2003-01, Vol.13 (1), p.1R-16R

2003

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The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection

The Journal of biological chemistry, 2008-08, Vol.283 (34), p.22942-22951

2008

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Tryptophan 80 and Leucine 143 Are Critical for the Hydride Transfer Step of Thymidylate Synthase by Controlling Active Site Access

Biochemistry (Easton), 2002-06, Vol.41 (22), p.7021-7029

2002

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Multi-targeted antifolates aimed at avoiding drug resistance form covalent closed inhibitory complexes with human and Escherichia coli thymidylate synthases

Journal of molecular biology, 2001-11, Vol.313 (4), p.813-829

2001

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Disaccharide Uptake and Priming in Animal Cells: Inhibition of Sialyl Lewis X by Acetylated Galβ1 → 4GlcNAcβ-O Naphthalenemethanol

Proceedings of the National Academy of Sciences - PNAS, 1995-04, Vol.92 (8), p.3323-3327

1995

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Identification of Common and Unique Peptide Substrate Preferences for the UDP-GalNAc:Polypeptide Î±-N-acetylgalactosaminyltransferases T1 and T2 Derived from Oriented Random Peptide Substrates

The Journal of biological chemistry, 2006-10, Vol.281 (43), p.32403

2006

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Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. VOLUME 281 (2006) PAGES 8613-8619

The Journal of biological chemistry, 2006-08, Vol.281 (34), p.25000-25000

2006

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Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide Î±-N-Acetylgalactosaminyltransferase-2

The Journal of biological chemistry, 2006-03, Vol.281 (13), p.8613

2006

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Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide [alpha]-N-Acetylgalactosaminyltransferase-2

The Journal of biological chemistry, 2006, Vol.281 (13), p.8613-8619

2006

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The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide Î±-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection

The Journal of biological chemistry, 2008-08, Vol.283 (34), p.22942

2008

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Biosynthesis of heparan sulfate on beta-D-xylosides depends on aglycone structure

The Journal of biological chemistry, 1994-01, Vol.269 (1), p.300-307

1994

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Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate

The Journal of biological chemistry, 1994-11, Vol.269 (46), p.28809-28814

1994

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Partial purification and substrate specificity of heparan sulfate α-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides

Glycobiology (Oxford), 1997-07, Vol.7 (5), p.587-595

1997

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The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae

The Journal of biological chemistry, 1994-10, Vol.269 (43), p.27143-27148

1994

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Heparan sulfate primed on β-D-xylosides restores binding of basic fibroblast growth factor

Journal of cellular biochemistry, 1995-02, Vol.57 (2), p.173-184

1995

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Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase

The Journal of biological chemistry, 1993-04, Vol.268 (11), p.8341-8349

1993

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Disaccharide uptake and priming in animal cells: Inhibition of sialyl Lewis X by acetylated GalBeta1yields4GlcNAcBeta-Omega-naphthalenemethanol

Proceedings of the National Academy of Sciences - PNAS, 1995-04, Vol.92 (8), p.3323

1995

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Predicting and harnessing protein flexibility in the design of species-specific inhibitors of thymidylate synthase

Chemistry & biology, 2001-10, Vol.8 (10), p.981-995

2001

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Ablation of the Galnt3 Gene Leads to Low-Circulating Intact Fibroblast Growth Factor 23 (Fgf23) Concentrations and Hyperphosphatemia Despite Increased Fgf23 Expression

Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family

The Beginnings of Mucin Biosynthesis: The Crystal Structure of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-T1

Glycopeptide-preferring Polypeptide GalNAc Transferase 10 (ppGalNAc T10), Involved in Mucin-type O-Glycosylation, Has a Unique GalNAc-O-Ser/Thr-binding Site in Its Catalytic Domain Not Found in ppGalNAc T1 or T2

Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase-2

Identification of Common and Unique Peptide Substrate Preferences for the UDP-GalNAc:Polypeptide α-N-acetylgalactosaminyltransferases T1 and T2 Derived from Oriented Random Peptide Substrates

All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

Heterozygosity for a Loss-of-Function Mutation in GALNT2 Improves Plasma Triglyceride Clearance in Man

The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection

Tryptophan 80 and Leucine 143 Are Critical for the Hydride Transfer Step of Thymidylate Synthase by Controlling Active Site Access

Multi-targeted antifolates aimed at avoiding drug resistance form covalent closed inhibitory complexes with human and Escherichia coli thymidylate synthases

Disaccharide Uptake and Priming in Animal Cells: Inhibition of Sialyl Lewis X by Acetylated Galβ1 → 4GlcNAcβ-O Naphthalenemethanol

Identification of Common and Unique Peptide Substrate Preferences for the UDP-GalNAc:Polypeptide Î±-N-acetylgalactosaminyltransferases T1 and T2 Derived from Oriented Random Peptide Substrates

Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. VOLUME 281 (2006) PAGES 8613-8619

Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide Î±-N-Acetylgalactosaminyltransferase-2

Dynamic Association between the Catalytic and Lectin Domains of Human UDP-GalNAc:Polypeptide [alpha]-N-Acetylgalactosaminyltransferase-2

The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide Î±-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection

Biosynthesis of heparan sulfate on beta-D-xylosides depends on aglycone structure

Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate

Partial purification and substrate specificity of heparan sulfate α-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides

The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae

Heparan sulfate primed on β-D-xylosides restores binding of basic fibroblast growth factor

Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase

Disaccharide uptake and priming in animal cells: Inhibition of sialyl Lewis X by acetylated GalBeta1yields4GlcNAcBeta-Omega-naphthalenemethanol

Predicting and harnessing protein flexibility in the design of species-specific inhibitors of thymidylate synthase

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