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Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology

The EMBO journal, 2013-05, Vol.32 (10), p.1478-1488

2013

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The GalNAc-type O-Glycoproteome of CHO Cells Characterized by the SimpleCell Strategy

Molecular & cellular proteomics, 2014-12, Vol.13 (12), p.3224-3235

2014

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An Atlas of Human Glycosylation Pathways Enables Display of the Human Glycome by Gene Engineered Cells

Molecular cell, 2019-07, Vol.75 (2), p.394-407.e5

2019

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Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines

Nature methods, 2011-11, Vol.8 (11), p.977-982

2011

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Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis

Glycobiology (Oxford), 2015-01, Vol.25 (1), p.55-65

2015

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Low Density Lipoprotein Receptor Class A Repeats Are O-Glycosylated in Linker Regions

The Journal of biological chemistry, 2014-06, Vol.289 (25), p.17312-17324

2014

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Expression of the O -Glycosylation Enzyme GalNAc-T3 in the Equatorial Segment Correlates with the Quality of Spermatozoa

International journal of molecular sciences, 2018-09, Vol.19 (10), p.2949

2018

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CDX2 regulates interleukin‐33 gene expression in intestinal epithelial cells (LS174T)

FEBS open bio, 2021-06, Vol.11 (6), p.1638-1644

2021

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INDEL detection, the 'Achilles heel' of precise genome editing: a survey of methods for accurate profiling of gene editing induced indels

Nucleic acids research, 2020-12, Vol.48 (21), p.11958-11981

2020

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Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family

Glycobiology (Oxford), 2016-04, Vol.26 (4), p.360-376

2016

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Precise integration of inducible transcriptional elements (PrIITE) enables absolute control of gene expression

Nucleic acids research, 2017-07, Vol.45 (13), p.e123-e123

2017

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Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation

The Journal of biological chemistry, 2006-07, Vol.281 (27), p.18370-18377

2006

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Fast and Quantitative Identification of Ex Vivo Precise Genome Targeting-Induced Indel Events by IDAA

Methods in molecular biology (Clifton, N.J.), 2019, Vol.1961, p.45

2019

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O-Glycosylation Modulates Proprotein Convertase Activation of Angiopoietin-like Protein 3: POSSIBLE ROLE OF POLYPEPTIDE GalNAc-TRANSFERASE-2 IN REGULATION OF CONCENTRATIONS OF PLASMA LIPIDS

The Journal of biological chemistry, 2010-11, Vol.285 (47), p.36293-36303

2010

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Glycoengineering of human cell lines using zinc finger nuclease gene targeting: SimpleCells with homogeneous GalNAc O-glycosylation allow isolation of the O-glycoproteome by one-step lectin affinity chromatography

Methods in molecular biology (Clifton, N.J.), 2013, Vol.1022, p.387

2013

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Evaluation of Histo-Blood Group ABO Genotyping in a Danish Population: Frequency of a Novel O Allele Defined as O2

Vox sanguinis, 1994-08, Vol.67 (2), p.210-215

1994

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cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3

The Journal of biological chemistry, 1996-07, Vol.271 (29), p.17006-17012

1996

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A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

FEBS letters, 1999-10, Vol.460 (2), p.226-230

1999

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Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy

The Journal of biological chemistry, 1999-09, Vol.274 (36), p.25362-25370

1999

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Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat

The Journal of biological chemistry, 1998-11, Vol.273 (46), p.30472-30481

1998

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Generation of monoclonal antibodies to native active human glycosyltransferases

Methods in molecular biology (Clifton, N.J.), 2013, Vol.1022, p.403

2013

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Purification and cDNA Cloning of a Human UDP-N-acetyl-α- D-galactosamine:polypeptide N-Acetylgalactosaminyltransferase (∗)

The Journal of biological chemistry, 1995-10, Vol.270 (41), p.24156-24165

1995

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Genomic Cloning of the Human Histo-Blood Group ABO Locus

Biochemical and biophysical research communications, 1995-01, Vol.206 (1), p.318-325

1995

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Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferase family

Glycobiology (Oxford), 1998-06, Vol.8 (6), p.547-555

1998

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Biosynthetic basis of incompatible histo-blood group A antigen expression : anti-A transferase antibodies reactive with gastric cancer tissue of type O individuals

Cancer research (Chicago, Ill.), 1993-11, Vol.53 (22), p.5494-5500

1993

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Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology

The GalNAc-type O-Glycoproteome of CHO Cells Characterized by the SimpleCell Strategy

An Atlas of Human Glycosylation Pathways Enables Display of the Human Glycome by Gene Engineered Cells

Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines

Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis

Low Density Lipoprotein Receptor Class A Repeats Are O-Glycosylated in Linker Regions

Expression of the O -Glycosylation Enzyme GalNAc-T3 in the Equatorial Segment Correlates with the Quality of Spermatozoa

CDX2 regulates interleukin‐33 gene expression in intestinal epithelial cells (LS174T)

INDEL detection, the 'Achilles heel' of precise genome editing: a survey of methods for accurate profiling of gene editing induced indels

Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family

Precise integration of inducible transcriptional elements (PrIITE) enables absolute control of gene expression

Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation

Fast and Quantitative Identification of Ex Vivo Precise Genome Targeting-Induced Indel Events by IDAA

O-Glycosylation Modulates Proprotein Convertase Activation of Angiopoietin-like Protein 3: POSSIBLE ROLE OF POLYPEPTIDE GalNAc-TRANSFERASE-2 IN REGULATION OF CONCENTRATIONS OF PLASMA LIPIDS

Glycoengineering of human cell lines using zinc finger nuclease gene targeting: SimpleCells with homogeneous GalNAc O-glycosylation allow isolation of the O-glycoproteome by one-step lectin affinity chromatography

Evaluation of Histo-Blood Group ABO Genotyping in a Danish Population: Frequency of a Novel O Allele Defined as O2

cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3

A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy

Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat

Generation of monoclonal antibodies to native active human glycosyltransferases

Purification and cDNA Cloning of a Human UDP-N-acetyl-α- D-galactosamine:polypeptide N-Acetylgalactosaminyltransferase (∗)

Genomic Cloning of the Human Histo-Blood Group ABO Locus

Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferase family

Biosynthetic basis of incompatible histo-blood group A antigen expression : anti-A transferase antibodies reactive with gastric cancer tissue of type O individuals

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