Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates (Q33254101)

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Language	Label	Description	Also known as
English	Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

author name string

Thomas A Gerken

1

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

Jayalakshmi Raman

2

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

Timothy A Fritz

3

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

Oliver Jamison

4

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Europe PubMed Central

PubMed publication ID

24 July 2017

language of work or name

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publication date

15 August 2006

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Europe PubMed Central

PubMed publication ID

24 July 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

24 July 2017

281

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Europe PubMed Central

PubMed publication ID

24 July 2017

43

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

32403-32416

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation

1 reference

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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

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Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family

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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

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Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity

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Molecular cloning of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene

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Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)

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Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9

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Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila

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Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster

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cDNA Cloning and Expression of a Family of UDP-N-acetyl-dgalactosamine:PolypeptideN-Acetylgalactosaminyltransferase Sequence Homologs fromCaenorhabditis elegans

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Mucin-type O-glycosylation in Fasciola hepatica: characterisation of carcinoma-associated Tn and sialyl-Tn antigens and evaluation of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase activity

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Sialyl-Tn antigen expression and O-linked GalNAc-Thr synthesis by Trypanosoma cruzi.

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O-glycosylation in Toxoplasma gondii: identification and analysis of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

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Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis

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

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Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides.

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The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities

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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

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Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling

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Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

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Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and cani

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Use of an oriented peptide library to determine the optimal substrates of protein kinases

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SH2 domains recognize specific phosphopeptide sequences

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Determination of the specific substrate sequence motifs of protein kinase C isozymes

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

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The acceptor specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

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The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1.

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Identifiers

10.1074/JBC.M605149200

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 July 2017

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