(Q43670680)

English

Studies of acceptor site specificities for three members of UDP-GalNAc:N-acetylgalactosaminyltransferases by using a synthetic peptide mimicking the tandem repeat of MUC5AC.

scientific article published in July 2001

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scholarly article

1 reference

Europe PubMed Central

25 November 2017

Studies of acceptor site specificities for three members of UDP-GalNAc:N-acetylgalactosaminyltransferases by using a synthetic peptide mimicking the tandem repeat of MUC5AC. (English)

1 reference

Europe PubMed Central

25 November 2017

1 reference

based on heuristic

inferred from title

3

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Europe PubMed Central

25 November 2017

author name string

Tetaert D

1

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Europe PubMed Central

25 November 2017

Richet C

2

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Europe PubMed Central

25 November 2017

Boersma A

4

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Europe PubMed Central

25 November 2017

Degand P

5

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Europe PubMed Central

25 November 2017

publication date

1 July 2001

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Europe PubMed Central

25 November 2017

Carbohydrate Research

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Europe PubMed Central

25 November 2017

333

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Europe PubMed Central

25 November 2017

165-171

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Europe PubMed Central

25 November 2017

2

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Europe PubMed Central

25 November 2017

describes a project that uses

synthetic peptide

1 reference

based on heuristic

inferred from title

Biological roles of oligosaccharides: all of the theories are correct

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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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Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold

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cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans

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Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3

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

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Characterization of the human mucin gene MUC5AC: a consensus cysteine-rich domain for 11p15 mucin genes?

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Incorporation of N-acetylgalactosamine into consecutive threonine residues in MUC2 tandem repeat by recombinant human N-acetyl-D-galactosamine transferase-T1, T2 and T3.

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

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Distinct selectin ligands on colon carcinoma mucins can mediate pathological interactions among platelets, leukocytes, and endothelium

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Interaction of human macrophage C-type lectin with O-linked N-acetylgalactosamine residues on mucin glycopeptides

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cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase

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Influence of the amino acid sequence on the MUC5AC motif peptide O-glycosylation by human gastric UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase(s)

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Improved capillary electrophoretic separation of glycosylated oligopeptides through addition of poly(vinyl alcohol), and analysis by electrospray mass spectrometry

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Identifiers

10.1016/S0008-6215(01)00135-5

1 reference

Europe PubMed Central

25 November 2017

1 reference

Europe PubMed Central

25 November 2017

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