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Delineation of the minimal catalytic domain of human Galbeta1-3GalNAc alpha2,3-sialyltransferase (hST3Gal I).
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Europe PubMed Central
PubMed publication ID
11690653
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11690653%20AND%20SRC:MED&resulttype=core&format=json
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2 December 2019
title
Delineation of the minimal catalytic domain of human Galbeta1-3GalNAc alpha2,3-sialyltransferase (hST3Gal I)
(English)
1 reference
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Europe PubMed Central
PubMed publication ID
11690653
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2 December 2019
author
Philippe Delannoy
series ordinal
7
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Europe PubMed Central
PubMed publication ID
11690653
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2 December 2019
Anne Harduin-Lepers
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8
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Europe PubMed Central
PubMed publication ID
11690653
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2 December 2019
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V Vallejo-Ruiz
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1
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PubMed publication ID
11690653
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2 December 2019
R Haque
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2
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2 December 2019
A M Mir
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3
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PubMed publication ID
11690653
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2 December 2019
T Schwientek
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4
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Europe PubMed Central
PubMed publication ID
11690653
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2 December 2019
U Mandel
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5
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11690653
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2 December 2019
R Cacan
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6
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PubMed publication ID
11690653
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2 December 2019
publication date
1 October 2001
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PubMed publication ID
11690653
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2 December 2019
published in
Biochimica et Biophysica Acta
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Europe PubMed Central
PubMed publication ID
11690653
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2 December 2019
volume
1549
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Europe PubMed Central
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11690653
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2 December 2019
issue
2
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Europe PubMed Central
PubMed publication ID
11690653
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11690653%20AND%20SRC:MED&resulttype=core&format=json
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2 December 2019
page(s)
161-173
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Europe PubMed Central
PubMed publication ID
11690653
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11690653%20AND%20SRC:MED&resulttype=core&format=json
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2 December 2019
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Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: implications for their mechanism of action
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The sialyltransferase "sialylmotif" participates in binding the donor substrate CMP-NeuAc
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Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates
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Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain
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Molecular cloning and expression of chick Gal beta 1,3GalNAc alpha 2,3-sialyltransferase
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Mouse beta-galactoside alpha 2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression
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Cloning, expression and gene organization of a human Neu5Ac alpha 2-3Gal beta 1-3GalNAc alpha 2,6-sialyltransferase: hST6GalNAcIV
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Molecular cloning and functional expression of human ST6GalNAc II. Molecular expression in various human cultured cells
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Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase 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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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 proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I. A seventh member of the human beta4-galactosyltransferase gene family
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A conserved disulphide bond in sialyltransferases
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Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity
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Defining the minimal size of catalytically active primate alpha 1,3 galactosyltransferase: structure-function studies on the recombinant truncated enzyme
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Removal of 106 amino acids from the N-terminus of UDP-GlcNAc: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I does not inactivate the enzyme
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Expression of deletion constructs of bovine beta-1,4-galactosyltransferase in Escherichia coli: importance of Cys134 for its activity.
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Crystal structures of the bovine beta 4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
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X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily
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7 January 2021
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Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases
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7 January 2021
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Sialyltransferase activity in FR3T3 cells transformed with ras oncogene: decreased CMP-Neu5Ac:Gal beta 1-3GalNAc alpha-2,3-sialyltransferase
1 reference
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Crossref
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7 January 2021
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Effect of N-glycosylation on turnover and subcellular distribution of N-acetylgalactosaminyltransferase I and sialyltransferase II in neuroblastoma cells
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The effects of the site-directed removal of N-glycosylation sites from beta-1,4-N-acetylgalactosaminyltransferase on its function
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Expression of stable human O-glycan core 2 beta-1,6-N-acetylglucosaminyltransferase in Sf9 insect cells
1 reference
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7 January 2021
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N-glycosylation site occupancy of rat alpha-1,3-fucosyltransferase IV and the effect of glycosylation on enzymatic activity
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The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity
1 reference
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Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase
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GM1 synthase depends on N-glycosylation for enzyme activity and trafficking to the Golgi complex
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Crossref
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Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking
1 reference
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
N-glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0167-4838%2801%2900257-6
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7 January 2021
based on heuristic
inferred from DOI database lookup
GM3 alpha2,8-sialyltransferase (GD3 synthase): protein characterization and sub-golgi location in CHO-K1 cells.
1 reference
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7 January 2021
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Assembly of asparagine-linked oligosaccharides
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Crossref
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https://api.crossref.org/works/10.1016%2FS0167-4838%2801%2900257-6
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0167-4838(01)00257-6
1 reference
stated in
Europe PubMed Central
PubMed publication ID
11690653
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11690653%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 December 2019
PubMed publication ID
11690653
1 reference
stated in
Europe PubMed Central
PubMed publication ID
11690653
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11690653%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 December 2019
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