(Q38333345)

English

Human alpha1,3/4-fucosyltransferases. III. A Lys/Arg residue located within the alpha1,3-FucT motif is required for activity but not substrate binding

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

Human alpha1,3/4-fucosyltransferases. III. A Lys/Arg residue located within the alpha1,3-FucT motif is required for activity but not substrate binding (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

author name string

Sherwood AL

1

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Europe PubMed Central

PubMed publication ID

2 September 2017

Nguyen AT

2

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Whitaker JM

3

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Macher BA

4

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Stroud MR

5

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Holmes EH

6

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Europe PubMed Central

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2 September 2017

language of work or name

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publication date

1 September 1998

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Europe PubMed Central

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2 September 2017

number of pages

5

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Journal of Biological Chemistry

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Europe PubMed Central

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2 September 2017

273

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Europe PubMed Central

PubMed publication ID

2 September 2017

39

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

25256-25260

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase

1 reference

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21 January 2018

ELFT: a gene that directs the expression of an ELAM-1 ligand

1 reference

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21 January 2018

The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand

1 reference

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21 January 2018

Identification of Dictyostelium G alpha genes expressed during multicellular development

1 reference

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21 January 2018

Molecular cloning, expression, chromosomal assignment, and tissue-specific expression of a murine alpha-(1,3)-fucosyltransferase locus corresponding to the human ELAM-1 ligand fucosyl transferase.

1 reference

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21 January 2018

Expression of the alpha(1,3)fucosyltransferase Fuc-TVII in lymphoid aggregate high endothelial venules correlates with expression of L-selectin ligands

1 reference

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21 January 2018

Molecular cloning and expression of a mouse alpha-1,3 fucosyltransferase gene that shows homology with the human alpha-1,3 fucosyltransferase IV gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.39.25256

21 January 2018

Molecular cloning and expression of a bovine alpha(1,3)-fucosyltransferase gene homologous to a putative ancestor gene of the human FUT3-FUT5-FUT6 cluster

1 reference

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21 January 2018

Molecular cloning and characterization of CFT1, a developmentally regulated avian alpha(1,3)-fucosyltransferase gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.39.25256

21 January 2018

Lewis X biosynthesis in Helicobacter pylori. Molecular cloning of an alpha(1,3)-fucosyltransferase gene

1 reference

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21 January 2018

Cloning and heterologous expression of an alpha1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori

1 reference

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21 January 2018

Presence of an essential lysine residue in a GDP-fucose protected site of the alpha 1----3fucosyltransferase from human small cell lung carcinoma NCl-H69 cells

1 reference

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21 January 2018

Structure-function analysis of human alpha 1-->3fucosyltransferases. A GDP-fucose-protected, N-ethylmaleimide-sensitive site in FucT-III and FucT-V corresponds to Ser178 in FucT-IV.

1 reference

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21 January 2018

Fucosylation of complex glycosphingolipids by recombinant fucosyltransferase-VII.

1 reference

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21 January 2018

Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals

1 reference

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21 January 2018

Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzi

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.39.25256

21 January 2018

Human alpha(1,3/1,4)-fucosyltransferases discriminate between different oligosaccharide acceptor substrates through a discrete peptide fragment

1 reference

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21 January 2018

Structure-function analysis of human alpha1,3-fucosyltransferase. Amino acids involved in acceptor substrate specificity

1 reference

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21 January 2018

A missense mutation in the FUT6 gene results in total absence of alpha3-fucosylation of human alpha1-acid glycoprotein

1 reference

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21 January 2018

Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels

1 reference

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21 January 2018

Chemical modification of an alpha 3-fucosyltransferase; definition of amino acid residues essential for enzyme activity

1 reference

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21 January 2018

Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.39.25256

21 January 2018

Human alpha1,3/4-fucosyltransferases. I. Identification of amino acids involved in acceptor substrate binding by site-directed mutagenesis

1 reference

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21 January 2018

Cloning of a rat alpha1,3-fucosyltransferase gene: a member of the fucosyltransferase IV family

1 reference

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21 January 2018

Human alpha1,3/4-fucosyltransferases. II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties

1 reference

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21 January 2018

Identifiers

10.1074/JBC.273.39.25256

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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