FUT5

FUT5

Fucosyltransferase 5 (alpha (1,3) fucosyltransferase), also known as FUT5, is a human gene.cite web | title = Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2527| accessdate = ]

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*cite journal | author=Chiu PC, Chung MK, Koistinen R, "et al." |title=Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding. |journal=J. Cell. Sci. |volume=120 |issue= Pt 1 |pages= 33–44 |year= 2007 |pmid= 17148576 |doi= 10.1242/jcs.03258
*cite journal | author=Inaba Y, Ohyama C, Kato T, "et al." |title=Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells. |journal=Int. J. Cancer |volume=107 |issue= 6 |pages= 949–57 |year= 2004 |pmid= 14601054 |doi= 10.1002/ijc.11513
*cite journal | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168–75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200
*cite journal | author=Nishihara S, Iwasaki H, Kaneko M, "et al." |title=Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue. |journal=FEBS Lett. |volume=462 |issue= 3 |pages= 289–94 |year= 2000 |pmid= 10622713 |doi=
*cite journal | author=McCurley RS, Recinos A, Olsen AS, "et al." |title=Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21. |journal=Genomics |volume=26 |issue= 1 |pages= 142–6 |year= 1995 |pmid= 7782074 |doi=
*cite journal | author=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112–22 |year= 1995 |pmid= 7650030 |doi=
*cite journal | author=Weston BW, Nair RP, Larsen RD, Lowe JB |title=Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. |journal=J. Biol. Chem. |volume=267 |issue= 6 |pages= 4152–60 |year= 1992 |pmid= 1740457 |doi=
*cite journal | author=Weston BW, Smith PL, Kelly RJ, Lowe JB |title=Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24575–84 |year= 1992 |pmid= 1339443 |doi=

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