The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

FUT6  -  fucosyltransferase 6 (alpha (1,3)...

Bos taurus

Synonyms: FUT, FUT3, FUT5, FUTB
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of FUT

 

High impact information on FUT

  • In contrast, substitution of Arg115 in bovine futb-encoded alpha1, 3-fucosyltransferase (Fuc-Tb) by Trp generated a protein unable to transfer fucose either on H-type 1 or H-type 2 acceptors [3].
  • Complete genomic organization of futb encoding a bovine alpha 3-fucosyltransferase: exons in human orthologous genes emerged from ancestral intronic sequences [4].
  • This organization suggests that duplication events that have generated the primate FUT3-FUT5-FUT6 cluster might have occurred through a long-interspersed-nuclear-element-based mechanism of unequal crossing over, as described for the globin cluster [4].
  • Determination of GDP-Fuc:Gal beta 1-4GlcNAc-R (Fuc to GlcNAc) alpha 1,3 fucosyltransferase activity by a solid-phase method [5].
 

Analytical, diagnostic and therapeutic context of FUT

  • 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 [6].
  • Only one bovine gene, corresponding to the human cluster of genes FUT3-FUT5-FUT6, was found by Southern blot analysis [6].

References

  1. Ovarian cancer alpha 1,3-L-fucosyltransferase. Differentiation of distinct catalytic species with the unique substrate, 3'-sulfo-N-acetyllactosamine in conjunction with other synthetic acceptors. Chandrasekaran, E.V., Jain, R.K., Matta, K.L. J. Biol. Chem. (1992) [Pubmed]
  2. Lewis X structure increases cell substratum adhesion in L cells. Sudou, A., Ozawa, M., Muramatsu, T. J. Biochem. (1995) [Pubmed]
  3. A single amino acid in the hypervariable stem domain of vertebrate alpha1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer. Characterization of acceptor substrate specificity of the lewis enzyme by site-directed mutagenesis. Dupuy, F., Petit, J.M., Mollicone, R., Oriol, R., Julien, R., Maftah, A. J. Biol. Chem. (1999) [Pubmed]
  4. Complete genomic organization of futb encoding a bovine alpha 3-fucosyltransferase: exons in human orthologous genes emerged from ancestral intronic sequences. Wierinckx, A., Mercier, D., Oulmouden, A., Petit, J.M., Julien, R. Mol. Biol. Evol. (1999) [Pubmed]
  5. Determination of GDP-Fuc:Gal beta 1-4GlcNAc-R (Fuc to GlcNAc) alpha 1,3 fucosyltransferase activity by a solid-phase method. Yan, L., Smith, D.F., Cummings, R.D. Anal. Biochem. (1994) [Pubmed]
  6. 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. Oulmouden, A., Wierinckx, A., Petit, J.M., Costache, M., Palcic, M.M., Mollicone, R., Oriol, R., Julien, R. J. Biol. Chem. (1997) [Pubmed]
 
WikiGenes - Universities