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The most typical plant glycosyltransferase, the β1,2 xylosyltransferase from A. thaliana, is analyzed in this study. The authors identified a Golgi-retention determinant that is sufficient to localize a protein specifically to the medial cisternae of Golgi. This study provides the first detailed characterization of a plant glycosyltransferase at the molecular level.
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The authors describe the simultaneous expression of human collagen I and proline-4-hydroxylase. Their results demonstrate that it is possible to engineer the proline hydroxylation pathway to provide increased quality and conformity of recombinant collagen in plants.
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Merle C., Perret S., Lacour T., Jonval V., Hudaverdian S., Garrone R., Ruggiero F., Theisen M. Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant. FEBS Lett. 515:2002;114-118 The authors describe the simultaneous expression of human collagen I and proline-4-hydroxylase. Their results demonstrate that it is possible to engineer the proline hydroxylation pathway to provide increased quality and conformity of recombinant collagen in plants.
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