Zobrazeno 1 - 8
of 8
pro vyhledávání: '"J F, Maune"'
Publikováno v:
Plant biology (Stuttgart, Germany). 14(4)
Wild potatoes are native to the Americas, where they present very wide geographical and ecological distribution. Most are diploid, obligate out-crossers due to a multiallelic gametophytic self-incompatibility (S) locus that prevents self-fertilisatio
Meiotic abnormalities underlying pollen sterility in wild potato hybrids and spontaneous populations
Publikováno v:
Plant biology (Stuttgart, Germany). 14(1)
Wild potato species are widely distributed in the Americas, where they spontaneously grow in very diverse habitats. These species - with low chromosome differentiation - form polyploid series with 2n = 2x, 3x, 4x and 6x (x =12). They are isolated in
Publikováno v:
Protein science : a publication of the Protein Society. 5(3)
We have generated mutants of Drosophila calmodulin in which pairs of calcium-binding sites are mutated so as to prevent calcium binding. In all sites, the mutation involves replacement of the -Z position glutamate residue with glutamine. Mutants inac
Autor:
Z H, Gao, J, Krebs, M F, VanBerkum, W J, Tang, J F, Maune, A R, Means, J T, Stull, K, Beckingham
Publikováno v:
The Journal of biological chemistry. 268(27)
Activation of four target enzymes by two series of calmodulin Ca2+ binding site mutants has been examined. In each mutant, the conserved bidentate glutamate of one of the Ca2+ binding sites is mutated to glutamine or lysine. The enzymes studied were
Publikováno v:
Biochemistry. 31(34)
The Ca(2+)-induced structural changes in mutant calmodulins from Drosophila melanogaster have been studied by circular dichroism. The proteins comprise eight site-specific mutants, in which a bidentate glutamic acid (at position 12 in each Ca2+ bindi
Publikováno v:
The Journal of biological chemistry. 267(8)
Two series of site-directed mutations to the individual Ca(2+)-binding sites of Drosophila melanogaster calmodulin have been generated and studied. In each mutant, a conserved glutamic acid residue at position 12 in all of the Ca(2+)-binding loops ha
Publikováno v:
The Journal of biological chemistry. 266(32)
The crystal structure of calmodulin (Mr 16,700, 148 residues) from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution. Starting with the structure of mammalian calmodulin, we produced an ext
Publikováno v:
Methods in enzymology. 139