Zobrazeno 1 - 10
of 60
pro vyhledávání: '"C B, Klee"'
Autor:
C. B. Klee, Jun O. Liu, Stuart L. Schreiber, Mark W. Albers, Thomas J. Wandless, Philip Cohen, D. G. Alberg, Sheng Luan, Carol MacKintosh, Peter J. Belshaw
Publikováno v:
Scopus-Elsevier
Calcineurin, a Ca2+, calmodulin-dependent protein phosphatase, was recently found to bind with high affinity to two different immunosuppressant binding proteins (immunophilins) with absolute dependence on the presence of the immunosuppressants FK506
Publikováno v:
Journal of Biological Chemistry. 267:5286-5295
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:
Nature structural biology. 8(11)
The solution structure of Ca(2+)-ligated calmodulin is determined from residual dipolar couplings measured in a liquid crystalline medium and from a large number of heteronuclear J couplings for defining side chains. Although the C-terminal domain so
Publikováno v:
Current topics in cellular regulation. 36
Publikováno v:
Cytogenetics and cell genetics. 72(2-3)
Calcineurin (also called protein phosphatase-2B) is a calmodulin-regulated protein phosphatase which plays an important role in signal transduction. The enzyme is a heterodimer of a 58–59 kDa calmodulin-binding catalytic subunit (calcineurin A) and
Publikováno v:
Biochemistry. 33(12)
The calmodulin- and calcium-stimulated protein phosphatase calcineurin, PP2B, consists of two subunits: calcineurin B, which binds Ca2+, and calcineurin A, which contains the catalytic site and a calmodulin binding site. Heteronuclear 3D and 4D NMR e
Publikováno v:
Journal of neurochemistry. 60(5)
The distribution of a novel calcium-binding protein with a molecular mass of 18 kDa (CBP-18) in the rat brain was studied by means of biochemical methods and immunohistochemistry on cryostat-sectioned tissue and compared with staining patterns of par
Publikováno v:
The Journal of biological chemistry. 267(31)
Genomic clones containing the full coding sequences of the two subunits of the Ca2+/calmodulin-stimulated protein phosphatase, calcineurin, were isolated from a Drosophila melanogaster genomic library using highly conserved human cDNA probes. Three c
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