Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Claude B. Klee"'
Autor:
Ernesto Carafoli, Claude B. Klee
Publikováno v:
Biochemical and biophysical research communications. 467(4)
Autor:
Charles R. Manclark, Claude B. Klee, Steven A. Berkowitz, G. Hope Cook, Erik L. Hewlett, Alan R. Goldhammer, J. Wolff
Publikováno v:
European Journal of Biochemistry. 115:605-609
A variety of proteins and tissue preparations (rabbit erythrocyte lysate, catalase, peroxidase, creatine phosphokinase, and lima bean trypsin inhibitor) contain protein activator(s) of the extracellular adenylate cyclase of intact Bordetella pertussi
Publikováno v:
Journal of Biological Chemistry. 278:29261-29266
Edema factor (EF), a toxin from Bacillus anthracis (anthrax), possesses adenylyl cyclase activity and requires the ubiquitous Ca2+-sensor calmodulin (CaM) for activity. CaM can exist in three major structural states: an apo state with no Ca2+ bound,
Autor:
Claude B. Klee, Anthony R. Means
Publikováno v:
EMBO reports. 3:823-827
The 12th International Symposium on Calcium‐Binding Proteins and Calcium Function in Helth and Disease was held in February, 2002, in Cavalese, Italy. The 4‐day meeting consisted of nearly 60 plenary presentations and over 180 posters. ![][1] Our
Publikováno v:
Nature Structural Biology. 8:990-997
The solution structure of Ca2+-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 solu
Autor:
Claude B. Klee, Seun-Ah Yang
Publikováno v:
Biochemistry. 39:16147-16154
Limited proteolysis of calcineurin in the presence of Ca(2+) suggested that its calmodulin-binding domain, readily degraded by proteases, was unfolded while calcineurin B was compactly folded [Hubbard, M. J., and Klee, C. B. (1989) Biochemistry 28, 1
Publikováno v:
Methods. 9:146-154
The calmodulin-dependent phosphatase calcineurin is an important molecular target of the immunosuppressive drugs cyclosporin A (CsA) and FK506. Complexes of CsA and FK506 with their immunophilin ligands interact with calcineurin in vitro, resulting i
Publikováno v:
FEBS Letters. 374:237-240
The Ca2+-dependent protein phosphatase activity of crude rat brain extracts measured in the presence of okadaic acid, exhibits the characteristic properties of the calmodulin-stimulated protein phosphatase, calcineurin. It is stimulated more than 200
Autor:
Paul M. Stemmer, Claude B. Klee
Publikováno v:
Biochemistry. 33:6859-6866
The dependence of calcineurin on Ca2+ for activity is the result of the concerted action of calmodulin, which increases the turnover rate of the enzyme and modulates its response to Ca2+ transients, and of calcineurin B, which decreases the Km of the