Search Results - "Bidwai, A.P"
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Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II
Published in The Journal of biological chemistry (08-07-1994)“…Casein kinase II of Saccharomyces cerevisiae is composed of two distinct catalytic subunits, alpha and alpha', and two distinct regulatory subunits, beta and…”
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Casein kinase II of Saccharomyces cerevisiae contains two distinct regulatory subunits, beta and beta
Published in Archives of biochemistry and biophysics (01-03-1994)“…The subunit composition of casein kinase II (CKII) from S. cerevisiae has been difficult to define, particularly with respect to the existence and number of…”
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3
Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo
Published in The Journal of biological chemistry (15-09-1992)“…Casein kinase II (CKII) is composed of a catalytic (alpha) and a regulatory (beta) subunit which unite to form an alpha 2 beta 2 holoenzyme. Saccharomyces…”
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4
Phosphorylation of calmodulin by the catalytic subunit of casein kinase II is inhibited by the regulatory subunit
Published in Archives of biochemistry and biophysics (01-01-1993)“…Casein kinase II (CKII) is composed of a catalytic subunit (alpha) and a regulatory subunit (beta) that combine to form an alpha 2 beta 2 holoenzyme. The…”
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5
Bacterial phytotoxin, syringomycin, induces a protein kinase-mediated phosphorylation of red beet plasma membrane polypeptides
Published in Proceedings of the National Academy of Sciences - PNAS (01-10-1987)“…Syringomycin, a peptide toxin and a virulence factor produced by the bacterial phytopathogen Pseudomonas syringae pv. syringae, stimulated the phosphorylation…”
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Studies on the active site of the Neurospora crassa plasma membrane H+-ATPase with periodate-oxidized nucleotides
Published in The Journal of biological chemistry (15-07-1989)“…The Neurospora crassa plasma membrane H+-ATPase is inactivated by the periodate-oxidized nucleotides, oATP, oADP, and oAMP, with oAMP the most effective…”
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