PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9048573-12 1997 The Kcat thio effects [Kcat(ATP)/Kcat(ATP gamma S)] were inversely correlated with metal thiophilicity in both wild-type and D314E mutant Csk reactions, although the relationship was less pronounced in the latter. Metals 83-88 C-terminal Src kinase Homo sapiens 138-141 11162381-0 2001 Affinity purification of Csk protein tyrosine kinase based on its catalytic requirement for divalent metal cations. Metals 101-106 C-terminal Src kinase Homo sapiens 25-28 10220355-0 1999 Substitution studies of the second divalent metal cation requirement of protein tyrosine kinase CSK. Metals 44-49 C-terminal Src kinase Homo sapiens 96-99 10220355-4 1999 In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+. Metals 47-52 C-terminal Src kinase Homo sapiens 137-140 10220355-6 1999 Substitution by these divalent metal cations resulted in varied levels of Csk activity, with Mn2+ even more effective than Mg2+. Metals 31-36 C-terminal Src kinase Homo sapiens 74-77 10220355-11 1999 These results suggest that the divalent metal activator is an important element in determining the affinity between Csk and the phosphate-accepting substrate. Metals 40-45 C-terminal Src kinase Homo sapiens 116-119 17149882-3 2006 Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase. Metals 68-73 C-terminal Src kinase Homo sapiens 102-123 17149882-3 2006 Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase. Metals 68-73 C-terminal Src kinase Homo sapiens 125-128 17149882-5 2006 Four classes of phenylalanine and tyrosine hydroxamate derivatives were synthesized and evaluated as metal-mediated inhibitors of Csk, leading to improved inhibition and a better understanding of the structure-activity relationships. Metals 101-106 C-terminal Src kinase Homo sapiens 130-133