Zobrazeno 1 - 10
of 33
pro vyhledávání: '"I. H. Goldberg"'
Publikováno v:
The Journal of biological chemistry. 269(6)
DNA damage in HeLa nuclei and isolated nucleosome core particles has been examined for several members of the enediyne family of antitumor antibiotics: calicheamicin gamma 1I (CAL), esperamicin A1 (ESP A1), esperamicin C (ESP C), and neocarzinostatin
Publikováno v:
Biochemistry. 31(38)
Glutathione-activated neocarzinostatin chromophore (NCS-Chrom) generates bistranded lesions at AGC.GCT sequences in DNA, consisting of an abasic site at the C residue and a strand break at the T residue on the complementary strand, due to hydrogen at
Autor:
P C, Dedon, I H, Goldberg
Publikováno v:
The Journal of biological chemistry. 265(25)
Direct double-strand breaks in DNA have been implicated in cellular lethality of the antitumor antibiotic neocarzinostatin, but the mechanism of their formation has not been elucidated. Evidence is presented that neocarzinostatin causes sequence-spec
Publikováno v:
Journal of the American Chemical Society. 84:430-440
Autor:
S H, Lee, I H, Goldberg
Publikováno v:
Molecular pharmacology. 33(4)
To determine the role of the epoxide moiety of the nonprotein chromophore of the antitumor antibiotic neocarzinostatin in its ability to damage DNA, the diol monomethyl ether derivative was prepared, and its stability and biological properties were s
Publikováno v:
Drugs under experimental and clinical research. 12(6-7)
Neocarzinostatin (NCS) belongs to a family of antitumour protein antibiotics that selectively inhibit DNA synthesis. Replicon initiation in mammalian cells is selectively inhibited by NCS, and cells defective in DNA repair, such as ataxia telangiecta
Publikováno v:
Basic life sciences. 49
Autor:
I H, Goldberg
Publikováno v:
Basic life sciences. 38
Publikováno v:
The Journal of biological chemistry. 255(8)
Reaction of the antitumor protein neocarzinostatin with 1,2-cyclohexanedione in 0.25 M borate buffer, pH 9.0, resulted in complete modification of arginine residues in positions 66, 67, and 78. The arginine-modified protein lost its native structure
Publikováno v:
Molecular biology, biochemistry, and biophysics. 32