Jin, Y Yu, J Yu, YG 2024-01-21T11:10:01Z 2024-01-21T11:10:01Z 2021-09-04 2002-02 1074-5521 https://pubs.kist.re.kr/handle/201004/139836 Doxorubicin is a widely used anti-cancer drug. It is assumed to act by inhibiting DNA replication or transcription, although its precise targets and mechanism of cytotoxicity remain unresolved. A T7 phage library expressing human liver cDNA was screened against immobilized doxorubicin to isolate doxorubicin binding proteins. The selected phage contained the C-terminal region of nucleolar phosphoprotein hNopp140, an important factor in the biogenesis of the nucleolus. When the cloned sequence was expressed in E. coli, the recombinant protein was phosphorylated by casein kinase II and oligomerized in the presence of magnesium and fluoride ions, as occurs in vivo. Doxorubicin bound to the expressed protein with a dissociation constant of 4.5 X 10(-6) M, and this interaction was inhibited by the phosphorylation of hNopp140. These results suggested that doxorubicin might disrupt the cellular function of hNopp140. English CELL PRESS COMBINATORIAL PEPTIDE LIBRARIES NUCLEOLAR PHOSPHOPROTEIN CDNA LIBRARIES ADRIAMYCIN PROTEIN DNA RECEPTOR NOPP140 CELLS BACTERIOPHAGE Identification of hNopp140 as a binding partner for doxorubicin with a phage display cloning method Article 10.1016/S1074-5521(02)00096-0 1 CHEMISTRY & BIOLOGY, v.9, no.2, pp.157 - 162 CHEMISTRY & BIOLOGY 9 2 157 162 scie scopus 000174098200003 2-s2.0-0036008842 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article COMBINATORIAL PEPTIDE LIBRARIES NUCLEOLAR PHOSPHOPROTEIN CDNA LIBRARIES ADRIAMYCIN PROTEIN DNA RECEPTOR NOPP140 CELLS BACTERIOPHAGE chemical geuomics