Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I.
about
The role of poly(ADP-ribose) in the DNA damage signaling networkEffect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics studyRotation of DNA around intact strand in human topoisomerase I implies distinct mechanisms for positive and negative supercoil relaxationStructural and dynamical effects induced by the anticancer drug topotecan on the human topoisomerase I - DNA complexBinding of an Indenoisoquinoline to the topoisomerase-DNA complex induces reduction of linker mobility and strengthening of protein-DNA interactionReplacement of the human topoisomerase linker domain with the plasmodial counterpart renders the enzyme camptothecin resistantMutagenesis analysis of the nsp4 main proteinase reveals determinants of arterivirus replicase polyprotein autoprocessing.Recovery of the poisoned topoisomerase II for DNA religation: coordinated motion of the cleavage core revealed with the microsecond atomistic simulation.Simulations of DNA topoisomerase 1B bound to supercoiled DNA reveal changes in the flexibility pattern of the enzyme and a secondary protein-DNA binding sitePoly(ADP-ribose) reactivates stalled DNA topoisomerase I and Induces DNA strand break resealing.The different cleavage DNA sequence specificity explains the camptothecin resistance of the human topoisomerase I Glu418Lys mutant.Peptide Inhibition of Topoisomerase IB from Plasmodium falciparum.DNA topoisomerase I domain interactions impact enzyme activity and sensitivity to camptothecin.Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin.Construction of a linker library with widely controllable flexibility for fusion protein design.A small organic compound enhances the religation reaction of human topoisomerase I and identifies crucial elements for the religation mechanism.Molecular mechanism of the camptothecin resistance of Glu710Gly topoisomerase IB mutant analyzed in vitro and in silico.Mutation of Gly721 alters DNA topoisomerase I active site architecture and sensitivity to camptothecin.DNA topoisomerases: harnessing and constraining energy to govern chromosome topology.Evidence of the crucial role of the linker domain on the catalytic activity of human topoisomerase I by experimental and simulative characterization of the Lys681Ala mutant.Sequence selectivity of the cleavage sites induced by topoisomerase I inhibitors: a molecular dynamics study.Trypanosomatids topoisomerase re-visited. New structural findings and role in drug discoveryTopoisomerases: Resistance versus Sensitivity, How Far We Can Go?Structural and functional interactions of the prostate cancer suppressor protein NKX3.1 with topoisomerase I.New Topoisomerase I mutations are associated with resistance to camptothecinRole of the linker domain and the 203-214 N-terminal residues in the human topoisomerase I DNA complex dynamics.Disulfide cross-links reveal conserved features of DNA topoisomerase I architecture and a role for the N terminus in clamp closure.Topoisomerase I gene mutations at F270 in the large subunit and N184 in the small subunit contribute to the resistance mechanism of the unicellular parasite Leishmania donovani towards 3,3'-diindolylmethane.A single mutation in the 729 residue modulates human DNA topoisomerase IB DNA binding and drug resistance.Erybraedin C, a natural compound from the plant Bituminaria bituminosa, inhibits both the cleavage and religation activities of human topoisomerase I.The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons.Understanding the role of domain-domain linkers in the spatial orientation of domains in multi-domain proteins.Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains.Subnuclear Localization of Human Topoisomerase I.Substitutions in Spodoptera exigua topoisomerase I modulate its relaxation activity and camptothecin sensitivity.
P2860
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P2860
Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Single mutation in the linker ...... ance to human topoisomerase I.
@en
type
label
Single mutation in the linker ...... ance to human topoisomerase I.
@en
prefLabel
Single mutation in the linker ...... ance to human topoisomerase I.
@en
P2860
P50
P356
P1476
Single mutation in the linker ...... ance to human topoisomerase I.
@en
P2093
Paola Fiorani
Piero Benedetti
P2860
P304
43268-43275
P356
10.1074/JBC.M303899200
P407
P577
2003-08-06T00:00:00Z