Characterisation of the DNA-dependent ATPase activity of human DNA topoisomerase IIbeta: mutation of Ser165 in the ATPase domain reduces the ATPase activity and abolishes the in vivo complementation ability.
about
Structure of a topoisomerase II–DNA–nucleotide complex reveals a new control mechanism for ATPase activityThe impact of the human DNA topoisomerase II C-terminal domain on activity.Catalytic inhibition of topoisomerase II by a novel rationally designed ATP-competitive purine analogueNitric oxide inhibits ATPase activity and induces resistance to topoisomerase II-poisons in human MCF-7 breast tumor cells.Selectable high-yield recombinant protein production in human cells using a GFP/YFP nanobody affinity support.Post-translational modifications in DNA topoisomerase 2α highlight the role of a eukaryote-specific residue in the ATPase domain.
P2860
Characterisation of the DNA-dependent ATPase activity of human DNA topoisomerase IIbeta: mutation of Ser165 in the ATPase domain reduces the ATPase activity and abolishes the in vivo complementation ability.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
@zh-my
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2002年學術文章
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name
Characterisation of the DNA-de ...... vivo complementation ability.
@en
Characterisation of the DNA-de ...... vivo complementation ability.
@nl
type
label
Characterisation of the DNA-de ...... vivo complementation ability.
@en
Characterisation of the DNA-de ...... vivo complementation ability.
@nl
prefLabel
Characterisation of the DNA-de ...... vivo complementation ability.
@en
Characterisation of the DNA-de ...... vivo complementation ability.
@nl
P2093
P2860
P356
P1476
Characterisation of the DNA-de ...... vivo complementation ability.
@en
P2093
Caroline A Austin
Elaine Willmore
Jeremy H Lakey
Katherine L West
Rosalind M Turnbull
P2860
P304
P356
10.1093/NAR/GKF677
P407
P577
2002-12-01T00:00:00Z