Dual DNA topoisomerase 1 and tyrosyl-DNA phosphodiesterase 1 inhibition for improved anticancer activity

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Dual DNA topoisomerase 1 and tyrosyl-DNA phosphodiesterase 1 inhibition for improved anticancer activity. / Zakharenko, Alexandra; Dyrkheeva, Nadezhda; Lavrik, Olga.

In: Medicinal Research Reviews, Vol. 39, No. 4, 01.07.2019, p. 1427-1441.

Research output: Contribution to journal › Review article › peer-review

Author

Zakharenko, Alexandra ; Dyrkheeva, Nadezhda ; Lavrik, Olga. / Dual DNA topoisomerase 1 and tyrosyl-DNA phosphodiesterase 1 inhibition for improved anticancer activity. In: Medicinal Research Reviews. 2019 ; Vol. 39, No. 4. pp. 1427-1441.

BibTeX

@article{0b17e0af9b854a3a896be111f220e28a,

title = "Dual DNA topoisomerase 1 and tyrosyl-DNA phosphodiesterase 1 inhibition for improved anticancer activity",

abstract = "Tyrosyl-DNA phosphodiesterase 1 (Tdp1) is a DNA repair enzyme that catalyzes the hydrolysis of the phosphodiester bond in the DNA-topoisomerase 1 (Top1) covalent complex and repairs some other 3′-end DNA adducts. Currently, Tdp1 functions as an important target in cancer drug design owing to its ability to break down various DNA adducts induced by chemotherapeutics. Tdp1 inhibitors may sensitize tumor cells to the action of Top1 poisons, thereby potentiating their effects. This mini-review summarizes findings from studies reporting the combined inhibition of Top1 and Tdp1. Two different approaches have been considered for developing such drug precursors.",

keywords = "Tdp1 inhibitors, Top1 poisons, topoisomerase 1, tyrosyl-DNA phosphodiesterase 1 (Tdp1), tyrosyl-DNA phosphodiesterase 2",

author = "Alexandra Zakharenko and Nadezhda Dyrkheeva and Olga Lavrik",

note = "Publisher Copyright: {\textcopyright} 2019 Wiley Periodicals, Inc.",

year = "2019",

month = jul,

day = "1",

doi = "10.1002/med.21587",

language = "English",

volume = "39",

pages = "1427--1441",

journal = "Medicinal Research Reviews",

issn = "0198-6325",

publisher = "John Wiley and Sons Inc.",

number = "4",

}

RIS

TY - JOUR

T1 - Dual DNA topoisomerase 1 and tyrosyl-DNA phosphodiesterase 1 inhibition for improved anticancer activity

AU - Zakharenko, Alexandra

AU - Dyrkheeva, Nadezhda

AU - Lavrik, Olga

PY - 2019/7/1

Y1 - 2019/7/1

N2 - Tyrosyl-DNA phosphodiesterase 1 (Tdp1) is a DNA repair enzyme that catalyzes the hydrolysis of the phosphodiester bond in the DNA-topoisomerase 1 (Top1) covalent complex and repairs some other 3′-end DNA adducts. Currently, Tdp1 functions as an important target in cancer drug design owing to its ability to break down various DNA adducts induced by chemotherapeutics. Tdp1 inhibitors may sensitize tumor cells to the action of Top1 poisons, thereby potentiating their effects. This mini-review summarizes findings from studies reporting the combined inhibition of Top1 and Tdp1. Two different approaches have been considered for developing such drug precursors.

AB - Tyrosyl-DNA phosphodiesterase 1 (Tdp1) is a DNA repair enzyme that catalyzes the hydrolysis of the phosphodiester bond in the DNA-topoisomerase 1 (Top1) covalent complex and repairs some other 3′-end DNA adducts. Currently, Tdp1 functions as an important target in cancer drug design owing to its ability to break down various DNA adducts induced by chemotherapeutics. Tdp1 inhibitors may sensitize tumor cells to the action of Top1 poisons, thereby potentiating their effects. This mini-review summarizes findings from studies reporting the combined inhibition of Top1 and Tdp1. Two different approaches have been considered for developing such drug precursors.

KW - Tdp1 inhibitors

KW - Top1 poisons

KW - topoisomerase 1

KW - tyrosyl-DNA phosphodiesterase 1 (Tdp1)

KW - tyrosyl-DNA phosphodiesterase 2

UR - http://www.scopus.com/inward/record.url?scp=85067282004&partnerID=8YFLogxK

U2 - 10.1002/med.21587

DO - 10.1002/med.21587

M3 - Review article

C2 - 31004352

AN - SCOPUS:85067282004

VL - 39

SP - 1427

EP - 1441

JO - Medicinal Research Reviews

JF - Medicinal Research Reviews

SN - 0198-6325

IS - 4

ER -

ID: 20589234