ライフサイエンスコーパス: m-AMSA

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1 reases in sensitivity to the antitumor agent m-AMSA [4'-(9-acridinylamino)methanesulfon-m-anisidide]

2 ubunit) causes resistance to antitumor agent m-AMSA but hypersensitivity to the quinolone oxolinic ac

3 is the major target for the antitumour agent m-AMSA (4'-(9-acridinylamino)methanesulphonm-ansidide) i

4 to the DNA intercalating anti-tumour agents m-AMSA and ellipticine, but confer resistance to the non

5 9-acridinylamino)methanesulphon-m-anisidide (m-AMSA) stabilizes the T4 type II topoisomerase at the s

6 (9-acridinylamino)methanesulfon-m-anisidide (m-AMSA)-resistant bacteriophage T4 topoisomerases have p

7 -cleaving subunit) causes resistance to both m-AMSA and oxolinic acid.

8 Inhibition of the purified enzyme by m-AMSA results in formation of a cleavage complex that c

9 antitumor drugs such as VM-26, doxorubicin, m-AMSA, and mitoxantrone.

10 Finally, m-AMSA induced the production of cleavage complexes invo

11 ep in the recombinational repair pathway for m-AMSA-induced damage.

12 These agents included m-AMSA (4'-(9-acridinylamino)methanesulfon-m-anisidide),

13 er of cleavage-inducing inhibitors including m-AMSA, VP-16, mitoxantrone, ellipticine, and oxolinic a

14 opoisomerase II poisons such as etoposide or m-AMSA which require micromolar concentrations to elicit

15 The resulting m-AMSA-dependent repair products do not form in the abse

16 n to be resistant to m-AMSA, indicating that m-AMSA inhibits growth by inducing the cleavage complex

17 Second, the m-AMSA sensitivity of the rnh-deletion mutant was shown

18 Third, m-AMSA stimulated recombination in phage-infected bacter

19 ce of Rnh protein causes hypersensitivity to m-AMSA.

20 icient mutants were shown to be resistant to m-AMSA, indicating that m-AMSA inhibits growth by induci

21 The substitutions alter sensitivity to m-AMSA and to oxolinic acid, sometimes in opposite direc

22 59) increased the sensitivity of phage T4 to m-AMSA, strongly suggesting that recombination participa

23 shown to confer hypersensitivity in vivo to m-AMSA and oxolinic acid.

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