ライフサイエンスコーパス: dolastatin 10

1 tween cysteine 12 and the thiazole moiety of dolastatin 10.

2 peptides--cryptophycin 1, hemiasterlin, and dolastatin 10.

3 so comparable with the effects observed with dolastatin 10.

4 A previously synthesized unit of dolastatin 10 (1), dolaphenine (Doe, 3), was converted i

5 ion at this site placed the thiazole ring of dolastatin 10 8-9 A from the sulfur atom of cysteine 12.

6 the hemiasterlin aggregate differed from the dolastatin 10 aggregate in that its formation was not as

7 he hemiasterlin aggregate (as opposed to the dolastatin 10 aggregate) did not change greatly when mic

8 s occurs with vinblastine (tight spirals) or dolastatin 10 (aggregated rings and spirals).

9 onjugates consisting of the potent synthetic dolastatin 10 analogs auristatin E (AE) and monomethylau

10 and its analog differ markedly from those of dolastatin 10 and closely resemble the properties of dol

11 e nucleotide, inhibited the binding of [5-3H]dolastatin 10 and cross-link formation more potently tha

12 lin was compared to the reactions induced by dolastatin 10 and cryptophycin 1.

13 maytansine, halichondrin B, and the peptides dolastatin 10 and phomopsin A.

14 rotubule assembly, equivalent in activity to dolastatin 10 and therefore far more potent than dolasta

15 e compared uptake and efflux of radiolabeled dolastatin 10 and vinblastine in human Burkitt lymphoma

16 hibited by probe 1, HTI-286, vinblastine, or dolastatin 10 (another peptide antimitotic agent that de

17 logues of the antineoplastic natural product Dolastatin 10, are ultrapotent cytotoxic microtubule inh

18 s revealed a highly favored binding site for dolastatin 10 at the + end of beta-tubulin in proximity

19 ubulin differing from the vinca alkaloid and dolastatin 10 binding sites, or that diazonamide A and t

20 ace so that it contacts the vinblastine- and dolastatin 10-binding sites believed to be in beta-tubul

21 (tight coils and pinwheels are observed with dolastatin 10 but not with hemiasterlin or cryptophycin

22 Computational docking of an energy-minimized dolastatin 10 conformation at this site placed the thiaz

23 have synthesized eight analogues (D1-D8) of dolastatin 10 containing several unique amino acid subun

24 itol inhibited formation of the beta-tubulin/dolastatin 10 cross-link but not the beta-tubulin/exchan

25 CP1) was compared to the antimitotic peptide dolastatin 10 (D10) as an antiproliferative agent and in

26 ed to drug-free medium, there was no loss of dolastatin 10 for at least 2 h, whereas vinblastine exit

27 Like dolastatin 10, hemiasterlin induced formation of a tubul

28 psipeptides which include the cryptophycins, dolastatin 10, hemiasterlin, and phomopsin A have been f

29 ng site for cryptophycin 1, cryptophycin 52, dolastatin 10, hemiasterlin, and phomopsin A on beta-tub

30 the ability of another antineoplastic drug, dolastatin 10, in inducing Bcl2 phosphorylation and apop

31 Dolastatin 10 is a highly cytotoxic antimitotic peptide

32 An equipotent analog of dolastatin 10, lacking the thiazole ring, did not form a

33 Optimal clinical use of dolastatin 10 may require administration by infusion rat

34 Opacification of tubulin-dolastatin 10 mixtures was inhibited by hemiasterlin at

35 nhibited the binding of [3H]vinblastine, [3H]dolastatin 10, or [8-14C]GTP to tubulin.

36 of 3 and the carboxy terminus dipeptides of dolastatin 10, or the dolastatin 15 analogue cemadotin,

37 The potency of dolastatin 10 probably derives from its tenacious bindin

38 Vinblastine and dolastatin 10 reached maximum intracellular concentratio

39 tubulin rings and promotes the formation of Dolastatin-10 ring stacks, implying that Tau can crossli

40 overlapped more extensively with the docked dolastatin 10 than with each other.

41 oM), competitively inhibiting the binding of dolastatin 10 to tubulin (apparent K(i) value, 2.0 micro

42 Conversely, binding of dolastatin 10 to tubulin inhibited formation of the cros

43 the binding of radiolabeled vinblastine and dolastatin 10 to tubulin.

44 We observed that Tau binds tightly to Dolastatin-10 tubulin rings and promotes the formation o

45 We show that stathmin binds tightly to Dolastatin-10 tubulin rings, which mimic curved tubulin

46 In the Burkitt cells, dolastatin 10 was 20-fold more cytotoxic than vinblastin

47 The accumulation factor observed for dolastatin 10 was 900 to 1800 versus 60 to 100 for vinbl

48 Tubulin with bound [5-3H]dolastatin 10 was exposed to ultraviolet light, and 8-10