ライフサイエンスコーパス: dolastatin

1 the amino terminus tripeptide region of the dolastatins.

2 lationship between the hemiasterlins and the dolastatins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

24 Dolastatin 10 is a highly cytotoxic antimitotic peptide

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

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

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

28 Vinblastine and dolastatin 10 reached maximum intracellular concentratio

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

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

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

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

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

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

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

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

37 Like dolastatin 10, hemiasterlin induced formation of a tubul

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

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

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

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

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

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

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

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

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

47 so comparable with the effects observed with dolastatin 10.

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

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

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

51 n contrast to jasplakinolide and phalloidin, dolastatin 11 did not inhibit the binding of a fluoresce

52 Like jasplakinolide, dolastatin 11 induced the hyperassembly of purified acti

53 ssembly (all are peptides or depsipeptides), dolastatin 11 may interact with actin polymers at a dist

54 nge-derived depsipeptide jasplakinolide, but dolastatin 11 was about 3-fold more cytotoxic than jaspl

55 Dolastatin 11 was qualitatively more active than jasplak

56 e and, in a quantitative assay we developed, dolastatin 11 was twice as active as jasplakinolide and

57 The effects of dolastatin 11 were most similar to those of the sponge-d

58 The successful synthesis of dolastatin 11, a depsipeptide originally isolated from t

59 terminus dipeptides of dolastatin 10, or the dolastatin 15 analogue cemadotin, were synthesized.

60 ration column was equilibrated with both [3H]dolastatin 15 and a second, nonradiolabeled drug.

61 proline (P5), a pentapeptide also present in dolastatin 15 and cemadotin.

62 Dolastatin 15 and cryptophycin 1 could also be docked in

63 idotin, the carboxyl-terminal ester group of dolastatin 15 has been replaced by a carboxy-terminal te

64 ed to gain insight into the binding site for dolastatin 15 on tubulin by studying inhibitory effects

65 56) is a water-soluble synthetic analogue of dolastatin 15 that inhibits cell proliferation in vitro

66 The antimitotic depsipeptide dolastatin 15 was radiolabeled with tritium in its amino

67 istent with the apparent weak interaction of dolastatin 15 with tubulin demonstrated indirectly in th

68 Dolastatin 15, although potently cytotoxic, is a relativ

69 erved with cemadotin, a structural analog of dolastatin 15, and with the depsipeptide cryptophycin 1.

70 ptide analog of the antimitotic depsipeptide dolastatin 15.

71 residue, and a diprolyl group reminiscent of dolastatin 15.

72 statin 10 and therefore far more potent than dolastatin 15.

73 in 10 and closely resemble the properties of dolastatin 15.

74 totoxic agent than tasidotin, cemadotin, and dolastatin 15.

75 rgeted derivative of the marine depsipeptide dolastatin-15, is currently undergoing clinical evaluati

76 The synthesis of dolastatin 18 (2) confirmed the R stereochemistry of the

77 ynthesis of the cancer cell growth inhibitor dolastatin 18 (2, Dhex-(S)-Leu-(R)-N-Me-Phe-Doe).

78 An X-ray crystal structure determination of dolastatin 18 was also completed.

79 d 44.6 nm mean diameter for hemiasterlin and dolastatin, as revealed by electron microscopy on microm

80 hether tubulin oligomers induced by the drug dolastatin could mimic microtubule ends.

81 tween the hemiasterlins and the more complex dolastatins, hybrid compounds composed of 3 and the carb

82 on to binding to the microtubule lattice and dolastatin-induced protofilament-like structures, we dem

83 croscopy, we visualised the kinesin-13 motor-dolastatin-tubulin oligomer interaction in nucleotide st

84 in-13 motor ATPase activity is stimulated by dolastatin-tubulin oligomers, suggesting, first, that th

85 In contrast, the dolastatin-tubulin rings demonstrate an intermediate lev