ライフサイエンスコーパス: cryptophycin

1 acids was synthesized and incorporated into cryptophycins.

2 ecame the C16 hydroxyl and C1' methyl of the cryptophycins.

3 The antimitotic depsipeptide cryptophycin 1 (CP1) was compared to the antimitotic pep

4 of about 40 nm, while the morphology of the cryptophycin 1 aggregate consisted primarily of smaller

5 At picomolar concentrations, cryptophycin 1 blocks cells in the G2/M phase of the cel

6 crotubules, perhaps in the form of a tubulin-cryptophycin 1 complex, resulting in the most potent sup

7 Dolastatin 15 and cryptophycin 1 could also be docked into positions that

8 The results suggest that cryptophycin 1 exerts its antiproliferative and antimito

9 Cryptophycin 1 is a remarkably potent antiproliferative

10 video microscopy, we examined the effects of cryptophycin 1 on the dynamics of individual microtubule

11 absence of net microtubule depolymerization, cryptophycin 1 potently stabilized microtubule dynamics.

12 grees C and stimulated at 0 degrees C, while cryptophycin 1 was inhibitory at both reaction temperatu

13 h dolastatin 10 but not with hemiasterlin or cryptophycin 1).

14 Cryptophycin 52 is a synthetic derivative of Cryptophycin 1, a potent antimicrotubule agent isolated

15 r docking studies, a common binding site for cryptophycin 1, cryptophycin 52, dolastatin 10, hemiaste

16 rs with three vinca domain-binding peptides--cryptophycin 1, hemiasterlin, and dolastatin 10.

17 of dolastatin 15, and with the depsipeptide cryptophycin 1.

18 o the reactions induced by dolastatin 10 and cryptophycin 1.

19 Cryptophycin-1 is the parent compound of a group of cycl

20 group into cryptophycin-4 (Cr-4) to produce cryptophycin-2 (Cr-2) in a regio- and stereospecific man

21 Epoxidation provided cryptophycin-24 (arenastatin A).

22 esults demonstrated that the 4'-MeO group in cryptophycin-24 is not essential and can be replaced wit

23 '-Cl, 4'-C1, and 3',4'-diCl C10 analogues of cryptophycin-24 were prepared via total synthesis and te

24 Substitution of the 4'-MeO group in cryptophycin-24 with a 4'-C1 moiety did not significantl

25 pi-C3-cryptophycin-24, epi-C3-m-chlorobenzyl-cryptophycin-24, and the corresponding styrenes were syn

26 Epi-C3-cryptophycin-24, epi-C3-m-chlorobenzyl-cryptophycin-24,

27 vity was very similar to the parent compound cryptophycin-24.

28 ccessfully applied to the total synthesis of cryptophycin-24.

29 wn to install this key functional group into cryptophycin-4 (Cr-4) to produce cryptophycin-2 (Cr-2) i

30 A synthesis of cryptophycin 52 (2) is reported using a Sharpless asymme

31 enantioselective and convergent synthesis of cryptophycin 52 (2), an exceedingly potent cytotoxic age

32 These Cryptophycin 52 analogues were accessed using a Wittig o

33 Cryptophycin 52 is a synthetic derivative of Cryptophyci

34 e analogues were equally or more potent than Cryptophycin 52 when evaluated in vitro in the CCRF-CEM

35 Cryptophycin 52, a synthetic variant of the cryptophycin

36 s, a common binding site for cryptophycin 1, cryptophycin 52, dolastatin 10, hemiasterlin, and phomop

37 C(50) = 54 pM, only 2-fold less than that of Cryptophycin-52 (3).

38 Cryptophycin-52 (LY355703) is a new synthetic member of

39 Cryptophycin-52 (LY355703) is currently undergoing clini

40 Conformational analysis of cryptophycin-52 and two synthetic analogues was performe

41 Cryptophycin-52 appears to be the most potent suppressor

42 Cryptophycin-52 became concentrated in cells 730-fold, a

43 high concentrations (>/=10 times the IC50), cryptophycin-52 blocked HeLa cell proliferation at mitos

44 termined that approximately 5-6 molecules of cryptophycin-52 bound to a microtubule were sufficient t

45 ls 730-fold, and the resulting intracellular cryptophycin-52 concentration was similar to that requir

46 However, we could remove [(3)H]cryptophycin-52 from [(3)H]cryptophycin-52-tubulin compl

47 However, low concentrations of cryptophycin-52 inhibited cell proliferation at mitosis

48 ty (Kd, 47 nM, maximum of approximately 19.5 cryptophycin-52 molecules per microtubule).

49 By analyzing the effects of cryptophycin-52 on dynamics in relation to its binding t

50 In addition, cryptophycin-52 perturbed the far-ultraviolet circular d

51 The data suggest that cryptophycin-52 potently perturbs kinetic events at micr

52 These data suggest that the binding of cryptophycin-52 to tubulin is not covalent.

53 e binding data indicated that the binding of cryptophycin-52 to tubulin is primarily entropy-driven w

54 The binding of cryptophycin-52 to tubulin was rapid, not appreciably te

55 Using [3H]cryptophycin-52, we found that the compound bound to mic

56 In the present study, using [(3)H]cryptophycin-52, we found that the compound bound to tub

57 ould remove [(3)H]cryptophycin-52 from [(3)H]cryptophycin-52-tubulin complex by denaturing the comple

58 sis and that it acts by forming a reversible cryptophycin-52-tubulin stabilizing cap at microtubule e

59 nd a key intermediate aldehyde prepared from Cryptophycin 53.

60 ated natural products include vancomycin and cryptophycin A.

61 A general synthetic approach to novel cryptophycin analogues 6 is described.

62 igated with a series of structurally related cryptophycin analogues generated by chemoenzymatic synth

63 The most potent natural cryptophycin analogues retain a beta-epoxide at the C2'-

64 a beta-epoxide between C2' and C3' of cyclic cryptophycin analogues.

65 d tubulin rings of 23.8 nm mean diameter for cryptophycin and 44.6 nm mean diameter for hemiasterlin

66 Cryptophycins are potent anticancer agents isolated from

67 Cryptophycins are thought to function by modulating the

68 -2, 7-octadienoate, a major component of the cryptophycins, are reported.

69 ping a novel chemoenzymatic synthesis of the cryptophycin/arenastatin class of antitumor agents.

70 this study, the thioesterase domain from the cryptophycin biosynthetic pathway was isolated and its f

71 Cryptophycin blocked the formation of vinblastine-tubuli

72 Cryptophycins (Crp) are a group of cyanobacterial depsip

73 Cryptophycin did not alter the critical concentration of

74 These results indicate that cryptophycin disrupts the Vinca alkaloid site of tubulin

75 peptides and depsipeptides which include the cryptophycins, dolastatin 10, hemiasterlin, and phomopsi

76 (LY355703) is a new synthetic member of the cryptophycin family of antimitotic antitumor agents that

77 Cryptophycin 52, a synthetic variant of the cryptophycin family, is currently undergoing clinical tr

78 ncoded by c rpE recently identified from the cryptophycin gene cluster was shown to install this key

79 o the synthesis of the macrolide core of the cryptophycins has been developed.

80 Cryptophycin inhibited the binding of [3H]vinblastine an

81 However, the detailed mechanisms whereby the cryptophycins interact with tubulin are not known.

82 The site of cryptophycin interaction with tubulin was examined using

83 Cryptophycin is a potent antitumor agent that depletes m

84 To determine the mechanism of action of cryptophycin, its effects on tubulin function in vitro w

85 Cryptophycins, naturally occurring cytotoxic cyclo-depsi

86 osis and final lysosomal localization of the cryptophycin prodrug.

87 Cryptophycin reduced the in vitro polymerization of bovi

88 Cryptophycin styrenes 7 and beta-epoxides 6, bearing div

89 ntrast to the standard direct epoxidation of cryptophycin substrates, which proceeds with poor diaste

90 P-CrpE toward natural and unnatural desepoxy cryptophycin substrates.

91 with its persistent effects on intact cells, cryptophycin-treated microtubule protein remained polyme

92 Cryptophycin-tubulin rings appear to be the most stable

93 nce for structural variation within the seco-cryptophycin unit C beta-alanine residue, but strict str

94 An azide-functionalized cryptophycin was connected by CuAAC to an alkyne-contain

95 Cryptophycin was found to protect both alpha- and beta-t

96 remained polymerization-defective even after cryptophycin was reduced to sub-inhibitory concentration

97 The effects of cryptophycin were not due to denaturation of tubulin and