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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 ding site of Cp-52, and its parent compound, cryptophycin-1, on HeLa tubulin, to a resolution of 3.3
21 a and B monomers and between Cp-52-bound and cryptophycin-1-bound tubulin.
22  group into cryptophycin-4 (Cr-4) to produce cryptophycin-2 (Cr-2) in a regio- and stereospecific man
23                         Epoxidation provided cryptophycin-24 (arenastatin A).
24 esults demonstrated that the 4'-MeO group in cryptophycin-24 is not essential and can be replaced wit
25 '-Cl, 4'-C1, and 3',4'-diCl C10 analogues of cryptophycin-24 were prepared via total synthesis and te
26          Substitution of the 4'-MeO group in cryptophycin-24 with a 4'-C1 moiety did not significantl
27 pi-C3-cryptophycin-24, epi-C3-m-chlorobenzyl-cryptophycin-24, and the corresponding styrenes were syn
28                                       Epi-C3-cryptophycin-24, epi-C3-m-chlorobenzyl-cryptophycin-24,
29 vity was very similar to the parent compound cryptophycin-24.
30 ccessfully applied to the total synthesis of cryptophycin-24.
31 wn to install this key functional group into cryptophycin-4 (Cr-4) to produce cryptophycin-2 (Cr-2) i
32                               A synthesis of cryptophycin 52 (2) is reported using a Sharpless asymme
33 enantioselective and convergent synthesis of cryptophycin 52 (2), an exceedingly potent cytotoxic age
34                                        These Cryptophycin 52 analogues were accessed using a Wittig o
35                                              Cryptophycin 52 is a synthetic derivative of Cryptophyci
36 e analogues were equally or more potent than Cryptophycin 52 when evaluated in vitro in the CCRF-CEM
37                                              Cryptophycin 52, a synthetic variant of the cryptophycin
38 s, a common binding site for cryptophycin 1, cryptophycin 52, dolastatin 10, hemiasterlin, and phomop
39 C(50) = 54 pM, only 2-fold less than that of Cryptophycin-52 (3).
40         We show that ChET rings induced with cryptophycin-52 (Cp-52) are smaller in diameter than HeL
41                                              Cryptophycin-52 (Cp-52) is potentially the most potent a
42                                              Cryptophycin-52 (LY355703) is a new synthetic member of
43                                              Cryptophycin-52 (LY355703) is currently undergoing clini
44                   Conformational analysis of cryptophycin-52 and two synthetic analogues was performe
45                                              Cryptophycin-52 appears to be the most potent suppressor
46                                              Cryptophycin-52 became concentrated in cells 730-fold, a
47  high concentrations (>/=10 times the IC50), cryptophycin-52 blocked HeLa cell proliferation at mitos
48 termined that approximately 5-6 molecules of cryptophycin-52 bound to a microtubule were sufficient t
49 lution cryo-electron microscopy structure of cryptophycin-52 bound to the maytansine site of beta-tub
50 ls 730-fold, and the resulting intracellular cryptophycin-52 concentration was similar to that requir
51               However, we could remove [(3)H]cryptophycin-52 from [(3)H]cryptophycin-52-tubulin compl
52               However, low concentrations of cryptophycin-52 inhibited cell proliferation at mitosis
53 ty (Kd, 47 nM, maximum of approximately 19.5 cryptophycin-52 molecules per microtubule).
54                  By analyzing the effects of cryptophycin-52 on dynamics in relation to its binding t
55                                 In addition, cryptophycin-52 perturbed the far-ultraviolet circular d
56                        The data suggest that cryptophycin-52 potently perturbs kinetic events at micr
57       These data suggest that the binding of cryptophycin-52 to tubulin is not covalent.
58 e binding data indicated that the binding of cryptophycin-52 to tubulin is primarily entropy-driven w
59                               The binding of cryptophycin-52 to tubulin was rapid, not appreciably te
60                                    Using [3H]cryptophycin-52, we found that the compound bound to mic
61            In the present study, using [(3)H]cryptophycin-52, we found that the compound bound to tub
62 ould remove [(3)H]cryptophycin-52 from [(3)H]cryptophycin-52-tubulin complex by denaturing the comple
63 sis and that it acts by forming a reversible cryptophycin-52-tubulin stabilizing cap at microtubule e
64 nd a key intermediate aldehyde prepared from Cryptophycin 53.
65 esis of intermediates of the natural product cryptophycin A and a cathepsin K inhibitor.
66 ated natural products include vancomycin and cryptophycin A.
67        A general synthetic approach to novel cryptophycin analogues 6 is described.
68 igated with a series of structurally related cryptophycin analogues generated by chemoenzymatic synth
69                      The most potent natural cryptophycin analogues retain a beta-epoxide at the C2'-
70 a beta-epoxide between C2' and C3' of cyclic cryptophycin analogues.
71 d tubulin rings of 23.8 nm mean diameter for cryptophycin and 44.6 nm mean diameter for hemiasterlin
72                                              Cryptophycins are microtubule-targeting agents (MTAs) th
73                                              Cryptophycins are potent anticancer agents isolated from
74                                              Cryptophycins are the first natural ligands found to bin
75                                              Cryptophycins are thought to function by modulating the
76 -2, 7-octadienoate, a major component of the cryptophycins, are reported.
77 ping a novel chemoenzymatic synthesis of the cryptophycin/arenastatin class of antitumor agents.
78        Interestingly, we discovered a second cryptophycin-binding site that involves the T5-loop of b
79 this study, the thioesterase domain from the cryptophycin biosynthetic pathway was isolated and its f
80                                              Cryptophycin blocked the formation of vinblastine-tubuli
81                                              Cryptophycins (Crp) are a group of cyanobacterial depsip
82 solution X-ray crystal structure of a potent cryptophycin derivative bound to the alphabeta-tubulin h
83                                              Cryptophycin did not alter the critical concentration of
84                  These results indicate that cryptophycin disrupts the Vinca alkaloid site of tubulin
85 peptides and depsipeptides which include the cryptophycins, dolastatin 10, hemiasterlin, and phomopsi
86  (LY355703) is a new synthetic member of the cryptophycin family of antimitotic antitumor agents that
87  Cryptophycin 52, a synthetic variant of the cryptophycin family, is currently undergoing clinical tr
88 ncoded by c rpE recently identified from the cryptophycin gene cluster was shown to install this key
89 o the synthesis of the macrolide core of the cryptophycins has been developed.
90                                              Cryptophycin inhibited the binding of [3H]vinblastine an
91 However, the detailed mechanisms whereby the cryptophycins interact with tubulin are not known.
92                                  The site of cryptophycin interaction with tubulin was examined using
93                                              Cryptophycin is a potent antitumor agent that depletes m
94      To determine the mechanism of action of cryptophycin, its effects on tubulin function in vitro w
95                                              Cryptophycins, naturally occurring cytotoxic cyclo-depsi
96 osis and final lysosomal localization of the cryptophycin prodrug.
97                                              Cryptophycin reduced the in vitro polymerization of bovi
98                                              Cryptophycin styrenes 7 and beta-epoxides 6, bearing div
99 ntrast to the standard direct epoxidation of cryptophycin substrates, which proceeds with poor diaste
100 P-CrpE toward natural and unnatural desepoxy cryptophycin substrates.
101 with its persistent effects on intact cells, cryptophycin-treated microtubule protein remained polyme
102                                              Cryptophycin-tubulin rings appear to be the most stable
103 nce for structural variation within the seco-cryptophycin unit C beta-alanine residue, but strict str
104                      An azide-functionalized cryptophycin was connected by CuAAC to an alkyne-contain
105                                              Cryptophycin was found to protect both alpha- and beta-t
106 remained polymerization-defective even after cryptophycin was reduced to sub-inhibitory concentration
107                               The effects of cryptophycin were not due to denaturation of tubulin and
108 r provides atomic details on interactions of cryptophycins, which had not been described previously,

 
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