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1 er, the smaller ring size represented by the didemnin analogue, tamandarin A, is equipotent to didemn
2 e binding by the unrelated natural products, didemnin and cytotrienin.
3 fications exhibit a parallel effect for both didemnins and tamandarins.
4            Synthetic and naturally occurring didemnins are potent and specific inhibitors of protein
5 two natural products similar in structure to didemnin B (3), were recently isolated from a Brazilian
6       The antineoplastic cyclic depsipeptide didemnin B (DB) inhibits protein synthesis in cells and
7                     The total synthesis of a didemnin B analogue containing a conformationally constr
8   The structurally unrelated cyclic peptides didemnin B and ternatin-4 bind to the eEF1A(GTP)-aa-tRNA
9                            We also show that didemnin B and ternatin-4 exhibit distinct effects on th
10        By binding to a common site on eEF1A, didemnin B and ternatin-4 trap eEF1A in an intermediate
11 wo conformationally constrained analogues of didemnin B are described.
12  Both 2E2 cells and HepG2 cells treated with didemnin B exhibited increased neutral lipid content, wh
13 ic analysis of this inhibition revealed that didemnin B inhibits PPT1 uncompetitively.
14    As the first described inhibitor of PPT1, didemnin B may prove to be a useful tool in the investig
15 the protein synthesis inhibitory activity of didemnin B observed at intermediate concentrations.
16 ding site of 1 with the anti-cancer compound didemnin B on EF-1alpha.
17                 Our initial investigation of didemnin B resulted in the discovery of its GTP-dependen
18 of the antiproliferative cyclic depsipeptide didemnin B to PPT1.
19 a indicating that MCF-7 cells can accumulate didemnin B up to 2-3 orders of magnitude compared to the
20              The [N,O-Me(2)Tyr(5)]residue of didemnin B was replaced with L-1,2,3,4-tetrahydroisoquin
21                                              Didemnin B was shown to inhibit recombinant human PPT1 w
22 tivities, and some, such as griselimycin and didemnin B, are membrane permeable and have intracellula
23                   The marine natural product didemnin B, currently in clinical trials as an antitumor
24 tostatic and immunosuppressive activities of didemnin B, observed at low concentrations, additional d
25 lls treated with selective EEF1A inhibitors, didemnin B, or plitidepsin.
26 nin analogue, tamandarin A, is equipotent to didemnin B.
27 es and shown to be slightly more potent than didemnin B.
28  in vitro and in vivo activities compared to didemnin B.
29 rt the purification of a 36-kDa glycosylated didemnin-binding protein from bovine brain lysate.
30 , observed at low concentrations, additional didemnin-binding proteins were sought.
31                          Bioactivities of 42 didemnin congeners, either isolated from the marine tuni
32 uirement for most of the bioactivites of the didemnins, especially for cytotoxicities and antiviral a
33 bition, in vitro binding studies of PPT1 and didemnin indicate that the natural product binds prefere
34 s and in in vivo studies in mice, as well as didemnin M, tested for the mixed lymphocyte reaction and
35 is observation supports tamandarins' role as didemnins' mimic.
36            Immunosuppressive activity of the didemnins was determined using a mixed lymphocyte reacti