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HeLa cells inhibition

HeLa TPA-Stimulated 32Pi incorporation in HeLa cell inhibition [28,29,39]... [Pg.46]

Marlovits, T.C., Abrahamsberg, C., Blaas, D., 1998. Very-low-density lipoprotein receptor fragment shed from HeLa cells inhibits human rhinovirus infection. J. Virol. 72, 10246-10250. [Pg.227]

HUNT, T. and EHRENFELB, E. Gytoplasm from poliovirus-infected HeLa cells inhibits cell-free haemoglobin synthesis. Nature New Biology (1971)> 230. 91-94. [Pg.98]

Etchison, D., Edery, I., Sonenberg, N., Hansen, J., Ehrenfeld, E., Milburn, S., and Hershey, J. W. B., Poliovirus infection of HeLa cells inhibits the activity of a cap binding protein complex in the translation of globin messenger RNA, submitted. [Pg.216]

HASEGAWA T, NisHiNO H and IWASHIMA A (1993) Isothiocyauates inhibit cell cycle progression of HeLa cells at G2/M phase . Anticancer Drugs, 4 273-9. [Pg.63]

Figure 6. The c-mos negative regulatory element (NRE). Nucleotide positions of the NRE are shown relative to the spermatocyte transcription start site, taken as 280 base pairs upstream of the c-mos ATG (see Fig. 4). The endpoints of the NRE are defined by deletions that allow c-mos expression in NIH 3T3 and other somatic cells. Mutations of the sequences designated by boxes 1,2, and 3 also allow c-mos transcription in NIH 3T3 cells, indicating that these sequences represent functional elements within the NRE. Boxes 1 and 2 are similar to sequences upstream of the protamine (Prot) promoter that inhibit in vitro transcription in HeLa cell extracts. A sequence just upstream of box 2 is also similar to a putative repressor-binding site in the regulatory region of Pgk2. Figure 6. The c-mos negative regulatory element (NRE). Nucleotide positions of the NRE are shown relative to the spermatocyte transcription start site, taken as 280 base pairs upstream of the c-mos ATG (see Fig. 4). The endpoints of the NRE are defined by deletions that allow c-mos expression in NIH 3T3 and other somatic cells. Mutations of the sequences designated by boxes 1,2, and 3 also allow c-mos transcription in NIH 3T3 cells, indicating that these sequences represent functional elements within the NRE. Boxes 1 and 2 are similar to sequences upstream of the protamine (Prot) promoter that inhibit in vitro transcription in HeLa cell extracts. A sequence just upstream of box 2 is also similar to a putative repressor-binding site in the regulatory region of Pgk2.
One day prior to the isolation of polysomes, approximately 5 million HeLa cells are plated into 10-cm dishes. The following day, the media is replaced with fresh DMEM and compound is added to a concentration previously determined to inhibit translation in vivo by 35S-methionine metabolic labeling (see previously). [Pg.325]

Further experiments focused therefore on [RuCl(en)(r 6-tha)]+ (12) and [RuCl(rj6-p-cym)(en)]+ (22), which represent the two different classes, and their conformational distortion of short oligonucleotide duplexes. Chemical probes demonstrated that the induced distortion extended over at least seven base pairs for [RuCl(rj6-p-cym)(en)]+ (22), whereas the distortion was less extensive for [RuCl(en)(rj6-tha)]+ (12). Isothermal titration calorimetry also showed that the thermodynamic destabilization of the duplex was more pronounced for [RuCl(r 6-p-cym)(en)]+ (22) (89). DNA polymerization was markedly more strongly inhibited by the monofunctional Ru(II) adducts than by monofunctional Pt(II) compounds. The lack of recognition of the DNA monofunctional adducts by HMGB1, an interaction that shields cisplatin-DNA adducts from repair, points to a different mechanism of antitumor activity for the ruthenium-arenes. DNA repair activity by a repair-proficient HeLa cell-free extract (CFE) showed a considerably lower level of damage-induced DNA repair synthesis (about six times) for [RuCl(en)(rj6-tha)] + compared to cisplatin. This enhanced persistence of the adduct is consistent with the higher cytotoxicity of this compound (89). [Pg.43]

Substituted analogues of /i-carbolin-l-onc 47 have also been found to inhibit tumor cell proliferation. For example, Hu and coworkers have reported that /l-carbolin-l-one 51 inhibited cell proliferation of HeLa cells with an... [Pg.116]

Eukaryotic organisms HeLa cells DNA synthesis inhibition - - Painter and Howard 1982 KCN... [Pg.108]

Radical polymerization of maleic anhydride and fullerene was used to obtain a new material, the photodynamic properties of which have been studied in vitro and in vivo. HeLa and bone tumor cell growth were inhibited by treatment with fullerene and light, so the polymer was tested on mice affected by bone tumor. After injection and irradiation, tumor size and weight were reduced and the mouse survival time was extended (Jiang and Li, 2007). The photodynamic properties of a supramolecular cucurbit[8]uril-fullerene complex have been studied by the same authors (Jiang and Li, 2006) who attributed HeLa cell death mainly to the damage of membrane phosphohpids and proteins. [Pg.8]

Both cyclo(Gly-Leu) and cyclo(Gly-Ile) at 10 and lOOpmolG exhibited moderate effects in inhibiting HT-29, MCF-7, and HeLa cancer cell lines, except for cyclo(Gly-Ile) that showed very little activity against HT-29 cells at a concentration of 10 pmol The greatest activity was noted for 100 pmol cyclo(Gly-Leu) against HeLa cells (28.64 1.51% inhibition, P= 0.0018). °... [Pg.687]


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See also in sourсe #XX -- [ Pg.45 ]

See also in sourсe #XX -- [ Pg.25 , Pg.45 , Pg.46 ]




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