PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6806278-3 1982 Part of the increase in the activity of ornithine decarboxylase was due to a decreased rate of degradation of the enzyme since activity declined more slowly (t1/2 80 min) in androgen-treated BALB/c mice than in controls (t1/2 20 min) when protein synthesis was inhibited by cycloheximide. Cycloheximide 274-287 ornithine decarboxylase, structural 1 Mus musculus 40-63 6806278-4 1982 When ornithine decarboxylase protein was labeled in vivo by injection of [5-14C]difluoromethylornithine, the rate of disappearance of the labeled protein was exactly the same as the rate of loss of ornithine decarboxylase activity when protein synthesis was inhibited by cycloheximide, confirming that ornithine decarboxylase protein does turn over rapidly in vivo. Cycloheximide 271-284 ornithine decarboxylase, structural 1 Mus musculus 5-28 7083470-8 1982 In contrast, the ODC activity of the mouse skin papillomas declined at a rate similar to that in TPA-treated epidermis for only the first 15-20 min after cycloheximide injection. Cycloheximide 154-167 ornithine decarboxylase, structural 1 Mus musculus 17-20 6102386-8 1980 Cycloheximide inhibited protein synthesis >95% within 30 min, and caused an immediate decline of stimulated ODCase activity with a half-time of 20-30 min. Cycloheximide 0-13 ornithine decarboxylase, structural 1 Mus musculus 111-117 6104755-4 1980 The half-life of ODC was determined after cycloheximide administration. Cycloheximide 42-55 ornithine decarboxylase, structural 1 Mus musculus 17-20 185201-7 1976 Actinomycin D with or without these inducers stimulated induction of ODC in L cells, whereas cycloheximide inhibited it, suggesting that these hormones affect the translational level of ODC synthesis. Cycloheximide 93-106 ornithine decarboxylase, structural 1 Mus musculus 186-189 198803-5 1977 In the salts/glucose medium, the rate of loss of ODC activity following the inhibition of protein synthesis by cycloheximide or puromycin depends upon the presence or absence of asparagine; loss is rapid only in the absence of asparagine and does not appear to be related to the inhibition of protein synthesis. Cycloheximide 111-124 ornithine decarboxylase, structural 1 Mus musculus 49-52 186774-8 1976 Cycloheximide effectively obliterates the ODC and SAMD activities during the entire infectious cycle. Cycloheximide 0-13 ornithine decarboxylase, structural 1 Mus musculus 42-45 186774-10 1976 The experiments with AMD and cycloheximide suggest that the formation of ODC is subject to post-transcriptional control, whereas that of SAMD is regulated primarily at the transcriptional level. Cycloheximide 29-42 ornithine decarboxylase, structural 1 Mus musculus 73-76 8707896-8 1996 Evidence was also obtained for a cycloheximide-sensitive regulator of ornithine decarboxylase gene expression whose effect, in combination with bFGF, resulted in a further augmentation of ornithine decarboxylase gene expression. Cycloheximide 33-46 ornithine decarboxylase, structural 1 Mus musculus 70-93 11235918-8 2001 In NR3 cells, alterations in ODC and in SAMDC gene expression was an event requiring de novo protein synthesis, whereas in highly malignant C2 cells, protein synthesis inhibition following cycloheximide treatment in cooperation with PMA resulted in an augmentation of both ODC and SAMDC gene expression. Cycloheximide 189-202 ornithine decarboxylase, structural 1 Mus musculus 273-276 9024798-5 1997 When the feedback repression of polyamine uptake was blocked with cycloheximide, C55.7 cells transfected with either ODC construct accumulated very high levels of putrescine from the medium, and underwent apoptosis in a putrescine dose-dependent manner. Cycloheximide 66-79 ornithine decarboxylase, structural 1 Mus musculus 117-120 8707896-8 1996 Evidence was also obtained for a cycloheximide-sensitive regulator of ornithine decarboxylase gene expression whose effect, in combination with bFGF, resulted in a further augmentation of ornithine decarboxylase gene expression. Cycloheximide 33-46 ornithine decarboxylase, structural 1 Mus musculus 188-211 8012939-2 1994 After 8 h of culture in the presence or absence of vinblastine, cycloheximide was added to the medium, a 4.5-fold increase in the half-life of the ornithine decarboxylase activity was observed in vinblastine-treated cells. Cycloheximide 64-77 ornithine decarboxylase, structural 1 Mus musculus 147-170 7525612-7 1994 Furthermore, we observed that cycloheximide treatment of malignant but not benign H-ras transformed cells significantly elevated ODC message level. Cycloheximide 30-43 ornithine decarboxylase, structural 1 Mus musculus 129-132 7525612-8 1994 Treatment of malignant cells with both cycloheximide and forskolin together resulted in a further additive elevation in ODC message, but a similar treatment of benign tumor cells reduced the forskolin-mediated increase in ODC message. Cycloheximide 39-52 ornithine decarboxylase, structural 1 Mus musculus 120-123 7525612-8 1994 Treatment of malignant cells with both cycloheximide and forskolin together resulted in a further additive elevation in ODC message, but a similar treatment of benign tumor cells reduced the forskolin-mediated increase in ODC message. Cycloheximide 39-52 ornithine decarboxylase, structural 1 Mus musculus 222-225 8344985-13 1993 In addition, evidence was obtained for a cycloheximide sensitive regulator of ornithine decarboxylase gene expression, since the presence of this protein synthesis inhibitor increased the levels of ornithine decarboxylase message, and this effect was synergistically augmented by exposure of cells to cycloheximide and induction of TGF-beta 1 gene expression together. Cycloheximide 41-54 ornithine decarboxylase, structural 1 Mus musculus 78-101 8344985-13 1993 In addition, evidence was obtained for a cycloheximide sensitive regulator of ornithine decarboxylase gene expression, since the presence of this protein synthesis inhibitor increased the levels of ornithine decarboxylase message, and this effect was synergistically augmented by exposure of cells to cycloheximide and induction of TGF-beta 1 gene expression together. Cycloheximide 41-54 ornithine decarboxylase, structural 1 Mus musculus 198-221 8344985-13 1993 In addition, evidence was obtained for a cycloheximide sensitive regulator of ornithine decarboxylase gene expression, since the presence of this protein synthesis inhibitor increased the levels of ornithine decarboxylase message, and this effect was synergistically augmented by exposure of cells to cycloheximide and induction of TGF-beta 1 gene expression together. Cycloheximide 301-314 ornithine decarboxylase, structural 1 Mus musculus 78-101 8344985-13 1993 In addition, evidence was obtained for a cycloheximide sensitive regulator of ornithine decarboxylase gene expression, since the presence of this protein synthesis inhibitor increased the levels of ornithine decarboxylase message, and this effect was synergistically augmented by exposure of cells to cycloheximide and induction of TGF-beta 1 gene expression together. Cycloheximide 301-314 ornithine decarboxylase, structural 1 Mus musculus 198-221 1733566-3 1992 Cycloheximide, an inhibitor of protein synthesis, inhibited the mancozeb-caused ODC induction, indicating the effect on enzyme protein synthesis. Cycloheximide 0-13 ornithine decarboxylase, structural 1 Mus musculus 80-83 1551904-9 1992 The presence of asparagine increased the half-life of ODC protein by 3-5-fold when measured in the presence of cycloheximide. Cycloheximide 111-124 ornithine decarboxylase, structural 1 Mus musculus 54-57 1597444-3 1992 Contrary to the commonly observed short half-life of mouse ODC in mammalian cells, however, the mouse ODC activity expressed in T. brucei remained stable for at least 6 h when protein synthesis was inhibited by cycloheximide. Cycloheximide 211-224 ornithine decarboxylase, structural 1 Mus musculus 102-105 2105957-6 1990 Moreover, hypoosmotic stress extended the half-life of ODC activity from 35 +/- 10 to 212 +/- 67 min and blocked any degradation of the radiolabeled immunoreactive protein, which had a half-life of 28 +/- 6 min under isotonic conditions, for at least 120 min after addition of cycloheximide. Cycloheximide 277-290 ornithine decarboxylase, structural 1 Mus musculus 55-58 1959325-2 1991 In the liver of the frog, Rana negromaculata, the activity of ornithine decarboxylase (ODC) was induced by dietary stimuli and was rapidly lost upon intraperitoneal injection of cycloheximide or putrescine. Cycloheximide 178-191 ornithine decarboxylase, structural 1 Mus musculus 62-85 1959325-2 1991 In the liver of the frog, Rana negromaculata, the activity of ornithine decarboxylase (ODC) was induced by dietary stimuli and was rapidly lost upon intraperitoneal injection of cycloheximide or putrescine. Cycloheximide 178-191 ornithine decarboxylase, structural 1 Mus musculus 87-90 2112424-5 1990 ODC induction was inhibited by cycloheximide and also, up to some extent, by actinomycin D. Cycloheximide 31-44 ornithine decarboxylase, structural 1 Mus musculus 0-3 2498115-9 1989 The half-life of ODC in procyclic forms grown in the presence of cycloheximide was greater than 6 hr, while that of bloodstream trypomastigotes in mice treated with cycloheximide was 5 hr. Cycloheximide 65-78 ornithine decarboxylase, structural 1 Mus musculus 17-20 2498115-9 1989 The half-life of ODC in procyclic forms grown in the presence of cycloheximide was greater than 6 hr, while that of bloodstream trypomastigotes in mice treated with cycloheximide was 5 hr. Cycloheximide 165-178 ornithine decarboxylase, structural 1 Mus musculus 17-20 3279036-9 1988 Transformation led also to about 3-fold stabilization of ODC as determined by an exposure of the cells to cycloheximide. Cycloheximide 106-119 ornithine decarboxylase, structural 1 Mus musculus 57-60 3178765-4 1988 On the contrary, the proportion of ODC present as a complex with antizyme was 24-fold higher in females than in males, and the decay of renal ODC activity after cycloheximide treatment was about 5-fold more rapid in females than in males. Cycloheximide 161-174 ornithine decarboxylase, structural 1 Mus musculus 35-38 3178765-4 1988 On the contrary, the proportion of ODC present as a complex with antizyme was 24-fold higher in females than in males, and the decay of renal ODC activity after cycloheximide treatment was about 5-fold more rapid in females than in males. Cycloheximide 161-174 ornithine decarboxylase, structural 1 Mus musculus 142-145 3390142-13 1988 Upon cycloheximide treatment, both free ODC activity and ODC-antizyme complex rapidly disappeared, although free antizyme and the inactive ODC protein were both quite stable. Cycloheximide 5-18 ornithine decarboxylase, structural 1 Mus musculus 40-43 3390142-13 1988 Upon cycloheximide treatment, both free ODC activity and ODC-antizyme complex rapidly disappeared, although free antizyme and the inactive ODC protein were both quite stable. Cycloheximide 5-18 ornithine decarboxylase, structural 1 Mus musculus 57-60 3390142-13 1988 Upon cycloheximide treatment, both free ODC activity and ODC-antizyme complex rapidly disappeared, although free antizyme and the inactive ODC protein were both quite stable. Cycloheximide 5-18 ornithine decarboxylase, structural 1 Mus musculus 57-60 3109985-7 1987 ODC activity was maximal by 4 to 8 hr and could be completely inhibited by preincubation of the cells with actinomycin D or cycloheximide, indicating that de novo synthesis of RNA and protein is necessary for enzyme induction. Cycloheximide 124-137 ornithine decarboxylase, structural 1 Mus musculus 0-3 2832424-9 1988 The induction of ODC mRNA by either LPS or TPA was blocked by the addition of cycloheximide (25 micrograms/ml) or anisomycin (0.1 mM) to the cellular incubation mixture. Cycloheximide 78-91 ornithine decarboxylase, structural 1 Mus musculus 17-20 2832424-11 1988 Experiments in which cycloheximide addition was delayed after LPS treatment indicated that some of the required protein synthesis occurred within the first 30 minutes and that complete expression of ODC mRNA was possible if protein synthesis continued for at least 2 hours before cycloheximide was added. Cycloheximide 21-34 ornithine decarboxylase, structural 1 Mus musculus 199-202 2832424-11 1988 Experiments in which cycloheximide addition was delayed after LPS treatment indicated that some of the required protein synthesis occurred within the first 30 minutes and that complete expression of ODC mRNA was possible if protein synthesis continued for at least 2 hours before cycloheximide was added. Cycloheximide 280-293 ornithine decarboxylase, structural 1 Mus musculus 199-202 3632665-4 1987 Additionally, we were able to detect stable ODC mRNAs in cycloheximide pretreated fibroblasts. Cycloheximide 57-70 ornithine decarboxylase, structural 1 Mus musculus 44-47 3871636-4 1985 The ornithine decarboxylase induction by the factor was suppressed by cycloheximide, but actinomycin D did not suppress the induction, or rather enhanced it. Cycloheximide 70-83 ornithine decarboxylase, structural 1 Mus musculus 4-27 3569711-7 1987 Pretreatment of mice with the protein synthesis inhibitor cycloheximide abolished both epidermal and hepatic ODC induction. Cycloheximide 58-71 ornithine decarboxylase, structural 1 Mus musculus 109-112 3027106-14 1987 In contrast, spermidine-mediated ODC degradation was substantially decreased by inhibitors of protein synthesis (cycloheximide, emetine, and puromycin). Cycloheximide 113-126 ornithine decarboxylase, structural 1 Mus musculus 33-36 3815331-3 1987 Both ODC activity and protein levels peak at 4.5 h after TPA treatment and rapidly fall to basal levels by 24 h. Cycloheximide treatment of mice in which ODC had been previously induced by TPA indicated a similar rapid turnover of both ODC catalytic activity and protein levels. Cycloheximide 113-126 ornithine decarboxylase, structural 1 Mus musculus 154-157 3815331-3 1987 Both ODC activity and protein levels peak at 4.5 h after TPA treatment and rapidly fall to basal levels by 24 h. Cycloheximide treatment of mice in which ODC had been previously induced by TPA indicated a similar rapid turnover of both ODC catalytic activity and protein levels. Cycloheximide 113-126 ornithine decarboxylase, structural 1 Mus musculus 154-157 3609441-4 1987 ODC induction in C3H/10T1/2 CL8 cells was completely inhibited by cycloheximide and actinomycin D. Cycloheximide 66-79 ornithine decarboxylase, structural 1 Mus musculus 0-3 3785214-5 1986 ODCase mRNA was rapidly reinduced by exposure of quiescent, differentiated cells to medium with 20% serum or by inhibition of protein synthesis with cycloheximide. Cycloheximide 149-162 ornithine decarboxylase, structural 1 Mus musculus 0-6 3785214-7 1986 The mechanisms whereby mitogens and protein synthesis inhibitors induced ODCase transcription appeared to be different since cycloheximide potentiated the effects of mitogens, resulting in superinduction of ODCase transcription to a level significantly greater than in the presence of mitogens alone. Cycloheximide 125-138 ornithine decarboxylase, structural 1 Mus musculus 73-79 3785214-7 1986 The mechanisms whereby mitogens and protein synthesis inhibitors induced ODCase transcription appeared to be different since cycloheximide potentiated the effects of mitogens, resulting in superinduction of ODCase transcription to a level significantly greater than in the presence of mitogens alone. Cycloheximide 125-138 ornithine decarboxylase, structural 1 Mus musculus 207-213 2423265-5 1986 This specific ODC staining in cells surrounding hair follicles was inhibited by pretreatment of mice with either retinoic acid or cycloheximide 1 h before TPA treatment. Cycloheximide 130-143 ornithine decarboxylase, structural 1 Mus musculus 14-17 6477895-7 1984 Both forms of the enzyme were rapidly labeled in vivo, and the immunoprecipitable ornithine decarboxylase protein was almost completely lost after 4-h exposure to cycloheximide, confirming directly the very rapid turnover of this enzyme. Cycloheximide 163-176 ornithine decarboxylase, structural 1 Mus musculus 82-105 6743356-6 1984 ODC induction by LPS was suppressed by dexamethasone and cycloheximide. Cycloheximide 57-70 ornithine decarboxylase, structural 1 Mus musculus 0-3 6423285-5 1984 The labeled ornithine decarboxylase was lost rapidly from both nucleus and cytoplasm of all the cell types examined, and labeling by radioactive alpha-difluoro-methylornithine was greatly reduced if the mice were pretreated for 5 h with cycloheximide to block protein synthesis. Cycloheximide 237-250 ornithine decarboxylase, structural 1 Mus musculus 12-35 6853503-11 1983 The half-life of immunoreactive ornithine decarboxylase in mouse kidney, as measured after inhibition of protein synthesis in vivo by cycloheximide administration, was 16 min in nontreated and 140 min in androgen-treated male animals, while the corresponding values for the catalytically active enzyme were 9 and 90 min. Cycloheximide 134-147 ornithine decarboxylase, structural 1 Mus musculus 32-55