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Translationally controlled tumor

Bhisutthibhan, J., Pan, X.-O., Hossler, P.A., Walker, D.J., Yowell, C.A., Carlton, J., Dame, J.B., and Meshnick, S.R. The plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin,. Biol. Chem., 273,16192,1998. [Pg.139]

Bhisutthibhan, J., Pan, X.-O., Hossler, P.A., Walker, D.J., Yowell, C.A., Carlton, J., Dame, J.B., and Meshnick, S.R. The plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin, /. Biol. Chem., 273,16192,1998. 21. Avery, M.A., Chong, W.K.M., and Jennings-White, C. Stereoselective total synthesis of (+)-artemisinin, the antimalarial constituent of Artemisia annua L., /. Am. Chem. Soc., 114,974,1992. Avery, M.A., Bonk, J.D., and Bupp, J. Radiolabeled antimalarials synthesis of 14C-artemisinin, /. Labelled Comp. Radiopharm., 38, 263, 1996. [Pg.132]

Gnanasekar M, K Ramaswamy. Translationally controlled tumor protein of Brugia malayi fimetions as an antioxidant protein. Parasitol Res 2007 101 1533-1540. [Pg.105]

Gnanasekar M, Rao KVN, Chen L et al. Molecular characterization of a calcium bindii translationally controlled tumor protein homologue fi ora the filarial parasites Brugia malayi and Wuchereria bancrofii. Mol Biochem Parasitol 2002 121 107-118. [Pg.107]

One of the most heavily labeled proteins was later isolated from parasite grown in the presence of [ Hjdihydroartemismin (300 mM) and identified as a 25-kDa translationally controlled tumor protein (TCTP) homolog, that is able to bind heme with modest affinity (17). In vitro, the reaction of dihydroartemisinin with recombinant TCTP is clearly dependent on the presence of heme the single cysteine of the protein also appears to be necessary for the reaction, probably serving as a source of electrons for the heme-mediated activation of e drug. [Pg.287]

Targeted cationic lipids, 321 Therapeutic vaccines, 475 Tissue-isolated perfused tumor, 424 Transcription factor, 96 Transcription regulatory elements, 2 Transcriptional termination sequences, 6 Translation control, 7 Translation and splicing factors, 97 Transport receptors, 265 Triplex, 34... [Pg.480]

A regulatory role for the cap structure in translational control in intact mammalian cells is particularly well illustrated by findings of Cordell et al. (1982). In normal pancreatic tissue, the two rat insulin genes are expressed about equally, but in tumor tissue, one of these genes is expressed ten-fold less, in spite of the fact that equivalent amounts of mRNA are produced. Insulin mRNA from the underexpressed gene is ten-fold less active in in vitro translation, but this defect can be repaired by treatment with vaccinia virus capping extract. [Pg.154]

Disproportionate expression of the two nonallelic rat insulin genes in a pancreatic tumor is due to translational control. Cell 31 531. [Pg.158]

We are currently on the cusp of a new era in the treatment of cancers whereby we will learn to incorporate new drugs that are likely not cytotoxic on their own but when used in combination with standard chemotherapy and radiation hold the promise of superior tumor responses that will hopefully translate into improved local control and improved survival. At the same time it is reasonable to expect an increased selectivity for malignant cells compared to normal tissues given that many of these targets are either not altered in normal cells or their expression is not usually increased in normal tissues. This leads to the anticipation of no increase in normal tissue toxicities when these novel targeted agents are used to treat patients. [Pg.16]


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Translational control

Translationally controlled tumor protein

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