George F. Vande Woude; George Klein (Eds.)'s Advances in Cancer Research PDF

By George F. Vande Woude; George Klein (Eds.)

ISBN-10: 0123747724

ISBN-13: 9780123747723

Advances in melanoma study presents beneficial info at the intriguing and fast-moving box of melanoma research. In this half A volume, outstanding and unique stories offer an summary and synthesis of the newest options and findings in relation to Clusterin. Chapters contain the shifiting stability among CLU kinds in the course of tumor development, uclear CLU and the destiny of the telephone, and Oxidative tension in malignant development.

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38, 273–298. , et al. (2005). MatInspector and beyond: Promoter analysis based on transcription factor binding sites. Bioinformatics 21, 2933–2942. Chan, J. , et al. (2006). Antisense oligonucleotides: From design to therapeutic application. Clin. Exp. Pharmacol. Physiol. 33, 533–540. Choi-Miura, N. , et al. (1992). Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J). J. Biochem. 112, 557–561. Cochrane, D. , et al. (2007). Differential regulation of clusterin and its isoforms by androgens in prostate cells.

1–37. Springer-Verlag, Heidelberg. , and Corti, A. (2004). The chemopreventive action of catechins in the TRAMP mouse model of prostate carcinogenesis is accompanied by clusterin over-expression. Carcinogenesis 25, 2217–2224. , and Spagnoli, L. G. (2007). Carnitine palmitoyltransferase I in human carcinomas: A novel role in histone deacetylation? Cancer Biol. Ther. 6, 1606–1613. Menendez, J. , and Lupu, R. (2005a). Targeting fatty acid synthase-driven lipid rafts: A novel strategy to overcome trastuzumab resistance in breast cancer cells.

Identification of novel RARbeta2 transcript variants with short 50 -UTRs in normal and cancerous breast epithelial cells. Oncogene 24, 1296–1301. , et al. (2000). Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry 39, 15953–15960. , et al. (2002a). Mildly acidic pH activates the extracellular molecular chaperone clusterin. J. Biol. Chem. 277, 39532–39540. , et al. (2002b). Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway.

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Advances in Cancer Research by George F. Vande Woude; George Klein (Eds.)

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