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10.1080/19336896.2015.1027855 http://scihub22266oqcxt.onion/10.1080/19336896.2015.1027855 C4601254!4601254 !26110608     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26110608 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26110608 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Prion 2015 ; 9 (3 ): 165-73 Nephropedia Template TP {{tp|p=26110608 |t=2015. Targeting prion protein interactions in cancer |pdf=|usr=}}{{26110608 }} gab.com Text Targeting prion protein interactions in cancer JO: Prion http://www.kidney.de/pget.php?&tw=1&pmid=26110608 #FOAvip In recent years, prion protein (PrP(C)) has been considered as a promising target molecule for cancer therapies, due its direct or indirect participation in tumor growth, metastasis, and resistance to cell death induced by chemotherapy. PrP(C) functions as a scaffold protein, forming multiprotein complexes on the plasma membrane, which elicits distinct signaling pathways involved in diverse biological phenomena and could be modulated depending on the cell type, complex composition, and organization. In addition, PrP(C) and its partners participate in self-renewal of embryonic, tissue-specific stem cells and cancer stem cells, which are suggested to be responsible for the origin, maintenance, relapse, and dissemination of tumors. Interference with protein-protein interaction has been recognized as an important therapeutic strategy in cancer; indeed, the possible interference in PrP(C) engagement with specific partners is a novel strategy. Recently, our group successfully used that approach to interfere with the interaction between PrP(C) and HSP-90/70 organizing protein (HOP, also known as stress-inducible protein 1 - STI1) to control the growth of human glioblastoma in animal models. Thus, PrP(C)-organized multicomplexes have emerged as feasible candidates for anti-tumor therapy, warranting further exploration. Twit Text FOAVip Targeting prion protein interactions in cancer ????Prion http://www.kidney.de/pget.php?&tw=1&pmid=26110608 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26110608 #FOAvip English Wikipedia <ref>{{Cite pmid|26110608 }}</ref> Targeting prion protein interactions in cancer #MMPMID26110608 Santos TG ; Lopes MH ; Martins VR Prion 2015[]; 9 (3 ): 165-73 PMID26110608 show ga In recent years, prion protein (PrP(C)) has been considered as a promising target molecule for cancer therapies, due its direct or indirect participation in tumor growth, metastasis, and resistance to cell death induced by chemotherapy. PrP(C) functions as a scaffold protein, forming multiprotein complexes on the plasma membrane, which elicits distinct signaling pathways involved in diverse biological phenomena and could be modulated depending on the cell type, complex composition, and organization. In addition, PrP(C) and its partners participate in self-renewal of embryonic, tissue-specific stem cells and cancer stem cells, which are suggested to be responsible for the origin, maintenance, relapse, and dissemination of tumors. Interference with protein-protein interaction has been recognized as an important therapeutic strategy in cancer; indeed, the possible interference in PrP(C) engagement with specific partners is a novel strategy. Recently, our group successfully used that approach to interfere with the interaction between PrP(C) and HSP-90/70 organizing protein (HOP, also known as stress-inducible protein 1 - STI1) to control the growth of human glioblastoma in animal models. Thus, PrP(C)-organized multicomplexes have emerged as feasible candidates for anti-tumor therapy, warranting further exploration. |Animals [MESH] |Humans [MESH] |Ligands [MESH] |Neoplasms/*metabolism [MESH] |Neoplastic Stem Cells/metabolism [MESH] |Prions/*metabolism [MESH] |Protein Binding [MESH]Targeting prion protein interactions in cancer (epmc).pdf DeepDyve Pubget Overpricing