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10.1038/nrc.2017.105 http://scihub22266oqcxt.onion/10.1038/nrc.2017.105 C6054770!6054770 !29242641     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29242641 &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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29242641 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Rev+Cancer 2018 ; 18 (2 ): 69-88 Nephropedia Template TP {{tp|p=29242641 |t=2018. Ubiquitin ligases in oncogenic transformation and cancer therapy |pdf=|usr=}}{{29242641 }} gab.com Text Ubiquitin ligases in oncogenic transformation and cancer therapy JO: Nat Rev Cancer http://www.kidney.de/pget.php?&tw=1&pmid=29242641 #FOAvip The cellular response to external stress signals and DNA damage depends on the activity of ubiquitin ligases (E3s), which regulate numerous cellular processes, including homeostasis, metabolism and cell cycle progression. E3s recognize, interact with and ubiquitylate protein substrates in a temporally and spatially regulated manner. The topology of the ubiquitin chains dictates the fate of the substrates, marking them for recognition and degradation by the proteasome or altering their subcellular localization or assembly into functional complexes. Both genetic and epigenetic alterations account for the deregulation of E3s in cancer. Consequently, the stability and/or activity of E3 substrates are also altered, in some cases leading to downregulation of tumour-suppressor activities and upregulation of oncogenic activities. A better understanding of the mechanisms underlying E3 regulation and function in tumorigenesis is expected to identify novel prognostic markers and to enable the development of the next generation of anticancer therapies. This Review summarizes the oncogenic and tumour-suppressor roles of selected E3s and highlights novel opportunities for therapeutic intervention. Twit Text FOAVip Ubiquitin ligases in oncogenic transformation and cancer therapy ????Nat Rev Cancer http://www.kidney.de/pget.php?&tw=1&pmid=29242641 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29242641 #FOAvip English Wikipedia <ref>{{Cite pmid|29242641 }}</ref> Ubiquitin ligases in oncogenic transformation and cancer therapy #MMPMID29242641 Senft D ; Qi J ; Ronai ZA Nat Rev Cancer 2018[Feb]; 18 (2 ): 69-88 PMID29242641 show ga The cellular response to external stress signals and DNA damage depends on the activity of ubiquitin ligases (E3s), which regulate numerous cellular processes, including homeostasis, metabolism and cell cycle progression. E3s recognize, interact with and ubiquitylate protein substrates in a temporally and spatially regulated manner. The topology of the ubiquitin chains dictates the fate of the substrates, marking them for recognition and degradation by the proteasome or altering their subcellular localization or assembly into functional complexes. Both genetic and epigenetic alterations account for the deregulation of E3s in cancer. Consequently, the stability and/or activity of E3 substrates are also altered, in some cases leading to downregulation of tumour-suppressor activities and upregulation of oncogenic activities. A better understanding of the mechanisms underlying E3 regulation and function in tumorigenesis is expected to identify novel prognostic markers and to enable the development of the next generation of anticancer therapies. This Review summarizes the oncogenic and tumour-suppressor roles of selected E3s and highlights novel opportunities for therapeutic intervention. |Animals [MESH] |Cell Proliferation [MESH] |Cell Transformation, Neoplastic [MESH] |Humans [MESH] |Neoplasms/drug therapy/*enzymology/genetics/physiopathology [MESH] |Ubiquitin-Protein Ligases/genetics/*metabolism [MESH]Ubiquitin ligases in oncogenic transformation and cancer therapy (epmc).pdf DeepDyve Pubget Overpricing