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10.1098/rsob.170167 http://scihub22266oqcxt.onion/10.1098/rsob.170167 C5666083!5666083 !29021212     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29021212 &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 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 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\29021212 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Open+Biol 2017 ; 7 (10 ): ä Nephropedia Template TP {{tp|p=29021212 |t=2017. Protein SUMOylation modification and its associations with disease |pdf=|usr=}}{{29021212 }} gab.com Text Protein SUMOylation modification and its associations with disease JO: Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=29021212 #FOAvip SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site. With the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease. Twit Text FOAVip Protein SUMOylation modification and its associations with disease ????Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=29021212 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29021212 #FOAvip English Wikipedia <ref>{{Cite pmid|29021212 }}</ref> Protein SUMOylation modification and its associations with disease #MMPMID29021212 Yang Y ; He Y ; Wang X ; Liang Z ; He G ; Zhang P ; Zhu H ; Xu N ; Liang S Open Biol 2017[Oct]; 7 (10 ): ä PMID29021212 show ga SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site. With the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease. |*Disease Susceptibility [MESH] |*Sumoylation [MESH] |Animals [MESH] |Humans [MESH] |Protein Processing, Post-Translational [MESH] |Proteins/genetics/*metabolism [MESH] |Signal Transduction [MESH] |Ubiquitin/metabolism [MESH]Protein SUMOylation modification and its associations with disease (epmc).pdf DeepDyve Pubget Overpricing