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10.1073/pnas.1515876112 http://scihub22266oqcxt.onion/10.1073/pnas.1515876112 C4672786!4672786 !26553978     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26553978 &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       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (48 ): 14811-6 Nephropedia Template TP {{tp|p=26553978 |t=2015. Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity |pdf=|usr=}}{{26553978 }} gab.com Text Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26553978 #FOAvip Crystallography of the cores of phosphotyrosine-activated dimers of STAT1 (132-713) and STAT3 (127-722) bound to a similar double-stranded deoxyoligonucleotide established the domain structure of the STATs and the structural basis for activation through tyrosine phosphorylation and dimerization. We reported earlier that mutants in the linker domain of STAT1 that connect the DNA-binding domain and SH2 domain can prevent transcriptional activation. Because of the pervasive importance of persistently activated STAT3 in many human cancers and the difficulty of finding useful drug candidates aimed at disrupting the pY interchange in active STAT3 dimers, we have examined effects of an array of mutants in the STAT3 linker domain. We have found several STAT3 linker domain mutants to have profound effects of inhibiting STAT3 transcriptional activation. From these results, we propose (i) there is definite functional interaction of the linker both with the DNA binding domain and with the SH2 domain, and (ii) these putative contacts provide potential new targets for small molecule-induced pSTAT3 inhibition. Twit Text FOAVip Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26553978 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26553978 #FOAvip English Wikipedia <ref>{{Cite pmid|26553978 }}</ref> Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity #MMPMID26553978 Mertens C ; Haripal B ; Klinge S ; Darnell JE Proc Natl Acad Sci U S A 2015[Dec]; 112 (48 ): 14811-6 PMID26553978 show ga Crystallography of the cores of phosphotyrosine-activated dimers of STAT1 (132-713) and STAT3 (127-722) bound to a similar double-stranded deoxyoligonucleotide established the domain structure of the STATs and the structural basis for activation through tyrosine phosphorylation and dimerization. We reported earlier that mutants in the linker domain of STAT1 that connect the DNA-binding domain and SH2 domain can prevent transcriptional activation. Because of the pervasive importance of persistently activated STAT3 in many human cancers and the difficulty of finding useful drug candidates aimed at disrupting the pY interchange in active STAT3 dimers, we have examined effects of an array of mutants in the STAT3 linker domain. We have found several STAT3 linker domain mutants to have profound effects of inhibiting STAT3 transcriptional activation. From these results, we propose (i) there is definite functional interaction of the linker both with the DNA binding domain and with the SH2 domain, and (ii) these putative contacts provide potential new targets for small molecule-induced pSTAT3 inhibition. |*Mutation, Missense [MESH] |*Transcriptional Activation [MESH] |Amino Acid Substitution [MESH] |Cell Line, Tumor [MESH] |Humans [MESH] |Neoplasm Proteins/genetics/*metabolism [MESH] |Neoplasms/genetics/*metabolism/pathology [MESH] |Phosphorylation [MESH] |Protein Multimerization [MESH] |STAT1 Transcription Factor/genetics/metabolism [MESH]Mutations in the linker domain affect phospho-STAT3 function and sugge(epmc).pdf DeepDyve Pubget Overpricing