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10.1002/humu.22534 http://scihub22266oqcxt.onion/10.1002/humu.22534 C4876038!4876038 !24599843     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24599843 &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       Hum+Mutat 2014 ; 35 (5 ): 585-93 Nephropedia Template TP {{tp|p=24599843 |t=2014. Elucidating common structural features of human pathogenic variations using large-scale atomic-resolution protein networks |pdf=|usr=}}{{24599843 }} gab.com Text Elucidating common structural features of human pathogenic variations using large-scale atomic-resolution protein networks JO: Hum Mutat http://www.kidney.de/pget.php?&tw=1&pmid=24599843 #FOAvip With the rapid growth of structural genomics, numerous protein crystal structures have become available. However, the parallel increase in knowledge of the functional principles underlying biological processes, and more specifically the underlying molecular mechanisms of disease, has been less dramatic. This notwithstanding, the study of complex cellular networks has made possible the inference of protein functions on a large scale. Here, we combine the scale of network systems biology with the resolution of traditional structural biology to generate a large-scale atomic-resolution interactome-network comprising 3,398 interactions between 2,890 proteins with a well-defined interaction interface and interface residues for each interaction. Within the framework of this atomic-resolution network, we have explored the structural principles underlying variations causing human-inherited disease. We find that in-frame pathogenic variations are enriched at both the interface and in the interacting domain, suggesting that variations not only at interface "hot-spots," but in the entire interacting domain can result in alterations of interactions. Further, the sites of pathogenic variations are closely related to the biophysical strength of the interactions they perturb. Finally, we show that biochemical alterations consequent to these variations are considerably more disruptive than evolutionary changes, with the most significant alterations at the protein interaction interface. Twit Text FOAVip Elucidating common structural features of human pathogenic variations using large-scale atomic-resolution protein networks ????Hum Mutat http://www.kidney.de/pget.php?&tw=1&pmid=24599843 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24599843 #FOAvip English Wikipedia <ref>{{Cite pmid|24599843 }}</ref> Elucidating common structural features of human pathogenic variations using large-scale atomic-resolution protein networks #MMPMID24599843 Das J ; Lee HR ; Sagar A ; Fragoza R ; Liang J ; Wei X ; Wang X ; Mort M ; Stenson PD ; Cooper DN ; Yu H Hum Mutat 2014[May]; 35 (5 ): 585-93 PMID24599843 show ga With the rapid growth of structural genomics, numerous protein crystal structures have become available. However, the parallel increase in knowledge of the functional principles underlying biological processes, and more specifically the underlying molecular mechanisms of disease, has been less dramatic. This notwithstanding, the study of complex cellular networks has made possible the inference of protein functions on a large scale. Here, we combine the scale of network systems biology with the resolution of traditional structural biology to generate a large-scale atomic-resolution interactome-network comprising 3,398 interactions between 2,890 proteins with a well-defined interaction interface and interface residues for each interaction. Within the framework of this atomic-resolution network, we have explored the structural principles underlying variations causing human-inherited disease. We find that in-frame pathogenic variations are enriched at both the interface and in the interacting domain, suggesting that variations not only at interface "hot-spots," but in the entire interacting domain can result in alterations of interactions. Further, the sites of pathogenic variations are closely related to the biophysical strength of the interactions they perturb. Finally, we show that biochemical alterations consequent to these variations are considerably more disruptive than evolutionary changes, with the most significant alterations at the protein interaction interface. |*Genetic Diseases, Inborn/genetics/pathology [MESH] |*Systems Biology [MESH] |Computational Biology [MESH] |Databases, Protein [MESH] |Humans [MESH] |Models, Theoretical [MESH] |Protein Interaction Maps/*genetics [MESH]Elucidating common structural features of human pathogenic variations (epmc).pdf DeepDyve Pubget Overpricing