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10.1038/nmeth.3395 http://scihub22266oqcxt.onion/10.1038/nmeth.3395 C4449307!4449307 !25938370     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25938370 &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\25938370 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Methods 2015 ; 12 (6 ): 553-60 Nephropedia Template TP {{tp|p=25938370 |t=2015. Rapid, optimized interactomic screening |pdf=|usr=}}{{25938370 }} gab.com Text Rapid, optimized interactomic screening JO: Nat Methods http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes. Twit Text FOAVip Rapid, optimized interactomic screening ????Nat Methods http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25938370 #FOAvip English Wikipedia <ref>{{Cite pmid|25938370 }}</ref> Rapid, optimized interactomic screening #MMPMID25938370 Hakhverdyan Z ; Domanski M ; Hough LE ; Oroskar AA ; Oroskar AR ; Keegan S ; Dilworth DJ ; Molloy KR ; Sherman V ; Aitchison JD ; Fenyö D ; Chait BT ; Jensen TH ; Rout MP ; LaCava J Nat Methods 2015[Jun]; 12 (6 ): 553-60 PMID25938370 show ga We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes. |Cell Line [MESH] |Escherichia coli [MESH] |Humans [MESH] |Macromolecular Substances/*metabolism [MESH] |Protein Interaction Mapping/*methods [MESH] |Protein Interaction Maps [MESH] |Proteins/*chemistry/metabolism [MESH] |Proteomics/methods [MESH]Rapid, optimized interactomic screening (epmc).pdf DeepDyve Pubget Overpricing