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10.1016/j.cell.2015.04.013 http://scihub22266oqcxt.onion/10.1016/j.cell.2015.04.013 C4441215!4441215 !25910212     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 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\25910212 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell 2015 ; 161 (3 ): 647-660 Nephropedia Template TP {{tp|p=25910212 |t=2015. Widespread macromolecular interaction perturbations in human genetic disorders |pdf=|usr=}}{{25910212 }} gab.com Text Widespread macromolecular interaction perturbations in human genetic disorders JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=25910212 #FOAvip How disease-associated mutations impair protein activities in the context of biological networks remains mostly undetermined. Although a few renowned alleles are well characterized, functional information is missing for over 100,000 disease-associated variants. Here we functionally profile several thousand missense mutations across a spectrum of Mendelian disorders using various interaction assays. The majority of disease-associated alleles exhibit wild-type chaperone binding profiles, suggesting they preserve protein folding or stability. While common variants from healthy individuals rarely affect interactions, two-thirds of disease-associated alleles perturb protein-protein interactions, with half corresponding to "edgetic" alleles affecting only a subset of interactions while leaving most other interactions unperturbed. With transcription factors, many alleles that leave protein-protein interactions intact affect DNA binding. Different mutations in the same gene leading to different interaction profiles often result in distinct disease phenotypes. Thus disease-associated alleles that perturb distinct protein activities rather than grossly affecting folding and stability are relatively widespread. Twit Text FOAVip Widespread macromolecular interaction perturbations in human genetic disorders ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=25910212 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25910212 #FOAvip English Wikipedia <ref>{{Cite pmid|25910212 }}</ref> Widespread macromolecular interaction perturbations in human genetic disorders #MMPMID25910212 Sahni N ; Yi S ; Taipale M ; Fuxman Bass JI ; Coulombe-Huntington J ; Yang F ; Peng J ; Weile J ; Karras GI ; Wang Y ; Kovács IA ; Kamburov A ; Krykbaeva I ; Lam MH ; Tucker G ; Khurana V ; Sharma A ; Liu YY ; Yachie N ; Zhong Q ; Shen Y ; Palagi A ; San-Miguel A ; Fan C ; Balcha D ; Dricot A ; Jordan DM ; Walsh JM ; Shah AA ; Yang X ; Stoyanova AK ; Leighton A ; Calderwood MA ; Jacob Y ; Cusick ME ; Salehi-Ashtiani K ; Whitesell LJ ; Sunyaev S ; Berger B ; Barabási AL ; Charloteaux B ; Hill DE ; Hao T ; Roth FP ; Xia Y ; Walhout AJM ; Lindquist S ; Vidal M Cell 2015[Apr]; 161 (3 ): 647-660 PMID25910212 show ga How disease-associated mutations impair protein activities in the context of biological networks remains mostly undetermined. Although a few renowned alleles are well characterized, functional information is missing for over 100,000 disease-associated variants. Here we functionally profile several thousand missense mutations across a spectrum of Mendelian disorders using various interaction assays. The majority of disease-associated alleles exhibit wild-type chaperone binding profiles, suggesting they preserve protein folding or stability. While common variants from healthy individuals rarely affect interactions, two-thirds of disease-associated alleles perturb protein-protein interactions, with half corresponding to "edgetic" alleles affecting only a subset of interactions while leaving most other interactions unperturbed. With transcription factors, many alleles that leave protein-protein interactions intact affect DNA binding. Different mutations in the same gene leading to different interaction profiles often result in distinct disease phenotypes. Thus disease-associated alleles that perturb distinct protein activities rather than grossly affecting folding and stability are relatively widespread. |*Mutation, Missense [MESH] |*Protein Interaction Maps [MESH] |DNA-Binding Proteins/genetics/metabolism [MESH] |Disease/*genetics [MESH] |Genome-Wide Association Study [MESH] |Humans [MESH] |Open Reading Frames [MESH] |Protein Folding [MESH] |Protein Stability [MESH]Widespread macromolecular interaction perturbations in human genetic d(epmc).pdf DeepDyve Pubget Overpricing