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10.1002/bit.25119 http://scihub22266oqcxt.onion/10.1002/bit.25119 C4492694!4492694!24114411     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biotechnol+Bioeng 2014 ; 111 (3): 462-74 Nephropedia Template TP {{tp|p=24114411|t=2014. Cis-Suppression to Arrest Protein Aggregation in Mammalian Cells |pdf=|usr=}}{{24114411}} gab.com Text Cis-Suppression to Arrest Protein Aggregation in Mammalian Cells JO: Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=24114411 #FOAvip Protein misfolding and aggregation are implicated in numerous human diseases and significantly lower production yield of proteins expressed in mammalian cells. Despite the importance of understanding and suppressing protein aggregation in mammalian cells, a protein design and selection strategy to modulate protein misfolding/aggregation in mammalian cells has not yet been reported. In this work, we address the particular challenge presented by mutation-induced protein aggregation in mammalian cells. We hypothesize that an additional mutation(s) can be introduced in an aggregation-prone protein variant, spatially near the original mutation, to suppress misfolding and aggregation (cis-suppression). As a model protein, we chose human copper, zinc superoxide dismutase mutant (SOD1A4V) containing an alanine to valine mutation at residue 4, associated with the familial form of amyotrophic lateral sclerosis. We used the program RosettaDesign to identify Phe20 in SOD1A4V as a key residue responsible for SOD1A4V conformational destabilization. This information was used to rationally develop a pool of candidate mutations at the Phe20 site. After two rounds of mammalian-cell based screening of the variants, three novel SOD1A4V variants with a significantly reduced aggregation propensity inside cells were selected. The enhanced stability and reduced aggregation propensity of the three novel SOD1A4V variants were verified using cell fractionation and in vitro stability assays. Twit Text FOAVip Cis-Suppression to Arrest Protein Aggregation in Mammalian Cells ????Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=24114411 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24114411 #FOAvip English Wikipedia <ref>{{Cite pmid|24114411}}</ref> Cis-Suppression to Arrest Protein Aggregation in Mammalian Cells #MMPMID24114411 Gregoire S; Zhang S; Costanzo J; Wilson K; Fernandez EJ; Kwon I Biotechnol Bioeng 2014[Mar]; 111 (3): 462-74 PMID24114411show ga Protein misfolding and aggregation are implicated in numerous human diseases and significantly lower production yield of proteins expressed in mammalian cells. Despite the importance of understanding and suppressing protein aggregation in mammalian cells, a protein design and selection strategy to modulate protein misfolding/aggregation in mammalian cells has not yet been reported. In this work, we address the particular challenge presented by mutation-induced protein aggregation in mammalian cells. We hypothesize that an additional mutation(s) can be introduced in an aggregation-prone protein variant, spatially near the original mutation, to suppress misfolding and aggregation (cis-suppression). As a model protein, we chose human copper, zinc superoxide dismutase mutant (SOD1A4V) containing an alanine to valine mutation at residue 4, associated with the familial form of amyotrophic lateral sclerosis. We used the program RosettaDesign to identify Phe20 in SOD1A4V as a key residue responsible for SOD1A4V conformational destabilization. This information was used to rationally develop a pool of candidate mutations at the Phe20 site. After two rounds of mammalian-cell based screening of the variants, three novel SOD1A4V variants with a significantly reduced aggregation propensity inside cells were selected. The enhanced stability and reduced aggregation propensity of the three novel SOD1A4V variants were verified using cell fractionation and in vitro stability assays. äCis-Suppression to Arrest Protein Aggregation in Mammalian Cells (epmc).pdf DeepDyve Pubget Overpricing