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10.1016/j.tibtech.2014.05.005 http://scihub22266oqcxt.onion/10.1016/j.tibtech.2014.05.005 C4146573!4146573!24908382     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Trends+Biotechnol 2014 ; 32 (7): 372-80 Nephropedia Template TP {{tp|p=24908382|t=2014. Therapeutic Protein Aggregation: Mechanisms, Design, and Control |pdf=|usr=}}{{24908382}} gab.com Text Therapeutic Protein Aggregation: Mechanisms, Design, and Control JO: Trends Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=24908382 #FOAvip While it is well known that proteins are only marginally stable in their folded states, it is often less well appreciated that most proteins are inherently aggregation-prone in their unfolded or partially unfolded states, and the resulting aggregates can be extremely stable and long-lived. For therapeutic proteins, aggregates are a significant risk factor for deleterious immune responses in patients, and can form via a variety of mechanisms. Controlling aggregation using a mechanistic approach may allow improved design of therapeutic protein stability, as a complement to existing design strategies that target desired protein structures and function. Recent results highlight the importance of balancing protein environment with the inherent aggregation propensities of polypeptide chains. Twit Text FOAVip Therapeutic Protein Aggregation: Mechanisms, Design, and Control ????Trends Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=24908382 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24908382 #FOAvip English Wikipedia <ref>{{Cite pmid|24908382}}</ref> Therapeutic Protein Aggregation: Mechanisms, Design, and Control #MMPMID24908382 Roberts CJ Trends Biotechnol 2014[Jul]; 32 (7): 372-80 PMID24908382show ga While it is well known that proteins are only marginally stable in their folded states, it is often less well appreciated that most proteins are inherently aggregation-prone in their unfolded or partially unfolded states, and the resulting aggregates can be extremely stable and long-lived. For therapeutic proteins, aggregates are a significant risk factor for deleterious immune responses in patients, and can form via a variety of mechanisms. Controlling aggregation using a mechanistic approach may allow improved design of therapeutic protein stability, as a complement to existing design strategies that target desired protein structures and function. Recent results highlight the importance of balancing protein environment with the inherent aggregation propensities of polypeptide chains. äTherapeutic Protein Aggregation: Mechanisms, Design, and Control (epmc).pdf DeepDyve Pubget Overpricing