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10.1146/annurev-biochem-072611-130030 http://scihub22266oqcxt.onion/10.1146/annurev-biochem-072611-130030 C4044913!4044913 !23451869     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\23451869 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Annu+Rev+Biochem 2013 ; 82 (ä): 745-74 Nephropedia Template TP {{tp|p=23451869 |t=2013. Systemic amyloidoses |pdf=|usr=}}{{23451869 }} gab.com Text Systemic amyloidoses JO: Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=23451869 #FOAvip The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses. Twit Text FOAVip Systemic amyloidoses ????Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=23451869 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23451869 #FOAvip English Wikipedia <ref>{{Cite pmid|23451869 }}</ref> Systemic amyloidoses #MMPMID23451869 Blancas-Mejía LM ; Ramirez-Alvarado M Annu Rev Biochem 2013[]; 82 (ä): 745-74 PMID23451869 show ga The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses. |*Protein Folding [MESH] |Amyloid/*metabolism [MESH] |Amyloidosis/etiology/*metabolism [MESH] |Animals [MESH] |Disease Models, Animal [MESH] |Humans [MESH] |Immunoglobulin Light Chains/chemistry/*metabolism [MESH]Systemic amyloidoses (epmc).pdf DeepDyve Pubget Overpricing