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10.1021/acs.biochem.5b00473 http://scihub22266oqcxt.onion/10.1021/acs.biochem.5b00473 C4787542!4787542!26305369     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26305369&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 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 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 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 298.79999999999995 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\26305369.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochemistry 2015 ; 54 (36): 5546-56 Nephropedia Template TP {{tp|p=26305369|t=2015. Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor Beta Induced Protein (TGFBIp) in Corneal Dystrophies Compared to the Non-Fibrillating R555W and R555Q Mutants |pdf=|usr=}}{{26305369}} gab.com Text Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor Beta Induced Protein (TGFBIp) in Corneal Dystrophies Compared to the Non-Fibrillating R555W and R555Q Mutants JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26305369 #FOAvip The human transforming growth factor beta induced protein (TGFBIp) is involved in several types of corneal dystrophies where protein aggregation and amyloid fibril formation severely impairs vision. Most disease-causing mutations are located in the last of four homologous fasciclin-1 (FAS1) domains of the protein, and it has been shown that when isolated, the fourth FAS1 domain (FAS1?4) mimics the behavior of full-length TGFBIp. In this study, we use molecular dynamics simulations and principal component analysis to study the wild type FAS1?4 domain along with three disease-causing mutations (R555W, R555Q, and A546T) to decipher any internal difference in dynamical properties of the domains that may explain their varied stabilities and aggregation properties. In addition, we use a protein-protein docking method in combination with chemical cross-linking experiments and mass spectrometry of the cross-linked species to obtain information about interaction faces between identical FAS1?4 domains. The results show that the pathogenic mutations A546T and R555W affect the packing in the hydrophobic core of FAS1?4 in different directions. We further show that the FAS1?4 monomers associate using their ?-rich regions consistent with peptides observed to be part of the amyloid fibril core in lattice corneal dystrophy patients. Twit Text FOAVip Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor Beta Induced Protein (TGFBIp) in Corneal Dystrophies Compared to the Non-Fibrillating R555W and R555Q Mutants ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26305369 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26305369 #FOAvip English Wikipedia <ref>{{Cite pmid|26305369}}</ref> Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor Beta Induced Protein (TGFBIp) in Corneal Dystrophies Compared to the Non-Fibrillating R555W and R555Q Mutants #MMPMID26305369 Koldsø H; Andersen OJ; Nikolajsen CL; Scavenius C; Sørensen CS; Underhaug J; Runager K; Nielsen NC; Enghild JJ; Schiøtt B Biochemistry 2015[Sep]; 54 (36): 5546-56 PMID26305369show ga The human transforming growth factor beta induced protein (TGFBIp) is involved in several types of corneal dystrophies where protein aggregation and amyloid fibril formation severely impairs vision. Most disease-causing mutations are located in the last of four homologous fasciclin-1 (FAS1) domains of the protein, and it has been shown that when isolated, the fourth FAS1 domain (FAS1?4) mimics the behavior of full-length TGFBIp. In this study, we use molecular dynamics simulations and principal component analysis to study the wild type FAS1?4 domain along with three disease-causing mutations (R555W, R555Q, and A546T) to decipher any internal difference in dynamical properties of the domains that may explain their varied stabilities and aggregation properties. In addition, we use a protein-protein docking method in combination with chemical cross-linking experiments and mass spectrometry of the cross-linked species to obtain information about interaction faces between identical FAS1?4 domains. The results show that the pathogenic mutations A546T and R555W affect the packing in the hydrophobic core of FAS1?4 in different directions. We further show that the FAS1?4 monomers associate using their ?-rich regions consistent with peptides observed to be part of the amyloid fibril core in lattice corneal dystrophy patients. äEarly Events in the Amyloid Formation of the A546T Mutant of Transform(epmc).pdf DeepDyve Pubget Overpricing