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10.3390/biom7030067 http://scihub22266oqcxt.onion/10.3390/biom7030067 C5618248!5618248 !28895938     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 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 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 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 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 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\28895938 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biomolecules 2017 ; 7 (3 ): ä Nephropedia Template TP {{tp|p=28895938 |t=2017. Functional Amyloid Protection in the Eye Lens: Retention of ?-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils |pdf=|usr=}}{{28895938 }} gab.com Text Functional Amyloid Protection in the Eye Lens: Retention of -Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=28895938 #FOAvip Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically associated with a loss of protein function and/or a gain of toxic function, as the native structure of the protein undergoes major alteration to form a cross ?-sheet array. It is now well recognised that some amyloid fibrils have a biological function, which has led to increased interest in the potential that these so-called functional amyloids may either retain the function of the native protein, or gain function upon adopting a fibrillar structure. Herein, we investigate the molecular chaperone ability of ?-crystallin, the predominant eye lens protein which is composed of two related subunits ?A- and ?B-crystallin, and its capacity to retain and even enhance its chaperone activity after forming aggregate structures under conditions of thermal and chemical stress. We demonstrate that both eye lens ?-crystallin and ?B-crystallin (which is also found extensively outside the lens) retain, to a significant degree, their molecular chaperone activity under conditions of structural change, including after formation into amyloid fibrils and amorphous aggregates. The results can be related directly to the effects of aging on the structure and chaperone function of ?-crystallin in the eye lens, particularly its ability to prevent crystallin protein aggregation and hence lens opacification associated with cataract formation. Twit Text FOAVip Functional Amyloid Protection in the Eye Lens: Retention of -Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=28895938 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28895938 #FOAvip English Wikipedia <ref>{{Cite pmid|28895938 }}</ref> Functional Amyloid Protection in the Eye Lens: Retention of ?-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils #MMPMID28895938 Garvey M ; Ecroyd H ; Ray NJ ; Gerrard JA ; Carver JA Biomolecules 2017[Sep]; 7 (3 ): ä PMID28895938 show ga Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically associated with a loss of protein function and/or a gain of toxic function, as the native structure of the protein undergoes major alteration to form a cross ?-sheet array. It is now well recognised that some amyloid fibrils have a biological function, which has led to increased interest in the potential that these so-called functional amyloids may either retain the function of the native protein, or gain function upon adopting a fibrillar structure. Herein, we investigate the molecular chaperone ability of ?-crystallin, the predominant eye lens protein which is composed of two related subunits ?A- and ?B-crystallin, and its capacity to retain and even enhance its chaperone activity after forming aggregate structures under conditions of thermal and chemical stress. We demonstrate that both eye lens ?-crystallin and ?B-crystallin (which is also found extensively outside the lens) retain, to a significant degree, their molecular chaperone activity under conditions of structural change, including after formation into amyloid fibrils and amorphous aggregates. The results can be related directly to the effects of aging on the structure and chaperone function of ?-crystallin in the eye lens, particularly its ability to prevent crystallin protein aggregation and hence lens opacification associated with cataract formation. |Amyloid/chemistry/*metabolism [MESH] |Animals [MESH] |Cattle [MESH] |Humans [MESH] |Lens, Crystalline [MESH] |Molecular Chaperones/chemistry/metabolism [MESH] |Protein Aggregates [MESH] |Protein Binding [MESH] |Protein Folding [MESH] |Protein Structure, Tertiary [MESH] |Protein Unfolding [MESH] |alpha-Crystallin A Chain/*chemistry/*metabolism [MESH]Functional Amyloid Protection in the Eye Lens: Retention of ?-Crystall(epmc).pdf DeepDyve Pubget Overpricing