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10.1016/j.jmb.2015.04.013 http://scihub22266oqcxt.onion/10.1016/j.jmb.2015.04.013 C4706738!4706738 !25936650     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25936650 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Mol+Biol 2015 ; 427 (18 ): 2919-30 Nephropedia Template TP {{tp|p=25936650 |t=2015. The Mechanism and Function of Group II Chaperonins |pdf=|usr=}}{{25936650 }} gab.com Text The Mechanism and Function of Group II Chaperonins JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=25936650 #FOAvip Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings of eight paralogous subunits each. TRiC facilitates folding of approximately 10% of the eukaryotic proteome, including many cytoskeletal components and cell cycle regulators. Folding of many cellular substrates of TRiC cannot be assisted by any other chaperone. A complete structural and mechanistic understanding of this highly conserved and essential chaperonin remains elusive. However, recent work is beginning to shed light on key aspects of chaperonin function and how their unique properties underlie their contribution to maintaining cellular proteostasis. Twit Text FOAVip The Mechanism and Function of Group II Chaperonins ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=25936650 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25936650 #FOAvip English Wikipedia <ref>{{Cite pmid|25936650 }}</ref> The Mechanism and Function of Group II Chaperonins #MMPMID25936650 Lopez T ; Dalton K ; Frydman J J Mol Biol 2015[Sep]; 427 (18 ): 2919-30 PMID25936650 show ga Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings of eight paralogous subunits each. TRiC facilitates folding of approximately 10% of the eukaryotic proteome, including many cytoskeletal components and cell cycle regulators. Folding of many cellular substrates of TRiC cannot be assisted by any other chaperone. A complete structural and mechanistic understanding of this highly conserved and essential chaperonin remains elusive. However, recent work is beginning to shed light on key aspects of chaperonin function and how their unique properties underlie their contribution to maintaining cellular proteostasis. |*Protein Folding [MESH] |Adenosine Triphosphate/metabolism [MESH] |Archaea [MESH] |Cell Cycle Proteins/chemistry/metabolism [MESH] |Chaperonin Containing TCP-1/*chemistry/metabolism [MESH] |Cytoskeleton/chemistry/*metabolism [MESH] |Eukaryota [MESH] |Group II Chaperonins/*chemistry/metabolism [MESH] |Protein Conformation [MESH]The Mechanism and Function of Group II Chaperonins (epmc).pdf DeepDyve Pubget Overpricing