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10.3389/fmolb.2018.00042 http://scihub22266oqcxt.onion/10.3389/fmolb.2018.00042 C5934643!5934643!29755985     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29755985&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       Front+Mol+Biosci 2018 ; 5 (ä): ä Nephropedia Template TP {{tp|p=29755985|t=2018. Single-Ring Intermediates Are Essential for Some Chaperonins |pdf=|usr=}}{{29755985}} gab.com Text Single-Ring Intermediates Are Essential for Some Chaperonins JO: Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=29755985 #FOAvip Chaperonins are macromolecular complexes found throughout all kingdoms of life that assist unfolded proteins reach a biologically active state. Historically, chaperonins have been classified into two groups based on sequence, subunit structure, and the requirement for a co-chaperonin. Here, we present a brief review of chaperonins that can form double- and single-ring conformational intermediates in their protein-folding catalytic pathway. To date, the bacteriophage encoded chaperonins ?-EL and OBP, human mitochondrial chaperonin and most recently, the bacterial groEL/ES systems, have been reported to form single-ring intermediates as part of their normal protein-folding activity. These double-ring chaperonins separate into single-ring intermediates that have the ability to independently fold a protein. We discuss the structural and functional features along with the biological relevance of single-ring intermediates in cellular protein folding. Of special interest are the ?-EL and OBP chaperonins which demonstrate features of both group I and II chaperonins in addition to their ability to function via single-ring intermediates. Twit Text FOAVip Single-Ring Intermediates Are Essential for Some Chaperonins ????Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=29755985 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29755985 #FOAvip English Wikipedia <ref>{{Cite pmid|29755985}}</ref> Single-Ring Intermediates Are Essential for Some Chaperonins #MMPMID29755985 Bhatt JM; Enriquez AS; Wang J; Rojo HM; Molugu SK; Hildenbrand ZL; Bernal RA Front Mol Biosci 2018[]; 5 (ä): ä PMID29755985show ga Chaperonins are macromolecular complexes found throughout all kingdoms of life that assist unfolded proteins reach a biologically active state. Historically, chaperonins have been classified into two groups based on sequence, subunit structure, and the requirement for a co-chaperonin. Here, we present a brief review of chaperonins that can form double- and single-ring conformational intermediates in their protein-folding catalytic pathway. To date, the bacteriophage encoded chaperonins ?-EL and OBP, human mitochondrial chaperonin and most recently, the bacterial groEL/ES systems, have been reported to form single-ring intermediates as part of their normal protein-folding activity. These double-ring chaperonins separate into single-ring intermediates that have the ability to independently fold a protein. We discuss the structural and functional features along with the biological relevance of single-ring intermediates in cellular protein folding. Of special interest are the ?-EL and OBP chaperonins which demonstrate features of both group I and II chaperonins in addition to their ability to function via single-ring intermediates. äSingle-Ring Intermediates Are Essential for Some Chaperonins (epmc).pdf DeepDyve Pubget Overpricing