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10.1007/s12192-017-0813-x http://scihub22266oqcxt.onion/10.1007/s12192-017-0813-x C5655371!5655371!28567569     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Stress+Chaperones 2017 ; 22 (6): 833-45 Nephropedia Template TP {{tp|p=28567569|t=2017. On the role, ecology, phylogeny, and structure of dual-family immunophilins |pdf=|usr=}}{{28567569}} gab.com Text On the role, ecology, phylogeny, and structure of dual-family immunophilins JO: Cell Stress Chaperones http://www.kidney.de/pget.php?&tw=1&pmid=28567569 #FOAvip The novel class of dual-family immunophilins (henceforth abbreviated as DFI) represents naturally occurring chimera of classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker that may include a three-unit tetratricopeptide (TPR) repeat. Here, I report a comprehensive analysis of all current DFI sequences and their host organisms. DFIs are of two kinds: CFBP (cyclosporin- and FK506-binding protein) and FCBP (FK506- and cyclosporin-binding protein), found in eukaryotes. The CFBP type occurs in select bacteria that are mostly extremophiles, such as psychrophilic, thermophilic, halophilic, and sulfur-reducing. Essentially all DFI organisms are unicellular. I suggest that DFIs are specialized bifunctional chaperones that use their flexible interdomain linker to associate with large polypeptides or multisubunit megacomplexes to promote simultaneous folding or renaturation of two clients in proximity, essential in stressful and denaturing environments. Analysis of sequence homology and predicted 3D structures of the FKBP and CYN domains as well as the TPR linkers upheld the modular nature of the DFIs and revealed the uniqueness of their TPR domain. The CFBP and FCBP genes appear to have evolved in parallel pathways with no obvious single common ancestor. The occurrence of both types of DFI in multiple unrelated phylogenetic clades supported their selection in metabolic and environmental niche roles rather than a traditional taxonomic relationship. Nonetheless, organisms with these rare immunophilins may define an operational taxonomic unit (OTU) bound by the commonality of chaperone function.Electronic supplementary material: The online version of this article (doi:10.1007/s12192-017-0813-x) contains supplementary material, which is available to authorized users. Twit Text FOAVip On the role, ecology, phylogeny, and structure of dual-family immunophilins ????Cell Stress Chaperones http://www.kidney.de/pget.php?&tw=1&pmid=28567569 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28567569 #FOAvip English Wikipedia <ref>{{Cite pmid|28567569}}</ref> On the role, ecology, phylogeny, and structure of dual-family immunophilins #MMPMID28567569 Barik S Cell Stress Chaperones 2017[Nov]; 22 (6): 833-45 PMID28567569show ga The novel class of dual-family immunophilins (henceforth abbreviated as DFI) represents naturally occurring chimera of classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker that may include a three-unit tetratricopeptide (TPR) repeat. Here, I report a comprehensive analysis of all current DFI sequences and their host organisms. DFIs are of two kinds: CFBP (cyclosporin- and FK506-binding protein) and FCBP (FK506- and cyclosporin-binding protein), found in eukaryotes. The CFBP type occurs in select bacteria that are mostly extremophiles, such as psychrophilic, thermophilic, halophilic, and sulfur-reducing. Essentially all DFI organisms are unicellular. I suggest that DFIs are specialized bifunctional chaperones that use their flexible interdomain linker to associate with large polypeptides or multisubunit megacomplexes to promote simultaneous folding or renaturation of two clients in proximity, essential in stressful and denaturing environments. Analysis of sequence homology and predicted 3D structures of the FKBP and CYN domains as well as the TPR linkers upheld the modular nature of the DFIs and revealed the uniqueness of their TPR domain. The CFBP and FCBP genes appear to have evolved in parallel pathways with no obvious single common ancestor. The occurrence of both types of DFI in multiple unrelated phylogenetic clades supported their selection in metabolic and environmental niche roles rather than a traditional taxonomic relationship. Nonetheless, organisms with these rare immunophilins may define an operational taxonomic unit (OTU) bound by the commonality of chaperone function.Electronic supplementary material: The online version of this article (doi:10.1007/s12192-017-0813-x) contains supplementary material, which is available to authorized users. äOn the role, ecology, phylogeny, and structure of dual-family immunoph(epmc).pdf DeepDyve Pubget Overpricing