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10.1128/JB.00769-15 http://scihub22266oqcxt.onion/10.1128/JB.00769-15 C4810614!4810614 !26644434     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26644434 &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 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 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\26644434 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Bacteriol 2015 ; 198 (5 ): 746-54 Nephropedia Template TP {{tp|p=26644434 |t=2015. Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |pdf=|usr=}}{{26644434 }} gab.com Text Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria JO: J Bacteriol http://www.kidney.de/pget.php?&tw=1&pmid=26644434 #FOAvip Disulfide bonds are important for the stability and function of many secreted proteins. In Gram-negative bacteria, these linkages are catalyzed by thiol-disulfide oxidoreductases (Dsb) in the periplasm. Protein oxidation has been well studied in these organisms, but it has not fully been explored in Gram-positive bacteria, which lack traditional periplasmic compartments. Recent bioinformatics analyses have suggested that the high-GC-content bacteria (i.e., actinobacteria) rely on disulfide-bond-forming pathways. In support of this, Dsb-like proteins have been identified in Mycobacterium tuberculosis, but their functions are not known. Actinomyces oris and Corynebacterium diphtheriae have recently emerged as models to study disulfide bond formation in actinobacteria. In both organisms, disulfide bonds are catalyzed by the membrane-bound oxidoreductase MdbA. Remarkably, unlike known Dsb proteins, MdbA is important for pathogenesis and growth, which makes it a potential target for new antibacterial drugs. This review will discuss disulfide-bond-forming pathways in bacteria, with a special focus on Gram-positive bacteria. Twit Text FOAVip Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria ????J Bacteriol http://www.kidney.de/pget.php?&tw=1&pmid=26644434 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26644434 #FOAvip English Wikipedia <ref>{{Cite pmid|26644434 }}</ref> Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria #MMPMID26644434 Reardon-Robinson ME ; Ton-That H J Bacteriol 2015[Dec]; 198 (5 ): 746-54 PMID26644434 show ga Disulfide bonds are important for the stability and function of many secreted proteins. In Gram-negative bacteria, these linkages are catalyzed by thiol-disulfide oxidoreductases (Dsb) in the periplasm. Protein oxidation has been well studied in these organisms, but it has not fully been explored in Gram-positive bacteria, which lack traditional periplasmic compartments. Recent bioinformatics analyses have suggested that the high-GC-content bacteria (i.e., actinobacteria) rely on disulfide-bond-forming pathways. In support of this, Dsb-like proteins have been identified in Mycobacterium tuberculosis, but their functions are not known. Actinomyces oris and Corynebacterium diphtheriae have recently emerged as models to study disulfide bond formation in actinobacteria. In both organisms, disulfide bonds are catalyzed by the membrane-bound oxidoreductase MdbA. Remarkably, unlike known Dsb proteins, MdbA is important for pathogenesis and growth, which makes it a potential target for new antibacterial drugs. This review will discuss disulfide-bond-forming pathways in bacteria, with a special focus on Gram-positive bacteria. |*Disulfides/chemistry/metabolism [MESH] |Actinomyces/genetics/*metabolism [MESH] |Bacterial Proteins/genetics/*metabolism [MESH] |Corynebacterium diphtheriae/genetics/*metabolism [MESH] |Gene Expression Regulation, Bacterial/*physiology [MESH] |Oxidoreductases/metabolism [MESH]Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria (epmc).pdf DeepDyve Pubget Overpricing