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10.1097/BCR.0000000000000335 http://scihub22266oqcxt.onion/10.1097/BCR.0000000000000335 C5086290!5086290!27058579     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 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       J+Burn+Care+Res 2016 ; 37 (6): e501-7 Nephropedia Template TP {{tp|p=27058579|t=2016. Apyrase Elicits Host Antimicrobial Responses and Resolves Infection in Burns |pdf=|usr=}}{{27058579}} gab.com Text Apyrase Elicits Host Antimicrobial Responses and Resolves Infection in Burns JO: J Burn Care Res http://www.kidney.de/pget.php?&tw=1&pmid=27058579 #FOAvip The authors previously reported that adenosine triphosphate (ATP) stimulates biofilm formation and removal of the ATP could reduce biofilm formation. The main objective of this study was to evaluate the effects of the ATP-hydrolyzing enzyme, apyrase, on control of Acinetabacter baumannii infection in the burn wound as well as to assess host skin antimicrobial responses. The authors found that apyrase stimulated nitric oxide formation at the wound site and reduced CD55 expression, thereby inducing the assembly of membrane attack complexes. Apyrase treatment nearly eradicated multidrug-resistant A. baumannii from burn wounds in the absence of antibiotics. Apyrase may be an effective therapy against antibiotic-resistant bacterial infections in burns. Twit Text FOAVip Apyrase Elicits Host Antimicrobial Responses and Resolves Infection in Burns ????J Burn Care Res http://www.kidney.de/pget.php?&tw=1&pmid=27058579 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27058579 #FOAvip English Wikipedia <ref>{{Cite pmid|27058579}}</ref> Apyrase Elicits Host Antimicrobial Responses and Resolves Infection in Burns #MMPMID27058579 Bayliss JM; Levi B; Wu J; Wang SC; Su GL; Xi C J Burn Care Res 2016[Nov]; 37 (6): e501-7 PMID27058579show ga The authors previously reported that adenosine triphosphate (ATP) stimulates biofilm formation and removal of the ATP could reduce biofilm formation. The main objective of this study was to evaluate the effects of the ATP-hydrolyzing enzyme, apyrase, on control of Acinetabacter baumannii infection in the burn wound as well as to assess host skin antimicrobial responses. The authors found that apyrase stimulated nitric oxide formation at the wound site and reduced CD55 expression, thereby inducing the assembly of membrane attack complexes. Apyrase treatment nearly eradicated multidrug-resistant A. baumannii from burn wounds in the absence of antibiotics. Apyrase may be an effective therapy against antibiotic-resistant bacterial infections in burns. äApyrase Elicits Host Antimicrobial Responses and Resolves Infection in(epmc).pdf DeepDyve Pubget Overpricing