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10.1016/j.tibtech.2014.08.001 http://scihub22266oqcxt.onion/10.1016/j.tibtech.2014.08.001 C4281928!4281928!25168413     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Trends+Biotechnol 2014 ; 32 (10): 506-12 Nephropedia Template TP {{tp|p=25168413|t=2014. Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology |pdf=|usr=}}{{25168413}} gab.com Text Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology JO: Trends Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=25168413 #FOAvip Biotechnology is often limited by weak interactions. We suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions. Here we summarize peptide tags able to form spontaneous amide bonds, based on harnessing reactions of adhesion proteins from the bacterium Streptococcus pyogenes. These include irreversible peptide-protein interaction of SpyTag with SpyCatcher, as well as irreversible peptide-peptide interaction via SpyLigase. We describe existing applications, including polymerization to enhance cancer cell capture, assembly of living biomaterial, access to diverse protein shapes, and improved enzyme resilience. We also point to future opportunities for resisting biological force and extending the scope of protein nanotechnology. Twit Text FOAVip Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology ????Trends Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=25168413 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25168413 #FOAvip English Wikipedia <ref>{{Cite pmid|25168413}}</ref> Superglue from Bacteria: Unbreakable Bridges for Protein Nanotechnology #MMPMID25168413 Veggiani G; Zakeri B; Howarth M Trends Biotechnol 2014[Oct]; 32 (10): 506-12 PMID25168413show ga Biotechnology is often limited by weak interactions. We suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions. Here we summarize peptide tags able to form spontaneous amide bonds, based on harnessing reactions of adhesion proteins from the bacterium Streptococcus pyogenes. These include irreversible peptide-protein interaction of SpyTag with SpyCatcher, as well as irreversible peptide-peptide interaction via SpyLigase. We describe existing applications, including polymerization to enhance cancer cell capture, assembly of living biomaterial, access to diverse protein shapes, and improved enzyme resilience. We also point to future opportunities for resisting biological force and extending the scope of protein nanotechnology. äSuperglue from Bacteria: Unbreakable Bridges for Protein Nanotechnolog(epmc).pdf DeepDyve Pubget Overpricing