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10.1002/pmic.201400386 http://scihub22266oqcxt.onion/10.1002/pmic.201400386 25492846!7167786!25492846     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proteomics 2015 ; 15 (5-6): 1075-88 Nephropedia Template TP {{tp|p=25492846|t=2015. Non-proteolytic functions of microbial proteases increase pathological complexity |pdf=|usr=}}{{25492846}} gab.com Text Non-proteolytic functions of microbial proteases increase pathological complexity JO: Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25492846 #FOAvip Proteases are enzymes that catalyse hydrolysis of peptide bonds thereby controlling the shape, size, function, composition, turnover and degradation of other proteins. In microbes, proteases are often identified as important virulence factors and as such have been targets for novel drug design. It is emerging that some proteases possess additional non-proteolytic functions that play important roles in host epithelia adhesion, tissue invasion and in modulating immune responses. These additional "moonlighting" functions have the potential to obfuscate data interpretation and have implications for therapeutic design. Moonlighting enzymes comprise a subcategory of multifunctional proteins that possess at least two distinct biological functions on a single polypeptide chain. Presently, identifying moonlighting proteins relies heavily on serendipitous empirical data with clues arising from proteins lacking signal peptides that are localised to the cell surface. Here, we describe examples of microbial proteases with additional non-proteolytic functions, including streptococcal pyrogenic exotoxin B, PepO and C5a peptidases, mycoplasmal aminopeptidases, mycobacterial chaperones and viral papain-like proteases. We explore how these non-proteolytic functions contribute to host cell adhesion, modulate the coagulation pathway, assist in non-covalent folding of proteins, participate in cell signalling, and increase substrate repertoire. We conclude by describing how proteomics has aided in moonlighting protein discovery, focusing attention on potential moonlighters in microbial exoproteomes. Twit Text FOAVip Non-proteolytic functions of microbial proteases increase pathological complexity ????Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=25492846 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25492846 #FOAvip English Wikipedia <ref>{{Cite pmid|25492846}}</ref> Non-proteolytic functions of microbial proteases increase pathological complexity #MMPMID25492846 Jarocki VM; Tacchi JL; Djordjevic SP Proteomics 2015[Mar]; 15 (5-6): 1075-88 PMID25492846show ga Proteases are enzymes that catalyse hydrolysis of peptide bonds thereby controlling the shape, size, function, composition, turnover and degradation of other proteins. In microbes, proteases are often identified as important virulence factors and as such have been targets for novel drug design. It is emerging that some proteases possess additional non-proteolytic functions that play important roles in host epithelia adhesion, tissue invasion and in modulating immune responses. These additional "moonlighting" functions have the potential to obfuscate data interpretation and have implications for therapeutic design. Moonlighting enzymes comprise a subcategory of multifunctional proteins that possess at least two distinct biological functions on a single polypeptide chain. Presently, identifying moonlighting proteins relies heavily on serendipitous empirical data with clues arising from proteins lacking signal peptides that are localised to the cell surface. Here, we describe examples of microbial proteases with additional non-proteolytic functions, including streptococcal pyrogenic exotoxin B, PepO and C5a peptidases, mycoplasmal aminopeptidases, mycobacterial chaperones and viral papain-like proteases. We explore how these non-proteolytic functions contribute to host cell adhesion, modulate the coagulation pathway, assist in non-covalent folding of proteins, participate in cell signalling, and increase substrate repertoire. We conclude by describing how proteomics has aided in moonlighting protein discovery, focusing attention on potential moonlighters in microbial exoproteomes. |*Bacteria/enzymology/pathogenicity[MESH] |*Bacterial Proteins/analysis/physiology[MESH] |*Peptide Hydrolases/analysis/physiology[MESH] |*Proteome/analysis/physiology[MESH] |*Virulence Factors/analysis/physiology[MESH]Non-proteolytic functions of microbial proteases increase pathological(epmc).pdf DeepDyve Pubget Overpricing