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10.1016/j.abb.2009.05.013 http://scihub22266oqcxt.onion/10.1016/j.abb.2009.05.013 19477160/?report=reader!3895411!19477160     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19477160&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 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Arch+Biochem+Biophys 2009 ; 487 (2): 105-14 Nephropedia Template TP {{tp|p=19477160|t=2009. A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions |pdf=|usr=}}{{19477160}} gab.com Text A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions JO: Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=19477160 #FOAvip We explored furin substrate requirements in addition to the motif R-X-K/R-R using synthetic fluorescent resonance energy transfer (FRET) decapeptides. These decapeptides were derived from furin cleavage sites in viral coat glycoproteins and human and bacterial protein precursors. The hydrolysis by furin of most substrate was activated by K(+) ion, whereas kosmotropic anions of the Hofmeister series were inhibitors. The analysis of furin hydrolytic activity showed that its efficiency is highly dependent on the particular combinations of amino acids at different substrate positions. There is a clear interdependence of furin subsites that must be taken in account in determining its specificity and also for the design of inhibitors. However, clear preferences were detected for substrates with S at P(1)', and V at P(2)', at P(3)' the amino acids D, S, L and A are almost equally frequent. In the non-prime subsites the best substrates presented S and H at P(6); basic amino acids at P(5); and no clear tendency at P(3). Interestingly, two amino acid substitutions on the prime side of the peptide derived from H5N1 influenza hemagglutinin furin processing site highly improved its hydrolysis. These modifications are possible by single point mutations, suggesting a potential yield of a more infectious virus. Twit Text FOAVip A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions ????Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=19477160 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19477160 #FOAvip English Wikipedia <ref>{{Cite pmid|19477160}}</ref> A study of human furin specificity using synthetic peptides derived from natural substrates, and effects of potassium ions #MMPMID19477160 Izidoro MA; Gouvea IE; Santos JA; Assis DM; Oliveira V; Judice WA; Juliano MA; Lindberg I; Juliano L Arch Biochem Biophys 2009[Jul]; 487 (2): 105-14 PMID19477160show ga We explored furin substrate requirements in addition to the motif R-X-K/R-R using synthetic fluorescent resonance energy transfer (FRET) decapeptides. These decapeptides were derived from furin cleavage sites in viral coat glycoproteins and human and bacterial protein precursors. The hydrolysis by furin of most substrate was activated by K(+) ion, whereas kosmotropic anions of the Hofmeister series were inhibitors. The analysis of furin hydrolytic activity showed that its efficiency is highly dependent on the particular combinations of amino acids at different substrate positions. There is a clear interdependence of furin subsites that must be taken in account in determining its specificity and also for the design of inhibitors. However, clear preferences were detected for substrates with S at P(1)', and V at P(2)', at P(3)' the amino acids D, S, L and A are almost equally frequent. In the non-prime subsites the best substrates presented S and H at P(6); basic amino acids at P(5); and no clear tendency at P(3). Interestingly, two amino acid substitutions on the prime side of the peptide derived from H5N1 influenza hemagglutinin furin processing site highly improved its hydrolysis. These modifications are possible by single point mutations, suggesting a potential yield of a more infectious virus. |Amino Acid Sequence[MESH] |Fluorescence Resonance Energy Transfer[MESH] |Furin/chemistry/*metabolism[MESH] |Humans[MESH] |Hydrogen-Ion Concentration[MESH] |Hydrolysis/drug effects[MESH] |Kinetics[MESH] |Molecular Sequence Data[MESH] |Oligopeptides/chemical synthesis/*chemistry/*metabolism[MESH] |Potassium Chloride/*pharmacology[MESH] |Sodium Chloride/pharmacology[MESH]A study of human furin specificity using synthetic peptides derived fr(epmc).pdf DeepDyve Pubget Overpricing