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10.1002/pmic.202000246 http://scihub22266oqcxt.onion/10.1002/pmic.202000246 33111431!7645863!33111431     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proteomics 2021 ; 21 (2): e2000246 Nephropedia Template TP {{tp|p=33111431|t=2021. N-Terminomics for the Identification of In Vitro Substrates and Cleavage Site Specificity of the SARS-CoV-2 Main Protease |pdf=|usr=}}{{33111431}} gab.com Text N-Terminomics for the Identification of In Vitro Substrates and Cleavage Site Specificity of the SARS-CoV-2 Main Protease JO: Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=33111431 #FOAvip The genome of coronaviruses, including SARS-CoV-2, encodes for two proteases, a papain like (PL(pro) ) protease and the so-called main protease (M(pro) ), a chymotrypsin-like cysteine protease, also named 3CL(pro) or non-structural protein 5 (nsp5). M(pro) is activated by autoproteolysis and is the main protease responsible for cutting the viral polyprotein into functional units. Aside from this, it is described that M(pro) proteases are also capable of processing host proteins, including those involved in the host innate immune response. To identify substrates of the three main proteases from SARS-CoV, SARS-CoV-2, and hCoV-NL63 coronviruses, an LC-MS based N-terminomics in vitro analysis is performed using recombinantly expressed proteases and lung epithelial and endothelial cell lysates as substrate pools. For SARS-CoV-2 M(pro) , 445 cleavage events from more than 300 proteins are identified, while 151 and 331 M(pro) derived cleavage events are identified for SARS-CoV and hCoV-NL63, respectively. These data enable to better understand the cleavage site specificity of the viral proteases and will help to identify novel substrates in vivo. All data are available via ProteomeXchange with identifier PXD021406. Twit Text FOAVip N-Terminomics for the Identification of In Vitro Substrates and Cleavage Site Specificity of the SARS-CoV-2 Main Protease ????Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=33111431 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33111431 #FOAvip English Wikipedia <ref>{{Cite pmid|33111431}}</ref> N-Terminomics for the Identification of In Vitro Substrates and Cleavage Site Specificity of the SARS-CoV-2 Main Protease #MMPMID33111431 Koudelka T; Boger J; Henkel A; Schonherr R; Krantz S; Fuchs S; Rodriguez E; Redecke L; Tholey A Proteomics 2021[Jan]; 21 (2): e2000246 PMID33111431show ga The genome of coronaviruses, including SARS-CoV-2, encodes for two proteases, a papain like (PL(pro) ) protease and the so-called main protease (M(pro) ), a chymotrypsin-like cysteine protease, also named 3CL(pro) or non-structural protein 5 (nsp5). M(pro) is activated by autoproteolysis and is the main protease responsible for cutting the viral polyprotein into functional units. Aside from this, it is described that M(pro) proteases are also capable of processing host proteins, including those involved in the host innate immune response. To identify substrates of the three main proteases from SARS-CoV, SARS-CoV-2, and hCoV-NL63 coronviruses, an LC-MS based N-terminomics in vitro analysis is performed using recombinantly expressed proteases and lung epithelial and endothelial cell lysates as substrate pools. For SARS-CoV-2 M(pro) , 445 cleavage events from more than 300 proteins are identified, while 151 and 331 M(pro) derived cleavage events are identified for SARS-CoV and hCoV-NL63, respectively. These data enable to better understand the cleavage site specificity of the viral proteases and will help to identify novel substrates in vivo. All data are available via ProteomeXchange with identifier PXD021406. |COVID-19/metabolism/*virology[MESH] |Cells, Cultured[MESH] |Coronavirus 3C Proteases/*metabolism[MESH] |Coronavirus NL63, Human/*enzymology[MESH] |Endothelial Cells/metabolism/virology[MESH] |Epithelial Cells/metabolism/virology[MESH] |Eukaryotic Initiation Factor-4G/metabolism[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Lung/metabolism/virology[MESH] |Peptide Fragments/*analysis[MESH] |SARS-CoV-2/*enzymology[MESH] |Severe acute respiratory syndrome-related coronavirus/*enzymology[MESH] |Substrate Specificity[MESH]N-Terminomics for the Identification of In Vitro Substrates and Cleava(epmc).pdf DeepDyve Pubget Overpricing