Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1096/fj.202002271 http://scihub22266oqcxt.onion/10.1096/fj.202002271 33368679!7883198!33368679     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33368679&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 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\33368679.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       FASEB+J 2021 ; 35 (1): e21197 Nephropedia Template TP {{tp|p=33368679|t=2021. Spatial and temporal roles of SARS-CoV PL(pro) -A snapshot |pdf=|usr=}}{{33368679}} gab.com Text Spatial and temporal roles of SARS-CoV PL(pro) -A snapshot JO: FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=33368679 #FOAvip SARS-CoV and SARS-CoV-2 encode four structural and accessory proteins (spike, envelope, membrane and nucleocapsid proteins) and two polyproteins (pp1a and pp1ab). The polyproteins are further cleaved by 3C-like cysteine protease (3CL(pro) ) and papain-like protease (PL(pro) ) into 16 nonstructural proteins (nsps). PL(pro) is released from nsp3 through autocleavage, and then it cleaves the sites between nsp1/2, between nsp2/3 and between nsp3/4 with recognition motif of LXGG, and the sites in the C-terminus of ubiquitin and of protein interferon-stimulated gene 15 (ISG15) with recognition motif of RLRGG. Alone or together with SARS unique domain (SUD), PL(pro) can stabilize an E3 ubiquitin ligase, the ring-finger, and CHY zinc-finger domain-containing 1 (RCHY1), through domain interaction, and thus, promote RCHY1 to ubiquitinate its target proteins including p53. However, a dilemma appears in terms of PL(pro) roles. On the one hand, the ubiquitination of p53 is good for SARS-CoV because the ubiquitinated p53 cannot inhibit SARS-CoV replication. On the other hand, the ubiquitination of NF-kappaB inhibitor (IkappaBalpha), TNF receptor-associated factors (TRAFs), and stimulator of interferon gene (STING), and the ISGylation of targeted proteins are bad for SARS-CoV because these ubiquitination and ISGylation initiate the innate immune response and antiviral state. This mini-review analyzes the dilemma and provides a snapshot on how the viral PL(pro) smartly manages its roles to avoid its simultaneously contradictory actions, which could shed lights on possible strategies to deal with SARS-CoV-2 infections. Twit Text FOAVip Spatial and temporal roles of SARS-CoV PL(pro) -A snapshot ????FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=33368679 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33368679 #FOAvip English Wikipedia <ref>{{Cite pmid|33368679}}</ref> Spatial and temporal roles of SARS-CoV PL(pro) -A snapshot #MMPMID33368679 Yan S; Wu G FASEB J 2021[Jan]; 35 (1): e21197 PMID33368679show ga SARS-CoV and SARS-CoV-2 encode four structural and accessory proteins (spike, envelope, membrane and nucleocapsid proteins) and two polyproteins (pp1a and pp1ab). The polyproteins are further cleaved by 3C-like cysteine protease (3CL(pro) ) and papain-like protease (PL(pro) ) into 16 nonstructural proteins (nsps). PL(pro) is released from nsp3 through autocleavage, and then it cleaves the sites between nsp1/2, between nsp2/3 and between nsp3/4 with recognition motif of LXGG, and the sites in the C-terminus of ubiquitin and of protein interferon-stimulated gene 15 (ISG15) with recognition motif of RLRGG. Alone or together with SARS unique domain (SUD), PL(pro) can stabilize an E3 ubiquitin ligase, the ring-finger, and CHY zinc-finger domain-containing 1 (RCHY1), through domain interaction, and thus, promote RCHY1 to ubiquitinate its target proteins including p53. However, a dilemma appears in terms of PL(pro) roles. On the one hand, the ubiquitination of p53 is good for SARS-CoV because the ubiquitinated p53 cannot inhibit SARS-CoV replication. On the other hand, the ubiquitination of NF-kappaB inhibitor (IkappaBalpha), TNF receptor-associated factors (TRAFs), and stimulator of interferon gene (STING), and the ISGylation of targeted proteins are bad for SARS-CoV because these ubiquitination and ISGylation initiate the innate immune response and antiviral state. This mini-review analyzes the dilemma and provides a snapshot on how the viral PL(pro) smartly manages its roles to avoid its simultaneously contradictory actions, which could shed lights on possible strategies to deal with SARS-CoV-2 infections. |COVID-19/immunology/therapy/*virology[MESH] |Coronavirus Papain-Like Proteases/genetics/*physiology[MESH] |Genes, Viral[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Molecular Targeted Therapy[MESH] |NF-kappa B/metabolism[MESH] |Protein Domains[MESH] |Protein Processing, Post-Translational[MESH] |SARS-CoV-2/genetics/*physiology[MESH] |Severe Acute Respiratory Syndrome/immunology/therapy/*virology[MESH] |Severe acute respiratory syndrome-related coronavirus/genetics/*physiology[MESH] |Substrate Specificity[MESH] |Ubiquitin-Activating Enzymes/metabolism[MESH] |Ubiquitin-Conjugating Enzymes/metabolism[MESH] |Ubiquitin-Protein Ligases/metabolism[MESH] |Ubiquitination[MESH] |Viral Proteins/metabolism[MESH]Spatial and temporal roles of SARS-CoV PL(pro) -A snapshot (epmc).pdf DeepDyve Pubget Overpricing