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.

10.1038/s41598-021-88630-9 http://scihub22266oqcxt.onion/10.1038/s41598-021-88630-9 33927258!8085067!33927258     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2021 ; 11 (1): 9283 Nephropedia Template TP {{tp|p=33927258|t=2021. The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors |pdf=|usr=}}{{33927258}} gab.com Text The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33927258 #FOAvip The maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease M(pro) to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the M(pro) monomer-dimer equilibrium dissociation constant. Since the functional unit of M(pro) is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (SAXS) to investigate the structural features of SARS-CoV-2 M(pro) in solution as a function of protein concentration and temperature. A detailed thermodynamic picture of the monomer-dimer equilibrium is derived, together with the temperature-dependent value of the dissociation constant. SAXS is also used to study how the M(pro) dissociation process is affected by small inhibitors selected by virtual screening. We find that these inhibitors affect dimerization and enzymatic activity to a different extent and sometimes in an opposite way, likely due to the different molecular mechanisms underlying the two processes. The M(pro) residues that emerge as key to optimize both dissociation and enzymatic activity inhibition are discussed. Twit Text FOAVip The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33927258 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33927258 #FOAvip English Wikipedia <ref>{{Cite pmid|33927258}}</ref> The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors #MMPMID33927258 Silvestrini L; Belhaj N; Comez L; Gerelli Y; Lauria A; Libera V; Mariani P; Marzullo P; Ortore MG; Palumbo Piccionello A; Petrillo C; Savini L; Paciaroni A; Spinozzi F Sci Rep 2021[Apr]; 11 (1): 9283 PMID33927258show ga The maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease M(pro) to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the M(pro) monomer-dimer equilibrium dissociation constant. Since the functional unit of M(pro) is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (SAXS) to investigate the structural features of SARS-CoV-2 M(pro) in solution as a function of protein concentration and temperature. A detailed thermodynamic picture of the monomer-dimer equilibrium is derived, together with the temperature-dependent value of the dissociation constant. SAXS is also used to study how the M(pro) dissociation process is affected by small inhibitors selected by virtual screening. We find that these inhibitors affect dimerization and enzymatic activity to a different extent and sometimes in an opposite way, likely due to the different molecular mechanisms underlying the two processes. The M(pro) residues that emerge as key to optimize both dissociation and enzymatic activity inhibition are discussed. |Antiviral Agents/*chemistry/pharmacology[MESH] |COVID-19/*metabolism/therapy[MESH] |Computational Biology[MESH] |Coronavirus 3C Proteases/*chemistry/genetics/metabolism[MESH] |Dimerization[MESH] |Drug Discovery[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Protease Inhibitors/*chemistry/pharmacology[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |SARS-CoV-2/*physiology[MESH] |Thermodynamics[MESH]The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected (epmc).pdf DeepDyve Pubget Overpricing