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.

10.1016/j.ijbiomac.2021.12.072 http://scihub22266oqcxt.onion/10.1016/j.ijbiomac.2021.12.072 34953805!8694786!34953805     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Biol+Macromol 2022 ; 197 (ä): 68-76 Nephropedia Template TP {{tp|p=34953805|t=2022. Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease?|pdf=|usr=}}{{34953805}} gab.com Text Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease JO: Int J Biol Macromol http://www.kidney.de/pget.php?&tw=1&pmid=34953805 #FOAvip The C-terminal domain of SARS-CoV main protease (M(pro)-C) can form 3D domain-swapped dimer by exchanging the alpha(1)-helices fully buried inside the protein hydrophobic core, under non-denaturing conditions. Here, we report that M(pro)-C can also form amyloid fibrils under the 3D domain-swappable conditions in vitro, and the fibrils are not formed through runaway/propagated domain swapping. It is found that there are positive correlations between the rates of domain swapping dimerization and amyloid fibrillation at different temperatures, and for different mutants. However, some M(pro)-C mutants incapable of 3D domain swapping can still form amyloid fibrils, indicating that 3D domain swapping is not essential for amyloid fibrillation. Furthermore, NMR H/D exchange data and molecular dynamics simulation results suggest that the protofibril core region tends to unpack at the early stage of 3D domain swapping, so that the amyloid fibrillation can proceed during the 3D domain swapping process. We propose that 3D domain swapping makes it possible for the unpacking of the amyloidogenic fragment of the protein and thus accelerates the amyloid fibrillation process kinetically, which explains the well-documented correlations between amyloid fibrillation and 3D domain swapping observed in many proteins. Twit Text FOAVip Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease ????Int J Biol Macromol http://www.kidney.de/pget.php?&tw=1&pmid=34953805 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34953805 #FOAvip English Wikipedia <ref>{{Cite pmid|34953805}}</ref> Is amyloid fibrillation related to 3D domain swapping for the C-terminal domain of SARS-CoV main protease? #MMPMID34953805 Yuan Z; Qu Z; Duan B; Wang T; Xu J; Xia B Int J Biol Macromol 2022[Feb]; 197 (ä): 68-76 PMID34953805show ga The C-terminal domain of SARS-CoV main protease (M(pro)-C) can form 3D domain-swapped dimer by exchanging the alpha(1)-helices fully buried inside the protein hydrophobic core, under non-denaturing conditions. Here, we report that M(pro)-C can also form amyloid fibrils under the 3D domain-swappable conditions in vitro, and the fibrils are not formed through runaway/propagated domain swapping. It is found that there are positive correlations between the rates of domain swapping dimerization and amyloid fibrillation at different temperatures, and for different mutants. However, some M(pro)-C mutants incapable of 3D domain swapping can still form amyloid fibrils, indicating that 3D domain swapping is not essential for amyloid fibrillation. Furthermore, NMR H/D exchange data and molecular dynamics simulation results suggest that the protofibril core region tends to unpack at the early stage of 3D domain swapping, so that the amyloid fibrillation can proceed during the 3D domain swapping process. We propose that 3D domain swapping makes it possible for the unpacking of the amyloidogenic fragment of the protein and thus accelerates the amyloid fibrillation process kinetically, which explains the well-documented correlations between amyloid fibrillation and 3D domain swapping observed in many proteins. |Amyloid/*chemistry/*metabolism[MESH] |Amyloidosis/genetics/*metabolism[MESH] |Coronavirus 3C Proteases/*chemistry/genetics/*metabolism[MESH] |Dimerization[MESH] |Disulfides/chemistry/metabolism[MESH] |Kinetics[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Mutation[MESH] |Polymerization[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Domains/genetics/*physiology[MESH] |Protein Folding[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH]Is amyloid fibrillation related to 3D domain swapping for the C-termin(epmc).pdf DeepDyve Pubget Overpricing