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10.1007/s13238-022-00905-7 http://scihub22266oqcxt.onion/10.1007/s13238-022-00905-7 35384603!8983322!35384603     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 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Cell 2022 ; 13 (8): 602-614 Nephropedia Template TP {{tp|p=35384603|t=2022. SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation |pdf=|usr=}}{{35384603}} gab.com Text SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation JO: Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=35384603 #FOAvip The nucleocapsid (N) protein of SARS-CoV-2 has been reported to have a high ability of liquid-liquid phase separation, which enables its incorporation into stress granules (SGs) of host cells. However, whether SG invasion by N protein occurs in the scenario of SARS-CoV-2 infection is unknow, neither do we know its consequence. Here, we used SARS-CoV-2 to infect mammalian cells and observed the incorporation of N protein into SGs, which resulted in markedly impaired self-disassembly but stimulated cell cellular clearance of SGs. NMR experiments further showed that N protein binds to the SG-related amyloid proteins via non-specific transient interactions, which not only expedites the phase transition of these proteins to aberrant amyloid aggregation in vitro, but also promotes the aggregation of FUS with ALS-associated P525L mutation in cells. In addition, we found that ACE2 is not necessary for the infection of SARS-CoV-2 to mammalian cells. Our work indicates that SARS-CoV-2 infection can impair the disassembly of host SGs and promote the aggregation of SG-related amyloid proteins, which may lead to an increased risk of neurodegeneration. Twit Text FOAVip SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation ????Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=35384603 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35384603 #FOAvip English Wikipedia <ref>{{Cite pmid|35384603}}</ref> SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation #MMPMID35384603 Li Y; Lu S; Gu J; Xia W; Zhang S; Zhang S; Wang Y; Zhang C; Sun Y; Lei J; Liu C; Su Z; Yang J; Peng X; Li D Protein Cell 2022[Aug]; 13 (8): 602-614 PMID35384603show ga The nucleocapsid (N) protein of SARS-CoV-2 has been reported to have a high ability of liquid-liquid phase separation, which enables its incorporation into stress granules (SGs) of host cells. However, whether SG invasion by N protein occurs in the scenario of SARS-CoV-2 infection is unknow, neither do we know its consequence. Here, we used SARS-CoV-2 to infect mammalian cells and observed the incorporation of N protein into SGs, which resulted in markedly impaired self-disassembly but stimulated cell cellular clearance of SGs. NMR experiments further showed that N protein binds to the SG-related amyloid proteins via non-specific transient interactions, which not only expedites the phase transition of these proteins to aberrant amyloid aggregation in vitro, but also promotes the aggregation of FUS with ALS-associated P525L mutation in cells. In addition, we found that ACE2 is not necessary for the infection of SARS-CoV-2 to mammalian cells. Our work indicates that SARS-CoV-2 infection can impair the disassembly of host SGs and promote the aggregation of SG-related amyloid proteins, which may lead to an increased risk of neurodegeneration. |*Amyotrophic Lateral Sclerosis/genetics[MESH] |*COVID-19[MESH] |Amyloidogenic Proteins/metabolism[MESH] |Animals[MESH] |Cytoplasmic Granules/metabolism[MESH] |Mammals[MESH] |SARS-CoV-2[MESH]SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS(epmc).pdf DeepDyve Pubget Overpricing