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10.15252/embj.2019102277 http://scihub22266oqcxt.onion/10.15252/embj.2019102277 33876849!8167360!33876849     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 Deprecated: Implicit conversion from float 265.2 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 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2021 ; 40 (11): e102277 Nephropedia Template TP {{tp|p=33876849|t=2021. The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation |pdf=|usr=}}{{33876849}} gab.com Text The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=33876849 #FOAvip The ongoing outbreak of severe acute respiratory syndrome (SARS) coronavirus 2 (SARS-CoV-2) demonstrates the continuous threat of emerging coronaviruses (CoVs) to public health. SARS-CoV-2 and SARS-CoV share an otherwise non-conserved part of non-structural protein 3 (Nsp3), therefore named as "SARS-unique domain" (SUD). We previously found a yeast-2-hybrid screen interaction of the SARS-CoV SUD with human poly(A)-binding protein (PABP)-interacting protein 1 (Paip1), a stimulator of protein translation. Here, we validate SARS-CoV SUD:Paip1 interaction by size-exclusion chromatography, split-yellow fluorescent protein, and co-immunoprecipitation assays, and confirm such interaction also between the corresponding domain of SARS-CoV-2 and Paip1. The three-dimensional structure of the N-terminal domain of SARS-CoV SUD ("macrodomain II", Mac2) in complex with the middle domain of Paip1, determined by X-ray crystallography and small-angle X-ray scattering, provides insights into the structural determinants of the complex formation. In cellulo, SUD enhances synthesis of viral but not host proteins via binding to Paip1 in pBAC-SARS-CoV replicon-transfected cells. We propose a possible mechanism for stimulation of viral translation by the SUD of SARS-CoV and SARS-CoV-2. Twit Text FOAVip The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=33876849 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33876849 #FOAvip English Wikipedia <ref>{{Cite pmid|33876849}}</ref> The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation #MMPMID33876849 Lei J; Ma-Lauer Y; Han Y; Thoms M; Buschauer R; Jores J; Thiel V; Beckmann R; Deng W; Leonhardt H; Hilgenfeld R; von Brunn A EMBO J 2021[Jun]; 40 (11): e102277 PMID33876849show ga The ongoing outbreak of severe acute respiratory syndrome (SARS) coronavirus 2 (SARS-CoV-2) demonstrates the continuous threat of emerging coronaviruses (CoVs) to public health. SARS-CoV-2 and SARS-CoV share an otherwise non-conserved part of non-structural protein 3 (Nsp3), therefore named as "SARS-unique domain" (SUD). We previously found a yeast-2-hybrid screen interaction of the SARS-CoV SUD with human poly(A)-binding protein (PABP)-interacting protein 1 (Paip1), a stimulator of protein translation. Here, we validate SARS-CoV SUD:Paip1 interaction by size-exclusion chromatography, split-yellow fluorescent protein, and co-immunoprecipitation assays, and confirm such interaction also between the corresponding domain of SARS-CoV-2 and Paip1. The three-dimensional structure of the N-terminal domain of SARS-CoV SUD ("macrodomain II", Mac2) in complex with the middle domain of Paip1, determined by X-ray crystallography and small-angle X-ray scattering, provides insights into the structural determinants of the complex formation. In cellulo, SUD enhances synthesis of viral but not host proteins via binding to Paip1 in pBAC-SARS-CoV replicon-transfected cells. We propose a possible mechanism for stimulation of viral translation by the SUD of SARS-CoV and SARS-CoV-2. |*Gene Expression Regulation, Viral[MESH] |Amino Acid Sequence[MESH] |Bacterial Proteins[MESH] |Chromatography, Gel[MESH] |Coronavirus Papain-Like Proteases/chemistry/*metabolism[MESH] |Crystallography, X-Ray[MESH] |Genes, Reporter[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Immunoprecipitation[MESH] |Luminescent Proteins[MESH] |Models, Molecular[MESH] |Peptide Initiation Factors/chemistry/*metabolism[MESH] |Protein Binding[MESH] |Protein Biosynthesis[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Interaction Mapping[MESH] |RNA, Viral/genetics[MESH] |RNA-Binding Proteins/chemistry/*metabolism[MESH] |RNA-Dependent RNA Polymerase/chemistry/*metabolism[MESH] |Recombinant Fusion Proteins/chemistry/metabolism[MESH] |Ribosome Subunits/metabolism[MESH] |SARS-CoV-2/genetics/*physiology[MESH] |Scattering, Small Angle[MESH] |Sequence Alignment[MESH] |Sequence Homology, Amino Acid[MESH] |Severe acute respiratory syndrome-related coronavirus/genetics/*physiology[MESH] |Viral Nonstructural Proteins/chemistry/*metabolism[MESH]The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with(epmc).pdf DeepDyve Pubget Overpricing