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10.1073/pnas.2112457118 http://scihub22266oqcxt.onion/10.1073/pnas.2112457118 34772761!8670474!34772761     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (49): ä Nephropedia Template TP {{tp|p=34772761|t=2021. A widespread viral entry mechanism: The C-end Rule motif-neuropilin receptor interaction |pdf=|usr=}}{{34772761}} gab.com Text A widespread viral entry mechanism: The C-end Rule motif-neuropilin receptor interaction JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=34772761 #FOAvip Many phylogenetically distant animal viruses, including the new coronavirus severe acute respiratory syndrome coronavirus 2, have surface proteins with polybasic sites that are cleaved by host furin and furin-like proteases. Other than priming certain viral surface proteins for fusion, cleavage generates a carboxy-terminal RXXR sequence. This C-end Rule (CendR) motif is known to bind to neuropilin (NRP) receptors on the cell surface. NRPs are ubiquitously expressed, pleiotropic cell surface receptors with important roles in growth factor signaling, vascular biology, and neurobiology, as well as immune homeostasis and activation. The CendR-NRP receptor interaction promotes endocytic internalization and tissue spreading of different cargo, including viral particles. We propose that the interaction between viral surface proteins and NRPs plays an underappreciated and prevalent role in the transmission and pathogenesis of diverse viruses and represents a promising broad-spectrum antiviral target. Twit Text FOAVip A widespread viral entry mechanism: The C-end Rule motif-neuropilin receptor interaction ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=34772761 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34772761 #FOAvip English Wikipedia <ref>{{Cite pmid|34772761}}</ref> A widespread viral entry mechanism: The C-end Rule motif-neuropilin receptor interaction #MMPMID34772761 Balistreri G; Yamauchi Y; Teesalu T Proc Natl Acad Sci U S A 2021[Nov]; 118 (49): ä PMID34772761show ga Many phylogenetically distant animal viruses, including the new coronavirus severe acute respiratory syndrome coronavirus 2, have surface proteins with polybasic sites that are cleaved by host furin and furin-like proteases. Other than priming certain viral surface proteins for fusion, cleavage generates a carboxy-terminal RXXR sequence. This C-end Rule (CendR) motif is known to bind to neuropilin (NRP) receptors on the cell surface. NRPs are ubiquitously expressed, pleiotropic cell surface receptors with important roles in growth factor signaling, vascular biology, and neurobiology, as well as immune homeostasis and activation. The CendR-NRP receptor interaction promotes endocytic internalization and tissue spreading of different cargo, including viral particles. We propose that the interaction between viral surface proteins and NRPs plays an underappreciated and prevalent role in the transmission and pathogenesis of diverse viruses and represents a promising broad-spectrum antiviral target. |*Virus Internalization[MESH] |COVID-19/metabolism/*virology[MESH] |Humans[MESH] |Neuropilins/chemistry/*metabolism[MESH] |SARS-CoV-2/metabolism/pathogenicity/physiology[MESH]A widespread viral entry mechanism: The C-end Rule motif-neuropilin re(epmc).pdf DeepDyve Pubget Overpricing