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10.1016/j.bbrc.2021.08.040 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2021.08.040 34416436!8364680!34416436     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34416436.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochem+Biophys+Res+Commun 2021 ; 573 (ä): 158-163 Nephropedia Template TP {{tp|p=34416436|t=2021. A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17 |pdf=|usr=}}{{34416436}} gab.com Text A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17 JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=34416436 #FOAvip The angiotensin Converting Enzyme 2 (ACE2) receptor is a key component of the renin-angiotensin-aldesterone system (RAAS) that mediates numerous effects in the cardiovascular system. It is also the cellular point of contact for the coronavirus spike protein. Cleavage of the receptor is both important to its physiological function as well as being necessary for cell entry by the virus. Shedding of ACE2 by the metalloprotease ADAM17 releases a catalytically active soluble form of ACE2, but cleavage by the serine protease TMPRSS2 is necessary for virion internalization. Complicating the issue is the observation that circulating ACE2 can also bind to the virus effectively blocking attachment to the membrane-bound receptor. This work investigates the possibility that the inflammatory response to coronavirus infection can abrogate shedding by ADAM17, thereby favoring cleavage by TMPRSS2 and thus cell entry by the virion. Twit Text FOAVip A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17 ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=34416436 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34416436 #FOAvip English Wikipedia <ref>{{Cite pmid|34416436}}</ref> A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17 #MMPMID34416436 Healy EF; Lilic M Biochem Biophys Res Commun 2021[Oct]; 573 (ä): 158-163 PMID34416436show ga The angiotensin Converting Enzyme 2 (ACE2) receptor is a key component of the renin-angiotensin-aldesterone system (RAAS) that mediates numerous effects in the cardiovascular system. It is also the cellular point of contact for the coronavirus spike protein. Cleavage of the receptor is both important to its physiological function as well as being necessary for cell entry by the virus. Shedding of ACE2 by the metalloprotease ADAM17 releases a catalytically active soluble form of ACE2, but cleavage by the serine protease TMPRSS2 is necessary for virion internalization. Complicating the issue is the observation that circulating ACE2 can also bind to the virus effectively blocking attachment to the membrane-bound receptor. This work investigates the possibility that the inflammatory response to coronavirus infection can abrogate shedding by ADAM17, thereby favoring cleavage by TMPRSS2 and thus cell entry by the virion. |ADAM17 Protein/*chemistry/*metabolism[MESH] |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH] |Binding Sites[MESH] |HSP20 Heat-Shock Proteins/chemistry/*metabolism[MESH] |Heat-Shock Response/physiology[MESH] |Host-Pathogen Interactions/*physiology[MESH] |Humans[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs[MESH] |SARS-CoV-2/*pathogenicity[MESH] |Serine Endopeptidases/metabolism[MESH]A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17 (epmc).pdf DeepDyve Pubget Overpricing