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10.1016/j.nbt.2021.01.010 http://scihub22266oqcxt.onion/10.1016/j.nbt.2021.01.010 33556628!7863792!33556628     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       N+Biotechnol 2021 ; 62 (ä): 79-85 Nephropedia Template TP {{tp|p=33556628|t=2021. FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein |pdf=|usr=}}{{33556628}} gab.com Text FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein JO: N Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=33556628 #FOAvip A phage library displaying 10(10) variants of the fibronectin type III (FN3) domain was affinity selected with the biotinylated form of the receptor binding domain (RBD, residues 319-541) of the SARS-CoV-2 virus spike protein. Nine binding FN3 variants (i.e. monobodies) were recovered, representing four different primary structures. Soluble forms of the monobodies bound to several different preparations of the RBD and the S1 spike subunit, with affinities ranging from 3 to 14?nM as measured by bio-layer interferometry. Three of the four monobodies bound selectively to the RBD of SARS-CoV-2, with the fourth monobody showing slight cross-reactivity to the RBD of SARS-CoV-1 virus. Examination of binding to the spike fragments and its trimeric form revealed that the monobodies recognise at least three overlapping epitopes on the RBD of SARS-CoV-2. While pairwise tests failed to identify a monobody pair that could bind simultaneously to the RBD, one monobody could simultaneously bind to the RBD with the ectodomain of the cellular receptor angiotensin converting enzyme 2 (ACE2). All four monobodies successfully bound the RBD after overexpression in Chinese hamster ovary (CHO) cells as fusions to the Fc domain of human IgG1. Twit Text FOAVip FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein ????N Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=33556628 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33556628 #FOAvip English Wikipedia <ref>{{Cite pmid|33556628}}</ref> FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein #MMPMID33556628 Miller CJ; McGinnis JE; Martinez MJ; Wang G; Zhou J; Simmons E; Amet T; Abdeen SJ; Van Huysse JW; Bowsher RR; Kay BK N Biotechnol 2021[May]; 62 (ä): 79-85 PMID33556628show ga A phage library displaying 10(10) variants of the fibronectin type III (FN3) domain was affinity selected with the biotinylated form of the receptor binding domain (RBD, residues 319-541) of the SARS-CoV-2 virus spike protein. Nine binding FN3 variants (i.e. monobodies) were recovered, representing four different primary structures. Soluble forms of the monobodies bound to several different preparations of the RBD and the S1 spike subunit, with affinities ranging from 3 to 14?nM as measured by bio-layer interferometry. Three of the four monobodies bound selectively to the RBD of SARS-CoV-2, with the fourth monobody showing slight cross-reactivity to the RBD of SARS-CoV-1 virus. Examination of binding to the spike fragments and its trimeric form revealed that the monobodies recognise at least three overlapping epitopes on the RBD of SARS-CoV-2. While pairwise tests failed to identify a monobody pair that could bind simultaneously to the RBD, one monobody could simultaneously bind to the RBD with the ectodomain of the cellular receptor angiotensin converting enzyme 2 (ACE2). All four monobodies successfully bound the RBD after overexpression in Chinese hamster ovary (CHO) cells as fusions to the Fc domain of human IgG1. |*Antibody Specificity[MESH] |Angiotensin-Converting Enzyme 2/*immunology[MESH] |Cell Line[MESH] |Cross Reactions[MESH] |Epitopes/*immunology[MESH] |Humans[MESH] |Protein Domains[MESH] |SARS-CoV-2/*immunology[MESH] |Single-Chain Antibodies/*immunology[MESH]FN3-based monobodies selective for the receptor binding domain of the (epmc).pdf DeepDyve Pubget Overpricing