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10.1128/JVI.68.7.4690-4694.1994 http://scihub22266oqcxt.onion/10.1128/JVI.68.7.4690-4694.1994 8207846!236400!8207846     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Virol 1994 ; 68 (7): 4690-4 Nephropedia Template TP {{tp|p=8207846|t=1994. Formation of empty B19 parvovirus capsids by the truncated minor capsid protein |pdf=|usr=}}{{8207846}} gab.com Text Formation of empty B19 parvovirus capsids by the truncated minor capsid protein JO: J Virol http://www.kidney.de/pget.php?&tw=1&pmid=8207846 #FOAvip We previously reported that empty capsids of B19 parvovirus were formed by the major capsid protein (VP2) alone expressed in a baculovirus system, but the minor capsid protein (VP1), longer by 227 amino acids, alone did not form empty capsids. We report here further investigations of the constraints on capsid formation by truncated versions of VP1. Studies were performed with recombinant baculoviruses expressed in Sf9 cells. Severely shortened VP1, extended beyond the VP2 core sequence by about 70 amino acids of the unique region, formed capsids normal in appearance; longer versions of VP1 also formed capsids but did so progressively less efficiently and produced capsids of more markedly dysmorphic appearance as the VP1-unique region was lengthened. Twit Text FOAVip Formation of empty B19 parvovirus capsids by the truncated minor capsid protein ????J Virol http://www.kidney.de/pget.php?&tw=1&pmid=8207846 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=8207846 #FOAvip English Wikipedia <ref>{{Cite pmid|8207846}}</ref> Formation of empty B19 parvovirus capsids by the truncated minor capsid protein #MMPMID8207846 Wong S; Momoeda M; Field A; Kajigaya S; Young NS J Virol 1994[Jul]; 68 (7): 4690-4 PMID8207846show ga We previously reported that empty capsids of B19 parvovirus were formed by the major capsid protein (VP2) alone expressed in a baculovirus system, but the minor capsid protein (VP1), longer by 227 amino acids, alone did not form empty capsids. We report here further investigations of the constraints on capsid formation by truncated versions of VP1. Studies were performed with recombinant baculoviruses expressed in Sf9 cells. Severely shortened VP1, extended beyond the VP2 core sequence by about 70 amino acids of the unique region, formed capsids normal in appearance; longer versions of VP1 also formed capsids but did so progressively less efficiently and produced capsids of more markedly dysmorphic appearance as the VP1-unique region was lengthened. |Animals[MESH] |Baculoviridae/genetics[MESH] |Base Sequence[MESH] |Capsid/*biosynthesis/genetics[MESH] |Cells, Cultured[MESH] |Cloning, Molecular[MESH] |DNA Primers[MESH] |Molecular Sequence Data[MESH] |Moths[MESH] |Parvovirus B19, Human/*metabolism/ultrastructure[MESH] |Recombinant Proteins/genetics[MESH]Formation of empty B19 parvovirus capsids by the truncated minor capsi(epmc).pdf DeepDyve Pubget Overpricing