Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.93.15.7502 http://scihub22266oqcxt.onion/10.1073/pnas.93.15.7502 8755503!38774!8755503     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 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 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 1996 ; 93 (15): 7502-6 Nephropedia Template TP {{tp|p=8755503|t=1996. Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor |pdf=|usr=}}{{8755503}} gab.com Text Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=8755503 #FOAvip The three-dimensional structures of human parvovirus B19 VP2 capsids, alone and complexed with its cellular receptor, globoside, have been determined to 26 resolution. The B19 capsid structure, reconstructed from cryo-electron micrographs of vitrified specimens, has depressions on the icosahedral 2-fold and 3-fold axes, as well as a canyon-like region around the 5-fold axes. Similar results had previously been found in an 8 angstrom resolution map derived from x-ray diffraction data. Other parvoviral structures have a cylindrical channel along the 5-fold icosahedral axes, whereas density covers the 5-fold axes in B19. The glycolipid receptor molecules bind into the depressions on the 3-fold axes of the B19:globoside complex. A model of the tetrasaccharide component of globoside, organized as a trimeric fiber, fits well into the difference density representing the globoside receptor. Escape mutations to neutralizing antibodies map onto th capsid surface at regions immediately surrounding the globoside attachment sites. The proximity of the antigenic epitopes to the receptor site suggests that neutralization of virus infectivity is caused by preventing attachment of viruses to cells. Twit Text FOAVip Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=8755503 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=8755503 #FOAvip English Wikipedia <ref>{{Cite pmid|8755503}}</ref> Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor #MMPMID8755503 Chipman PR; Agbandje-McKenna M; Kajigaya S; Brown KE; Young NS; Baker TS; Rossmann MG Proc Natl Acad Sci U S A 1996[Jul]; 93 (15): 7502-6 PMID8755503show ga The three-dimensional structures of human parvovirus B19 VP2 capsids, alone and complexed with its cellular receptor, globoside, have been determined to 26 resolution. The B19 capsid structure, reconstructed from cryo-electron micrographs of vitrified specimens, has depressions on the icosahedral 2-fold and 3-fold axes, as well as a canyon-like region around the 5-fold axes. Similar results had previously been found in an 8 angstrom resolution map derived from x-ray diffraction data. Other parvoviral structures have a cylindrical channel along the 5-fold icosahedral axes, whereas density covers the 5-fold axes in B19. The glycolipid receptor molecules bind into the depressions on the 3-fold axes of the B19:globoside complex. A model of the tetrasaccharide component of globoside, organized as a trimeric fiber, fits well into the difference density representing the globoside receptor. Escape mutations to neutralizing antibodies map onto th capsid surface at regions immediately surrounding the globoside attachment sites. The proximity of the antigenic epitopes to the receptor site suggests that neutralization of virus infectivity is caused by preventing attachment of viruses to cells. |Capsid/*ultrastructure[MESH] |Carbohydrate Conformation[MESH] |Carbohydrate Sequence[MESH] |Crystallography, X-Ray[MESH] |Freezing[MESH] |Globosides/chemistry/physiology[MESH] |Humans[MESH] |Microscopy, Electron/methods[MESH] |Models, Structural[MESH] |Molecular Sequence Data[MESH] |Oligosaccharides/chemistry/metabolism[MESH] |Parvovirus B19, Human/physiology/*ultrastructure[MESH]Cryo-electron microscopy studies of empty capsids of human parvovirus (epmc).pdf DeepDyve Pubget Overpricing