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10.1128/JVI.73.8.6882-6891.1999 http://scihub22266oqcxt.onion/10.1128/JVI.73.8.6882-6891.1999 10400786!112773!10400786     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Virol 1999 ; 73 (8): 6882-91 Nephropedia Template TP {{tp|p=10400786|t=1999. Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity |pdf=|usr=}}{{10400786}} gab.com Text Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity JO: J Virol http://www.kidney.de/pget.php?&tw=1&pmid=10400786 #FOAvip The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A resolution by cryo-electron microscopy and image reconstruction techniques. A structure-based sequence alignment of the VP2 capsid protein of canine parvovirus (CPV) provided a means to construct an atomic model of the ADVG-VP2 capsid. The ADVG-VP2 reconstruction reveals a capsid structure with a mean external radius of 128 A and several surface features similar to those found in human parvovirus B19 (B19), CPV, feline panleukopenia virus (FPV), and minute virus of mice (MVM). Dimple-like depressions occur at the icosahedral twofold axes, canyon-like regions encircle the fivefold axes, and spike-like protrusions decorate the threefold axes. These spikes are not present in B19, and they are more prominent in ADV compared to the other parvoviruses owing to the presence of loop insertions which create mounds near the threefold axes. Cylindrical channels along the fivefold axes of CPV, FPV, and MVM, which are surrounded by five symmetry-related beta-ribbons, are closed in ADVG-VP2 and B19. Immunoreactive peptides made from segments of the ADVG-VP2 capsid protein map to residues in the mound structures. In vitro tissue tropism and in vivo pathogenic properties of ADV map to residues at the threefold axes and to the wall of the dimples. Twit Text FOAVip Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity ????J Virol http://www.kidney.de/pget.php?&tw=1&pmid=10400786 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=10400786 #FOAvip English Wikipedia <ref>{{Cite pmid|10400786}}</ref> Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity #MMPMID10400786 McKenna R; Olson NH; Chipman PR; Baker TS; Booth TF; Christensen J; Aasted B; Fox JM; Bloom ME; Wolfinbarger JB; Agbandje-McKenna M J Virol 1999[Aug]; 73 (8): 6882-91 PMID10400786show ga The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A resolution by cryo-electron microscopy and image reconstruction techniques. A structure-based sequence alignment of the VP2 capsid protein of canine parvovirus (CPV) provided a means to construct an atomic model of the ADVG-VP2 capsid. The ADVG-VP2 reconstruction reveals a capsid structure with a mean external radius of 128 A and several surface features similar to those found in human parvovirus B19 (B19), CPV, feline panleukopenia virus (FPV), and minute virus of mice (MVM). Dimple-like depressions occur at the icosahedral twofold axes, canyon-like regions encircle the fivefold axes, and spike-like protrusions decorate the threefold axes. These spikes are not present in B19, and they are more prominent in ADV compared to the other parvoviruses owing to the presence of loop insertions which create mounds near the threefold axes. Cylindrical channels along the fivefold axes of CPV, FPV, and MVM, which are surrounded by five symmetry-related beta-ribbons, are closed in ADVG-VP2 and B19. Immunoreactive peptides made from segments of the ADVG-VP2 capsid protein map to residues in the mound structures. In vitro tissue tropism and in vivo pathogenic properties of ADV map to residues at the threefold axes and to the wall of the dimples. |*Protein Structure, Secondary[MESH] |Aleutian Mink Disease Virus/*chemistry/pathogenicity/ultrastructure[MESH] |Aleutian Mink Disease/pathology/*virology[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |Capsid Proteins[MESH] |Capsid/*chemistry/ultrastructure[MESH] |Cats[MESH] |Cell Line[MESH] |Cryoelectron Microscopy[MESH] |Dogs[MESH] |Humans[MESH] |Mice[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Recombinant Fusion Proteins/chemistry/ultrastructure[MESH] |Sequence Homology, Amino Acid[MESH]Three-dimensional structure of Aleutian mink disease parvovirus: impli(epmc).pdf DeepDyve Pubget Overpricing