|1.||Almendral, J M: 2 articles (12/2000 - 02/2000)|
|2.||Maroto, B: 1 article (12/2000)|
|3.||Ramírez, J C: 1 article (12/2000)|
|4.||Foces-Foces, C: 1 article (02/2000)|
|5.||McKenna, R: 1 article (02/2000)|
|6.||Hernando, E: 1 article (02/2000)|
|7.||Portman, I: 1 article (02/2000)|
|8.||Agbandje-McKenna, M: 1 article (02/2000)|
|9.||Llamas-Saiz, A L: 1 article (02/2000)|
02/15/2000 - "Immunogold electron microscopy of infected Sf9 cells showed VP-2 localized in the nucleus and cytoplasm as is observed in mammalian cells during natural infections. "
02/01/1992 - "The proteins produced were the same size as the authentic CPV VP-2 protein, and were produced late after infection; the quantity of proteins recovered from the insect cell cultures was similar to those produced in CPV infections. "
12/01/2000 - "Chromatographic analysis of purified wild-type (wt) and mutant peptide B digested with a panel of specific proteases allowed us to identify the VP-2 residues Ser-2, Ser-6, and Ser-10 as the main phosphate acceptors for MVMp capsid during the natural viral infection. "
12/01/2000 - "The core of the VP-1 and VP-2 proteins forming the T=1 icosahedral capsid of the prototype strain of the parvovirus minute virus of mice (MVMp) share amino acids sequence and a common three-dimensional structure; however, the roles of these polypeptides in the virus infection cycle differ. "
|1.||Proteins (Proteins, Gene)
|3.||Peptide Hydrolases (Proteases)
|4.||DNA (Deoxyribonucleic Acid)