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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Plum Pox Virus

 
 
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Disease relevance of Plum Pox Virus

  • As suggested from the high level of sequence similarity of these viral proteins with the recently described superfamilies of helicase-like proteins (3-5), the NTBM-containing cylindrical inclusion (CI) protein from plum pox virus (PPV), which belongs to the potyvirus group of positive strand RNA viruses, is shown to be able to unwind RNA duplexes [1].
 

High impact information on Plum Pox Virus

  • By using a yeast two-hybrid system, the CI protein from Plum pox virus (PPV) was found to interact with the photosystem I PSI-K protein, the product of the gene psaK, of Nicotiana benthamiana [2].
  • Processing of the plum pox virus polyprotein at the P3-6K1 junction is not required for virus viability [3].
  • Generation and characterisation of functional recombinant antibody fragments against RNA replicase NIb from plum pox virus [4].
  • The map is based on an F(2) population (76 individuals) derived from self-pollination of an F(1) individual ('Lito') originated from a cross between 'Stark Early Orange' and 'Tyrinthos'. This family, designated as 'Lito' x 'Lito', segregated for two important agronomical traits: plum pox virus resistance (PPV) and self-incompatibility [5].
  • Transgenic plums transformed with the plum pox virus coat protein (PPV CP) gene displayed a resistance to the sharka disease (Ravelonandro et al., 1997) [6].
 

Chemical compound and disease context of Plum Pox Virus

  • One of the probes was biotinylated capture RNA specific for plum pox virus (PPV) strain SK-68; the other RNA probe was synthesized from a plasmid bearing the adjacent sequence of this strain and was labelled with digoxigenin (DIG) [7].
 

Gene context of Plum Pox Virus

  • The NIa-like protein of plum pox virus is a protease with high sequence specificity that is autocatalytically released from the viral polyprotein [8].

References

  1. RNA helicase: a novel activity associated with a protein encoded by a positive strand RNA virus. Laín, S., Riechmann, J.L., García, J.A. Nucleic Acids Res. (1990) [Pubmed]
  2. Identification of a plum pox virus CI-interacting protein from chloroplast that has a negative effect in virus infection. Jiménez, I., López, L., Alamillo, J.M., Valli, A., García, J.A. Mol. Plant Microbe Interact. (2006) [Pubmed]
  3. Processing of the plum pox virus polyprotein at the P3-6K1 junction is not required for virus viability. Riechmann, J.L., Cervera, M.T., García, J.A. J. Gen. Virol. (1995) [Pubmed]
  4. Generation and characterisation of functional recombinant antibody fragments against RNA replicase NIb from plum pox virus. Esteban, O., García, J.A., Gorris, M.T., Domínguez, E., Cambra, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  5. An apricot (Prunus armeniaca L.) F2 progeny linkage map based on SSR and AFLP markers, mapping plum pox virus resistance and self-incompatibility traits. Vilanova, S., Romero, C., Abbott, A.G., Llácer, G., Badenes, M.L. Theor. Appl. Genet. (2003) [Pubmed]
  6. High resistance and control of biological risks in transgenic plants expressing modified plum pox virus coat protein. Jacquet, C., Ravelonandro, M., Dunez, J. Acta Virol. (1998) [Pubmed]
  7. Sensitive non-radioactive nucleic acid hybridization assay for plum pox virus detection. Palkovics, L., Burgyán, J., Balázs, E. Res. Virol. (1994) [Pubmed]
  8. Detection of the trans activity of the plum pox virus NIa-like protease in infected plants. Himmler, G., Frank, S., Steinkellner, H., Rüker, F., Mattanovich, D., Katinger, H.W. J. Gen. Virol. (1990) [Pubmed]
 
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