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

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

MeSH Review:

Cystoviridae

Yang, H. et al., Alimova, A. et al., Kainov, D.E. et al., Lísal, J. et al., Mancini, E.J. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Cystoviridae

P4 is a hexameric ATPase that serves as the RNA packaging motor in double-stranded RNA bacteriophages from the Cystoviridae family [1].
Native fluorescence spectroscopy (NFS), primarily from tryptophan (trp), was used for in situ investigation of the virus-receptor attachment process in phi6, a lipid-containing bacteriophage from the Cystoviridae family [2].

High impact information on Cystoviridae

Thus, P4 proteins of Cystoviridae exhibit extensive similarity to hexameric helicases and are simple models for studying viral packaging motor mechanisms [3].
Based on these and earlier observations, we propose a model of transcriptional polarity in Cystoviridae controlled on two independent levels: Pol affinity to plus-strand initiation sites and accessibility of these sites to the Pol in a single-stranded form [4].
The packaging of genomic RNA in members of the Cystoviridae is performed by P4, a hexameric protein with NTPase activity [5].

References

Cooperative mechanism of RNA packaging motor. Lísal, J., Tuma, R. J. Biol. Chem. (2005) [Pubmed]
Virus particles and receptor interaction monitored by fluorescence spectroscopy. Alimova, A., Katz, A., Podder, R., Minko, G., Wei, H., Berriman, J., Alfano, R.R., Gottlieb, P. Photochem. Photobiol. (2005) [Pubmed]
RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein. Kainov, D.E., Pirttimaa, M., Tuma, R., Butcher, S.J., Thomas, G.J., Bamford, D.H., Makeyev, E.V. J. Biol. Chem. (2003) [Pubmed]
Two distinct mechanisms ensure transcriptional polarity in double-stranded RNA bacteriophages. Yang, H., Makeyev, E.V., Butcher, S.J., Gaidelyte, A., Bamford, D.H. J. Virol. (2003) [Pubmed]
Order and disorder in crystals of hexameric NTPases from dsRNA bacteriophages. Mancini, E.J., Grimes, J.M., Malby, R., Sutton, G.C., Kainov, D.E., Juuti, J.T., Makeyev, E.V., Tuma, R., Bamford, D.H., Stuart, D.I. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

Editor

Share