The motif V of plum pox potyvirus CI RNA helicase is involved in NTP hydrolysis and is essential for virus RNA replication
- 15 November 1997
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 25 (22) , 4474-4480
- https://doi.org/10.1093/nar/25.22.4474
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Crystal structure of a DExx box DNA helicaseNature, 1996
- The RNA helicase CI from plum pox potyvirus has two regions involved in binding to RNAFEBS Letters, 1996
- Replacement of Gly815 in Helicase Motif V Alters the Single-stranded DNA-dependent ATPase Activity of the Herpes Simplex Virus Type 1 Helicase-PrimasePublished by Elsevier ,1996
- Mutational Analysis of the Tobacco Vein Mottling Virus GenomeVirology, 1994
- Helicase Motifs V and VI of the Escherichia coli UvrB Protein of the UvrABC Endonuclease Are Essential for the Formation of the Preincision ComplexJournal of Molecular Biology, 1994
- Structural Proteins of Three Viruses in the Potyviridae Adhere Only to Their Homologous Cylindrical Inclusions in Mixed InfectionsJournal of Structural Biology, 1993
- D‐E‐A‐D protein family of putative RNA helicasesMolecular Microbiology, 1992
- Highlights and prospects of potyvirus molecular biologyJournal of General Virology, 1992
- Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase-like proteinsGene, 1989
- The complete nucleotide sequence of plum pox potyvirus RNAVirus Research, 1989