Active truncated form of the RNA polymerase of flavivirus

Details Active truncated form of the RNA polymerase of flavivirus Active truncated form of the RNA polymerase of flavivirus

2004-05-28

2008-12-02

Mosher, Mary E (Department: 1648)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Transferase other than ribonuclease

C435S005000

Reexamination Certificate

active

07459297

ABSTRACT:
The isolation and purification of two domains from a from a flavivirus is provided. Each domain can function independently. Moreover, one domain codes for a sequence that provide polymerase activity. A process for screening possible modulators of the polymerase activity of an isolated and purified polypeptide from flavivirus is also disclosed.

REFERENCES:
patent: 2654113 (1991-05-01), None
patent: WO01/60847 (2001-08-01), None
See Score sequence search result 14.rag (search done Jun. 1, 2006).
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Johansen et al (Journal of General Virology 82:735-745, 2001).
Vasudevan et al (II Farmaco 56:33-36, 2001).
Brooks et al., “The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals,” The journal of Biological Chemistry, vol. 277, No. 39 (2002), 36399-36407.
Johansson et al., “A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin- and the viral helicase, NS3,” Journal of General Virology, 82: 735-45 (2001).
Yaegashi et al., “Partial sequence analysis of cloned dengue virus type 2 genome,” Gene, 46: 257-267 (1986).
Result 8, .rpr, 2006.
Sequence search result 3 from .rag, 2006.
Sequence search results 1-5 from .rpr; search results 1-60 from.rup, 2006.

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