Fluorescence polarization method for determining viral...

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S018000, C435S069200

Reexamination Certificate

active

07132231

ABSTRACT:
Methods for determining inhibitors of protein interactions are provided. The method involves evaluation of potential inhibitors that can inhibit or prevent protein interactions. The method provides for high-throughput identification of novel therapeutics that can treat a disease or disorder by inhibiting protein interactions.

REFERENCES:
patent: 5223391 (1993-06-01), Coen et al.
patent: 6162931 (2000-12-01), Gee et al.
patent: 6207397 (2001-03-01), Lynch et al.
patent: WO 00/68185 (2000-11-01), None
Keating S, Marsters J, Beresini M, Ladner C, Zioncheck K, Clark K, Arellano F, Bodary S (Jun. 2000) Proceedings of SPIE 3913, 128-137 and title page.
Bridges et al., “Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase,”J. Biol. Chem., 275(1):472-478 (2000).
Bridges et al., “Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches,”J. Virol., 75(11):4990-4998 (2001).
Chow and Coen, “Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42,”J. Virol., 69(11):6965-6971 (1995).
Coen et al., “Sensitivity of arabinosyladenine-resistant mutants of herpes simplex virus to other antiviral drugs and mapping of drug hypersensitivity mutations to the DNA polymerase locus,”J. Virol., 53(2):477-488 (1985).
Degterev et al., “Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL,”Natl. Cell Biol., 3(2):173-182 (2001).
Digard and Coen “A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein,”J. Biol. Chem., 265(29):17393-17396 (1990).
Digard et al., “Functional analysis of herpes simplex virus UL42 protein,”J. Virol., 67:1159-1168 (1993).
Digard et al., “The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication,”J. Virol., 67(1):398-406 (1993).
Digard et al., “Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface,”Proc. National. Acad. Sci. U SA., 92:1456-1460 (1995).
Digard et al., “Mutational analysis of DNA polymerase substrate recognition and subunit interactions using herpes simplex virus as prototype,”Methods Enzymol., 262:303-322 (1995).
Gottlieb et al., “The Herpes Simplex Virus Type 1 UL42 Gene Product; a Subunit of DNA Polymerase that Functions to Increase Processivity,”J. Virol., 64(12):5976-5987 (1990).
Gottlieb and Challberg, “Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template,”J. Virol., 68(8):4937-4945 (1994).
Hamatake et al., “The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domain,”J. Gen, Virol., 74 ( Pt 10):2181-2189 (1993).
Loregian et al., “Intranuclear delivery of an antiviral peptide mediated by the B subunit ofEscherichia coliheat-labile enterotoxin,”Proc. Natl. Acad. Sci. USA., 96:5221-5226 (1999).
Marsden et al., “Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42,”J. Gen. Virol., 75:3127-3135 (1994).
Pritchard and Stefano, “Amplified detection of viral nucleic acid at subattomole levels using Q beta replicase,”Ann. Biol. Clin., (Paris) 48(7):492-497 (1990).
Stow et al., “Inhibition of herpes simplex virus type 1 DNA replication by mutant forms of the origin-binding protein,”Virology, 196:413-418 (1993).
Tenney et al., “Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain,”J. Virol., 67(4):1959-1966 (1993).
Tenney et al., “Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect bonding and stimulation by its accessory protein UL42 without affecting basal polymerase activity,”J. Virol., 67(1):543-547 (1993).
Weisshart et al., “Structural and functional organization of herpes simplex virus DNA polymerase investigated by limited proteolysis,”J. Biol. Chem., 269(36):22788-22796 (1994).
Weisshart et al., “Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.”J. Virol., 73(1):55-66 (1999).
Zuccola et al., “The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase,”Mol. Cell., 5:267-278 (2000).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Fluorescence polarization method for determining viral... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Fluorescence polarization method for determining viral..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Fluorescence polarization method for determining viral... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3621926

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.