Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2006-06-16
2010-02-02
Aeder, Sean E (Department: 1642)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C530S402000, C424S185100
Reexamination Certificate
active
07655757
ABSTRACT:
This invention relates to cytotoxic variants of human ribonuclease 1 (RNase 1) identified through analysis of the interaction between RNase 1 and the human ribonuclease inhibitor (hRI) as defined by the three dimensional (3-D) atomic structure of the RNase 1 hRI complex. Also disclosed is the 3-D structure of the hRI.RNase 1 complex and methods for designing the RNase 1 variants.
REFERENCES:
patent: 5840296 (1998-11-01), Raines et al.
patent: 6280991 (2001-08-01), Raines
patent: 2005/0261232 (2005-11-01), Strong et al.
patent: WO0031242 (2000-03-01), None
patent: WO 00/40608 (2000-07-01), None
two sequence comparisons.
Gura (Science, 1997, 278:1041-1042.).
Pous et al (2000, J. Mol. Biol., 303:49-60).
Kobe and Delsenhofer (Mar. 9, 1995, Nature, 374(9):183-186).
Murthy and Sideshmukh (Biochem. J., 1992, 281: 343-348).
Burgess et al. (J. Cell. Biol. 111:2129-2138, 1990).
Lazar et al. (Mol. Cell Biol. 8:1247-1252, 1998).
Ontjes et al (PNAS, Oct. 1969, 64(2): 428-35).
Boix, E., et al., “Role of the N Terminus in RNase A Homologues: Differences in Catalytic Activity, Ribonuclease Inhibitor Interaction and Cytotoxicity,” J. Mol. Biol. 257:992-1007 (1996).
Bosch, M., et al., “A Nuclear Localization Sequence Endows Human Pancreatic Ribonuclease With Cytotoxic Activity,” Biochemistry 43:2167-2177 (2004).
Gaur, D., et al., “Interaction of Human Pancreatic Ribonuclease with Human Ribonuclease Inhibitor,” The Journal of Biological Chemistry 276:24978-24984 (2001).
Kobe, B., et al., “A structural basis of the interactions between leucine-rich repeats and protein ligands,” Nature 374:183-186 (1995).
Kobe, G., et al., “Mechanism of Ribonuclease Inhibition by Ribonuclease Inhibitor Protein Based on the crystal Structure of its Complex with Ribonuclease A,” J. Mol. Biol. 264:1028-1043(1996).
Kumar, K., et al., “Selective abolition of pancreatic RNase binding to its inhibitor protein,” PNAS 101:53-58 (2004).
Lee, J.E., et al., “Cytotoxicity of Bovine Seminal Ribonuclease: Monomer versus Dimer,” Biochemistry 44:15760-15767 (2005).
Leland, P.A., et al., “Ribonuclease A variants with potent cytotoxic activity,” Proc. Natl. Acad. Sci. USA 95:10407-10412 (1998).
Leland, P.A., et al., “Endowing Human Pancreatic Ribonuclease with Toxicity for Cancer Cells,” The Journal of Biological Chemistry 276:43095-43102 (2001).
Mitchell, J.C., et al., “Rapid atomic density methods for molecular shape characterization,” Journal of Molecular Graphics and Modelling 19:325-330 (2001).
Pous, J., et al., “Three-dimensional Structure of a Human Pancreatic Ribonuclease Variant, a Step Forward in the Design of Cytotoxic Ribonucleases,” J. Mol. Biol. 303:49-59 (2000).
Pous, J., et al., “Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution,” Acta Cryst. D57:498-505 (2001).
Rajamani, D., et al., “Archor residues in protein-protein interactions,” PNAS 101:11287-11292 (2004).
Rutkoski, T.J., et al., “Disruption of Shape-Complementarity Markers to Create Cytotoxic Variants of Ribonuclease A,” J. Mol. Biol. 354:41-54 (2005).
Shaul, Y., et al., “Exploring the Charge Space of Protein-Protein Association: A Proteomic Study,” Proteins: Structure, Function, and Bioinformatics 60:331-352 (2005).
Murphy, B.S., et al., “Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor,” Biochem. J. 281:343-348 (1992).
Quintessence/Biosciences webpage on Evade TM Ribonucleases.
Johnson R. Jeremy
McCoy Jason G.
Phillips, Jr. George N.
Raines Ronald T.
Aeder Sean E
Quarles & Brady LLP
Wisconsin Alumni Research Foundation
LandOfFree
Cytotoxic ribonuclease variants does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Cytotoxic ribonuclease variants, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Cytotoxic ribonuclease variants will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4190086