Single-crystal – oriented-crystal – and epitaxy growth processes; – Processes of growth from liquid or supercritical state
Reexamination Certificate
2011-08-23
2011-08-23
Steadman, David J (Department: 1656)
Single-crystal, oriented-crystal, and epitaxy growth processes;
Processes of growth from liquid or supercritical state
C117S068000, C435S194000
Reexamination Certificate
active
08002891
ABSTRACT:
The present invention relates to molecules and molecular complexes which comprise the active site binding pockets of JNK3 or close structural homologues of the active site binding pockets.
REFERENCES:
patent: 4833233 (1989-05-01), Carter
patent: 5353236 (1994-10-01), Subbiah
patent: 5557535 (1996-09-01), Srinivasan et al.
patent: 6162613 (2000-12-01), Su et al.
patent: 6849716 (2005-02-01), Su et al.
patent: 6943000 (2005-09-01), Davis et al.
patent: 7383135 (2008-06-01), Xie et al.
patent: 2008/0201123 (2008-08-01), Cosgrove
patent: WO 92/14211 (1992-08-01), None
patent: WO 93/02209 (1993-02-01), None
patent: WO 94/25860 (1994-11-01), None
patent: WO 97/06246 (1997-02-01), None
patent: WO 97/15588 (1997-05-01), None
patent: WO 98/35048 (1998-08-01), None
patent: WO 99/57253 (1999-11-01), None
Balbes et al., “A Perspective of Modern Methods in Computer-Aided Drug Design,” inReviews in Computational Chemistry, K.B. Lipkowitz and D.B. Boyd, Eds., VCH Publishers, New York, 5:337-379 (1994).
Bartlett et al., “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules,” inMolecular Recognition in Chemical and Biological Problems, S.M. Roberts, Ed., Royal Society of Chemistry, Special Publication No. 78:182-196 (1989).
Böhm, “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”,Journal of Computer-Aided Molecular Design, 6:61-78 (1992).
Bossemeyer et al., “Phosphotransferase and Substrate Binding Mechanishm of the cAMP-Dependent Protein Kinase Catalytic Subunit from Porcine Heart as Deduced from the 2.0Å Structure of the Complex with Mn2+Adenylyl Imidodiphosphate and Inhibitor Peptide PKI(5-24),”The EMBO Journal, 12:849-859 (1993).
Boulton et al., “ERKs: A Family of Protein-Serine/Threonine Kinases that are Activated and Tyrosine Phosphorylated in Response to Insulin and NGF,”Cell, 65:663-675 (1991).
Brown et al., “Crystallography in the Study of Protein-DNA Interactions,”Methods in Molecular Biology, 56:293-318 (1996).
Bryan, “Protein Engineering,”Biotech Adv., 5:221-234 (1987).
Campbell et al., “Diffraction, in Biological Spectroscopy,”The Benjamin/Cummings Publishing Company, Inc., Menlo Park, CA, 299-326 (1984).
Canagarajah et al., “Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation,”Cell, 90:859-869 (1997).
Cohen et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”,Journal of Medicinal Chemistry, 33(3):883-894 (1990).
Drenth, “Principles of Protein X-Ray Crystallography,”Springer-Verlag, 16-17 (1995).
Eisen et al., “HOOK: A Program for Finding Novel Molecular Architectures that Satisfy the Chemical and Steric Requirements of a Macromolecule Binding Site,”Proteins Struct. Funct. Genet., 19:199-221 (1994).
Gillet et al., “SPROUT: A Program for Structure Generation,”J. Comp. Aid. Molec. Design, 7:127-153 (1993).
Goldsmith et al., “Protein Kinases,”Current Opinion in Structural Biology, 4:833-840 (1994).
Goodford, “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules,”J. Med. Chem., 28:849-857 (1985).
Goodsell et al., “Automated Docking of Substrates to Proteins by Simulated Annealing,”Proteins Struct. Funct. Genet., 8:195-202 (1990).
Gregory et al., “Treatment With Rapamycin and Mycophenolic Acid Reduces Arterial Intimal Thickening Produced by Mechanical Injury and Allows Endothelial Replacement,”Transplantation, 59(5):655-661 (Mar. 1995).
Guida, “Software for Structure-Based Drug Design,”Curr. Opin. Struct. Biology, 4:777-781 (1994).
Gupta et al., “Selective Interaction of JNK Protein Kinase Isoforms with Transcription Factors,”The EMBO Journal, 15:2760-2770 (1996).
Jancarik et al., “Sparse Matrix Sampling: A Screening Method for Crystallization of Proteins,”J. Appl. Cryst., 24:409-411 (1991).
Johnson et al., “Active and Inactive Protein Kinases: Structural Basis for Regulation,”Cell, 85:149-158 (1996).
Kajihara et al., “Protein Modeling Using a Chimera Reference Protein Derived From Exons,”Protein Eng'g, 6: 615-620 (1993).
Knighton et al., “Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase,”Science, 253:407-413 (1991).
Knighton et al., “Structure of Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase,”Science, 253:414-420 (1991).
Kuntz et al., “A Geometric Approach to Macromolecule-Ligand Interactions,”J. Mol. Biol., 161:269-288 (1982).
Lauri et al., “CAVEAT: A Program to Facilitate the Design of Organic Molecules,”J. Comp. Aid. Molec. Design, 8:51-66 (1994).
Lee et al., “A Protein Kinase Involved in the Regulation of Inflammatory Cytokine Biosynthesis,”Nature, 372:739-746 (1994).
Martin, “3D Database Searching in Drug Design,”Journal of Medicinal Chemistry, 35(12):2145-54, (1992).
Meng, et al., “Automated Docking with Grid-Based Energy Evaluation,”Journal of Computational Chemistry, 13:505-524 (1992).
Miranker et al., “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method,”Proteins Struct. Funct. Genet., 11:29-34 (1991).
Morris, “New Small Molecule Immunosuppressants for Transplantation: Review of Essential Concepts,”The Journal of Heart and Lung Transplantation, 12:S275-S286 (1993).
Navia et al., “Use of Structural Information in Drug Design,”Current Opinion in Structural Biology, 2:202-210 (1992).
Nishibata et al., “Automatic Creation of Drug Candidate Structures Based on Receptor Structure. Starting Point for Artificial Lead Generation,”Tetrahedron, 47:8985-8990 (1991).
Russell et al., “Rational Modification of Enzyme Catalysis by Engineering Surface Charge,”Nature, 328:496-500 (1987).
Scapin et al., “The Structure of JNK3 in Complex with Small Molecule Inhibitors: Structural Basis for Potency and Selectivity,”Chemistry&Biology, 10:705-712 (2003).
Service, “Tapping DNA for Structures Produces a Trickle,”Science, 298:948-950 (2002).
Singh et al., “Structure-Based Design of a Potent, Selective, and Irreversible Inhibitor of the Catalytic Domain of the erbB Receptor Subfamily of Protein Tyrosine Kinases”,J. Med. Chem., 40:1130-1135 (1997).
Taylor et al., “Three Protein Kinase Structures Define a Common Motif,”Structure, 2:345-355 (1994).
Uhlin et al., “Crystallization and Crystallographic Investigations of Ribonucleotide Reductase Protein R1 FromEscherichia Coli,”FEBS, 336:148-152 (1993).
Wilson et al., “Crystal Structure of p38 Mitogen-activated Protein Kinase,”J. Biol. Chem., 271:27696-27700 (1996).
Wilson et al., “The Structural Basis for the Specificity of Pyridinylimidazole Inhibitors of p38 MAP Kinase,”Chem.&Biol., 4:423-431 (1997).
Xie et al., “Crystal Structure of JNK3: A Kinase Implicated in Neuronal Apoptosis,”Structure, 6:983-991 (1998).
Zhang et al., “Activity of the MAP Kinase ERK2 is Controlled by a Flexible Surface Loop,”Structure, 3:299-307 (1995).
Zhang et al., “Atomic Structure of the MAP Kinase ERK2 at 2.3 Å Resolution,”Nature, 367:704-711 (1994).
Zheng et al., “2.2 Å Refined Crystal Structure of the Catalytic Subunit of cAMP-Dependent Protein Kinase Complexed with MnATP and a Peptide Inhibitor,”Acta Cryst., D49:362-365 (1993).
Caron Paul R.
Fox Edward
Gu Yong
Markland William
Su Michael S.
Doss Raymond M.
Haley Jr. James F.
Ropes & Gray LLP
Steadman David J
Vertex Pharmaceuticals Incorporated
LandOfFree
Crystallization of C-Jun N-Terminal Kinase 3 (JNK3) does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Crystallization of C-Jun N-Terminal Kinase 3 (JNK3), we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Crystallization of C-Jun N-Terminal Kinase 3 (JNK3) will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2706117