Curagen Corporation

Meijia Yang

Krishnan Nandabalan

Vincent Peter Schulz

Henri Lichenstein

Richard August Shimkets

Jonathan Marc Rothberg

Ferenc L Boldog

Catherine Burgess

Michael Jeffers

John L Herrmann

William LaRochelle

Sudhirdas K Prayaga

Elma Fernandes

Theodore Samuel Kalbfleisch

James Robert Knight

Muralidhara Padigaru

William F McDonald

Denise M Lepley

William Grosse

Linda L Gorman

Daniel K Rieger

Carol E A Pena

John P Alsobrook, Ii

Mei Zhong

Vincent Peter Schultz

The present invention provides FGF-CX, a novel isolated polypeptide, as well as a polynucleotide encoding FGF-CX and antibodies that immunospecifically bind to FGF-CX or any derivative, variant, mutant, or fragment of the FGF-CX polypeptide, polynucleotide or antibody. The invention additionally provides methods in which the FGF-CX polypeptide, polynucleotide and antibody are used in detection and treatment of a broad range of pathological states, as well as other uses.

Polypeptides of FGF-CX

The present invention provides FGF-CX polypeptides and polynucleotides, and antibodies that immunospecifically bind to FGF-CX or any derivative, variant, mutant, or fragment of the FGF-CX polypeptide, polynucleotide or antibody. The invention additionally provides methods of use for the FGF-CX polypeptide, polynucleotide and antibody.

Fibroblast growth factor and nucleic acids encoding same

Disclosed are osteoprotegerin-like polypeptides, nucleic acids encoding osteoprotegerin-like polypeptides, and methods of using these molecules. The osteoprotegerin-like polypeptides sequence homology to osteoprotegerin and tumor necrosis factor receptor molecules.

Nucleic acids encoding osteoprotegern-like proteins and methods of using same

The present invention relates to complexes of the 53BP2 protein with proteins identified as interacting with 53BP2 by a yeast two hybrid assay system. The proteins identified to interact with 53BP2 are &bgr;-tubulin, p62, hnRNP G, and three gene products, 53BP2-IP1, 53BP2-IP2, and 53BP2-IP3 encoded, in part, by the EST R72810 sequence. Thus, the invention provides complexes of 53BP2 and &bgr;-tubulin, p62, hnRNP G, 53BP2-IP1, 53BP2-IP2, and 53BP2-IP3 and derivatives, fragments and analogs thereof. The invention also provides the 53BP2-IP1, 53BP2-IP2 and 53BP2-IP3 genes and proteins and derivatives, fragments and analogs thereof. Methods of screening the complexes for efficacy in treating and/or preventing certain diseases and disorders, particularly cancer, autoimmune disease and neurodegenerative disease are also provided.

53BP2 complexes

The present invention relates to complexes of the HPS protein with proteins identified as interacting with HPS protein by a modified yeast two hybrid assay system. The proteins identified to interact with HPS protein are 14-3-3 protein, Hrs, atrophin-1, DGS-I, nuclear factor NF90, HPIP1 and human HN1 homolog protein. Accordingly, the present invention discloses complexes of HPS protein and 14-3-3 protein, Hrs, atrophin-1, DGS-I, nuclear factor NF90, HPIP1 and human HN1 homolog protein, and derivatives, fragments and analogs thereof. Additionally, the present invention also discloses nucleic acids encoding the HPIP1 and human HN1 homolog protein, or derivatives, fragments and analogs thereof. Methods of screening the complexes or proteins for efficacy in treating and/or preventing certain diseases and disorders, particularly atopic diseases, autoimmune diseases, neurodegenerative disease, cancer, pigmentation disorders, platelet dysfunction and viral diseases, are also disclosed herein.

Isolation and characterization of Hermansky Pudlak Syndrome (HPS) protein complexes and HPS protein-interacting proteins

The present invention relates to complexes of the CDK2 protein with proteins identified as interacting with CDK2 by a modified yeast two hybrid assay system. The proteins identified to interact with CDK2 are cyclin H, cyclin I, ERH, and two gene products, hsReq*-1 and hsReq*-2, which are splice variants of the gene hsReq. Thus, the invention provides complexes of CDK2 and cyclin H, cyclin I, ERH, hsReq*-1, and hsReq*-2, and derivatives, fragments and analogs thereof. The invention also provides nucleic acids encoding the hsReq*-1 and hsReq*-2, and proteins and derivatives, fragments and analogs thereof. Methods of screening the complexes for efficacy in treating and/or preventing certain diseases and disorders, particularly cancer, atherosclerosis and neurodegenerative disease are also provided.

HsReq*1 and hsReq*2proteins and use thereof to detect CDK2

Methods are described for detecting protein-protein interactions, among two populations of proteins, each having a complexity of at least 100. Encoded proteins are fused either to the DNA-binding domain of a transcriptional activator or to the activation domain of a transcriptional activator. Two yeast strains, of the opposite mating type and carrying one type each of the fusion proteins are mated together. Productive interactions between the two halves due to protein-protein interactions lead to the reconstitution of the transcriptional activator, which in turn leads to the activation of a reporter gene containing a binding site for the DNA-binding domain. This analysis can be carried out for two or more populations of proteins. The differences in the genes encoding the proteins involved in the protein-protein interactions are characterized, thus leading to the identification of specific protein-protein interactions, and the genes encoding the interacting proteins, relevant to a particular tissue, stage or disease. Furthermore, inhibitors that interfere with these protein-protein interactions are identified by their ability to inactivate a reporter gene. The screening for such inhibitors can be in a multiplexed format where a set of inhibitors will be screened against a library of interactors. Further, information-processing methods and systems are described. These methods and systems pro vide for identification of the genes coding for detected interacting proteins, for assembling a unified database of protein-protein interaction data, and for processing this unified database to obtain protein interaction domain and protein pathway information.

Identification and comparison of protein&mdash;protein interactions that occur in populations and identification of inhibitors of these interactors

Disclosed are complexes of the MDM2 protein and a novel MDM2-interacting protein (MDMIP). Also disclosed are nucleic acids encoding the MDMIP polypeptide, as well as derivatives, fragments, analogs and homologs of the MDMIP polypeptide and MDM2-MDMIP complexes.

Nucleic acid encoding the MDM interacting protein

Methods are described for detecting protein-protein interactions, among two populations of proteins, each having a complexity of at least 1,000. For example, proteins are fused either to the DNA-binding domain of a transcriptional activator or to the activation domain of a transcriptional activator. Two yeast strains, of the opposite mating type and carrying one type each of the fusion proteins are mated together. Productive interactions between the two halves due to protein-protein interactions lead to the reconstitution of the transcriptional activator, which in turn leads to the activation of a reporter gene containing a binding site for the DNA-binding domain. This analysis can be carried out for two or more populations of proteins. The differences in the genes encoding the proteins involved in the protein-protein interactions are characterized, thus leading to the identification of specific protein-protein interactions, and the genes encoding the interacting proteins, relevant to a particular tissue, stage or disease. Furthermore, inhibitors that interfere with these protein-protein interactions are identified by their ability to inactivate a reporter gene. The screening for such inhibitors can be in a multiplexed format where a set of inhibitors will be screened against a library of interactors. Further, information-processing methods and systems are described. These methods and systems provide for identification of the genes coding for detected interacting proteins, for assembling a unified database of protein-protein interaction data, and for processing this unified database to obtain protein interaction domain and protein pathway information.

Identification and comparison of protein-protein interactions that occur

CDK2 interactions

The present invention relates to complexes of the 53BP2 protein with proteins identified as interacting with 53BP2 by a yeast two hybrid assay system. The proteins identified to interact with 53BP2 are .beta.-tubulin, p62, hnRNP G, and three gene products, 53BP2-IP1, 53BP2-IP2, and 53BP2-IP3 encoded, in part, by the EST R72810 sequence. Thus, the invention provides complexes of 53BP2 and .beta.-tubulin, p62, hnRNP G, 53BP2-IP1, 53BP2-IP2, and 53BP2-IP3 and derivatives, fragments and analogs thereof. The invention also provides the 53BP2-IP1, 53BP2-IP2 and 53BP2-IP3 genes and proteins and derivatives, fragments and analogs thereof. Methods of screening the complexes for efficacy in treating and/or preventing certain diseases and disorders, particularly cancer, autoimmune disease and neurodegenerative disease are also provided.

Growing community of inventors

East Lyme, CT, United States of America

Meijia Yang