Abstract: Provided by the invention are methods for identifying therapeutic agents for treating multiple myeloma or another hematological malignancy, as well as methods for determining the prognosis of a patient with multiple myeloma or another hematological malignancy. The methods are based in part on the inventors' discovery that an extracellular form of cyclophilin A binds to CD147 expressed on multiple myeloma cells.

Abstract: The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to ?-catenin in vitro, in cellulo, and in vivo, disrupting the BCL9/?-catenin interaction, and thereby interfering with deregulated Wnt/?-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.

Abstract: The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to ?-catenin in vitro, in cellulo, and in vivo, disrupting the BCL9/?-catenin interaction, and thereby interfering with deregulated Wnt/?-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.

Abstract: The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to ?-catenin in vitro, in cellulo, and in vivo, disrupting the BCL-9/?-catenin interaction, and thereby interfering with deregulated Wnt/?-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.

Abstract: The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to ?-catenin in vitro, in cellulo, and in vivo, disrupting the BCL-9/?-catenin interaction, and thereby interfering with deregulated Wnt/?-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.

Abstract: Provided by the invention are methods for identifying therapeutic agents for treating multiple myeloma or another hematological malignancy, as well as methods for determining the prognosis of a patient with multiple myeloma or another hematological malignancy. The methods are based in part on the inventors' discovery that an extracellular form of cyclophilin A binds to CD147 expressed on multiple myeloma cells.

Abstract: Provided by the invention are methods for identifying therapeutic agents for treating multiple myeloma or another hematological malignancy, as well as methods for determining the prognosis of a patient with multiple myeloma or another hematological malignancy. The methods are based in part on the inventors' discovery that an extracellular form of cyclophilin A binds to CD147 expressed on multiple myeloma cells.

Abstract: Provided by the invention are methods for identifying therapeutic agents for treating multiple myeloma or another hematological malignancy, as well as methods for determining the prognosis of a patient with multiple myeloma or another hematological malignancy. The methods are based in part on the inventors' discovery that an extracellular form of cyclophilin A binds to CD147 expressed on multiple myeloma cells.

Abstract: Provided are compositions and methods for treating hematological malignancies, such as multiple myeloma, in a subject by increasing levels or activity of miR-30 RNA in plasma cells of the subject.

Abstract: Provided are compositions and methods for treating hematological malignancies, such as multiple myeloma, in a subject by increasing levels or activity of miR-30 RNA in plasma cells of the subject.

Abstract: The invention provides structurally-constrained peptides by hydrocarbon stapling of a BCL9 HD2 helix for use as a therapeutic agent. The invention further provides methods and kits for use of the structurally-constrained peptide of the instant invention. The invention is based, at least in part, on the results provided herein demonstrating that hydrocarbon stapled helical peptides display excellent proteolytic, acid, and thermal stability, restore the native helical structure of the peptide, possess superior pharmacokinetic properties compared to the corresponding unmodified peptides, and are highly effective in binding to ?-catenin in vitro, in cellulo, and in vivo, disrupting the BCL-9/?-catenin interaction, and thereby interfering with deregulated Wnt/?-catenin signaling for therapeutic benefit in a variety of human diseases including human cancer.