Investigational IV small-molecule inhibitor of the TRPV6 calcium channel intended to suppress Ca2+-dependent tumor growth and survival signaling.
Bispecific ligand–drug conjugate that targets folate receptor alpha (FRa) and the TRPV6 calcium channel on tumor cells; upon binding and internalization, it releases the camptothecin analog exatecan to inhibit topoisomerase I, blocking DNA replication and inducing cell-cycle arrest and apoptosis in FRa/TRPV6-expressing tumors.
CBP-1019 binds FRa on tumor cells, is internalized, and releases the topoisomerase I inhibitor exatecan, which blocks DNA replication and triggers cell-cycle arrest and apoptosis in FRa-expressing cells.
Investigational IV small-molecule inhibitor of the TRPV6 calcium channel intended to suppress Ca2+-dependent tumor growth and survival signaling.
Bispecific ligand–drug conjugate that targets folate receptor alpha (FRa) and the TRPV6 calcium channel on tumor cells; upon binding and internalization, it releases the camptothecin analog exatecan to inhibit topoisomerase I, blocking DNA replication and inducing cell-cycle arrest and apoptosis in FRa/TRPV6-expressing tumors.
CBP-1019 binds TRPV6 on tumor cells, is internalized, and releases the exatecan payload, a topoisomerase I inhibitor, causing DNA replication blockade and apoptosis of TRPV6-expressing cells.
Lentivirally transduced CAR T cells recognizing EBV latent membrane protein 1 (LMP1); IV infusion with dose escalation; targets LMP1-expressing EBV-associated malignancies through CAR-triggered cytotoxicity.
T cells are lentivirally engineered to express a chimeric antigen receptor that recognizes EBV latent membrane protein 1 (LMP1). CAR engagement of LMP1 on tumor cells triggers MHC-independent T-cell activation, leading to perforin/granzyme-mediated cytotoxicity and cytokine-driven tumor clearance in EBV-associated malignancies.
CAR T cells recognize LMP1 on target cells and directly kill them via T‑cell activation with perforin/granzyme-mediated cytotoxicity (and related apoptotic pathways).
An antibody-drug conjugate composed of a humanized anti–Trop-2 IgG1 monoclonal antibody linked via a cleavable linker to SN-38 (the active metabolite of irinotecan). After binding Trop-2 on tumor cells and internalization, it releases SN-38 to inhibit topoisomerase I, inducing DNA damage and apoptosis; the cleavable linker enables bystander killing, with potential Fc-mediated effector functions.
Humanized anti–Trop-2 IgG1 antibody delivers the topoisomerase I–inhibiting payload SN-38 via a cleavable linker; after Trop-2 binding and internalization, SN-38 is released to stabilize Topo I–DNA complexes, causing DNA damage and apoptosis, with a cleavable linker enabling bystander killing and potential Fc-mediated effector functions.
The ADC binds TROP-2, is internalized, and releases SN-38 (a topoisomerase I inhibitor) that induces DNA damage and apoptosis in the target cell; the cleavable linker can also enable local bystander killing.
TROP2-directed antibody-drug conjugate composed of a human monoclonal antibody linked to the microtubule inhibitor prodrug MMAE; binds TROP2 on tumor cells, is internalized, and releases MMAE to disrupt microtubules and induce apoptosis.
TROP2-targeted human IgG1 antibody-drug conjugate linked via a beta-glucuronidase-cleavable linker to the microtubule inhibitor MMAE. After binding TROP2 and internalization, linker cleavage releases MMAE, which binds tubulin, inhibits microtubule polymerization, causes G2/M arrest, and induces apoptosis (with potential bystander killing).
ADC binds TROP2, is internalized, beta‑glucuronidase cleaves the linker to release MMAE, which inhibits tubulin polymerization causing G2/M arrest and apoptosis (with potential bystander killing).