A HER2-targeting humanized monoclonal antibody conjugated via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd); binds HER2, is internalized, and releases DXd to cause DNA damage with a bystander effect in HER2-expressing (including HER2-low) breast cancer.
Humanized anti-HER2 monoclonal antibody (trastuzumab) linked via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd). After binding HER2 on tumor cells, the ADC is internalized and the linker is cleaved to release DXd, which inhibits topoisomerase I, causing DNA damage and cell death. The membrane-permeable payload produces a bystander effect that can kill adjacent HER2-expressing and HER2-low tumor cells.
The ADC binds HER2, is internalized, and releases deruxtecan (DXd), a topoisomerase I inhibitor, causing DNA damage and apoptosis in the target cell; the membrane-permeable payload can also kill nearby cells (bystander effect).
A TROP-2–targeting humanized monoclonal antibody linked via a hydrolyzable linker to SN-38, a topoisomerase I inhibitor; binds TROP-2, internalizes, and can release SN-38 extracellularly to induce DNA damage with a bystander effect in TROP-2–positive tumors.
Humanized monoclonal antibody targeting TROP-2 linked via a hydrolyzable linker to SN-38 (topoisomerase I inhibitor). Upon binding TROP-2 on tumor cells, the ADC is internalized and/or releases SN-38 extracellularly, causing DNA damage and cell death with a bystander effect in TROP-2–positive tumors.
ADC binds TROP-2 on tumor cells and delivers SN-38 (topoisomerase I inhibitor) via internalization or local release, causing DNA damage and apoptosis; also enables bystander killing.
Patient-derived T cells engineered to express a CAR targeting BCMA (TNFRSF17) on plasma cells; CAR signaling activates T cells to proliferate and kill BCMA-expressing multiple myeloma cells via cytotoxic mechanisms.
Autologous T cells are genetically engineered to express a chimeric antigen receptor targeting BCMA (TNFRSF17) on plasma cells. BCMA engagement triggers CAR CD3zeta and co-stimulatory signaling, leading to T-cell activation, proliferation, cytokine release, and perforin/granzyme-mediated cytotoxic killing of BCMA-expressing multiple myeloma cells via HLA-independent recognition.
CAR engagement of BCMA activates T cells to kill BCMA+ cells via perforin/granzyme-mediated cytotoxicity (and related apoptotic/lytic pathways).
A subcutaneous bispecific T-cell–engaging antibody that binds BCMA on malignant plasma cells and CD3 on T cells to redirect T-cell cytotoxicity.
Bispecific T‑cell–engaging antibody that binds BCMA on myeloma cells and CD3 on T cells, forming an immunologic synapse to activate T cells and induce targeted cytotoxic killing of BCMA‑expressing plasma cells.
Elranatamab links CD3 on T cells to BCMA on target cells, activating T cells to form an immunologic synapse and kill BCMA-expressing cells via perforin/granzyme-mediated apoptosis (and Fas–FasL signaling).
PBMC-derived chimeric antigen receptor macrophage (CAR-M) cell therapy targeting mesothelin; designed to recognize mesothelin-positive tumor cells, enhance phagocytosis, secrete inflammatory cytokines, and present tumor antigens to T cells.
PBMC-derived macrophages engineered to express an anti-mesothelin chimeric antigen receptor that recognizes mesothelin-positive tumor cells, enhances phagocytosis, secretes pro-inflammatory cytokines, and presents tumor antigens to activate T cells and remodel the tumor microenvironment.
Anti-mesothelin CAR-engineered macrophages bind mesothelin on target cells and directly kill them via CAR-triggered phagocytosis and macrophage cytotoxic effector functions; inflammatory cytokines may augment this.