Chimeric anti-CD20 monoclonal antibody that mediates B-cell depletion via antibody-dependent cellular cytotoxicity, complement activation, and apoptosis.
Rituximab is a chimeric monoclonal antibody against CD20 that depletes CD20-positive B cells via antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and induction of apoptosis.
Anti-CD20 antibody binds CD20+ cells and triggers killing via Fc-mediated ADCC (e.g., NK cells/macrophages), complement-dependent cytotoxicity, and can induce apoptosis upon crosslinking.
Autologous CD19-directed CAR T-cell therapy composed of genetically modified T cells that mediate CAR-dependent recognition and cytotoxic killing of CD19-positive B-cell lymphoma.
Autologous T cells are genetically engineered to express a CD19-directed chimeric antigen receptor; upon binding CD19 on malignant B cells, the CAR activates T-cell effector functions, leading to proliferation and perforin/granzyme-mediated cytotoxic killing of CD19-positive cells.
CD19-directed CAR T cells bind CD19 on target cells and trigger T-cell effector functions, primarily perforin/granzyme-mediated apoptosis.
A small-molecule PSMA-targeted beta-emitting radiopharmaceutical. The PSMA ligand binds PSMA (FOLH1) on PSMA-expressing tumor cells, is internalized, and delivers 177Lu beta radiation to induce DNA double-strand breaks and tumor cell death, including a crossfire effect.
PSMA-targeted small-molecule ligand (vipivotide tetraxetan/PSMA-617) chelated to 177Lu binds PSMA on tumor cells, is internalized, and emits beta radiation that induces DNA double-strand breaks, causing tumor cell death with a crossfire effect on adjacent cells.
PSMA-targeted 177Lu radioligand binds and is internalized by PSMA-expressing cells, emitting beta particles that cause DNA double‑strand breaks leading to cell death (with crossfire to nearby cells).
Autologous gene-modified CAR T-cell therapy for relapsed/refractory multiple myeloma; patient T cells are engineered to express a CAR that recognizes myeloma-associated antigens and, upon binding, activates T-cell cytotoxicity.
Autologous patient T cells are genetically modified to express a chimeric antigen receptor that recognizes myeloma-associated surface antigens; upon antigen binding, CAR signaling activates and expands the T cells, inducing cytokine release and perforin/granzyme-mediated cytotoxic killing of malignant plasma cells.
Engineered CAR T cells bind GPRC5D on target cells, activate, and kill them via perforin/granzyme-mediated cytolysis and cytokine-driven apoptosis.
A HER2-directed antibody–drug conjugate (RC48) that binds ERBB2 on tumor cells, is internalized, and releases the microtubule inhibitor MMAE to inhibit microtubule polymerization, leading to mitotic arrest and apoptosis; its IgG1 backbone can mediate ADCC and a bystander effect.
HER2-directed antibody–drug conjugate (RC48) that binds ERBB2/HER2 on tumor cells, is internalized, and releases the microtubule inhibitor MMAE to inhibit tubulin polymerization, leading to G2/M arrest and apoptosis; the IgG1 Fc can mediate ADCC and the membrane-permeable payload enables a bystander effect.
HER2-binding ADC is internalized and releases MMAE, which inhibits tubulin polymerization causing G2/M arrest and apoptosis; Fc can also mediate ADCC, with a membrane-permeable payload enabling bystander killing.