An antibody-drug conjugate (also known as izalontamab brengitecan, BMS-986507, iza-bren) targeting TROP2 that delivers the camptothecin-derived topoisomerase I inhibitor payload brengitecan to induce DNA damage and apoptosis.
TROP2-targeting antibody-drug conjugate that binds TROP2 on tumor cells, is internalized, and releases the camptothecin-derived topoisomerase I inhibitor brengitecan to induce DNA damage and apoptosis.
The ADC binds HER3 on tumor cells, is internalized, and releases a cytotoxic payload that induces DNA damage and apoptosis, directly killing HER3-expressing cells.
Gene-modified natural killer (NK) cells engineered to express an NKG2D-based chimeric antigen receptor (CAR) that recognizes NKG2D ligands (MICA, MICB, ULBP family) on tumor cells, activating NK cytotoxicity for treatment of relapsed/refractory multiple myeloma.
Gene‑modified NK cells expressing an NKG2D‑based CAR recognize stress‑induced NKG2D ligands (MICA, MICB, ULBP family) on tumor cells. CAR signaling activates NK cytotoxic functions, inducing degranulation (perforin/granzyme), cytokine‑mediated killing, and apoptosis of malignant cells, targeting relapsed/refractory multiple myeloma.
NKG2D-CAR NK cells bind ULBP4 on target cells, triggering CAR signaling and NK effector functions (degranulation with perforin/granzyme and death receptor pathways), leading to apoptotic lysis of the target cells.
Chimeric IgG1 monoclonal antibody against EGFR that competitively blocks ligand binding and EGFR activation; used to curb feedback/reactivation of MAPK signaling.
Chimeric IgG1 monoclonal antibody against EGFR that competitively blocks ligand binding, preventing EGFR activation and dimerization and thereby inhibiting downstream RAS–RAF–MEK–ERK (MAPK) signaling and tumor cell proliferation; may also mediate Fc-dependent ADCC.
Cetuximab binds EGFR on target cells and engages Fcγ receptors on immune effectors (e.g., NK cells) to mediate antibody‑dependent cellular cytotoxicity (and some complement-mediated lysis); signaling blockade is mainly cytostatic.
Autologous T cells engineered to express a chimeric antigen receptor targeting CD5, enabling HLA-independent recognition and killing of CD5+ T-ALL cells via CD3ζ/costimulatory signaling, leading to T-cell activation, proliferation, cytokine release, and perforin/granzyme-mediated cytotoxicity.
Autologous T cells engineered to express a CD5-specific chimeric antigen receptor bind CD5 on target cells in an HLA-independent manner; CAR signaling via CD3ζ and costimulatory domains activates the T cells, driving proliferation, cytokine release, and perforin/granzyme-mediated cytotoxic killing of CD5+ cells (including malignant T-ALL cells).
CD5-specific CAR T cells bind CD5 and, upon CAR signaling, directly kill CD5+ cells via perforin/granzyme-mediated cytotoxicity (and Fas/FasL pathways).
Autologous anti-CD19 CAR T-cell therapy with a 4-1BB costimulatory domain; engineered CD4+/CD8+ T cells recognize CD19 and kill malignant B cells.
Autologous CD4+/CD8+ T cells engineered with an anti‑CD19 CAR containing a 4‑1BB costimulatory domain bind CD19 on malignant B cells, triggering T‑cell activation, expansion, cytokine release, and perforin/granzyme‑mediated cytotoxic killing.
Anti‑CD19 CAR T cells bind CD19 on target cells, form an immune synapse, and induce death via perforin/granzyme release (and Fas/FasL signaling) following CAR activation.