A subcutaneous bispecific T‑cell–engaging monoclonal antibody (Lunsumio) that binds CD20 on B cells and CD3 on T cells to recruit and activate cytotoxic T cells against malignant B cells.
Humanized bispecific monoclonal antibody that simultaneously binds CD20 on B cells and CD3 on T cells, cross-linking T cells to malignant B cells to activate cytotoxic T-lymphocyte responses (immune synapse formation, perforin/granzyme release) and kill CD20-positive tumor cells.
Mosunetuzumab bridges CD3+ T cells to CD20+ cells, forming an immune synapse that activates T cells to kill the CD20-expressing cells via perforin/granzyme-mediated apoptosis (and Fas/FasL pathways).
An intravenous antibody‑drug conjugate (Polivy) targeting CD79b on B cells that delivers the microtubule inhibitor MMAE, leading to cell cycle arrest and apoptosis.
Anti‑CD79b monoclonal antibody linked via a protease‑cleavable linker to the microtubule inhibitor MMAE. After binding CD79b on B cells and internalization, MMAE is released to inhibit tubulin polymerization, causing G2/M arrest and apoptosis of malignant B cells.
An anti-CD79b ADC binds CD79b, is internalized, and releases MMAE intracellularly; MMAE inhibits tubulin polymerization, causing G2/M arrest and apoptosis of CD79b-positive cells.
Patient-derived T cells genetically engineered to express a T-cell receptor recognizing the TP53 R248Q mutant peptide presented by HLA-A*11:01; reinfused to mediate antigen-specific cytotoxicity against TP53 R248Q–positive tumor cells.
Autologous T cells are engineered to express an HLA-A*11:01–restricted T-cell receptor that recognizes the TP53 R248Q mutant peptide on MHC class I. Upon binding the mutant peptide–MHC complex on tumor cells, the T cells activate TCR signaling and mediate antigen-specific cytotoxicity via perforin/granzyme release and cytokine-driven killing, selectively targeting TP53 R248Q–positive cancer cells.
Engineered TCR T cells recognize the TP53 R248Q peptide–HLA-A*11:01 complex and directly lyse target cells via TCR-activated perforin/granzyme cytotoxicity (and Fas–FasL pathways).
Patient-derived T cells genetically engineered to express a T-cell receptor recognizing the TP53 R248Q mutant peptide presented by HLA-A*11:01; reinfused to mediate antigen-specific cytotoxicity against TP53 R248Q–positive tumor cells.
Autologous T cells are engineered to express an HLA-A*11:01–restricted T-cell receptor that recognizes the TP53 R248Q mutant peptide on MHC class I. Upon binding the mutant peptide–MHC complex on tumor cells, the T cells activate TCR signaling and mediate antigen-specific cytotoxicity via perforin/granzyme release and cytokine-driven killing, selectively targeting TP53 R248Q–positive cancer cells.
Engineered TCR T cells recognize the TP53 R248Q peptide presented by HLA-A*11:01 on target cells and directly kill them via TCR-triggered cytolytic synapse with perforin/granzyme release (and death receptor/cytokine-mediated apoptosis).
An antibody–drug conjugate consisting of a humanized anti–Trop-2 IgG1 monoclonal antibody linked to SN-38 (irinotecan’s active metabolite), a topoisomerase I inhibitor; binding to Trop-2 leads to internalization and SN-38 release, causing DNA damage and tumor cell death.
Humanized anti–Trop-2 IgG1 monoclonal antibody conjugated to SN-38 (irinotecan’s active metabolite). After binding Trop-2 on tumor cells, the complex is internalized and the linker is cleaved to release SN-38, which inhibits topoisomerase I by stabilizing Top1–DNA complexes, causing DNA strand breaks, replication arrest, and apoptosis; released SN-38 can also exert a bystander effect.
ADC binds TROP-2 on tumor cells, is internalized, and releases SN-38, a topoisomerase I inhibitor, causing DNA strand breaks and apoptosis; released SN-38 can also kill nearby cells (bystander effect).