An antibody–drug conjugate targeting tissue factor (TF/CD142) with a human IgG1 linked to the cytotoxic payload monomethyl auristatin E (MMAE). Upon binding TF, it is internalized and releases MMAE to inhibit microtubules, causing G2/M arrest and apoptosis; may also engage Fc-mediated effector functions.
Anti–tissue factor (TF/CD142) IgG1 linked via a protease-cleavable linker to monomethyl auristatin E (MMAE). After TF binding and internalization, MMAE is released to inhibit tubulin polymerization, inducing G2/M arrest and apoptosis; may also engage Fc-mediated effector functions and modestly interfere with TF/FVIIa signaling.
The anti–TF ADC binds TF (CD142) on the cell surface, is internalized, and releases MMAE via linker cleavage; MMAE disrupts microtubules, causing G2/M arrest and apoptosis (with possible added Fc-mediated cytotoxicity).
Anti-CD38 IgG1 monoclonal antibody that mediates ADCC, CDC, and ADCP and induces apoptosis of CD38+ clonal plasma cells.
Human IgG1κ monoclonal antibody targeting CD38 on clonal plasma cells; binding triggers immune effector–mediated killing (ADCC, CDC, ADCP) and direct apoptosis, and depletes CD38+ immunosuppressive cells (e.g., Tregs, Bregs, MDSCs), resulting in antitumor activity.
Anti-CD38 IgG1 binds CD38 on target cells and triggers immune effector killing (ADCC by NK cells, CDC via complement, ADCP by phagocytes) and can induce direct apoptosis upon binding/crosslinking.
EGFR-targeting IgG1 monoclonal antibody that blocks ligand binding and receptor activation, inhibiting MAPK/ERK and PI3K/AKT signaling; may also trigger ADCC.
Chimeric IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization/activation, thereby inhibiting downstream MAPK/ERK and PI3K/AKT signaling to suppress tumor cell proliferation; its Fc domain can also trigger antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab binds EGFR on target cells and its IgG1 Fc engages Fcγ receptors on NK cells/macrophages to trigger ADCC (and some CDC), leading to killing of EGFR-expressing cells; EGFR signaling blockade is mainly antiproliferative.
Allogeneic T cells from the patient's prior HSCT donor engineered to express an anti-CD7 chimeric antigen receptor; upon CD7 binding, initiates cytotoxic killing of CD7+ malignant T cells via TCR-like signaling, perforin/granzyme pathways, and cytokine release. Expected on-target depletion of normal CD7+ T cells and some NK cells, causing T-cell aplasia.
Allogeneic T cells from the prior HSCT donor are engineered to express an anti‑CD7 chimeric antigen receptor. CAR engagement with CD7 on malignant T cells triggers TCR-like signaling that activates cytotoxic effector functions, leading to perforin/granzyme-mediated lysis and cytokine release. On‑target effects include depletion of normal CD7+ T cells (and some NK cells), causing T‑cell aplasia.
Anti-CD7 CAR T cells bind CD7 on target cells and, upon CAR engagement, activate T-cell cytotoxic programs leading to perforin/granzyme-mediated lysis (and potentially Fas/FasL), directly killing CD7+ cells.
Allogeneic, off-the-shelf T cells engineered with an anti-CD19 chimeric antigen receptor to target and eliminate CD19-expressing B-lineage cells, inducing transient B-cell aplasia to reduce autoantibody production and reset humoral immunity in refractory SLE.
Allogeneic T cells engineered with an anti-CD19 chimeric antigen receptor recognize and kill CD19-expressing B-lineage cells. CAR engagement triggers T-cell cytotoxicity (perforin/granzyme) leading to depletion of CD19+ B cells and plasmablasts, inducing transient B-cell aplasia, reducing autoantibody production, and resetting humoral immunity in refractory SLE.
Anti-CD19 CAR T cells bind CD19 on target cells and trigger T-cell cytotoxicity, lysing targets via perforin/granzyme-mediated apoptosis (and death receptor pathways).