Endophilin I inhibitors constitute a diverse group of compounds that either directly target Endophilin I or indirectly modulate its activity by influencing key cellular pathways involved in membrane remodeling and endocytosis. Dynasore, a small molecule inhibitor of dynamin, indirectly modulates Endophilin I by disrupting endocytosis processes. Dynasore-induced dynamin inhibition leads to impaired endocytosis, influencing the recruitment and function of Endophilin I in membrane remodeling and vesicle formation. Ionomycin, a calcium ionophore, indirectly modulates Endophilin I by influencing calcium-dependent cellular processes. Ionomycin-induced calcium influx leads to altered calcium signaling, affecting the recruitment and function of Endophilin I in membrane remodeling and vesicle formation. ML141, a Cdc42 inhibitor, indirectly influences Endophilin I by disrupting Rho GTPase signaling. 
Dyngo-4a, a dynamin inhibitor, indirectly modulates Endophilin I by disrupting clathrin-mediated endocytosis. Dyngo-4a-induced dynamin inhibition leads to impaired endocytosis, influencing the recruitment and function of Endophilin I in membrane remodeling and vesicle formation. NSC23766, a Rac1 inhibitor, indirectly influences Endophilin I by disrupting Rho GTPase signaling. CK666, an Arp2/3 complex inhibitor, indirectly modulates Endophilin I by disrupting actin polymerization. CK666-induced Arp2/3 complex inhibition leads to altered actin dynamics, affecting the recruitment and function of Endophilin I in membrane remodeling and endocytosis processes. SMIFH2, an inhibitor of formin homology 2 (FH2) domains, indirectly influences Endophilin I by disrupting actin dynamics. Jasplakinolide, an actin polymerization stabilizer, indirectly modulates Endophilin I by influencing actin dynamics. Jasplakinolide-induced actin stabilization leads to altered actin polymerization, affecting the recruitment and function of Endophilin I in membrane remodeling and endocytosis processes. Wiskostatin, an N-WASP inhibitor, indirectly influences Endophilin I by disrupting actin polymerization. CK869, a myosin II inhibitor, indirectly modulates Endophilin I by disrupting actin dynamics. CK869-induced myosin II inhibition leads to altered actin polymerization, affecting the recruitment and function of Endophilin I in membrane remodeling and endocytosis processes. ML7, a myosin light chain kinase (MLCK) inhibitor, indirectly influences Endophilin I by disrupting actin dynamics.