PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34987017-10 2021 Most important, distinct conformations were observed when purifying and imaging prestin bound to either its physiological ligand, chloride, or to competitively inhibitory anions, sulfate or salicylate. Salicylates 190-200 solute carrier family 26 member 5 Homo sapiens 80-87 21757707-8 2011 The molecular mechanism that facilitates motor function appeared to be the same as prestin because the motor activity depended on the concentration of intracellular chloride and was blocked by salicylate treatment. Salicylates 193-203 solute carrier family 26 member 5 Homo sapiens 83-90 18560754-0 2008 Prestin up-regulation in chronic salicylate (aspirin) administration: an implication of functional dependence of prestin expression. Salicylates 33-43 solute carrier family 26 member 5 Homo sapiens 0-7 18560754-3 2008 Here we report that, consistency with increase in distortion product otoacoustic emission, long-term administration of salicylate can increase prestin expression and OHC electromotility. Salicylates 119-129 solute carrier family 26 member 5 Homo sapiens 143-150 18560754-7 2008 After cessation of salicylate administration, the prestin expression returned to normal. Salicylates 19-29 solute carrier family 26 member 5 Homo sapiens 50-57 18560754-9 2008 The data suggest that prestin expression in vivo is dynamically up-regulated to increase OHC electromotility in long-term administration of salicylate via the Cox-II-independent pathways. Salicylates 140-150 solute carrier family 26 member 5 Homo sapiens 22-29 17442754-6 2007 Transport is blocked by salicylate, an inhibitor of electromotility generated by mammalian prestin. Salicylates 24-34 solute carrier family 26 member 5 Homo sapiens 91-98 12835843-4 2003 Substances, that compete for the chloride combining site of the motor protein prestin, such as salicylate, might have a blocking effect on the regulation of electromotility. Salicylates 95-105 solute carrier family 26 member 5 Homo sapiens 78-85 24843217-3 2014 Chronic salicylate dosing affects the peripheral system by causing a compensatory temporary enhancement in DPOAE amplitudes and up-regulation of prestin mRNA and protein expression. Salicylates 8-18 solute carrier family 26 member 5 Homo sapiens 145-152 21071769-3 2011 For understanding the electromechanical coupling mechanism of prestin, we simultaneously measured voltage-dependent charge movement and electromotility under conditions in which the magnitudes of both charge movement and electromotility are gradually manipulated by the prestin inhibitor, salicylate. Salicylates 289-299 solute carrier family 26 member 5 Homo sapiens 62-69 21071769-3 2011 For understanding the electromechanical coupling mechanism of prestin, we simultaneously measured voltage-dependent charge movement and electromotility under conditions in which the magnitudes of both charge movement and electromotility are gradually manipulated by the prestin inhibitor, salicylate. Salicylates 289-299 solute carrier family 26 member 5 Homo sapiens 270-277 20388516-0 2010 Salicylate-induced translocation of prestin having mutation in the GTSRH sequence to the plasma membrane. Salicylates 0-10 solute carrier family 26 member 5 Homo sapiens 36-43 20388516-2 2010 The present study investigated changes in characteristics of prestin by culturing prestin-transfected cells with salicylate, an antagonist of prestin. Salicylates 113-123 solute carrier family 26 member 5 Homo sapiens 61-68 20388516-2 2010 The present study investigated changes in characteristics of prestin by culturing prestin-transfected cells with salicylate, an antagonist of prestin. Salicylates 113-123 solute carrier family 26 member 5 Homo sapiens 82-89 20388516-2 2010 The present study investigated changes in characteristics of prestin by culturing prestin-transfected cells with salicylate, an antagonist of prestin. Salicylates 113-123 solute carrier family 26 member 5 Homo sapiens 82-89 20388516-5 2010 Thus, the present study discovered a new effect of salicylate on prestin, namely, the promotion of the plasma membrane expression of prestin mutants in an active state. Salicylates 51-61 solute carrier family 26 member 5 Homo sapiens 65-72 20388516-5 2010 Thus, the present study discovered a new effect of salicylate on prestin, namely, the promotion of the plasma membrane expression of prestin mutants in an active state. Salicylates 51-61 solute carrier family 26 member 5 Homo sapiens 133-140 18225604-3 2007 Salicylate acts as a competitive antagonist at the anion-binding site of prestin, the motor protein of sensory outer hair cells. Salicylates 0-10 solute carrier family 26 member 5 Homo sapiens 73-80 34390643-4 2021 Cryoelectron microscopy (cryo-EM) structures of human prestin bound with chloride or salicylate at a common "anion site" adopt contracted or expanded states, respectively. Salicylates 85-95 solute carrier family 26 member 5 Homo sapiens 54-61 35022426-7 2022 Mutation of prestin"s chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function. Salicylates 52-62 solute carrier family 26 member 5 Homo sapiens 12-19 34695838-6 2021 Salicylate, a drug that can cause reversible hearing loss, competes for the anion-binding site of Prestin, and inhibits its function by immobilizing Prestin in a novel conformation. Salicylates 0-10 solute carrier family 26 member 5 Homo sapiens 98-105 34695838-6 2021 Salicylate, a drug that can cause reversible hearing loss, competes for the anion-binding site of Prestin, and inhibits its function by immobilizing Prestin in a novel conformation. Salicylates 0-10 solute carrier family 26 member 5 Homo sapiens 149-156