PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31053797-2	2019	Because our previous work showed that a calmodulin binding site (CBS) was located in prestin"s C-terminal, specifically within the intrinsically disordered region, we sought to delete the IDR to study the functional significance of calcium-dependent, calmodulin binding on OHC function.	Calcium	232-239	solute carrier family 26 member 5	Homo sapiens	85-92
31884787-5	2020	An ultrasound pulse of low frequency and low pressure efficiently evoked cellular calcium responses after transfecting with prestin(N7T, N308S).	Calcium	82-89	solute carrier family 26 member 5	Homo sapiens	124-131
31884787-5	2020	An ultrasound pulse of low frequency and low pressure efficiently evoked cellular calcium responses after transfecting with prestin(N7T, N308S).	AT-308	137-142	solute carrier family 26 member 5	Homo sapiens	124-131
27744409-4	2017	Site-directed mutagenesis shows that the amino acid 308S in FM bats is responsible for the similar functional changes of prestin We strongly support that the occurrence of serine at position 308 is a case of hemiplasy, caused by incomplete lineage sorting of an ancestral polymorphism.	Serine	172-178	solute carrier family 26 member 5	Homo sapiens	121-128
30532536-0	2018	A666-conjugated nanoparticles target prestin of outer hair cells preventing cisplatin-induced hearing loss.	Cisplatin	76-85	solute carrier family 26 member 5	Homo sapiens	37-44
30532536-6	2018	Furthermore, A666-coumarin 6-labeled NP could be significantly internalized by HEI-OC1 cells via the A666-prestin interaction.	a666	13-17	solute carrier family 26 member 5	Homo sapiens	106-113
30532536-6	2018	Furthermore, A666-coumarin 6-labeled NP could be significantly internalized by HEI-OC1 cells via the A666-prestin interaction.	coumarin 6	18-28	solute carrier family 26 member 5	Homo sapiens	106-113
28422190-2	2017	Prestin"s voltage sensitivity is influenced by intracellular chloride.	Chlorides	61-69	solute carrier family 26 member 5	Homo sapiens	0-7
28422190-4	2017	We determine that prestin itself possesses a stretch-sensitive, non-selective conductance that is largest in the presence of thiocyanate ions.	thiocyanate	125-136	solute carrier family 26 member 5	Homo sapiens	18-25
28422190-6	2017	Prestin has been modeled, based on structural data from related anion transporters (SLC26Dg and UraA), to have a 7 + 7 inverted repeat structure with anion transport initiated by chloride binding at the intracellular cleft.	Chlorides	179-187	solute carrier family 26 member 5	Homo sapiens	0-7
28422190-11	2017	We suggest that prestin itself is the main regulator of intracellular chloride concentration via a route distinct from its transporter pathway.	Chlorides	70-78	solute carrier family 26 member 5	Homo sapiens	16-23
27276272-0	2016	Chloride Anions Regulate Kinetics but Not Voltage-Sensor Qmax of the Solute Carrier SLC26a5.	Chlorides	0-8	solute carrier family 26 member 5	Homo sapiens	84-91
27276272-3	2016	The mechanical activity of the OHC imparted by prestin is driven by voltage and controlled by anions, chiefly intracellular chloride.	Chlorides	124-132	solute carrier family 26 member 5	Homo sapiens	47-54
27276272-4	2016	Current opinion is that chloride anions control the Boltzmann characteristics of the voltage sensor responsible for prestin activity, including Qmax, the total sensor charge moved within the membrane, and Vh, a measure of prestin"s operating voltage range.	Chlorides	24-32	solute carrier family 26 member 5	Homo sapiens	116-123
27276272-4	2016	Current opinion is that chloride anions control the Boltzmann characteristics of the voltage sensor responsible for prestin activity, including Qmax, the total sensor charge moved within the membrane, and Vh, a measure of prestin"s operating voltage range.	Chlorides	24-32	solute carrier family 26 member 5	Homo sapiens	222-229
27276272-6	2016	Prestin"s slow transition rates and chloride-binding kinetics adversely influence these estimates, contributing to the prevalent concept that intracellular chloride level controls the quantity of sensor charge moved.	Chlorides	156-164	solute carrier family 26 member 5	Homo sapiens	0-7
27276272-7	2016	By monitoring charge movement across frequency, using measures of multifrequency admittance, expanded displacement current integration, and OHC electromotility, we find that chloride influences prestin kinetics, thereby controlling charge magnitude at any particular frequency of interrogation.	Chlorides	174-182	solute carrier family 26 member 5	Homo sapiens	194-201
26869218-0	2016	The chloride-channel blocker 9-anthracenecarboxylic acid reduces the nonlinear capacitance of prestin-associated charge movement.	9-anthroic acid	29-56	solute carrier family 26 member 5	Homo sapiens	94-101
26869218-7	2016	In the prestin-transfected cells, cytosolic application of 9-AC approximately halved the blocking efficacy of extracellularly applied 9-AC.	9-anthroic acid	59-63	solute carrier family 26 member 5	Homo sapiens	7-14
26869218-7	2016	In the prestin-transfected cells, cytosolic application of 9-AC approximately halved the blocking efficacy of extracellularly applied 9-AC.	9-anthroic acid	134-138	solute carrier family 26 member 5	Homo sapiens	7-14
26869218-10	2016	We conclude that 9-AC acts on the electromechanical transducer principally by interaction with prestin rather than acting via the cytoskeleton, chloride channels or pH.	9-anthroic acid	17-21	solute carrier family 26 member 5	Homo sapiens	95-102
26869218-12	2016	9-AC provides a new tool for elucidating the molecular dynamics of prestin function.	9-anthroic acid	0-4	solute carrier family 26 member 5	Homo sapiens	67-74
25485080-3	2014	The model takes into account the possible chloride-bicarbonate exchange function of prestin, a protein highly expressed in the plasma membrane of OHCs.	Chlorides	42-50	solute carrier family 26 member 5	Homo sapiens	84-91
26635354-1	2016	Prestin is a unique ATP- and Ca(2+)-independent molecular motor with piezoelectric characteristics responsible for the electromotile properties of mammalian cochlear outer hair cells, i.e. the capacity of these cells to modify their length in response to electric stimuli.	Adenosine Triphosphate	20-23	solute carrier family 26 member 5	Homo sapiens	0-7
26283790-4	2015	Our three-dimensional model of prestin using molecular dynamics simulations predicts that prestin contains eight transmembrane-spanning segments and two helical re-entry loops and that tyrosyl residues are the structural specialization of the molecule for the unique function of prestin.	cyclo(tyrosyl-tyrosyl)	185-192	solute carrier family 26 member 5	Homo sapiens	31-38
25687712-8	2015	Under DC + AC conditions, the strong frequency dependence of the prestin mobile charge has a relatively small effect on the amplitude and phase of the resulting potential.	dc + ac	6-13	solute carrier family 26 member 5	Homo sapiens	65-72
25485080-3	2014	The model takes into account the possible chloride-bicarbonate exchange function of prestin, a protein highly expressed in the plasma membrane of OHCs.	Bicarbonates	51-62	solute carrier family 26 member 5	Homo sapiens	84-91
24710176-4	2014	Here we derive a structural model of prestin and related transporters by combining homology modelling, MD simulations and cysteine accessibility scanning.	Cysteine	122-130	solute carrier family 26 member 5	Homo sapiens	37-44
24988347-0	2014	Chloride-driven electromechanical phase lags at acoustic frequencies are generated by SLC26a5, the outer hair cell motor protein.	Chlorides	0-8	solute carrier family 26 member 5	Homo sapiens	86-93
24988347-4	2014	This stretched exponential behavior, which we accurately recapitulate with a new kinetic model, the meno presto model of prestin, influences the protein"s responsiveness to chloride binding and provides for delays in eM relative to membrane voltage driving force.	Chlorides	173-181	solute carrier family 26 member 5	Homo sapiens	121-128
23083705-0	2012	Membrane cholesterol strongly influences confined diffusion of prestin.	Cholesterol	9-20	solute carrier family 26 member 5	Homo sapiens	63-70
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
23762468-2	2013	We studied in real time the delivery of YFP-prestin to the plasma membrane of cells from a tetracycline-inducible cell line.	Tetracycline	91-103	solute carrier family 26 member 5	Homo sapiens	44-51
23431177-0	2013	Disparities in voltage-sensor charge and electromotility imply slow chloride-driven state transitions in the solute carrier SLC26a5.	Chlorides	68-76	solute carrier family 26 member 5	Homo sapiens	124-131
23431177-3	2013	Here we report on simultaneous measures of prestin"s voltage-sensor charge movement (nonlinear capacitance, NLC) and eM that evidence disparities in their voltage dependence and magnitude as a function of intracellular chloride, challenging decades" old dogma that NLC reports on eM steady-state behavior.	Chlorides	219-227	solute carrier family 26 member 5	Homo sapiens	43-50
22890707-0	2012	Mammalian prestin is a weak Cl-/HCO3- electrogenic antiporter.	Bicarbonates	32-36	solute carrier family 26 member 5	Homo sapiens	10-17
22890707-2	2012	The protein belongs to the SLC26 family of transporters whose members are characterised as able to exchange halides for SO(4)(2-) or HCO(3)(-) yet previous analyses of mammalian prestin have suggested that such exchange functions were minimal.	halides	108-115	solute carrier family 26 member 5	Homo sapiens	178-185
22890707-4	2012	In the presence of extracellular HCO(3)(-), pH(i) recovered from an acid load 4 times faster in prestin-transfected cells.	Bicarbonates	33-39	solute carrier family 26 member 5	Homo sapiens	96-103
22890707-8	2012	These data therefore suggest that prestin can act as a weak Cl(-)/HCO(3)(-) antiporter and it is proposed that, in addition to participating in wide band cochlear sound amplification, prestin may also be involved in the slow time scale (>10 s) phenomena where changes in cell stiffness and internal pressure have been implicated.	7 alpha-hydroxy-4-cholesten-3-one	66-69	solute carrier family 26 member 5	Homo sapiens	34-41
22890707-9	2012	The results show the importance of considering the effects of the endogenous bicarbonate buffering system in evaluating the function of prestin in cochlear outer hair cells.	Bicarbonates	77-88	solute carrier family 26 member 5	Homo sapiens	136-143
23083705-2	2012	Prestin function is sensitive to membrane cholesterol levels, and numerous studies have suggested that prestin localizes in cholesterol-rich membrane microdomains.	Cholesterol	42-53	solute carrier family 26 member 5	Homo sapiens	0-7
23083705-2	2012	Prestin function is sensitive to membrane cholesterol levels, and numerous studies have suggested that prestin localizes in cholesterol-rich membrane microdomains.	Cholesterol	124-135	solute carrier family 26 member 5	Homo sapiens	103-110
23083705-3	2012	Previously, fluorescence recovery after photobleaching experiments were performed in HEK cells expressing prestin-GFP after cholesterol manipulations, and revealed evidence of transient confinement.	Cholesterol	124-135	solute carrier family 26 member 5	Homo sapiens	106-113
23083705-8	2012	A complementary analysis of the distribution of squared displacements confirmed that cholesterol depletion reduces prestin confinement.	Cholesterol	85-96	solute carrier family 26 member 5	Homo sapiens	115-122
23083705-9	2012	These findings support the hypothesis that prestin function is intimately linked to membrane organization, and further promote a regulatory role for cholesterol in OHC and auditory function.	Cholesterol	149-160	solute carrier family 26 member 5	Homo sapiens	43-50
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
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.	Chlorides	165-173	solute carrier family 26 member 5	Homo sapiens	83-90
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
21813750-0	2011	The roles of conserved and nonconserved cysteinyl residues in the oligomerization and function of mammalian prestin.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	40-49	solute carrier family 26 member 5	Homo sapiens	108-115
21813750-3	2011	Several studies have suggested that prestin forms homo-oligomers that may be stabilized by disulfide bonds.	Disulfides	91-100	solute carrier family 26 member 5	Homo sapiens	36-43
21813750-4	2011	Our phylogenetic analysis of prestin sequences across chordate classes suggested that the cysteinyl residues could be divided into three groups, depending on the extent of their conservation between prestin orthologs and paralogs or homologs.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	90-99	solute carrier family 26 member 5	Homo sapiens	29-36
21813750-4	2011	Our phylogenetic analysis of prestin sequences across chordate classes suggested that the cysteinyl residues could be divided into three groups, depending on the extent of their conservation between prestin orthologs and paralogs or homologs.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	90-99	solute carrier family 26 member 5	Homo sapiens	199-206
21813750-5	2011	An alanine scan functional analysis was performed of all nine cysteinyl positions in mammalian prestin.	Alanine	3-10	solute carrier family 26 member 5	Homo sapiens	95-102
21813750-5	2011	An alanine scan functional analysis was performed of all nine cysteinyl positions in mammalian prestin.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	62-71	solute carrier family 26 member 5	Homo sapiens	95-102
21813750-10	2011	We assessed the relationship of prestin oligomerization to cysteine position using fluorescence resonance energy transfer.	Cysteine	59-67	solute carrier family 26 member 5	Homo sapiens	32-39
21813750-13	2011	We suggest that no disulfide bond is essential for prestin function.	Disulfides	19-28	solute carrier family 26 member 5	Homo sapiens	51-58
21651892-4	2011	We find that fusion of the biotin-acceptor peptide (BAP) and transmembrane domain of the platelet-derived growth factor receptor (PDGFR) to the N-terminus of prestin-GFP yields a membrane protein that can be metabolically-labeled with biotin, trafficked to the plasma membrane, and selectively detected at the plasma membrane using fluorescently-tagged streptavidin.	Biotin	27-33	solute carrier family 26 member 5	Homo sapiens	158-165
21651892-4	2011	We find that fusion of the biotin-acceptor peptide (BAP) and transmembrane domain of the platelet-derived growth factor receptor (PDGFR) to the N-terminus of prestin-GFP yields a membrane protein that can be metabolically-labeled with biotin, trafficked to the plasma membrane, and selectively detected at the plasma membrane using fluorescently-tagged streptavidin.	benzylaminopurine	52-55	solute carrier family 26 member 5	Homo sapiens	158-165
21651892-4	2011	We find that fusion of the biotin-acceptor peptide (BAP) and transmembrane domain of the platelet-derived growth factor receptor (PDGFR) to the N-terminus of prestin-GFP yields a membrane protein that can be metabolically-labeled with biotin, trafficked to the plasma membrane, and selectively detected at the plasma membrane using fluorescently-tagged streptavidin.	Biotin	235-241	solute carrier family 26 member 5	Homo sapiens	158-165
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
20471983-7	2010	Prestin STAS significantly deviates from the related bacterial ASA proteins, especially in the N-terminal region, which-although previously considered merely as a generic linker between the domain and the last transmembrane helix-is indeed fully part of the domain.	Aspirin	63-66	solute carrier family 26 member 5	Homo sapiens	0-7
20418376-8	2010	Furthermore, co-expression of prestin with MAP1S resulted in a 2.7-fold increase in Q(sp) in single cells that was paralleled by a 2.8-fold increase in protein surface expression, indicating that the interactions are physiological.	q(sp)	84-89	solute carrier family 26 member 5	Homo sapiens	30-37
20418376-9	2010	Quantitative PCR data showed gradients in the expression of prestin and MAP1S across the tonotopic axis that may partially contribute to a previously observed 6-fold increase in Q(sp) in high frequency hair cells.	q(sp)	178-183	solute carrier family 26 member 5	Homo sapiens	60-67
20631244-0	2010	A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin"s Boltzmann characteristics and reveals early maturational events.	tetramethylenedisulfotetramine	20-23	solute carrier family 26 member 5	Homo sapiens	91-98
20631244-3	2010	We have developed a tetracycline-inducible prestin-expressing cell line that we have used to model prestin"s functional maturation.	Tetracycline	20-32	solute carrier family 26 member 5	Homo sapiens	43-50
20631244-3	2010	We have developed a tetracycline-inducible prestin-expressing cell line that we have used to model prestin"s functional maturation.	Tetracycline	20-32	solute carrier family 26 member 5	Homo sapiens	99-106
20655836-0	2010	Combinatorial cysteine mutagenesis reveals a critical intramonomer role for cysteines in prestin voltage sensing.	Cysteine	14-22	solute carrier family 26 member 5	Homo sapiens	89-96
20655836-0	2010	Combinatorial cysteine mutagenesis reveals a critical intramonomer role for cysteines in prestin voltage sensing.	Cysteine	76-85	solute carrier family 26 member 5	Homo sapiens	89-96
20655836-3	2010	We determine the role these cysteine residues play in the voltage sensing capabilities of prestin.	Cysteine	28-36	solute carrier family 26 member 5	Homo sapiens	90-97
20655836-9	2010	Taken together, we believe these data indicate that intramembranous cysteines are constrained, possibly via disulfide bond formation, to ensure structural features of prestin required for normal voltage sensing and mechanical activity.	Cysteine	68-77	solute carrier family 26 member 5	Homo sapiens	167-174
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
19898896-3	2010	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.	Nitrogen	46-47	solute carrier family 26 member 5	Homo sapiens	0-7
20138822-7	2010	Because chloride is important for prestin function and for the efferent-mediated inhibition of cochlear output, the prestin-directed localization of CFTR to the lateral membrane of OHCs has a potential physiological significance.	Chlorides	8-16	solute carrier family 26 member 5	Homo sapiens	34-41
20138822-7	2010	Because chloride is important for prestin function and for the efferent-mediated inhibition of cochlear output, the prestin-directed localization of CFTR to the lateral membrane of OHCs has a potential physiological significance.	Chlorides	8-16	solute carrier family 26 member 5	Homo sapiens	116-123
20347723-7	2010	This suggests that each IMP contains four prestin molecules, based on the general notion that each prestin transfers a single elementary charge.	Inosine Monophosphate	24-27	solute carrier family 26 member 5	Homo sapiens	42-49
20347723-7	2010	This suggests that each IMP contains four prestin molecules, based on the general notion that each prestin transfers a single elementary charge.	Inosine Monophosphate	24-27	solute carrier family 26 member 5	Homo sapiens	99-106
19898896-4	2010	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.	Cholesterol	137-148	solute carrier family 26 member 5	Homo sapiens	37-44
19898896-7	2010	In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking.	Cholesterol	114-125	solute carrier family 26 member 5	Homo sapiens	66-73
19898896-7	2010	In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking.	Cholesterol	114-125	solute carrier family 26 member 5	Homo sapiens	78-85
19898896-8	2010	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.	Cholesterol	68-79	solute carrier family 26 member 5	Homo sapiens	27-34
19898896-11	2010	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.	Cholesterol	22-33	solute carrier family 26 member 5	Homo sapiens	48-55
19926791-0	2010	Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.	Cysteine	0-8	solute carrier family 26 member 5	Homo sapiens	92-99
19926791-4	2010	We have performed cysteine-scanning mutagenesis with serine or valine replacement to investigate the importance of cysteine residues to prestin structure and function.	Cysteine	115-123	solute carrier family 26 member 5	Homo sapiens	136-143
17442754-5	2007	Using patch-clamp recordings, we show that these prestin orthologs, but not mammalian prestin, generate robust transport currents in the presence of the divalent anions sulfate or oxalate.	Sulfates	169-176	solute carrier family 26 member 5	Homo sapiens	49-56
19490917-6	2009	The movement of the combined charge (i.e., anion and protein charges) across the membrane is described with a Fokker-Planck equation coupled to a kinetic equation that describes the binding of chloride ions to prestin.	Chlorides	193-201	solute carrier family 26 member 5	Homo sapiens	210-217
19515900-5	2009	We heterologously expressed prestin labeled with fluorophores at the COOH- or NH(2)-terminus in human embryonic kidney-293T cells, and monitored FRET changes on depolarization-inducing high KCl application.	Carbonic Acid	69-73	solute carrier family 26 member 5	Homo sapiens	28-35
19515900-5	2009	We heterologously expressed prestin labeled with fluorophores at the COOH- or NH(2)-terminus in human embryonic kidney-293T cells, and monitored FRET changes on depolarization-inducing high KCl application.	Potassium Chloride	190-193	solute carrier family 26 member 5	Homo sapiens	28-35
18556757-0	2008	Probing conformational changes of prestin with thiol-reactive optical switches.	Sulfhydryl Compounds	47-52	solute carrier family 26 member 5	Homo sapiens	34-41
18556757-1	2008	Thiol-reactive optical switch probes were used to examine conformational changes of prestin-based membrane motor.	Sulfhydryl Compounds	0-5	solute carrier family 26 member 5	Homo sapiens	84-91
18556757-3	2008	When the plasma membrane is conjugated with the probes, optically induced spiro-merocyanine transition positively shifted nonlinear capacitance of outer hair cells and prestin-transfected cells by approximately 10 mV.	spiro-merocyanine	74-91	solute carrier family 26 member 5	Homo sapiens	168-175
17933870-5	2007	To study the effects of cholesterol on hearing at the molecular level, we altered cholesterol levels in the OHC wall, which contains the membrane protein prestin.	Cholesterol	82-93	solute carrier family 26 member 5	Homo sapiens	154-161
17933870-6	2007	We show a dynamic and reversible relationship between membrane cholesterol levels and voltage dependence of prestin-associated charge movement in both OHCs and prestin-transfected HEK 293 cells.	Cholesterol	63-74	solute carrier family 26 member 5	Homo sapiens	108-115
17933870-6	2007	We show a dynamic and reversible relationship between membrane cholesterol levels and voltage dependence of prestin-associated charge movement in both OHCs and prestin-transfected HEK 293 cells.	Cholesterol	63-74	solute carrier family 26 member 5	Homo sapiens	160-167
17933870-7	2007	Cholesterol levels also modulate the distribution of prestin within plasma membrane microdomains and affect prestin self-association in HEK 293 cells.	Cholesterol	0-11	solute carrier family 26 member 5	Homo sapiens	53-60
17933870-7	2007	Cholesterol levels also modulate the distribution of prestin within plasma membrane microdomains and affect prestin self-association in HEK 293 cells.	Cholesterol	0-11	solute carrier family 26 member 5	Homo sapiens	108-115
17933870-8	2007	These findings indicate that alterations in membrane cholesterol affect prestin function and functionally tune the outer hair cell.	Cholesterol	53-64	solute carrier family 26 member 5	Homo sapiens	72-79
17468166-5	2007	A single point mutation of alanine to tryptophan (A100W) in prestin eliminates prestin-associated charge movement and diminishes EMF but does not alter passive membrane mechanics.	Alanine	27-34	solute carrier family 26 member 5	Homo sapiens	60-67
17468166-5	2007	A single point mutation of alanine to tryptophan (A100W) in prestin eliminates prestin-associated charge movement and diminishes EMF but does not alter passive membrane mechanics.	Alanine	27-34	solute carrier family 26 member 5	Homo sapiens	79-86
17468166-5	2007	A single point mutation of alanine to tryptophan (A100W) in prestin eliminates prestin-associated charge movement and diminishes EMF but does not alter passive membrane mechanics.	Tryptophan	38-48	solute carrier family 26 member 5	Homo sapiens	60-67
17468166-5	2007	A single point mutation of alanine to tryptophan (A100W) in prestin eliminates prestin-associated charge movement and diminishes EMF but does not alter passive membrane mechanics.	Tryptophan	38-48	solute carrier family 26 member 5	Homo sapiens	79-86
17442754-7	2007	The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry.	Chlorides	196-204	solute carrier family 26 member 5	Homo sapiens	114-121
19737539-2	2009	In the present study, to clarify contributions of unique amino acids of prestin, namely, Met-122, Met-225 and Thr-428, to the characteristics of prestin, mutations were introduced into those amino acids.	Methionine	89-92	solute carrier family 26 member 5	Homo sapiens	72-79
19737539-2	2009	In the present study, to clarify contributions of unique amino acids of prestin, namely, Met-122, Met-225 and Thr-428, to the characteristics of prestin, mutations were introduced into those amino acids.	Methionine	98-101	solute carrier family 26 member 5	Homo sapiens	72-79
19153847-2	2009	The data show that cholesterol modulates electromotility mainly by influencing the motor protein prestin, less by affecting the passive membrane properties.	Cholesterol	19-30	solute carrier family 26 member 5	Homo sapiens	97-104
19153847-3	2009	OBJECTIVES: Elevated serum cholesterol is linked to inner ear disorders and may influence hearing by altering membrane properties of outer hair cells (OHCs) and by affecting the motor protein prestin.	Cholesterol	27-38	solute carrier family 26 member 5	Homo sapiens	192-199
19517190-2	2009	The importance of the plasma membrane environment in modulating OHC electromotility has been substantiated by recent studies demonstrating that membrane cholesterol alters prestin activity in a manner consistent with cholesterol-induced changes in auditory function.	Cholesterol	153-164	solute carrier family 26 member 5	Homo sapiens	172-179
19517190-8	2009	These results support the idea that the cholesterol-dependent regulation of prestin function and electromotility correlates with changes in the properties of the lipid environment that surrounds and supports prestin.	Cholesterol	40-51	solute carrier family 26 member 5	Homo sapiens	76-83
19517190-8	2009	These results support the idea that the cholesterol-dependent regulation of prestin function and electromotility correlates with changes in the properties of the lipid environment that surrounds and supports prestin.	Cholesterol	40-51	solute carrier family 26 member 5	Homo sapiens	208-215
18839359-3	2009	Here, we describe two fluorescence microscopic methodologies applied to the outer hair cell-specific membrane protein prestin: the intensity and fluorescence lifetime (FLIM) variants of FRET (Fluorescence Resonance Energy Transfer), used in the study of protein-protein interactions, and the Scanning Cysteine Accessibility Method (SCAM), used for the determination of protein conformation.	Cysteine	301-309	solute carrier family 26 member 5	Homo sapiens	118-125
18567583-3	2008	We have previously shown that membrane cholesterol modulates the peak voltage of prestin-associated nonlinear capacitance in vivo and in vitro.	Cholesterol	39-50	solute carrier family 26 member 5	Homo sapiens	81-88
18567583-4	2008	The present study explores the effects of membrane cholesterol and docosahexaenoic acid content on the peak and magnitude of prestin-associated charge movement in a human embryonic kidney (HEK 293) cell model.	Cholesterol	51-62	solute carrier family 26 member 5	Homo sapiens	125-132
18567583-4	2008	The present study explores the effects of membrane cholesterol and docosahexaenoic acid content on the peak and magnitude of prestin-associated charge movement in a human embryonic kidney (HEK 293) cell model.	Docosahexaenoic Acids	67-87	solute carrier family 26 member 5	Homo sapiens	125-132
18567583-11	2008	Our results quantify the relation between membrane cholesterol concentration and prestin-associated charge movement and enhance our understanding of how membrane composition modulates prestin function.	Cholesterol	51-62	solute carrier family 26 member 5	Homo sapiens	81-88
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
18560754-0	2008	Prestin up-regulation in chronic salicylate (aspirin) administration: an implication of functional dependence of prestin expression.	Aspirin	45-52	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
17442754-5	2007	Using patch-clamp recordings, we show that these prestin orthologs, but not mammalian prestin, generate robust transport currents in the presence of the divalent anions sulfate or oxalate.	Oxalates	180-187	solute carrier family 26 member 5	Homo sapiens	49-56
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
17442754-7	2007	The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry.	Sulfates	54-61	solute carrier family 26 member 5	Homo sapiens	114-121
17442754-7	2007	The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry.	Chlorides	66-74	solute carrier family 26 member 5	Homo sapiens	114-121
17442754-7	2007	The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry.	Sulfates	173-180	solute carrier family 26 member 5	Homo sapiens	114-121
17442754-7	2007	The dependence of transport equilibrium potentials on sulfate and chloride concentration gradients shows that the prestin orthologs are electrogenic antiporters, exchanging sulfate or oxalate for chloride in a strictly coupled manner with a 1:1 stoichiometry.	Oxalates	184-191	solute carrier family 26 member 5	Homo sapiens	114-121
18003225-3	2007	Our results suggest that prestin appears to change membrane tension and amplify electrically-evoked force generation, while a single point mutation of alanine to tryptophan in prestin reduces electrically-evoked force generation without affecting the membrane tension.	Alanine	151-158	solute carrier family 26 member 5	Homo sapiens	176-183
17321873-6	2007	RESULTS & DISCUSSION: Prestin targets to the membrane by 24 hours post-transfection when NLC is measurable.	Adenosine Monophosphate	9-12	solute carrier family 26 member 5	Homo sapiens	26-33
17321873-8	2007	Depleting membrane cholesterol content altered prestin localization and NLC.	Cholesterol	19-30	solute carrier family 26 member 5	Homo sapiens	47-54
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
18003225-3	2007	Our results suggest that prestin appears to change membrane tension and amplify electrically-evoked force generation, while a single point mutation of alanine to tryptophan in prestin reduces electrically-evoked force generation without affecting the membrane tension.	Tryptophan	162-172	solute carrier family 26 member 5	Homo sapiens	176-183
16525055-4	2006	However, the movements were also diminished by Na salicylate and depended on the intracellular anion, properties implying involvement of the prestin motor.	na salicylate	47-60	solute carrier family 26 member 5	Homo sapiens	141-148
16611815-1	2006	Chloride ions have been hypothesized to interact with the membrane outer hair cell (OHC) motor protein, prestin on its intracellular domain to confer voltage sensitivity (Oliver et al., 2001).	Chlorides	0-8	solute carrier family 26 member 5	Homo sapiens	104-111
16611815-5	2006	Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm.	Chlorides	166-174	solute carrier family 26 member 5	Homo sapiens	180-187
16611815-5	2006	Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm.	Chlorides	229-237	solute carrier family 26 member 5	Homo sapiens	116-123
16611815-5	2006	Using the well known ototoxicant, salicylate, which competes with the putative anion binding or interaction site of prestin to assess level-dependent interactions of chloride with prestin, we determined that the resting level of chloride in OHCs is near or below 10 mm, whereas perilymphatic levels are known to be approximately 140 mm.	Chlorides	229-237	solute carrier family 26 member 5	Homo sapiens	180-187
15596517-1	2005	The outer hair cell (OHC) underlies mammalian cochlea amplification, and its lateral membrane motor, prestin, which drives the cell"s mechanical activity, is modulated by intracellular chloride ions.	Chlorides	185-193	solute carrier family 26 member 5	Homo sapiens	101-108
17120772-6	2006	Here, we review and extend data indicating that charge movement by prestin and consequently electromotility depend on the presence of small monovalent anions such as chloride and bicarbonate at the cytoplasmic side of the membrane.	Chlorides	166-174	solute carrier family 26 member 5	Homo sapiens	67-74
17120772-6	2006	Here, we review and extend data indicating that charge movement by prestin and consequently electromotility depend on the presence of small monovalent anions such as chloride and bicarbonate at the cytoplasmic side of the membrane.	Bicarbonates	179-190	solute carrier family 26 member 5	Homo sapiens	67-74
15596517-4	2005	Capitalizing on measures of prestin-derived nonlinear capacitance to gauge Cl flux across the lateral membrane, we show that the Cl ionophore TBT, which affects neither the motor nor G(metL) directly, is capable of augmenting the native flux of Cl in OHCs.	tributyltin	142-145	solute carrier family 26 member 5	Homo sapiens	28-35
15596517-7	2005	Using malate as an anion replacement, we quantify chloride effects on the nonlinear charge density and operating voltage range of prestin.	malic acid	6-12	solute carrier family 26 member 5	Homo sapiens	130-137
15596517-7	2005	Using malate as an anion replacement, we quantify chloride effects on the nonlinear charge density and operating voltage range of prestin.	Chlorides	50-58	solute carrier family 26 member 5	Homo sapiens	130-137
15649974-0	2005	Effects of cyclic nucleotides on the function of prestin.	Nucleotides, Cyclic	11-29	solute carrier family 26 member 5	Homo sapiens	49-56
15649974-4	2005	There are two potential cAMP/cGMP-dependent protein kinase phosphorylation sites on prestin.	Cyclic AMP	24-28	solute carrier family 26 member 5	Homo sapiens	84-91
15649974-4	2005	There are two potential cAMP/cGMP-dependent protein kinase phosphorylation sites on prestin.	Cyclic GMP	29-33	solute carrier family 26 member 5	Homo sapiens	84-91
15649974-10	2005	The neutral amino acid alanine replaced serine/threonine at phosphorylation sites to change the conserved phosphorylation motif in order to mimic the dephosphorylated state of prestin, whereas replacement with the negatively charged aspartic acid mimicked the phosphorylated state.	Alanine	23-30	solute carrier family 26 member 5	Homo sapiens	176-183
15649974-12	2005	Our data demonstrate that cGMP is significantly more influential than cAMP in modifying the non-linear, voltage-dependent charge displacement in prestin-transfected cells.	Cyclic GMP	26-30	solute carrier family 26 member 5	Homo sapiens	145-152
15649974-12	2005	Our data demonstrate that cGMP is significantly more influential than cAMP in modifying the non-linear, voltage-dependent charge displacement in prestin-transfected cells.	Cyclic AMP	70-74	solute carrier family 26 member 5	Homo sapiens	145-152
12938672-4	2003	Direct measurements of labelled fructose transport into COS-7 cells expressing prestin are reported here.	Fructose	32-40	solute carrier family 26 member 5	Homo sapiens	79-86
15140192-0	2004	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	Nitrogen	0-1	solute carrier family 26 member 5	Homo sapiens	50-57
15140192-2	2004	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.	Nitrogen	22-23	solute carrier family 26 member 5	Homo sapiens	0-7
15140192-5	2004	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.	Nitrogen	107-108	solute carrier family 26 member 5	Homo sapiens	143-150
15140192-7	2004	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.	Nitrogen	50-51	solute carrier family 26 member 5	Homo sapiens	19-26
12938672-9	2003	The data are consistent with fructose being transported by prestin with an apparent Km=24 nm.	Fructose	29-37	solute carrier family 26 member 5	Homo sapiens	59-66
11867734-4	2002	Prestin(TRE) bound TH receptors as a monomer or presumptive heterodimer and mediated a triiodothyronine-dependent transactivation of a heterologous promotor in response to triiodothyronine receptors alpha and beta.	Triiodothyronine	87-103	solute carrier family 26 member 5	Homo sapiens	0-7
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.	Chlorides	33-41	solute carrier family 26 member 5	Homo sapiens	78-85
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
34109172-0	2021	Spatiotemporal Developmental Upregulation of Prestin Correlates With the Severity and Location of Cyclodextrin-Induced Outer Hair Cell Loss and Hearing Loss.	Cyclodextrins	98-110	solute carrier family 26 member 5	Homo sapiens	45-52
34987017-1	2021	Prestin (SLC26A5), a member of the SLC26 transporter family, is the molecular actuator that drives OHC electromotility (eM).	ohc	99-102	solute carrier family 26 member 5	Homo sapiens	0-7
34987017-1	2021	Prestin (SLC26A5), a member of the SLC26 transporter family, is the molecular actuator that drives OHC electromotility (eM).	ohc	99-102	solute carrier family 26 member 5	Homo sapiens	9-16
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.	Chlorides	130-138	solute carrier family 26 member 5	Homo sapiens	80-87
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.	Sulfates	179-186	solute carrier family 26 member 5	Homo sapiens	80-87
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
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
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.	Chlorides	73-81	solute carrier family 26 member 5	Homo sapiens	54-61
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
11914517-5	2002	Nevertheless, the association of the cloned motor protein "prestin" with an anion transporter superfamily provides clues about the molecular nature of the OHC motor in the basolateral membrane, the utilisation of chloride in hair cells and the long-term stability of small basal turn cochlear hair cells.	Chlorides	213-221	solute carrier family 26 member 5	Homo sapiens	59-66
11914518-8	2002	Recently, intracellular anions (chloride or bicarbonate) were found to be essential for OHC electromotility and prestin"s function.	Chlorides	32-40	solute carrier family 26 member 5	Homo sapiens	112-119
11914518-8	2002	Recently, intracellular anions (chloride or bicarbonate) were found to be essential for OHC electromotility and prestin"s function.	Bicarbonates	44-55	solute carrier family 26 member 5	Homo sapiens	112-119
11423665-3	2001	Here, we show that voltage sensitivity is conferred to prestin by the intracellular anions chloride and bicarbonate.	Chlorides	91-99	solute carrier family 26 member 5	Homo sapiens	55-62
11423665-3	2001	Here, we show that voltage sensitivity is conferred to prestin by the intracellular anions chloride and bicarbonate.	Bicarbonates	104-115	solute carrier family 26 member 5	Homo sapiens	55-62
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Chlorides	175-183	solute carrier family 26 member 5	Homo sapiens	244-251
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Chlorides	175-183	solute carrier family 26 member 5	Homo sapiens	253-260
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Iodine	185-191	solute carrier family 26 member 5	Homo sapiens	244-251
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Iodine	185-191	solute carrier family 26 member 5	Homo sapiens	253-260
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Bicarbonates	193-204	solute carrier family 26 member 5	Homo sapiens	244-251
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Bicarbonates	193-204	solute carrier family 26 member 5	Homo sapiens	253-260
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Oxalates	206-213	solute carrier family 26 member 5	Homo sapiens	244-251
11087667-3	2000	Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell.	Oxalates	206-213	solute carrier family 26 member 5	Homo sapiens	253-260
34695838-5	2021	Our structural and functional data suggest that Prestin adopts a unique and complex set of states, tunable by the identity of bound anions (Cl- or SO42-).	Sulfates	147-152	solute carrier family 26 member 5	Homo sapiens	48-55
33667636-0	2021	Calmodulin binds to the STAS domain of SLC26A5 prestin with a calcium-dependent, one-lobe, binding mode.	Calcium	62-69	solute carrier family 26 member 5	Homo sapiens	39-46
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.	Chlorides	22-30	solute carrier family 26 member 5	Homo sapiens	12-19
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.	Chlorides	22-30	solute carrier family 26 member 5	Homo sapiens	107-114
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
33667636-0	2021	Calmodulin binds to the STAS domain of SLC26A5 prestin with a calcium-dependent, one-lobe, binding mode.	Calcium	62-69	solute carrier family 26 member 5	Homo sapiens	47-54
33667636-5	2021	There is evidence of a calcium/calmodulin regulation of prestin mediated by the STAS domain.	Calcium	23-30	solute carrier family 26 member 5	Homo sapiens	56-63