IndraLab

Statements

APETx1 inhibits KCNH2. 15 / 15
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"Therefore , no information could be obtained regarding the APETx1 residues crucial for hERG inhibition , and it remains unclear how APETx1 binds to the S4-down conformation of the VSD to inhibit hERG activation ."
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"APETx1 is a 42-residue peptide toxin of sea anemone Anthopleura elegantissima and inhibits hERG by stabilizing the resting state."
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"A previous study that conducted cysteine-scanning analysis of hERG identified two residues in the S3-S4 region of the VSD that play important roles in hERG inhibition by APETx1 [ 28 ] ."
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"We identified the hydrophobic residues of APETx1 , as well as those in the hERG S3-S4 region related to hERG inhibition by APETx1 ."
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"Therefore, no information could be obtained regarding the APETx1 residues crucial for hERG inhibition, and it remains unclear how APETx1 binds to the S4-down conformation of the VSD to inhibit hERG activation."
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"Electrophysiological analyses using wild type and mutants of APETx1 and hERG revealed that their hydrophobic residues, F15, Y32, F33, and L34, in APETx1, and F508 and I521 in hERG, in addition to a previously reported acidic hERG residue, E518, play key roles in the inhibition of hERG by APETx1."
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"Figure  xref shows the mapping of the residues that are key to hERG inhibition by APETx1 (see also Fig. S xref c-h)."
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"APETx1 inhibits HERG currents in a heterologous system with an IC50 value of 34 nM by modifying the voltage dependence of the channel gating."
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"Conclusions The present study identified the key residues of APETx1 and hERG that are involved in hERG inhibition by APETx1 ."
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"A previous study that conducted cysteine-scanning analysis of hERG identified two residues in the S3-S4 region of the VSD that play important roles in hERG inhibition by APETx1 ."
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"For example , APETx1 ( inhibits KV11.1 , KV11.3 and blocks NaV1.2 , NaV1.3 , NaV1.4 , NaV1.5 , NaV1.6 , NaV1.8 of mammals ) and APETx2 ( inhibits mammalian KV3.4 , KV11.1 , some NaV and blocks ASIC3-containing trimers ) were isolated from Anthopleura elegantissima venom [ 57,58,59 ] ."
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"APETx1 is a 42-residue peptide toxin of sea anemone Anthopleura elegantissima and inhibits hERG by stabilizing the resting state ."
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"`` Open-book '' representations of the interaction interfaces are also drawn as semi-transparent molecular surfaces with ribbon representation Figure 5 shows the mapping of the residues that are key to hERG inhibition by APETx1 ( see also Fig. S11c-h ) ."
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"Electrophysiological analyses using wild type and mutants of APETx1 and hERG revealed that their hydrophobic residues , F15 , Y32 , F33 , and L34 , in APETx1 , and F508 and I521 in hERG , in addition to a previously reported acidic hERG residue , E518 , play key roles in the inhibition of hERG by APETx1 ."
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sparser
"The present study identified the key residues of APETx1 and hERG that are involved in hERG inhibition by APETx1."
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