PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30425124-4 2019 The intrinsic ligand is located at the PAS-CNBHD interface, but its mechanism of action in hERG is not well understood. Aminosalicylic Acid 39-42 ETS transcription factor ERG Homo sapiens 91-95 31315662-4 2019 METHODS: Here we describe a surface plasmon resonance (SPR)-based screening method aimed in identifying small molecule binders of PAS and CNBH domains for three KCNH channel subfamilies: ether-a-go-go (EAG), EAG-related gene (ERG), and EAG-like K+ (ELK). Aminosalicylic Acid 130-133 ETS transcription factor ERG Homo sapiens 208-224 31315662-4 2019 METHODS: Here we describe a surface plasmon resonance (SPR)-based screening method aimed in identifying small molecule binders of PAS and CNBH domains for three KCNH channel subfamilies: ether-a-go-go (EAG), EAG-related gene (ERG), and EAG-like K+ (ELK). Aminosalicylic Acid 130-133 ETS transcription factor ERG Homo sapiens 226-229 27516548-0 2016 Enhancement of hERG channel activity by scFv antibody fragments targeted to the PAS domain. Aminosalicylic Acid 80-83 ETS transcription factor ERG Homo sapiens 15-19 29725305-5 2018 To test our method, we focused on 16 LQT2 mutations in the hERG Per-Arnt-Sim (PAS) domain that were previously studied via a widely used biochemical approach that compares levels of 135-kDa immature and 155-kDa fully glycosylated hERG protein to infer surface expression. Aminosalicylic Acid 78-81 ETS transcription factor ERG Homo sapiens 59-63 27516548-6 2016 We have uncovered a family of positive modulators of hERG that specifically bind to the PAS domain. Aminosalicylic Acid 88-91 ETS transcription factor ERG Homo sapiens 53-57 27516548-10 2016 Overall, these molecules constitute a previously unidentified class of positive modulators and establish that allosteric modulation of hERG channel function through ligand binding to the PAS domain can be attained. Aminosalicylic Acid 187-190 ETS transcription factor ERG Homo sapiens 135-139 24325597-3 2013 Here, we describe hybrid hERG molecules, termed chimeric hERG channels, in which the N-terminal Per-Arnt-Sim (PAS) domain is deleted and the C-terminal C-linker as well as the cyclic nucleotide binding domain (CNBD) portion is replaced by an artificial tetramerization domain. Aminosalicylic Acid 110-113 ETS transcription factor ERG Homo sapiens 25-29 25923442-2 2015 The N-terminal "eag" domain, which is composed of a Per-Arnt-Sim (PAS) domain and a short PAS-cap region, is a critical regulator of hERG channel function. Aminosalicylic Acid 90-93 ETS transcription factor ERG Homo sapiens 133-137 27487920-6 2016 By comparing it with the structures of the Homo sapiens EAG-related gene (hERG) channel and the Drosophila EAG-like K(+) (dELK) channel and analyzing the structural features of the hEAG channel, it was identified that a hydrophobic patch on the beta-sheet may mediate interaction between the PAS domain and other regions of the channel to regulate its functions. Aminosalicylic Acid 292-295 ETS transcription factor ERG Homo sapiens 74-78 25923442-2 2015 The N-terminal "eag" domain, which is composed of a Per-Arnt-Sim (PAS) domain and a short PAS-cap region, is a critical regulator of hERG channel function. Aminosalicylic Acid 66-69 ETS transcription factor ERG Homo sapiens 133-137 24325597-3 2013 Here, we describe hybrid hERG molecules, termed chimeric hERG channels, in which the N-terminal Per-Arnt-Sim (PAS) domain is deleted and the C-terminal C-linker as well as the cyclic nucleotide binding domain (CNBD) portion is replaced by an artificial tetramerization domain. Aminosalicylic Acid 110-113 ETS transcription factor ERG Homo sapiens 57-61 34716268-0 2021 Conformation-sensitive antibody reveals an altered cytosolic PAS/CNBh assembly during hERG channel gating. Aminosalicylic Acid 61-64 ETS transcription factor ERG Homo sapiens 86-90 23721480-7 2013 Our results highlight a critical role for interactions between the PAS domain and the remainder of the channel in the hERG assembly and that mutants that affect PAS domain interactions with the remainder of the channel have a more severe trafficking defect than that caused by domain unfolding alone. Aminosalicylic Acid 67-70 ETS transcription factor ERG Homo sapiens 118-122 21536673-3 2011 Only a small percentage of hERG channels containing PAS domain LQT2 mutations (hERG PAS-LQT2) have been characterized in mammalian cells, so the functional effect of these mutations is unclear. Aminosalicylic Acid 52-55 ETS transcription factor ERG Homo sapiens 27-31 21536673-3 2011 Only a small percentage of hERG channels containing PAS domain LQT2 mutations (hERG PAS-LQT2) have been characterized in mammalian cells, so the functional effect of these mutations is unclear. Aminosalicylic Acid 52-55 ETS transcription factor ERG Homo sapiens 79-83 21536673-11 2011 Thus, our results reveal a putative "gating face" in the PAS domain where mutations within this region form functional channels with altered gating properties, and we show that NPAS is a general means for rescuing aberrant gating in hERG LQT2 mutant channels and may be a potential biological therapeutic. Aminosalicylic Acid 57-60 ETS transcription factor ERG Homo sapiens 233-237 21357734-2 2011 A Per-Arnt-Sim (PAS) domain in the cytoplasmic N-terminal region of hERG regulates slow deactivation by making a direct interaction with another part of the hERG channel. Aminosalicylic Acid 16-19 ETS transcription factor ERG Homo sapiens 68-72 21357734-2 2011 A Per-Arnt-Sim (PAS) domain in the cytoplasmic N-terminal region of hERG regulates slow deactivation by making a direct interaction with another part of the hERG channel. Aminosalicylic Acid 16-19 ETS transcription factor ERG Homo sapiens 157-161 21357734-5 2011 We report that hERG channels with deletions of the cyclic nucleotide-binding domain (CNBD) had accelerated deactivation kinetics that were similar to those seen in hERG channels lacking the PAS domain. Aminosalicylic Acid 190-193 ETS transcription factor ERG Homo sapiens 15-19 21357734-10 2011 Together, these data suggest that the mechanism for regulation of slow deactivation in hERG channels is an interaction between the N-terminal PAS domain and the C-terminal CNBD. Aminosalicylic Acid 142-145 ETS transcription factor ERG Homo sapiens 87-91 21249148-3 2011 Here we show that the solution NMR structure of the N-terminal 135 residues of hERG contains a previously described Per-Arnt-Sim (PAS) domain (residues 26-135) as well as an amphipathic alpha-helix (residues 13-23) and an initial unstructured segment (residues 2-9). Aminosalicylic Acid 130-133 ETS transcription factor ERG Homo sapiens 79-83 23721480-5 2013 Six mutants, located in the vicinity of a hydrophobic patch on the PAS domain surface, also affected binding of the isolated PAS domain to an N-terminal truncated hERG (human ether-a-go-go-related gene) channel. Aminosalicylic Acid 67-70 ETS transcription factor ERG Homo sapiens 163-167 23721480-5 2013 Six mutants, located in the vicinity of a hydrophobic patch on the PAS domain surface, also affected binding of the isolated PAS domain to an N-terminal truncated hERG (human ether-a-go-go-related gene) channel. Aminosalicylic Acid 125-128 ETS transcription factor ERG Homo sapiens 163-167 23555008-5 2013 We determined high resolution structures of PAS domains from the mouse EAG (mEAG), drosophila ELK (dELK) and human ERG (hERG) channels and also of the hERG domain without the first nine amino acids. Aminosalicylic Acid 44-47 ETS transcription factor ERG Homo sapiens 115-118 23555008-7 2013 In particular, we have found cavities in the hERG and mEAG structures that share similarities with the ligand binding sites from other PAS domains. Aminosalicylic Acid 135-138 ETS transcription factor ERG Homo sapiens 45-49 22124116-2 2011 Cardiac hERG channels comprise two primary isoforms: hERG1a, which has a regulatory N-terminal Per-Arnt-Sim (PAS) domain, and hERG1b, which does not. Aminosalicylic Acid 109-112 ETS transcription factor ERG Homo sapiens 8-12 21536673-2 2011 hERG channels have slow deactivation kinetics that are regulated by an N-terminal Per-Arnt-Sim (PAS) domain. Aminosalicylic Acid 96-99 ETS transcription factor ERG Homo sapiens 0-4