PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27293999-3 2016 Previously, we have shown that L1 reactivation in several human cell lines is dependent upon the activation of aryl hydrocarbon receptor (AhR), a ligand-activated transcription factor member of the PAS superfamily of proteins. Protactinium 198-201 aryl hydrocarbon receptor Homo sapiens 111-136 27293999-3 2016 Previously, we have shown that L1 reactivation in several human cell lines is dependent upon the activation of aryl hydrocarbon receptor (AhR), a ligand-activated transcription factor member of the PAS superfamily of proteins. Protactinium 198-201 aryl hydrocarbon receptor Homo sapiens 138-141 25349783-6 2014 We constructed and purified the PAS domain from AhR. Protactinium 32-35 aryl hydrocarbon receptor Homo sapiens 48-51 26727491-6 2016 In order to understand structural and ligand binding features we compared the stability and dynamics of the promiscuous AhR PAS-B to other PAS domains exhibiting specific interactions or no ligand binding function. Protactinium 124-127 aryl hydrocarbon receptor Homo sapiens 120-123 18940186-1 2009 The aryl hydrocarbon receptor (AhR) is an orphan receptor in the basic helix-loop-helix PAS family of transcriptional regulators. Protactinium 88-91 aryl hydrocarbon receptor Homo sapiens 4-29 21245039-0 2011 Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR. Protactinium 45-48 aryl hydrocarbon receptor Homo sapiens 96-99 21245039-3 2011 Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Protactinium 139-142 aryl hydrocarbon receptor Homo sapiens 203-228 21245039-3 2011 Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Protactinium 139-142 aryl hydrocarbon receptor Homo sapiens 230-233 21245039-5 2011 Arnt uses the same face of the N-terminal PAS domain for homo- and heterodimerization and mutational analysis of AhR demonstrated that the equivalent region is used by AhR when dimerizing with Arnt. Protactinium 42-45 aryl hydrocarbon receptor Homo sapiens 168-171 18940186-1 2009 The aryl hydrocarbon receptor (AhR) is an orphan receptor in the basic helix-loop-helix PAS family of transcriptional regulators. Protactinium 88-91 aryl hydrocarbon receptor Homo sapiens 31-34 17023418-6 2006 The differential binding of AhR by Arnt and Arnt2 can be ascribed to a single His/Pro amino acid difference in the PASB region of Arnt and Arnt2, suggesting that the PASB/PASB interaction between bHLH-PAS transcription factors plays a selective role for their specific partner molecule. Protactinium 115-118 aryl hydrocarbon receptor Homo sapiens 28-31 11868388-8 2002 Findings on AhR/Arnt and HIF1 systems demonstrating that they are members of the same PAS family seem to support this hypothesis. Protactinium 86-89 aryl hydrocarbon receptor Homo sapiens 12-15 12213382-4 2002 In this review we describe the current state of knowledge with respect to naturally occurring AhR ligands and present and discuss the first theoretical model of the AhR LBD based on crystal structures of homologous PAS family members. Protactinium 215-218 aryl hydrocarbon receptor Homo sapiens 165-168 9395531-9 1997 The implication that an amino acid within the PAS region may be involved in DNA binding indicates that the DNA binding behavior of AHR may be more anomalous than previously suspected. Protactinium 46-49 aryl hydrocarbon receptor Homo sapiens 131-134 10413464-3 1999 Mapping studies indicate that XAP2 requires the PAS, hsp90, and ligand binding domain(s) of the AhR for binding, and that both proteins directly interact in the absence of hsp90. Protactinium 48-51 aryl hydrocarbon receptor Homo sapiens 96-99 9079689-2 1997 We characterized five new "members of the PAS superfamily," or MOPs 1-5, that are similar in size and structural organization to the AHR and ARNT. Protactinium 42-45 aryl hydrocarbon receptor Homo sapiens 133-136 9391097-3 1997 As part of a phylogenetic approach to understanding the function and evolutionary origin of the AHR, we sequenced the PAS homology domain of AHRs from several species of early vertebrates and performed phylogenetic analyses of these AHR amino acid sequences in relation to mammalian AHRs and 24 other members of the PAS family. Protactinium 118-121 aryl hydrocarbon receptor Homo sapiens 96-99 9391097-3 1997 As part of a phylogenetic approach to understanding the function and evolutionary origin of the AHR, we sequenced the PAS homology domain of AHRs from several species of early vertebrates and performed phylogenetic analyses of these AHR amino acid sequences in relation to mammalian AHRs and 24 other members of the PAS family. Protactinium 118-121 aryl hydrocarbon receptor Homo sapiens 141-144 29164305-6 2018 Combining these observations with our structural investigations using a homology model of the AHR-PAS B domain, we suggest a dual role of histidine 291: (1) a major role for shaping the ligand binding site including direct interactions with ligands and, (2) an essential role for the conformational dynamics of a PAS B loop, which most likely influences the association of the AHR with the AHR nuclear translocator through interference with their protein-protein interface. Protactinium 98-101 aryl hydrocarbon receptor Homo sapiens 94-97 7654172-1 1995 The PAS domain of a teleost Ah receptor was amplified using reverse transcription-PCR with degenerate primers containing inosine. Protactinium 4-7 aryl hydrocarbon receptor Homo sapiens 28-39 7539918-2 1995 We show that both HIF-1 subunits are basic-helix-loop-helix proteins containing a PAS domain, defined by its presence in the Drosophila Per and Sim proteins and in the mammalian ARNT and AHR proteins. Protactinium 82-85 aryl hydrocarbon receptor Homo sapiens 187-190 29092071-5 2018 AhR consists of the N-terminal bHLH domain containing NLS and NES, the middle PAS domain and the C-terminal transactivation domain. Protactinium 78-81 aryl hydrocarbon receptor Homo sapiens 0-3 29274782-1 2018 The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor and member of the basic helix-loop-helix-PAS family. Protactinium 120-123 aryl hydrocarbon receptor Homo sapiens 4-29 29274782-1 2018 The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor and member of the basic helix-loop-helix-PAS family. Protactinium 120-123 aryl hydrocarbon receptor Homo sapiens 31-34