PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 96-99 aryl-hydrocarbon receptor Mus musculus 179-182 11784293-3 2002 The three structures reveal a highly conserved structural framework in evolutionary rather distant PAS domains, provide a more general view of how these domains can recognize their ligands and suggest a structure-function relationship that we exploited to build a three-dimensional model of the ligand binding domain (LBD) of the mouse aryl hydrocarbon receptor (mAhR). Protactinium 99-102 aryl-hydrocarbon receptor Mus musculus 336-361 11784293-3 2002 The three structures reveal a highly conserved structural framework in evolutionary rather distant PAS domains, provide a more general view of how these domains can recognize their ligands and suggest a structure-function relationship that we exploited to build a three-dimensional model of the ligand binding domain (LBD) of the mouse aryl hydrocarbon receptor (mAhR). Protactinium 99-102 aryl-hydrocarbon receptor Mus musculus 363-367 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 96-99 aryl-hydrocarbon receptor Mus musculus 87-90 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 96-99 aryl-hydrocarbon receptor Mus musculus 152-177 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 233-236 aryl-hydrocarbon receptor Mus musculus 87-90 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 233-236 aryl-hydrocarbon receptor Mus musculus 152-177 10630574-1 1999 The aryl hydrocarbon nuclear translocator (Arnt) is a basic helix-loop-helix (per/Arnt/Ahr/sim) PAS-containing protein that can heterodimerize with the aryl hydrocarbon receptor (AhR), the hypoxia-inducible factor-1 alpha, and other PAS-containing proteins to form transcriptionally active complexes. Protactinium 233-236 aryl-hydrocarbon receptor Mus musculus 179-182 8828811-10 1996 Thus, the AhR appears to be a unique member of the PAS domain family of proteins that binds a known ligand and stably interacts with hsp90. Protactinium 51-54 aryl-hydrocarbon receptor Mus musculus 10-13 8287061-6 1993 Adjacent to the PAS domain in the AH-receptor, ARNT and Sim proteins is a basic/helix-loop-helix (bHLH) domain that appears to mediate heterodimerization and sequence specific DNA binding properties. Protactinium 16-19 aryl-hydrocarbon receptor Mus musculus 34-45 28102700-2 2017 The aryl hydrocarbon receptor (AhR) shares structural homology to clock genes, containing both PAS domains and basic helix-loop helix structural motifs, allowing for interaction with components of the primary circadian feedback loop. Protactinium 95-98 aryl-hydrocarbon receptor Mus musculus 4-29 28102700-2 2017 The aryl hydrocarbon receptor (AhR) shares structural homology to clock genes, containing both PAS domains and basic helix-loop helix structural motifs, allowing for interaction with components of the primary circadian feedback loop. Protactinium 95-98 aryl-hydrocarbon receptor Mus musculus 31-34