PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25563188-6	2015	DMR profiling using catechol as a conformational probe detects the presence of multiple conformations of the beta2AR.	catechol	20-28	adrenoceptor beta 2	Homo sapiens	109-116	
11041870-1	2000	To develop molecules capable of directly probing the catechol binding region of the beta(2)-adrenergic receptor (beta(2)AR), novel benzophenone- and fluorenone-based beta(2)AR antagonists were prepared as potential photoaffinity probes.	catechol	53-61	adrenoceptor beta 2	Homo sapiens	84-111	
11041870-1	2000	To develop molecules capable of directly probing the catechol binding region of the beta(2)-adrenergic receptor (beta(2)AR), novel benzophenone- and fluorenone-based beta(2)AR antagonists were prepared as potential photoaffinity probes.	catechol	53-61	adrenoceptor beta 2	Homo sapiens	113-122	
9440817-9	1998	Our results support the hypothesis that the ligand-binding pocket in the GHS-R is spatially disposed similarly to the well characterized catechol-binding site in the beta2-adrenergic receptor.	catechol	137-145	adrenoceptor beta 2	Homo sapiens	166-191	
8626427-12	1996	Furthermore, since Ser188 and Ser192 are separated by three residues on the TMV alpha-helix, whereas Ser204 and Ser207 of the beta2-AR are separated by only two residues, the orientation of the catechol ring in the alpha1-AR binding pocket appears to be unique and rotated approximately 120 degrees to that in the beta2-AR.	catechol	194-202	adrenoceptor beta 2	Homo sapiens	126-134	
11041870-4	2000	With this potential for directly probing the catechol binding region of the beta(2)AR, we synthesized and tested IAmF in carrier-free radioiodinated form ([(125)I]IAmF).	catechol	45-53	adrenoceptor beta 2	Homo sapiens	76-85	
11041870-7	2000	[(125)I]IAmF represents a new class of beta(2)AR photoaffinity labels that can directly probe the catechol-analogous antagonist pharmacophore binding site in the beta(2)AR ligand binding pocket.	catechol	98-106	adrenoceptor beta 2	Homo sapiens	39-48	
11041870-7	2000	[(125)I]IAmF represents a new class of beta(2)AR photoaffinity labels that can directly probe the catechol-analogous antagonist pharmacophore binding site in the beta(2)AR ligand binding pocket.	catechol	98-106	adrenoceptor beta 2	Homo sapiens	162-171	
16551744-4	2006	The predicted structures for apo-beta2AR and butoxamine-beta2AR are stable in MD, but in epinephrine-beta2AR, extracellular water trickles into the binding pocket to mediate hydrogen bonding between the catechol of epinephrine and Ser-204 on helix 5.	catechol	203-211	adrenoceptor beta 2	Homo sapiens	33-40	
16551744-4	2006	The predicted structures for apo-beta2AR and butoxamine-beta2AR are stable in MD, but in epinephrine-beta2AR, extracellular water trickles into the binding pocket to mediate hydrogen bonding between the catechol of epinephrine and Ser-204 on helix 5.	catechol	203-211	adrenoceptor beta 2	Homo sapiens	56-63	
16551744-4	2006	The predicted structures for apo-beta2AR and butoxamine-beta2AR are stable in MD, but in epinephrine-beta2AR, extracellular water trickles into the binding pocket to mediate hydrogen bonding between the catechol of epinephrine and Ser-204 on helix 5.	catechol	203-211	adrenoceptor beta 2	Homo sapiens	56-63	
15817484-3	2005	In the present study, we use catechol (1,2-benzenediol, a structural component of catecholamine agonists) as a molecular probe to identify mechanistic differences between beta(2)AR activation by catecholamine agonists, such as isoproterenol, and by the structurally related non-catechol partial agonist salbutamol.	catechol	29-37	adrenoceptor beta 2	Homo sapiens	171-180