PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17936703-4	2007	Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP.	Adenosine Diphosphate	90-93	heat shock protein 90 beta family member 1	Homo sapiens	57-62	
31202885-5	2019	Under ATP turnover conditions, Grp94 populates two distinct closed states, a relatively static ATP/ATP closed state that adopts one conformation, and a dynamic ATP/ADP closed state that can adopt two conformations.	Adenosine Diphosphate	164-167	heat shock protein 90 beta family member 1	Homo sapiens	31-36	
31202885-6	2019	We constructed a Grp94 heterodimer with one arm that is catalytically dead, to extend the lifetime of the ATP/ADP state by preventing hydrolysis of the second ATP.	Adenosine Diphosphate	110-113	heat shock protein 90 beta family member 1	Homo sapiens	17-22	
30787103-0	2019	The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.	Adenosine Diphosphate	97-100	heat shock protein 90 beta family member 1	Homo sapiens	50-55	
30787103-7	2019	Importantly, the direct interaction between BiP and Grp94 is nucleotide-specific, with BiP and Grp94 having higher affinity under ADP conditions and lower affinity under ATP conditions.	Adenosine Diphosphate	130-133	heat shock protein 90 beta family member 1	Homo sapiens	52-57	
30787103-7	2019	Importantly, the direct interaction between BiP and Grp94 is nucleotide-specific, with BiP and Grp94 having higher affinity under ADP conditions and lower affinity under ATP conditions.	Adenosine Diphosphate	130-133	heat shock protein 90 beta family member 1	Homo sapiens	95-100	
30787103-9	2019	When BiP is in the ATP conformation its substrate-binding domain blocks Grp94; in contrast, Grp94 can readily associate with the ADP conformation of BiP, which represents the client-bound state of BiP.	Adenosine Diphosphate	129-132	heat shock protein 90 beta family member 1	Homo sapiens	92-97	
29805488-9	2018	Furthermore, a number of gene-drug interactions, including between HSP90B1 and adenosine-5"-diphosphate and radicicol, were identified.	Adenosine Diphosphate	79-103	heat shock protein 90 beta family member 1	Homo sapiens	67-74	
10816561-9	2000	In [(3)H]NECA displacement assays, GRP94 displayed binding interactions with ATP, dATP, ADP, AMP, cAMP, and adenosine, but not GTP, CTP, or UTP.	Adenosine Diphosphate	88-91	heat shock protein 90 beta family member 1	Homo sapiens	35-40	
15292259-4	2004	We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP.	Adenosine Diphosphate	79-82	heat shock protein 90 beta family member 1	Homo sapiens	52-57	
15951571-7	2005	ADP soaked into crystals of the unliganded protein reveals an intermediate conformation midway between the open and closed states and demonstrates that in GRP94 the conversion between the open and closed states is driven by ligand binding.	Adenosine Diphosphate	0-3	heat shock protein 90 beta family member 1	Homo sapiens	155-160	
15236592-6	2004	We report that apo-GRP94 undergoes a time- and temperature-dependent tertiary conformational change that exposes a site(s) of protein-protein interaction; ATP, ADP, and radicicol markedly suppress this conformational change.	Adenosine Diphosphate	160-163	heat shock protein 90 beta family member 1	Homo sapiens	19-24	
15236592-7	2004	In concert with these findings, ATP and ADP act identically to suppress GRP94 homooligomerization, as well as both local and global conformational activity.	Adenosine Diphosphate	40-43	heat shock protein 90 beta family member 1	Homo sapiens	72-77	
15236592-9	2004	Whereas ATP elicited efficient release of BiP from both wild-type and mutant Ig heavy chain intermediates, GRP94 remained in stable association with Ig heavy chains in the presence of ATP or ADP.	Adenosine Diphosphate	191-194	heat shock protein 90 beta family member 1	Homo sapiens	107-112	
10816561-11	2000	A hypothesis on the regulation of GRP94 conformation and activity by adenosine-based ligand(s) other than ATP and ADP is presented.	Adenosine Diphosphate	114-117	heat shock protein 90 beta family member 1	Homo sapiens	34-39	
10478836-7	1999	In contrast to Hsp90, binding of radicicol to Grp94 requires both the N-terminal ATP/ADP-binding domain as well as the adjacent negatively charged region.	Adenosine Diphosphate	85-88	heat shock protein 90 beta family member 1	Homo sapiens	46-51