PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12970348-5 2003 The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. Adenosine-5'-(N-ethylcarboxamide) 125-152 heat shock protein 90 beta family member 1 Homo sapiens 103-108 33738064-4 2021 5"-(N-Ethylcarboxamido)adenosine (NECA) was identified from a high-throughput screen as one of the first molecules to exhibit isoform selectivity toward Grp94, with the ethyl group projecting into a unique pocket within the ATP binding site of Grp94. Adenosine-5'-(N-ethylcarboxamide) 34-38 heat shock protein 90 beta family member 1 Homo sapiens 153-158 33738064-4 2021 5"-(N-Ethylcarboxamido)adenosine (NECA) was identified from a high-throughput screen as one of the first molecules to exhibit isoform selectivity toward Grp94, with the ethyl group projecting into a unique pocket within the ATP binding site of Grp94. Adenosine-5'-(N-ethylcarboxamide) 34-38 heat shock protein 90 beta family member 1 Homo sapiens 244-249 31501246-0 2019 NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90. Adenosine-5'-(N-ethylcarboxamide) 0-4 heat shock protein 90 beta family member 1 Homo sapiens 86-91 31501246-9 2019 We found that derivatives that lengthen the 5" moiety of NECA improve selectivity for Grp94 over Hsp90alpha. Adenosine-5'-(N-ethylcarboxamide) 57-61 heat shock protein 90 beta family member 1 Homo sapiens 86-91 20667832-7 2010 Experiments using RNA interference or N-ethylcarboxamidoadenosine, a drug that inhibits ER-localized GRP94 but not cytosolic Hsp90, confirmed that the inhibitory effects of GA resulted specifically from the loss of Hsp90 activity. Adenosine-5'-(N-ethylcarboxamide) 38-65 heat shock protein 90 beta family member 1 Homo sapiens 101-106 10816561-4 2000 In this report, N-ethylcarboxamidoadenosine (NECA) was used to investigate the nucleotide binding properties of GRP94, the endoplasmic reticulum paralog of Hsp90. Adenosine-5'-(N-ethylcarboxamide) 16-43 heat shock protein 90 beta family member 1 Homo sapiens 112-117 10816561-4 2000 In this report, N-ethylcarboxamidoadenosine (NECA) was used to investigate the nucleotide binding properties of GRP94, the endoplasmic reticulum paralog of Hsp90. Adenosine-5'-(N-ethylcarboxamide) 45-49 heat shock protein 90 beta family member 1 Homo sapiens 112-117 10816561-6 2000 NECA binding to GRP94 was efficiently blocked by geldanamycin and radicicol. Adenosine-5'-(N-ethylcarboxamide) 0-4 heat shock protein 90 beta family member 1 Homo sapiens 16-21