PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21224997-11	2011	Subunits of alphaAG98R-crystallin, isolated either by size exclusion chromatography or filtration showed chaperone activity against heat-denatured alcohol dehydrogenase, citrate synthase, bovine betaB2-crystallin, and chemically denatured ovatransferrin.	alphaag98r-crystallin	12-33	aldo-keto reductase family 1 member A1	Bos taurus	147-168
29676852-10	2018	All substitutions decreased the chaperone function of alphaA-crystallin for aggregates of bovine betaL-crystallin and alcohol dehydrogenase.	alphaa-crystallin	54-71	aldo-keto reductase family 1 member A1	Bos taurus	97-139
18700180-7	2008	The chaperonic property of alpha(s)-casein, which enables it to inhibit thermal aggregation of alcohol dehydrogenase, is shown to be partially destroyed by Zn(II)-induced structural alterations, due possibly to loss of flexibility of the natively unfolded casein chains.	Zinc	156-162	aldo-keto reductase family 1 member A1	Bos taurus	95-116
14670742-5	2004	After elution of bovine liver proteins in the homogenate, ADH still retained in the stationary phase was collected from the column by eluting with the PEG 1000-rich upper phase.	Polyethylene Glycols	151-154	aldo-keto reductase family 1 member A1	Bos taurus	58-61
6830260-3	1983	The structural requirements for the interaction of alkaloids with glutamate dehydrogenase and alcohol dehydrogenase are different.	Alkaloids	51-60	aldo-keto reductase family 1 member A1	Bos taurus	94-115
7030476-4	1981	2-Bromoethylene oxide and 2-bromoacetaldehyde, suspected metabolites of VBR, were synthesized and found to be substrates for rat liver epoxide hydrolase and equine liver alcohol dehydrogenase, respectively.	2-bromoethylene oxide	0-21	aldo-keto reductase family 1 member A1	Bos taurus	170-191
7030476-4	1981	2-Bromoethylene oxide and 2-bromoacetaldehyde, suspected metabolites of VBR, were synthesized and found to be substrates for rat liver epoxide hydrolase and equine liver alcohol dehydrogenase, respectively.	bromoacetaldehyde	26-45	aldo-keto reductase family 1 member A1	Bos taurus	170-191
7030476-4	1981	2-Bromoethylene oxide and 2-bromoacetaldehyde, suspected metabolites of VBR, were synthesized and found to be substrates for rat liver epoxide hydrolase and equine liver alcohol dehydrogenase, respectively.	vbr	72-75	aldo-keto reductase family 1 member A1	Bos taurus	170-191