PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31597378-0	2019	C-terminal Redox Domain of Arabidopsis APR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function.	Carbon	0-1	APS reductase 1	Arabidopsis thaliana	39-43	
31597378-3	2019	Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase.	Carbon	37-38	APS reductase 1	Arabidopsis thaliana	58-61	
31597378-4	2019	The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved alpha/beta thioredoxin fold, but not a glutaredoxin fold.	Carbon	29-30	APS reductase 1	Arabidopsis thaliana	68-72	
31597378-4	2019	The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved alpha/beta thioredoxin fold, but not a glutaredoxin fold.	Carbon	29-30	APS reductase 1	Arabidopsis thaliana	74-80	
12754263-11	2003	These results demonstrate that (i) exogenously supplied glucose can replace the function of photoassimilates in roots; (ii) APR is subject to co-ordinated metabolic control by carbon metabolism; (iii) positive sugar signalling overrides negative signalling from nitrate assimilation in APR regulation.	Carbon	176-182	APS reductase 1	Arabidopsis thaliana	124-127	
12754263-12	2003	Furthermore, signals originating from nitrogen and carbon metabolism regulate APR synergistically.	Carbon	51-57	APS reductase 1	Arabidopsis thaliana	78-81