PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24030823-3	2013	Recent studies have employed isotope tracers to show that in cancer cells grown in hypoxia or with defective mitochondria, a major fraction of acetyl-CoA is produced via another route, reductive carboxylation of glutamine-derived alpha-ketoglutarate (catalyzed by reverse flux through isocitrate dehydrogenase, IDH).	Acetyl Coenzyme A	143-153	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	285-309	
31676791-4	2019	However, its main role is to consume acetyl-CoA, which unlocks isocitrate dehydrogenase (IDH)-dependent reductive carboxylation, producing the reductive power necessary to quench reactive oxygen species (ROS) originated during the switch from two-dimensional (2D) to three-dimensional (3D) growth (a necessary hallmark of cancer).	Acetyl Coenzyme A	37-47	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	63-87	
31676791-4	2019	However, its main role is to consume acetyl-CoA, which unlocks isocitrate dehydrogenase (IDH)-dependent reductive carboxylation, producing the reductive power necessary to quench reactive oxygen species (ROS) originated during the switch from two-dimensional (2D) to three-dimensional (3D) growth (a necessary hallmark of cancer).	Acetyl Coenzyme A	37-47	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	89-92	
25960387-7	2015	The recent discoveries that IDH1(R132H) interferes with the metabolism of phospholipids in gliomas and that IDH1 activity could participate in the synthesis of acetyl-CoA from glutamine in hypoxic tumors highlight roles for IDH1 in lipid metabolism in a broad spectrum of tissues.	Acetyl Coenzyme A	160-170	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	28-32	
25960387-7	2015	The recent discoveries that IDH1(R132H) interferes with the metabolism of phospholipids in gliomas and that IDH1 activity could participate in the synthesis of acetyl-CoA from glutamine in hypoxic tumors highlight roles for IDH1 in lipid metabolism in a broad spectrum of tissues.	Acetyl Coenzyme A	160-170	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	108-112	
25960387-7	2015	The recent discoveries that IDH1(R132H) interferes with the metabolism of phospholipids in gliomas and that IDH1 activity could participate in the synthesis of acetyl-CoA from glutamine in hypoxic tumors highlight roles for IDH1 in lipid metabolism in a broad spectrum of tissues.	Acetyl Coenzyme A	160-170	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	108-112	
26137220-10	2015	By deleting the cytosolic isoform of IDH (IDH1), the enhanced contribution of glutamine to the lipogenic acetyl-CoA pool during PDHA1 suppression was eliminated, and growth was modestly suppressed.	Acetyl Coenzyme A	105-115	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	37-40	
26137220-10	2015	By deleting the cytosolic isoform of IDH (IDH1), the enhanced contribution of glutamine to the lipogenic acetyl-CoA pool during PDHA1 suppression was eliminated, and growth was modestly suppressed.	Acetyl Coenzyme A	105-115	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	42-46	
26137220-13	2015	We also identify the compensatory mechanisms that are activated under PDH deficiency, namely scavenging of extracellular lipids and lipogenic acetyl-CoA production from reductive glutamine metabolism through IDH1.	Acetyl Coenzyme A	142-152	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	208-212	
24986863-2	2014	By altering IDH1, these mutations target a critical step in reductive glutamine metabolism, the metabolic pathway that converts glutamine ultimately to acetyl-CoA for biosynthetic processes.	Acetyl Coenzyme A	152-162	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	12-16	
24030823-3	2013	Recent studies have employed isotope tracers to show that in cancer cells grown in hypoxia or with defective mitochondria, a major fraction of acetyl-CoA is produced via another route, reductive carboxylation of glutamine-derived alpha-ketoglutarate (catalyzed by reverse flux through isocitrate dehydrogenase, IDH).	Acetyl Coenzyme A	143-153	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	311-314	
34968705-4	2022	The results reveal that isocitrate is blocked from conversion to alpha-ketoglutarate and that acetyl-coenzyme A (CoA) accumulates, which is consistent with a reduction in oxygen consumption rate and inactivation of isocitrate dehydrogenase (IDH) activity.	Acetyl Coenzyme A	94-111	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	215-239	
22442146-7	2012	Cells expressing the mutant IDH are thus deficient in their capacity for reductive carboxylation and may be compromised in their ability to produce acetyl-CoA under hypoxia or when mitochondrial function is otherwise impaired.	Acetyl Coenzyme A	148-158	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	28-31	
34968705-4	2022	The results reveal that isocitrate is blocked from conversion to alpha-ketoglutarate and that acetyl-coenzyme A (CoA) accumulates, which is consistent with a reduction in oxygen consumption rate and inactivation of isocitrate dehydrogenase (IDH) activity.	Acetyl Coenzyme A	94-111	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	241-244	
34968705-4	2022	The results reveal that isocitrate is blocked from conversion to alpha-ketoglutarate and that acetyl-coenzyme A (CoA) accumulates, which is consistent with a reduction in oxygen consumption rate and inactivation of isocitrate dehydrogenase (IDH) activity.	Acetyl Coenzyme A	113-116	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	215-239	
34968705-4	2022	The results reveal that isocitrate is blocked from conversion to alpha-ketoglutarate and that acetyl-coenzyme A (CoA) accumulates, which is consistent with a reduction in oxygen consumption rate and inactivation of isocitrate dehydrogenase (IDH) activity.	Acetyl Coenzyme A	113-116	isocitrate dehydrogenase (NADP(+)) 1	Homo sapiens	241-244