PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32966340-11	2020	Pharmacological AMPK activation by AICAR decreased EtOH-induced reduction of DeltaPsim and ATP in EPC2.	Ethanol	51-55	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	16-20	
34898362-5	2021	Over-expression of miR-378b exacerbated the lipid accumulation induced by EtOH and inhibited CaMKK2 and the AMPK cascade while inhibition of miR-378b ameliorated lipid metabolism dysfunction in vivo and in vitro.	Ethanol	74-78	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	108-112	
31211863-0	2019	Ethanol Exposure Impairs AMPK Signaling and Phagocytosis in Human Alveolar Macrophages: Role of Ethanol Metabolism.	Ethanol	0-7	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	25-29	
32966340-12	2020	Taken together, acute EtOH exposure leads to mitochondrial dysfunction and oxidative stress in esophageal keratinocytes, where the AMPK-mTORC1 axis may serve as a regulatory mechanism to activate autophagy to provide cytoprotection against EtOH-induced cell injury.	Ethanol	22-26	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	131-135	
32966340-12	2020	Taken together, acute EtOH exposure leads to mitochondrial dysfunction and oxidative stress in esophageal keratinocytes, where the AMPK-mTORC1 axis may serve as a regulatory mechanism to activate autophagy to provide cytoprotection against EtOH-induced cell injury.	Ethanol	240-244	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	131-135	
31211863-8	2019	RESULTS: EtOH exposure to AM increased oxidative stress, ER stress, and synthesis of FAEEs, decreased phosphorylated AMPK, and impaired phagocytosis.	Ethanol	9-13	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	117-121	
31211863-9	2019	Attenuation or exacerbation of EtOH-induced oxidative stress by AICAR or Compound C, respectively, suggests a link between AMPK signaling, EtOH metabolism, and related oxidative stress.	Ethanol	31-35	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	123-127	
31211863-9	2019	Attenuation or exacerbation of EtOH-induced oxidative stress by AICAR or Compound C, respectively, suggests a link between AMPK signaling, EtOH metabolism, and related oxidative stress.	Ethanol	139-143	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	123-127	
31211863-12	2019	CONCLUSIONS: EtOH-induced impaired phagocytosis, oxidative stress, ER stress, and dysregulated AMPK signaling are plausibly associated with the formation of FAEEs and may participate in the pathogenesis of nonspecific pulmonary inflammation.	Ethanol	13-17	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	95-99	
17577393-5	2007	Serum adiponectin, liver transcripts of adiponectin receptor-1 (AdipoR1), and phosphorylated adenosine monophosphate kinase-beta (p-AMPKbeta) were each reduced by ethanol feeding and were sustained at normal levels by SAM supplementation of the ethanol diets.	Ethanol	163-170	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	132-140	
18922957-4	2008	In agreement, blocking the activity of AMPK in anoxic fish in vivo with 20 mg/kg Compound C resulted in an elevated metabolic rate (as indicated by increased ethanol production) and tended to reduce energy charge.	Ethanol	158-165	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	39-43