PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19248197-6	2009	COX-1 and -2 mRNA levels were significantly increased in the EA group as compared to the control and ASA groups, and NO levels were also significantly increased in the EA group as compared to the ASA group.	Aspirin	101-104	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	0-12	
27161407-16	2016	DHI strengthened the inhibition activity of ASA on both COX-1 and COX-2, which showed that DHI alleviated ASA induced gastric mucosal damage but not antagonized anti-COX effect of ASA.	Aspirin	44-47	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	56-61	
26612417-5	2016	The present study investigated the effect of a common COX1/2 inhibitor (Aspirin) on macrophage phenotype and tissue remodeling in a rodent model of ECM scaffold treated skeletal muscle injury.	Aspirin	72-79	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	54-60	
26612417-13	2016	The COX1/2 inhibitor, Aspirin, was found to mitigate the ECM scaffold-mediated constructive remodeling response both in an in vitro co-culture system and an in vivo rat model of skeletal muscle injury.	Aspirin	22-29	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	4-10	
29439623-9	2018	The increased messenger RNA and protein levels of Cox1 and Cox2 induced by T0070907 were markedly reduced by aspirin treatment.	Aspirin	109-116	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	50-54	
17876871-10	2007	CONCLUSION: These results suggest that the effect of ULDA on platelet activity in portal hypertensive rats, could act through a COX 2 pathway more than the COX 1, predominant for aspirin at higher doses.	Aspirin	179-186	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	156-161	
12852480-5	2003	Hence, the developmental toxicity seen in rats after exposure to aspirin may be due to the irreversible inhibition of COX-1 and/or COX-2.	Aspirin	65-72	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	118-123	
17325651-8	2007	CONCLUSIONS AND IMPLICATIONS: Aspirin"s gastric toxicity in combination with a coxib can be dissociated from its ability to inhibit COX-1 and appears to be dependent, in part, on its ability to attenuate the stomach"s surface hydrophobic barrier.	Aspirin	30-37	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	132-137	
14592556-4	2003	Pretreatment with COX-1 and COX-3 inhibitors (aspirin at a low dose of 1 mg kg(-1), SC 560 and acetaminophen, 0.3-3 mg kg(-1)) slightly augmented thrombolysis by ACE-I, while COX-2 inhibitors (nimesulide and coxibs at doses <1 mg kg(-1) and aspirin at a high dose of 50 mg kg(-1)) or a kinin B2 receptor antagonist (icatibant) abolished it.	Aspirin	46-53	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	18-23	
14592556-4	2003	Pretreatment with COX-1 and COX-3 inhibitors (aspirin at a low dose of 1 mg kg(-1), SC 560 and acetaminophen, 0.3-3 mg kg(-1)) slightly augmented thrombolysis by ACE-I, while COX-2 inhibitors (nimesulide and coxibs at doses <1 mg kg(-1) and aspirin at a high dose of 50 mg kg(-1)) or a kinin B2 receptor antagonist (icatibant) abolished it.	Aspirin	244-251	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	18-23	
12852484-10	2003	Correlation of COX-1 and CA-4 expression with ASA sensitivity suggested that embryonic COX-1 and possibly CA4 are much more likely candidates for mediators of ASA developmental toxicity.	Aspirin	46-49	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	15-20	
12852480-20	2003	Such a finding is consistent with the concept that reversible inhibition of COX-1 and/or COX-2 by other NSAIDs would produce weaker developmental toxicity signals than aspirin.	Aspirin	168-175	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	76-81	
12852484-10	2003	Correlation of COX-1 and CA-4 expression with ASA sensitivity suggested that embryonic COX-1 and possibly CA4 are much more likely candidates for mediators of ASA developmental toxicity.	Aspirin	159-162	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	87-92	
8554334-2	1996	Clofibrate, perfluorooctanoic acid, and acetylsalicylic acid all increased the mRNA levels for the mitochondrial-encoded respiratory-chain components cytochrome c oxidase subunit I and NADH dehydrogenase subunit I. Mitochondrial 16S rRNA was also induced by clofibrate.	Aspirin	40-60	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	150-203	
11665868-11	2001	In vivo and in vitro studies suggest that NO-aspirin (acetylsalicylic acid) exerts more potent antithrombotic action than aspirin, probably by coupling the ability to inhibit COX-1 with the anti-adhesive effect of NO.	Aspirin	45-52	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	175-180	
11665868-11	2001	In vivo and in vitro studies suggest that NO-aspirin (acetylsalicylic acid) exerts more potent antithrombotic action than aspirin, probably by coupling the ability to inhibit COX-1 with the anti-adhesive effect of NO.	Aspirin	54-74	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	175-180	
11665868-11	2001	In vivo and in vitro studies suggest that NO-aspirin (acetylsalicylic acid) exerts more potent antithrombotic action than aspirin, probably by coupling the ability to inhibit COX-1 with the anti-adhesive effect of NO.	Aspirin	122-129	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	175-180	
9726391-0	1998	Activation of genes for spasmolytic peptide, transforming growth factor alpha and for cyclooxygenase (COX)-1 and COX-2 during gastric adaptation to aspirin damage in rats.	Aspirin	148-155	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	86-108	
9726391-13	1998	COX-1 expression was detected in vehicle-control gastric mucosa and after single exposure to ASA or after six consecutive ASA insults, while COX-2 mRNA was not detected in vehicle-control gastric mucosa, but appeared after single ASA insult and was sustained after subsequent ASA doses.	Aspirin	93-96	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	0-5	
9726391-13	1998	COX-1 expression was detected in vehicle-control gastric mucosa and after single exposure to ASA or after six consecutive ASA insults, while COX-2 mRNA was not detected in vehicle-control gastric mucosa, but appeared after single ASA insult and was sustained after subsequent ASA doses.	Aspirin	122-125	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	0-5	
9726391-13	1998	COX-1 expression was detected in vehicle-control gastric mucosa and after single exposure to ASA or after six consecutive ASA insults, while COX-2 mRNA was not detected in vehicle-control gastric mucosa, but appeared after single ASA insult and was sustained after subsequent ASA doses.	Aspirin	122-125	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	0-5	
9726391-13	1998	COX-1 expression was detected in vehicle-control gastric mucosa and after single exposure to ASA or after six consecutive ASA insults, while COX-2 mRNA was not detected in vehicle-control gastric mucosa, but appeared after single ASA insult and was sustained after subsequent ASA doses.	Aspirin	122-125	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	0-5	
9622204-3	1998	Experiments with acetylsalicylic acid showed that 80% of PGE2 production after 1 h of treatment with LPS is accounted for by COX-1; this figure decreases to about 30% after a 24-h treatment.	Aspirin	17-37	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	125-130	
9627095-10	1998	Aspirin, but not NCX-4016, markedly suppressed systemic COX-1 and COX-2 activity, and colonic prostaglandin synthesis.	Aspirin	0-7	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	56-61	
9152412-7	1997	After the macrophages were treated with aspirin to inactivate existing COX-1 and COX-2, however, treatment with 12-0-tetradecanoylphorbol 13-acetate increased PGE2 production.	Aspirin	40-47	cytochrome c oxidase I, mitochondrial	Rattus norvegicus	71-76