PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1445329-4	1992	One N-glycosylation site exists in sEPO-R but the glycosylation did not affect the binding affinity to EPO.	Nitrogen	4-5	erythropoietin	Mus musculus	36-39	
10340394-4	1999	When maintained in IL-3, about 3% of N-Fms cells formed large hemoglobinized colonies in semisolid cultures supplemented with erythropoietin (EPO).	Nitrogen	37-38	erythropoietin	Mus musculus	126-140	
10340394-4	1999	When maintained in IL-3, about 3% of N-Fms cells formed large hemoglobinized colonies in semisolid cultures supplemented with erythropoietin (EPO).	Nitrogen	37-38	erythropoietin	Mus musculus	142-145	
11877405-11	2002	Collectively, our results demonstrate that: 1) MPO and EPO contribute to tyrosine nitration in vivo; 2) the major reactive nitrogen species formed by leukocyte peroxidase-catalyzed oxidation of NO(2)(-) is the one-electron oxidation product, (*)NO(2); 3) as a minor reaction, peroxidases may also catalyze the two-electron oxidation of NO(2)(-), producing a ONOO(-)-like product.	Nitrogen	123-131	erythropoietin	Mus musculus	55-58	
33928100-7	2021	The results showed that EPO significantly decreased serum creatinine, blood urea nitrogen, and cystatin C levels and alleviated renal histological changes in vivo.	Nitrogen	81-89	erythropoietin	Mus musculus	24-27	
2545067-4	1989	These results suggest that N-linked sugars of the erythropoietin receptor protein are involved in the interaction of erythropoietin with the cell-surface receptors on B8 cells.	Nitrogen	27-28	erythropoietin	Mus musculus	50-64	
2545067-4	1989	These results suggest that N-linked sugars of the erythropoietin receptor protein are involved in the interaction of erythropoietin with the cell-surface receptors on B8 cells.	Nitrogen	27-28	erythropoietin	Mus musculus	117-131	
32579360-4	2020	To overcome this, we recently developed an effectorless TfRMAb-EPO fusion protein, designated TfRMAb-N292G-EPO, by eliminating the Fc N-linked glycosylation site at position 292 of the antibody heavy chain.	Nitrogen	101-102	erythropoietin	Mus musculus	56-66	
32579360-4	2020	To overcome this, we recently developed an effectorless TfRMAb-EPO fusion protein, designated TfRMAb-N292G-EPO, by eliminating the Fc N-linked glycosylation site at position 292 of the antibody heavy chain.	Nitrogen	101-102	erythropoietin	Mus musculus	63-66	
32579360-20	2020	Overall, elimination of Fc N-linked glycosylation, to mitigate TfRMAb effector function side-effects, has a profound effect on the plasma exposure of TfRMAb-N292G-EPO at therapeutic as well as high doses (3-20 mg/kg).	Nitrogen	27-28	erythropoietin	Mus musculus	163-166	
22126194-3	2012	METHODS: Erythropoietin was injected in the peritoneal space of ICR mice after ischemia/reperfusion injury and its effect was assessed by measuring blood urea nitrogen and creatinine, and by histological analysis.	Nitrogen	159-167	erythropoietin	Mus musculus	9-23	
22126194-6	2012	RESULTS: Erythropoietin administration significantly inhibited the increase in blood urea nitrogen and creatinine after ischemia/reperfusion injury compared with control mice.	Nitrogen	90-98	erythropoietin	Mus musculus	9-23	
21847101-6	2011	Also, Epo-MSCs led to significantly better kidney function as shown by lower levels of blood urea nitrogen (72 +- 9.5 mg/dl versus 131 +- 9.20 mg/dl) and creatinine (74 +- 17 micromol/l versus 148+-19.4 micromol/l).	Nitrogen	98-106	erythropoietin	Mus musculus	6-9