PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27485471-2	2016	In the present study, we evaluated histone H3 acetylation levels of bone marrow CD8+ T cells in SAA patients, and analyzed its correlation with clinical condition parameters.	saa	96-99	CD8a molecule	Homo sapiens	80-83	
27485471-3	2016	We found that the percentages of CD8+ T cell histone H3 acetylation in patients with untreated SAA, recovering SAA (R-SAA) and normal control, were 1.21 +- 0.08, 1.05 +- 0.36, and 1.00 +- 0.41, respectively, with no significant statistical differences.	saa	95-98	CD8a molecule	Homo sapiens	33-36	
27485471-3	2016	We found that the percentages of CD8+ T cell histone H3 acetylation in patients with untreated SAA, recovering SAA (R-SAA) and normal control, were 1.21 +- 0.08, 1.05 +- 0.36, and 1.00 +- 0.41, respectively, with no significant statistical differences.	saa	111-114	CD8a molecule	Homo sapiens	33-36	
27485471-4	2016	However, the amount of CD8+ T cell histone H3 acetylation from untreated SAA was 176.21 +- 32.22 mug/mg protein, which was significantly higher than that of complete response (CR)-SAA (104.29 +- 62.06 mug/mg protein) and normal control (133.94 +- 56.27 mug/mg protein) (P < 0.05) groups.	saa	73-76	CD8a molecule	Homo sapiens	23-26	
27485471-7	2016	Abnormal histone H3 acetylation of CD8+ T cells may thus play a role in the immune pathogenesis of SAA.	saa	99-102	CD8a molecule	Homo sapiens	35-38