PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16269408-6	2006	To our surprise, the significant increase of the alpha-helical content in endostatin induced by trifluoroethanol can also facilitate fibril formation.	Trifluoroethanol	96-112	collagen type XVIII alpha 1 chain	Homo sapiens	74-84	
14992592-7	2004	Trifluoroethanol (TFE) destabilizes native endostatin, while it makes endostatin even more acid-resistant in the low pH region.	Trifluoroethanol	0-16	collagen type XVIII alpha 1 chain	Homo sapiens	43-53	
14992592-7	2004	Trifluoroethanol (TFE) destabilizes native endostatin, while it makes endostatin even more acid-resistant in the low pH region.	Trifluoroethanol	0-16	collagen type XVIII alpha 1 chain	Homo sapiens	70-80	
14992592-7	2004	Trifluoroethanol (TFE) destabilizes native endostatin, while it makes endostatin even more acid-resistant in the low pH region.	Trifluoroethanol	18-21	collagen type XVIII alpha 1 chain	Homo sapiens	43-53	
14992592-7	2004	Trifluoroethanol (TFE) destabilizes native endostatin, while it makes endostatin even more acid-resistant in the low pH region.	Trifluoroethanol	18-21	collagen type XVIII alpha 1 chain	Homo sapiens	70-80	
14992592-10	2004	Surprisingly, the alpha-helical content of endostatin is increased when it is unfolded at pH 1.6, and the alpha-helical content of the polypeptide chain of unfolded endostatin increases linearly with TFE concentration in the range of 0-30%.	Trifluoroethanol	200-203	collagen type XVIII alpha 1 chain	Homo sapiens	43-53	
14992592-10	2004	Surprisingly, the alpha-helical content of endostatin is increased when it is unfolded at pH 1.6, and the alpha-helical content of the polypeptide chain of unfolded endostatin increases linearly with TFE concentration in the range of 0-30%.	Trifluoroethanol	200-203	collagen type XVIII alpha 1 chain	Homo sapiens	165-175