PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22777780-5	2012	Protein engineering, or the addition of Cu(2+) ions, sodium dodecyl sulphate, trifluoroethanol, heparin, or protein stabilisers, was employed to perturb the conformational dynamics of beta(2)m.	Trifluoroethanol	78-94	beta-2-microglobulin	Homo sapiens	184-192	
20558175-3	2010	This article gives some insights into the structural properties and the conformational states of beta(2)-microglobulin in the presence of TFE, using both the wild-type protein and the mutant Trp60Gly.	Trifluoroethanol	138-141	beta-2-microglobulin	Homo sapiens	97-118	
22566695-0	2012	Polymorphism of beta2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol.	Trifluoroethanol	111-127	beta-2-microglobulin	Homo sapiens	16-35	
22566695-2	2012	Here, we have found that, in combination with an enhancing effect of ultrasonication on nucleation, beta(2)-microglobulin, a protein responsible for dialysis-related amyloidosis, generates distinct fibril conformations in a concentration-dependent manner in the presence of 2,2,2-trifluoroethanol (TFE).	Trifluoroethanol	274-296	beta-2-microglobulin	Homo sapiens	100-121	
22566695-2	2012	Here, we have found that, in combination with an enhancing effect of ultrasonication on nucleation, beta(2)-microglobulin, a protein responsible for dialysis-related amyloidosis, generates distinct fibril conformations in a concentration-dependent manner in the presence of 2,2,2-trifluoroethanol (TFE).	Trifluoroethanol	298-301	beta-2-microglobulin	Homo sapiens	100-121	
21766392-2	2011	This study describes conformational properties of beta2m under two distinct, in vitro amyloidogenic conditions: neutral pH in the presence of 20% 2,2,2-trifluoroethanol (TFE) and acidic pH in the absence of TFE.	Trifluoroethanol	146-168	beta-2-microglobulin	Homo sapiens	50-56	
21766392-2	2011	This study describes conformational properties of beta2m under two distinct, in vitro amyloidogenic conditions: neutral pH in the presence of 20% 2,2,2-trifluoroethanol (TFE) and acidic pH in the absence of TFE.	Trifluoroethanol	170-173	beta-2-microglobulin	Homo sapiens	50-56	
21766392-2	2011	This study describes conformational properties of beta2m under two distinct, in vitro amyloidogenic conditions: neutral pH in the presence of 20% 2,2,2-trifluoroethanol (TFE) and acidic pH in the absence of TFE.	Trifluoroethanol	207-210	beta-2-microglobulin	Homo sapiens	50-56	
14694164-0	2004	Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH.	Trifluoroethanol	31-47	beta-2-microglobulin	Homo sapiens	69-89	
15628856-3	2005	A 22-residue peptide of beta(2)-microglobulin, Ser20-Lys41 (L-K3 peptide), obtained by digestion with Acromobacter protease I, formed amyloid-like fibrils in 50% (v/v) 2,2,2-trifluoroethanol and 10 mM HCl at 25 degrees C, as confirmed by thioflavin T fluorescence, circular dichroism spectra, and atomic force microscopy images.	Trifluoroethanol	174-190	beta-2-microglobulin	Homo sapiens	24-45	
16084781-4	2005	Very recently, low concentrations of 2,2,2-trifluoroethanol (TFE) and the sub-micellar concentration of sodium dodecyl sulfate, a model for anionic phospholipids, have been reported to cause the extension of Abeta(2)M amyloid fibrils at a neutral pH, inducing partial unfolding of beta(2)-m and stabilization of the fibrils.	Trifluoroethanol	37-59	beta-2-microglobulin	Homo sapiens	281-290	
16084781-4	2005	Very recently, low concentrations of 2,2,2-trifluoroethanol (TFE) and the sub-micellar concentration of sodium dodecyl sulfate, a model for anionic phospholipids, have been reported to cause the extension of Abeta(2)M amyloid fibrils at a neutral pH, inducing partial unfolding of beta(2)-m and stabilization of the fibrils.	Trifluoroethanol	61-64	beta-2-microglobulin	Homo sapiens	281-290	
14694164-4	2004	Trifluoroethanol at concentrations of up to 20% (vol/vol) caused fibril extension of heparin-stabilized seeds, inducing a subtle change in the tertiary structure of beta(2)-microglobulin and stabilizing the fibrils at a neutral pH.	Trifluoroethanol	0-16	beta-2-microglobulin	Homo sapiens	165-186	
11418618-4	2001	Upon treatment of wild-type beta(2)-microglobulin with acetonitrile or trifluoroethanol, two conformations were also observed.	Trifluoroethanol	71-87	beta-2-microglobulin	Homo sapiens	28-49