PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9017939-0	1997	Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans.	Isoleucine	32-42	transthyretin	Homo sapiens	17-30	
12039669-3	2002	DNA analysis of the TTR gene revealed a point mutation responsible for substitution of valine for isoleucine at position 107 of the TTR molecule.	Isoleucine	98-108	transthyretin	Homo sapiens	20-23	
12039669-3	2002	DNA analysis of the TTR gene revealed a point mutation responsible for substitution of valine for isoleucine at position 107 of the TTR molecule.	Isoleucine	98-108	transthyretin	Homo sapiens	132-135	
9268242-3	1997	DNA sequencing analysis of the TTR gene from patient 2 showed a G to T transversion at position 3830 in exon 3, resulting in an amino acid replacement of serine-50 (Ser) with isoleucine (Ile).	Isoleucine	175-185	transthyretin	Homo sapiens	31-34	
9268242-3	1997	DNA sequencing analysis of the TTR gene from patient 2 showed a G to T transversion at position 3830 in exon 3, resulting in an amino acid replacement of serine-50 (Ser) with isoleucine (Ile).	Isoleucine	187-190	transthyretin	Homo sapiens	31-34	
8019560-0	1994	A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli patient "SKO" with familial amyloidotic polyneuropathy.	Isoleucine	46-49	transthyretin	Homo sapiens	17-30	
8692810-7	1996	Conformational stability and unfolding behavior of the Ile-20 monomer in urea gradients was found to be almost indistinguishable from that of wild-type TTR.	Isoleucine	55-58	transthyretin	Homo sapiens	152-155	
8089102-0	1994	The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein.	Isoleucine	4-7	transthyretin	Homo sapiens	47-60	
8089102-2	1994	The Ile-84-->Ser mutation and several other point mutations in TTR are associated with familial amyloidotic polyneuropathy, which is characterized by extracellular depositions of amyloid fibrils mainly consisting of mutated TTRs.	Isoleucine	4-7	transthyretin	Homo sapiens	66-69	
8089102-5	1994	This result indicates the participation of a region on the outer surface of TTR that comprises Ile-84 in the recognition of RBP.	Isoleucine	95-98	transthyretin	Homo sapiens	76-79	
33928732-1	2021	AIMS: African-American carriers of the transthyretin (TTR) valine-to-isoleucine substitution (V122I) are at increased risk of heart failure, yet many have relatively subtle abnormalities of left ventricular (LV) function.	Isoleucine	69-79	transthyretin	Homo sapiens	39-52	
34974181-1	2021	BACKGROUND: The valine-to-isoleucine substitution (Val122Ile) is the most common variant of transthyretin (TTR) amyloidosis in the U.S., primarily affecting individuals of African descent.	Isoleucine	26-36	transthyretin	Homo sapiens	92-105	
34974181-1	2021	BACKGROUND: The valine-to-isoleucine substitution (Val122Ile) is the most common variant of transthyretin (TTR) amyloidosis in the U.S., primarily affecting individuals of African descent.	Isoleucine	26-36	transthyretin	Homo sapiens	107-110	
33928732-1	2021	AIMS: African-American carriers of the transthyretin (TTR) valine-to-isoleucine substitution (V122I) are at increased risk of heart failure, yet many have relatively subtle abnormalities of left ventricular (LV) function.	Isoleucine	69-79	transthyretin	Homo sapiens	54-57	
25551524-1	2015	BACKGROUND: Approximately 4% of black Americans carry a valine-to-isoleucine substitution (V122I) in the transthyretin protein, which has been associated with late-onset restrictive amyloid cardiomyopathy and increased risks of death and heart failure.	Isoleucine	66-76	transthyretin	Homo sapiens	105-118	
31020184-1	2018	Background: Approximately 4% of the African-American population possess a valine-to-isoleucine (V122I) substitution within the transthyretin protein that results in a tendency for a normally tetrameric protein to dissociate into misfolded, monomeric subunits.	Isoleucine	84-94	transthyretin	Homo sapiens	127-140