PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9632693-2	1998	In vitro expression of the FAF-mutant (Asp187 --> Asn/Tyr) secretory gelsolin in COS cells leads to generation of an aberrant polypeptide presumably representing the precursor for tissue amyloid.	Asparagine	53-56	gelsolin	Homo sapiens	72-80	
10767822-1	2000	BACKGROUND: Familial amyloidosis of the Finnish type (FAF, Finnish hereditary amyloidosis) is caused by a 654G-A mutation in the gelsolin gene on chromosome 9 resulting in the expression of mutant Asn-187 gelsolin which is abnormally proteolytically processed generating amyloidogenic fragments that polymerize into amyloid fibrils.	Asparagine	197-200	gelsolin	Homo sapiens	129-137	
10767822-1	2000	BACKGROUND: Familial amyloidosis of the Finnish type (FAF, Finnish hereditary amyloidosis) is caused by a 654G-A mutation in the gelsolin gene on chromosome 9 resulting in the expression of mutant Asn-187 gelsolin which is abnormally proteolytically processed generating amyloidogenic fragments that polymerize into amyloid fibrils.	Asparagine	197-200	gelsolin	Homo sapiens	205-213	
10322122-2	1999	The Asp 187-->Asn (D187N) Asp 187-->Tyr (D187Y) gelsolin mutations facilitate two proteolytic cuts in the parent protein generating a 71-residue fragment that forms amyloid fibrils in humans, putatively causing Finnish type familial amyloidosis (FAF).	Asparagine	17-20	gelsolin	Homo sapiens	54-62	
14640038-10	2003	In homozygous FAF(Asn-187) the 65-kDa fragment containing the amyloid forming region and the 55-kDa fragment, devoid of that region, was the major gelsolin species in the plasma.	Asparagine	18-21	gelsolin	Homo sapiens	147-155	
9354764-2	1997	Herein we show that patients with the Asn-187 gelsolin mutation have, in addition to full-sized gelsolin, a series of lower-Mr C-terminal fragments of gelsolin (Mr of 70,000-45,000) in the circulation, and that a 50 to 55-kd fragment of gelsolin is excreted in the urine.	Asparagine	38-41	gelsolin	Homo sapiens	46-54	
9354764-2	1997	Herein we show that patients with the Asn-187 gelsolin mutation have, in addition to full-sized gelsolin, a series of lower-Mr C-terminal fragments of gelsolin (Mr of 70,000-45,000) in the circulation, and that a 50 to 55-kd fragment of gelsolin is excreted in the urine.	Asparagine	38-41	gelsolin	Homo sapiens	96-104	
9354764-2	1997	Herein we show that patients with the Asn-187 gelsolin mutation have, in addition to full-sized gelsolin, a series of lower-Mr C-terminal fragments of gelsolin (Mr of 70,000-45,000) in the circulation, and that a 50 to 55-kd fragment of gelsolin is excreted in the urine.	Asparagine	38-41	gelsolin	Homo sapiens	96-104	
9354764-2	1997	Herein we show that patients with the Asn-187 gelsolin mutation have, in addition to full-sized gelsolin, a series of lower-Mr C-terminal fragments of gelsolin (Mr of 70,000-45,000) in the circulation, and that a 50 to 55-kd fragment of gelsolin is excreted in the urine.	Asparagine	38-41	gelsolin	Homo sapiens	96-104	
9354764-4	1997	In patients heterozygous for the Asn-187 mutation--the usual form of the expression of the dominant disease--normal-sized gelsolin is the major circulating form; the 65- and 55-kd fragments represent minor components.	Asparagine	33-36	gelsolin	Homo sapiens	122-130	
8176895-6	1994	RESULTS: Ultrastructurally, amyloid-like fibrils were formed from the mutant Asn-187 and Tyr-187 gelsolin peptides corresponding to the naturally occurring missense mutations found in familial gelsolin amyloidosis syndromes, as well as from a gelsolin peptide having a Val-187 substitution.	Asparagine	77-80	gelsolin	Homo sapiens	193-201	
8176895-10	1994	CONCLUSIONS: We have defined the amyloidogenic region of gelsolin to a 9-residue sequence in the highly conserved repetitive motif B and showed that residue 187 represents a critical site where a substitution of an amino acid with a charged side chain (Asp) with an amino acid with an uncharged (Asn) or hydrophobic side chain (Tyr, Val) creates a conformation that is highly amyloidogenic thus providing an explanation for the amyloidogenicity of the Asn-187 and Tyr-187 gelsolin variants.	Asparagine	296-299	gelsolin	Homo sapiens	57-65	
8176895-10	1994	CONCLUSIONS: We have defined the amyloidogenic region of gelsolin to a 9-residue sequence in the highly conserved repetitive motif B and showed that residue 187 represents a critical site where a substitution of an amino acid with a charged side chain (Asp) with an amino acid with an uncharged (Asn) or hydrophobic side chain (Tyr, Val) creates a conformation that is highly amyloidogenic thus providing an explanation for the amyloidogenicity of the Asn-187 and Tyr-187 gelsolin variants.	Asparagine	452-455	gelsolin	Homo sapiens	57-65	
1849145-7	1991	When compared with the predicted primary structure of human gelsolin a single amino acid substitution is present in amyloid: at position 15 of the amyloid proteins an asparagine is found instead of an aspartic acid residue at the corresponding position (187) in gelsolin.	Asparagine	167-177	gelsolin	Homo sapiens	60-68	
7881424-2	1994	All the analyzed patients are found to carry a nucleotide substitution of A or T for G654 in their gelsolin gene, which at the protein level results in the conversion of the 187 amino acid residue, aspartic acid, to asparagine or tyrosine, respectively.	Asparagine	216-226	gelsolin	Homo sapiens	99-107	
8383491-2	1993	The mutation leads to the expression of mutant Asn-187 gelsolin and the accumulation of amyloid in tissues.	Asparagine	47-50	gelsolin	Homo sapiens	55-63	
1338910-0	1992	Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187.	Asparagine	48-58	gelsolin	Homo sapiens	0-8	
1338910-7	1992	We conclude that substitution of the uncharged Asn or Tyr for the acidic Asp at residue 187 creates a conformation that may be preferentially amyloidogenic for GSN.	Asparagine	47-50	gelsolin	Homo sapiens	160-163	
2176481-0	1990	Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type.	Asparagine	18-21	gelsolin	Homo sapiens	0-8	
2176481-7	1990	We designate this variant of gelsolin-associated amyloidosis "Agel Asn-187".	Asparagine	67-70	gelsolin	Homo sapiens	29-37