PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9632693-3	1998	Here, we provide evidence that this abnormal processing results from defective initial folding of the secreted FAF gelsolin due to the lack of the Cys188-Cys201 disulfide bond, normally formed next to the FAF mutation site.	Disulfides	161-170	gelsolin	Homo sapiens	115-123	
9003812-0	1997	Functional consequences of disulfide bond formation in gelsolin.	Disulfides	27-36	gelsolin	Homo sapiens	55-63	
9003812-1	1997	Gelsolin is an actin monomer binding and filament severing protein synthesized in plasma and cytoplasmic forms differing by an N-terminal amino acid extension and a disulfide bond between Cys-188 and Cys-201.	Disulfides	165-174	gelsolin	Homo sapiens	0-8	
9003812-3	1997	The results indicate that the disulfide bond in domain 2 of gelsolin influences the transmission of information from C-terminal regulatory sites to functional sites in the N-terminus.	Disulfides	30-39	gelsolin	Homo sapiens	60-68	
8703941-0	1996	The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.	Disulfides	61-70	gelsolin	Homo sapiens	42-50	
8703941-5	1996	We have used a combination of cysteine-specific modification with 4-vinylpyridine, HPLC peptide mapping methods, and mass spectrometry to analyze the disulfide structures of human plasma and cytoplasmic gelsolin.	Disulfides	150-159	gelsolin	Homo sapiens	203-211	
8703941-7	1996	Cys residues 188 and 201 in domain 2 of plasma gelsolin were disulfide linked.	Disulfides	61-70	gelsolin	Homo sapiens	47-55