PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33093204-0	2020	Amyloid formation of fish beta-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.	Disulfides	84-93	oncomodulin	Homo sapiens	26-42	
33093204-4	2020	We performed biophysical experiments in combination with mathematical modeling of aggregation kinetics and discovered that the aggregation of beta-parvalbumin is initiated by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation and fibril elongation processes.	Disulfides	213-222	oncomodulin	Homo sapiens	142-158	
3179268-0	1988	Disulfide-linked dimer of oncomodulin: comparison to calmodulin.	Disulfides	0-9	oncomodulin	Homo sapiens	26-37	
3179268-4	1988	Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol.	Disulfides	78-87	oncomodulin	Homo sapiens	35-46	
3179268-6	1988	The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin.	Disulfides	4-13	oncomodulin	Homo sapiens	30-41