PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20441567-6	2010	Moreover, by regulating the degree of disulfide linkages, we were able to investigate how oligomerization of kappa-casein influences its propensity for fibril formation under conditions of physiological pH and temperature.	Disulfides	38-47	casein kappa	Bos taurus	109-121	
4209784-0	1974	Evidence for the role of disulfide bonds in the masking of chromophore groups in bovine kappa-casein.	Disulfides	25-34	casein kappa	Bos taurus	88-100	
20441567-7	2010	Thus, using fractions containing different proportions of multimeric species, we demonstrate that the propensity of the disulfide-linked multimers to form fibrils is inversely related to their size, with monomeric kappa-casein being the most aggregation prone.	Disulfides	120-129	casein kappa	Bos taurus	214-226	
9535269-0	1998	Environmental effects on disulfide bonding patterns of bovine kappa-casein.	Disulfides	25-34	casein kappa	Bos taurus	62-74	
15675819-2	2004	Disulfide bonding patterns between bovine beta-lactoglobulin and kappa-casein.	Disulfides	0-9	casein kappa	Bos taurus	65-77	
16947075-1	2006	In milk, kappa-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca2+ and inorganic phosphate (Pi) termed the casein (CN) micelle.	Disulfides	36-45	casein kappa	Bos taurus	9-21	
15675819-3	2004	Heat treatment of milk causes the heat-denaturable whey proteins to aggregate with kappa-casein (kappa-CN) via thiol-disulfide bond interchange reactions.	Disulfides	117-126	casein kappa	Bos taurus	83-95	
15675819-3	2004	Heat treatment of milk causes the heat-denaturable whey proteins to aggregate with kappa-casein (kappa-CN) via thiol-disulfide bond interchange reactions.	Disulfides	117-126	casein kappa	Bos taurus	97-105	
15675819-5	2004	The reaction at 60 degrees C between beta-LG A and an activated kappa-CN formed small disulfide-bonded aggregates.	Disulfides	86-95	casein kappa	Bos taurus	64-72	
10609639-1	1999	kappa-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE.	Disulfides	67-76	casein kappa	Bos taurus	0-12	
9535269-1	1998	Bovine kappa-casein, the stabilizing protein of the colloidal milk protein complex, has a unique disulfide bonding pattern.	Disulfides	97-106	casein kappa	Bos taurus	7-19	
8895088-1	1996	kappa-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE.	Disulfides	67-76	casein kappa	Bos taurus	0-12	
1628650-0	1992	The multimeric structure and disulfide-bonding pattern of bovine kappa-casein.	Disulfides	29-38	casein kappa	Bos taurus	65-77	
1628650-1	1992	Bovine kappa-casein was analyzed by SDS/PAGE, MS and amino acid sequence analysis in order to determine its multimeric composition and disulfide-bonding pattern.	Disulfides	135-144	casein kappa	Bos taurus	7-19	
1628650-3	1992	Three types of interchain disulfide linkage, Cys11-Cys11, Cys11-Cys88 and Cys88-Cys88, were all assigned in multimers purified from [14C]carboxymethylated and untreated bulk milk, as well as a milk sample from a kappa-casein-variant-B homozygote Co20.	Disulfides	26-35	casein kappa	Bos taurus	212-224	
1515031-9	1992	Similar gel patterns were observed in whole caseins and partially purified kappa-caseins, indicating that this size distribution is a natural disulfide-linked reporter for the distribution of kappa-casein in casein colloids (micelles).	Disulfides	142-151	casein kappa	Bos taurus	75-87