PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25466060-4	2015	The least degradation of beta-carotene occurred in the emulsion stabilised with the alpha-La-EGCG covalent complex when stored at 25  C. These results implied that protein-polyphenol covalent complexes were able to enhance the physical stability of beta-carotene emulsion and inhibit the degradation of beta-carotene in oil-in-water emulsion, and the effect was influenced by the types of the phenolic compounds.	Oils	320-323	lactalbumin alpha	Homo sapiens	84-92	
29166117-8	2017	Decomposing the different contributions to the protein energy at oil-water interfaces suggests that conformational change for alpha-lactalbumin, unlike lysozyme, is driven by favourable protein-oil interactions.	Oils	65-68	lactalbumin alpha	Homo sapiens	126-143	
29166117-8	2017	Decomposing the different contributions to the protein energy at oil-water interfaces suggests that conformational change for alpha-lactalbumin, unlike lysozyme, is driven by favourable protein-oil interactions.	Oils	194-197	lactalbumin alpha	Homo sapiens	126-143	
27006216-0	2016	Characterization of catechin-alpha-lactalbumin conjugates and the improvement in beta-carotene retention in an oil-in-water nanoemulsion.	Oils	111-114	lactalbumin alpha	Homo sapiens	29-46	
26916155-6	2016	In its anti-tumorigenic function, oligomeric alpha-lactalbumin serves as a founding member of a new family of anticancer drugs termed liprotides (for lipids and partially denatured proteins), where an oligomeric molten globular protein acts as an "oil container" or cargo for the delivery of oleic acid to the cell membranes.	Oils	248-251	lactalbumin alpha	Homo sapiens	45-62	
22201548-3	2012	The far-UV SRCD results showed that adsorption of alpha-La at oil-water interfaces created a new non-native secondary structure that was more stable to thermally induced conformational changes.	Oils	62-65	lactalbumin alpha	Homo sapiens	50-58	
24573329-3	2014	We have studied the effect of surface curvature on the association of two proteins, alpha-lactalbumin (alpha-LA) and beta-lactoglobulin (beta-LG), which perform their function at the oil-water interface in milk emulsions.	Oils	183-186	lactalbumin alpha	Homo sapiens	84-101	
24573329-3	2014	We have studied the effect of surface curvature on the association of two proteins, alpha-lactalbumin (alpha-LA) and beta-lactoglobulin (beta-LG), which perform their function at the oil-water interface in milk emulsions.	Oils	183-186	lactalbumin alpha	Homo sapiens	103-111	
22201548-0	2012	Conformational changes of alpha-lactalbumin adsorbed at oil-water interfaces: interplay between protein structure and emulsion stability.	Oils	56-59	lactalbumin alpha	Homo sapiens	26-43	
22201548-11	2012	This study reports new information on the secondary and tertiary structural changes of alpha-La upon adsorption to oil-water interfaces.	Oils	115-118	lactalbumin alpha	Homo sapiens	87-95	
16256563-3	2003	As a small amount of alpha-lactalbumin is added to the mixture, there is a substantial increase (up to 80%) in the maximum water solubility in the water-in-oil microemulsion phase.	Oils	156-159	lactalbumin alpha	Homo sapiens	21-38	
33555192-0	2021	alpha-Lactalbumin Self-Assembled Nanoparticles with Various Morphologies, Stiffnesses, and Sizes as Pickering Stabilizers for Oil-in-Water Emulsions and Delivery of Curcumin.	Oils	126-129	lactalbumin alpha	Homo sapiens	0-17