PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
189830-5	1977	Pig apoC-II had a molecular weight of approximately 10 000 as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	114-136	apolipoprotein C2	Homo sapiens	4-11	
11331005-0	2001	NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	62-84	apolipoprotein C2	Homo sapiens	23-42	
15209504-2	2004	The resulting structural information is compared to that available for apoC-II in the presence of sodium dodecyl sulfate, revealing a high level of overall similarity but several significant differences.	Sodium Dodecyl Sulfate	98-120	apolipoprotein C2	Homo sapiens	71-78	
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Sodium Dodecyl Sulfate	99-121	apolipoprotein C2	Homo sapiens	76-82	
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Sodium Dodecyl Sulfate	123-126	apolipoprotein C2	Homo sapiens	76-82	
12590574-6	2003	In addition, global constraints were derived from the fact that apoCII helices are attached to the surface of the SDS micelle and that the hydrophobic moments of each helix faces the interior of the micelle.	Sodium Dodecyl Sulfate	114-117	apolipoprotein C2	Homo sapiens	64-70	
12590574-7	2003	These three categories of global constraints, together with the local classical NMR constraints, were sufficient to define the 3D structure of the apoCII-SDS micelle complex.	Sodium Dodecyl Sulfate	154-157	apolipoprotein C2	Homo sapiens	147-153	
11331005-1	2001	The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein.	Sodium Dodecyl Sulfate	101-104	apolipoprotein C2	Homo sapiens	52-71	
11331005-1	2001	The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein.	Sodium Dodecyl Sulfate	101-104	apolipoprotein C2	Homo sapiens	73-80	
11331005-2	2001	Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism.	Sodium Dodecyl Sulfate	9-12	apolipoprotein C2	Homo sapiens	94-101	
10903476-0	2000	Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.	Sodium Dodecyl Sulfate	98-120	apolipoprotein C2	Homo sapiens	59-78	
10903476-3	2000	A comparison of alpha-proton secondary shifts and CD spectroscopic data indicates that the structure of apoC-II(44-79) is similar in the presence of dodecylphosphocholine and sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	175-197	apolipoprotein C2	Homo sapiens	104-111	
10903476-4	2000	The three-dimensional structure of apoC-II(44-79) in the presence of sodium dodecyl sulfate, determined by relaxation matrix calculations, contains two amphipathic helical domains formed by residues 50-58 and 67-75, separated by a non-helical linker centered at Tyr63.	Sodium Dodecyl Sulfate	69-91	apolipoprotein C2	Homo sapiens	35-42