PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18250299-6	2008	Point mutations in PCSK9 that altered key residues contributing to EGF-A binding (Arg-194 and Phe-379) greatly diminished binding to the LDLR"s extracellular domain.	Arginine	82-85	low density lipoprotein receptor	Homo sapiens	137-141	
28334946-3	2017	The more centrally in the transmembrane domain an arginine was located, the lower amounts of the 120 kDa precursor LDLR in the endoplasmic reticulum were observed.	Arginine	50-58	low density lipoprotein receptor	Homo sapiens	115-119	
28334946-7	2017	Introducing arginines in the transmembrane domain of the LDLR also affected metalloproteinase cleavage of the ectodomain and gamma-secretase cleavage within the transmembrane domain.	Arginine	12-21	low density lipoprotein receptor	Homo sapiens	57-61	
28290784-2	2017	This mutation designated c.1327 T>C (W443R [W422R]) was predicted to cause substitution of arginine for tryptophan residue in the very conservative -propeller domain of the LDL receptor.	Arginine	94-102	low density lipoprotein receptor	Homo sapiens	176-188	
20129366-8	2009	RESULTS: DGGE screening of the LDLR gene identified a tryptophan (W) to arginine (R) substitution at residue 556 (p.W556R) in the fifth conserved YWTD repeat of the LDLR-beta-propeller in FH(Marburg).	Arginine	72-80	low density lipoprotein receptor	Homo sapiens	31-35	
20129366-8	2009	RESULTS: DGGE screening of the LDLR gene identified a tryptophan (W) to arginine (R) substitution at residue 556 (p.W556R) in the fifth conserved YWTD repeat of the LDLR-beta-propeller in FH(Marburg).	Arginine	72-80	low density lipoprotein receptor	Homo sapiens	165-169	
20237569-7	2010	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.	Arginine	174-182	low density lipoprotein receptor	Homo sapiens	62-100	
19828345-7	2010	In addition, a mutant LDLR, which has the three lysines in the intracellular domain substituted with arginines, was also degraded by D374Y-PCSK9.	Arginine	101-110	low density lipoprotein receptor	Homo sapiens	22-26	
9108789-1	1997	A glutamine-for-arginine substitution at amino acid position 3500 of apolipoprotein B (apo B) causes synthesis of LDL with reduced binding affinity to the LDL receptor (LDLR).	Arginine	16-24	low density lipoprotein receptor	Homo sapiens	155-167	
9108789-1	1997	A glutamine-for-arginine substitution at amino acid position 3500 of apolipoprotein B (apo B) causes synthesis of LDL with reduced binding affinity to the LDL receptor (LDLR).	Arginine	16-24	low density lipoprotein receptor	Homo sapiens	169-173	
8290568-8	1994	Biochemical analysis of one FHC mutant (Arg-249-->Gln) demonstrates that the structures formed by the mutant are solubilized at a lower ionic strength than those formed by wild-type MHC.	Arginine	40-43	low density lipoprotein receptor	Homo sapiens	28-31	
17335829-4	2007	Here we describe a single nucleotide substitution in the coding region of exon 9 of LDLR that is an apparently silent polymorphism: CGG (Arg406) to AGG (Arg).	Arginine	137-140	low density lipoprotein receptor	Homo sapiens	84-88	
10884290-2	2000	Conserved lysines and arginines within amino acids 140-150 of apolipoprotein (apo) E are crucial for the interaction between apoE and the low density lipoprotein receptor (LDLR).	Arginine	22-31	low density lipoprotein receptor	Homo sapiens	138-170	
10884290-2	2000	Conserved lysines and arginines within amino acids 140-150 of apolipoprotein (apo) E are crucial for the interaction between apoE and the low density lipoprotein receptor (LDLR).	Arginine	22-31	low density lipoprotein receptor	Homo sapiens	172-176	
10644716-0	2000	Effect of arginine 172 on the binding of apolipoprotein E to the low density lipoprotein receptor.	Arginine	10-18	low density lipoprotein receptor	Homo sapiens	65-97	
10644716-1	2000	The region of apolipoprotein E (apoE) that interacts directly with the low density lipoprotein (LDL) receptor lies in the vicinity of residues 136-150, where lysine and arginine residues are crucial for full binding activity.	Arginine	169-177	low density lipoprotein receptor	Homo sapiens	71-109	
10644716-8	2000	Thus, the association of apoE with phospholipids allows Arg(172) to interact directly with the LDL receptor or with other residues in apoE to promote its receptor-active conformation.	Arginine	56-59	low density lipoprotein receptor	Homo sapiens	95-107	
1466657-2	1992	This creates a substitution of glutamine for arginine in the codon for amino acid 3500 and results in reduced affinity of low density lipoprotein (LDL) to the LDL receptor.	Arginine	45-53	low density lipoprotein receptor	Homo sapiens	159-171	
1619387-8	1992	One missense mutation in the apoB gene (an Arg----Gln substitution at apoB amino acid 3500) is associated with very poor binding of apoB100 to the cellular LDL receptor.	Arginine	43-46	low density lipoprotein receptor	Homo sapiens	156-168	
3241126-8	1988	Human apoB arginine-3,359 corresponds to a critical arginine (position 142) residue in the apoE LDL receptor binding domain.	Arginine	11-19	low density lipoprotein receptor	Homo sapiens	96-108