PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27862954-6	2017	We optimized the XPI workflow using in vitro synthesized and clinical samples of D0/D3-Leu labeled apoA-I.	Leucine	87-90	apolipoprotein A1	Homo sapiens	99-105	
23415437-4	2013	APOA-I gene sequencing revealed a novel heterozygous in-frame insertion mutation with duplication of nucleotides 1535 through 1552 inserted at position 1553, causing a new amino acid glycine at codon 157 and a duplication of amino acids alanine, arginine, alanine, histidine, and leucine at codons 158-162.	Leucine	280-287	apolipoprotein A1	Homo sapiens	0-6	
26797122-2	2016	We previously identified a highly solvent-exposed apoA-I loop domain (Leu(159)-Leu(170)) in nascent HDL, the so-called "solar flare" (SF) region, and proposed that it serves as an LCAT docking site (Wu, Z., Wagner, M. A., Zheng, L., Parks, J. S., Shy, J. M., 3rd, Smith, J. D., Gogonea, V., and Hazen, S. L. (2007) Nat.	Leucine	70-73	apolipoprotein A1	Homo sapiens	50-56	
26797122-2	2016	We previously identified a highly solvent-exposed apoA-I loop domain (Leu(159)-Leu(170)) in nascent HDL, the so-called "solar flare" (SF) region, and proposed that it serves as an LCAT docking site (Wu, Z., Wagner, M. A., Zheng, L., Parks, J. S., Shy, J. M., 3rd, Smith, J. D., Gogonea, V., and Hazen, S. L. (2007) Nat.	Leucine	79-82	apolipoprotein A1	Homo sapiens	50-56	
18719109-9	2008	Discoidal HDL prepared with apoA-I containing a Met-148-->Leu mutation was significantly resistant to inactivation by MPO.	Leucine	61-64	apolipoprotein A1	Homo sapiens	28-34	
18688016-8	2008	ApoAI tryptophan residues were identified as essential in apoAI function and oxidant sensitivity as substitution of all four apoAI tryptophan residues to leucine led to loss of function, but the conservative substitution to phenylalanine retained full function and was resistant to oxidative inactivation.	Leucine	154-161	apolipoprotein A1	Homo sapiens	0-5	
21840419-6	2012	With apoA-I (F225L/F229L/A232L/Y236L) where the hydrophobicity is restored by the presence of only leucine residues in the helix non-polar face, the catalytic efficiencies of vesicle solubilization and cholesterol efflux are similar to those of WT apoA-I; this variant forms smaller HDL particles.	Leucine	99-106	apolipoprotein A1	Homo sapiens	5-11	
15086357-5	2004	Leucine enrichments found in HDL-UC were higher compared with alphaHDL, suggesting that HDL-UC were composed of a mixture of Apo A-I-alphaHDL and Apo A-I-prebeta(1) HDL.	Leucine	0-7	apolipoprotein A1	Homo sapiens	125-130	
15086357-5	2004	Leucine enrichments found in HDL-UC were higher compared with alphaHDL, suggesting that HDL-UC were composed of a mixture of Apo A-I-alphaHDL and Apo A-I-prebeta(1) HDL.	Leucine	0-7	apolipoprotein A1	Homo sapiens	146-151	
2108924-2	1990	The variant, ApoA1 Baltimore, was due to a mutation at codon 34 of the third exon of the APOA1 gene (CGA to CTA) that resulted in an arginine-to-leucine substitution at the tenth amino acid of the mature ApoA1 and a change in charge of -1.	Leucine	145-152	apolipoprotein A1	Homo sapiens	13-18	
12401898-7	2002	The higher leucine enrichment found in total HDL-UC compared to alphaHDL suggested the existence of a mixture of apoA-I-HDL sub-classes.	Leucine	11-18	apolipoprotein A1	Homo sapiens	113-119	
1502149-3	1992	The propositus was heterozygous; the coding region of his apoAI gene contained both the normal sequence and a single-base substitution changing the codon for residue 60 of the mature protein from CTG (leucine) to CGG (arginine).	Leucine	201-208	apolipoprotein A1	Homo sapiens	58-63	
1502149-6	1992	Electrospray mass spectrometry of the purified 10-kDa material revealed components with mass corresponding to the N-terminal 88, 92, 93, and 94 residues of apoAI each with substitution of arginine for leucine.	Leucine	201-208	apolipoprotein A1	Homo sapiens	156-161	
1640859-4	1992	Using highly specific antibodies, we have found that ethanol increases apo A-I secretion and the incorporation of radiolabeled leucine into apo A-I by human hepatocytes (Hep-G2 cells).	Leucine	127-134	apolipoprotein A1	Homo sapiens	140-145	
2123232-6	1990	The absolute production rates for high density lipoprotein apoA-I were 9.7 +/- 0.2 (leucine), 9.4 +/- 1.7 (valine, and 9.1 +/- 1.3 (lysine) mg per kg per day.	Leucine	84-91	apolipoprotein A1	Homo sapiens	59-65	
10487826-0	1999	The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide.	Leucine	35-38	apolipoprotein A1	Homo sapiens	8-26	
10487826-1	1999	We identified a novel missense mutation in the apolipoprotein A-I gene, T2069C Leu(174) --> Ser, in a patient affected by familial systemic nonneuropathic amyloidosis.	Leucine	79-82	apolipoprotein A1	Homo sapiens	47-65	
7861243-4	1995	Furthermore, after two passages of 2,3,2-tetramine treatment, cells were pulsed for 10 min with [3H]leucine and chased up to 2 h. At the end of the pulse, the amount of [3H]leucine incorporated into apolipoprotein A-I was twofold greater (P < 0.05) in treated than in control cells.	Leucine	173-180	apolipoprotein A1	Homo sapiens	199-217	
2108924-2	1990	The variant, ApoA1 Baltimore, was due to a mutation at codon 34 of the third exon of the APOA1 gene (CGA to CTA) that resulted in an arginine-to-leucine substitution at the tenth amino acid of the mature ApoA1 and a change in charge of -1.	Leucine	145-152	apolipoprotein A1	Homo sapiens	89-94	
2108924-2	1990	The variant, ApoA1 Baltimore, was due to a mutation at codon 34 of the third exon of the APOA1 gene (CGA to CTA) that resulted in an arginine-to-leucine substitution at the tenth amino acid of the mature ApoA1 and a change in charge of -1.	Leucine	145-152	apolipoprotein A1	Homo sapiens	204-209	
32676531-1	2020	The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt).	Leucine	122-129	apolipoprotein A1	Homo sapiens	69-87	
32676531-1	2020	The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I) with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the protein with the native sequence (Wt).	Leucine	122-129	apolipoprotein A1	Homo sapiens	89-95	
33779078-8	2021	Four proteins were significantly differentially expressed between non-HF and the specific subtypes of HF (HFrEF and HFpEF); Leucine-rich-alpha-2-glycoprotein (LRG1, P < 0.001), zinc-alpha-2-glycoprotein (P = 0.005), serum paraoxanse/arylesterase (P = 0.013), and APOA1 (P = 0.038).	Leucine	124-131	apolipoprotein A1	Homo sapiens	263-268	
193555-6	1977	Treatment of apoA-I with carboxypeptidase A indicated a carboxyl-terminal sequence of Leu-Ser-Thr-Gln.	Leucine	86-89	apolipoprotein A1	Homo sapiens	13-19