PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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