PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 207344-11 1978 However, in the lipoproteins apoA-II, which contains lysine but no arginine, was cleaved more rapidly and extensively by agarose-trypsin than apoA-I. Lysine 53-59 apolipoprotein A1 Homo sapiens 29-35 24308268-5 2013 This study reports the conformation of lipid-free human apoA-I using lysine-to-lysine chemical cross-linking in conjunction with disulfide cross-linking achieved using selective cysteine mutations. Lysine 69-75 apolipoprotein A1 Homo sapiens 56-62 32900591-7 2020 Mass spectrophotometric analysis revealed that lysine residues in APOA1 and APOA2 of HDL modified by GAD and MDA in vitro differed from those modified by glucose, which resembled that seen with HDL from patients with type1 diabetes. Lysine 47-53 apolipoprotein A1 Homo sapiens 66-71 30092227-0 2018 Lysine glycation of apolipoprotein A-I impairs its anti-inflammatory function in type 2 diabetes mellitus. Lysine 0-6 apolipoprotein A1 Homo sapiens 20-38 30092227-7 2018 We identified seven specific lysine (Lys, K) residues of apoA-I (K12, K23, K40, K96, K106, K107 and K238) that were susceptible to be glycated either in vitro or in vivo. Lysine 29-35 apolipoprotein A1 Homo sapiens 57-63 30092227-7 2018 We identified seven specific lysine (Lys, K) residues of apoA-I (K12, K23, K40, K96, K106, K107 and K238) that were susceptible to be glycated either in vitro or in vivo. Lysine 37-40 apolipoprotein A1 Homo sapiens 57-63 29155052-11 2018 Histidines and lysines in helices 5-8 of apoA-I were highly susceptible to oxPL modifications, while lysines in helices 1, 2, 4 and 10 were resistant to modification by oxPL. Lysine 15-22 apolipoprotein A1 Homo sapiens 41-47 29077935-9 2018 Proteomics analysis identified several nonenzymatic early (Amadori) glycations of ApoAI at lysine sites. Lysine 91-97 apolipoprotein A1 Homo sapiens 82-87 30092227-11 2018 We generated mutant apoA-I (K107E, M-apoA-I) with a substitution of glutamic acid (Glu, E) for lysine at the 107th site, and found that compared to wild type apoA-I (WT-apoA-I), M-apoA-I decreased its anti-inflammatory effects in THP-1 cells. Lysine 95-101 apolipoprotein A1 Homo sapiens 20-26 30092227-11 2018 We generated mutant apoA-I (K107E, M-apoA-I) with a substitution of glutamic acid (Glu, E) for lysine at the 107th site, and found that compared to wild type apoA-I (WT-apoA-I), M-apoA-I decreased its anti-inflammatory effects in THP-1 cells. Lysine 95-101 apolipoprotein A1 Homo sapiens 37-43 30092227-11 2018 We generated mutant apoA-I (K107E, M-apoA-I) with a substitution of glutamic acid (Glu, E) for lysine at the 107th site, and found that compared to wild type apoA-I (WT-apoA-I), M-apoA-I decreased its anti-inflammatory effects in THP-1 cells. Lysine 95-101 apolipoprotein A1 Homo sapiens 37-43 30092227-11 2018 We generated mutant apoA-I (K107E, M-apoA-I) with a substitution of glutamic acid (Glu, E) for lysine at the 107th site, and found that compared to wild type apoA-I (WT-apoA-I), M-apoA-I decreased its anti-inflammatory effects in THP-1 cells. Lysine 95-101 apolipoprotein A1 Homo sapiens 37-43 30092227-11 2018 We generated mutant apoA-I (K107E, M-apoA-I) with a substitution of glutamic acid (Glu, E) for lysine at the 107th site, and found that compared to wild type apoA-I (WT-apoA-I), M-apoA-I decreased its anti-inflammatory effects in THP-1 cells. Lysine 95-101 apolipoprotein A1 Homo sapiens 37-43 27487295-2 2016 In this report, fructated apoA-I (fA-I) induced by fructose treatment showed a covalently multimerized band without cross-linking, and lysine residues were irreversibly modified to prevent crosslinking. Lysine 135-141 apolipoprotein A1 Homo sapiens 26-32 25170076-5 2014 First, we generated high purity apoA-I from human plasma, using thiophilic interaction chromatography followed by enzymatic digestion specifically at lysine or arginine residues. Lysine 150-156 apolipoprotein A1 Homo sapiens 32-38 24308268-5 2013 This study reports the conformation of lipid-free human apoA-I using lysine-to-lysine chemical cross-linking in conjunction with disulfide cross-linking achieved using selective cysteine mutations. Lysine 79-85 apolipoprotein A1 Homo sapiens 56-62 23454085-0 2013 Apolipoprotein A-I binding to anionic vesicles and lipopolysaccharides: role for lysine residues in antimicrobial properties. Lysine 81-87 apolipoprotein A1 Homo sapiens 0-18 23454085-5 2013 Lysine side chains of apoA-I were acetylated to evaluate the importance of electrostatic forces in the binding interaction with both membrane components. Lysine 0-6 apolipoprotein A1 Homo sapiens 22-28 23454085-8 2013 These results indicate the potential for apoA-I to function as an antimicrobial protein and exerts this function through lysine residues. Lysine 121-127 apolipoprotein A1 Homo sapiens 41-47 21749932-0 2012 Lysine residues of ABCA1 are required for the interaction with apoA-I. Lysine 0-6 apolipoprotein A1 Homo sapiens 63-69 23741493-3 2013 Glycation of lipid-free apoA-I by methylglyoxal and glycolaldehyde resulted in Arg, Lys and Trp loss, advanced glycation end-product formation and protein cross-linking. Lysine 84-87 apolipoprotein A1 Homo sapiens 24-30 22178192-8 2012 Tandem mass spectrometric analyses revealed that these reactive carbonyls target specific Lys residues in the C-terminus of apoA-I. Lysine 90-93 apolipoprotein A1 Homo sapiens 124-130 21749932-5 2012 The apoA-I binding to ABCA1 and the cross-linking between them were inhibited by the highly charged molecules heparin and poly-L-lysine. Lysine 122-135 apolipoprotein A1 Homo sapiens 4-10 21749932-8 2012 These results suggest that lysine residues in the extracellular domains of ABCA1 contribute to the interaction with apoA-I. Lysine 27-33 apolipoprotein A1 Homo sapiens 116-122 21501700-7 2011 Tandem mass spectrometry and investigations of mutated forms of apoA-I demonstrate that tyrosine residues in apoA-I are chlorinated in a site-specific manner by chloramine intermediates on suitably juxtaposed lysine residues. Lysine 209-215 apolipoprotein A1 Homo sapiens 109-115 20378541-6 2010 Liquid chromatography-electrospray ionization-tandem mass spectrometry of MDA-modified apoA-I revealed that Lys residues at specific sites had been modified. Lysine 108-111 apolipoprotein A1 Homo sapiens 87-93 20378541-8 2010 Lys residues in the C terminus of apoA-I were targeted for cross-linking in high yield, and this process may hinder the interaction of apoA-I with lipids and ABCA1, two key steps in reverse cholesterol transport. Lysine 0-3 apolipoprotein A1 Homo sapiens 34-40 20378541-8 2010 Lys residues in the C terminus of apoA-I were targeted for cross-linking in high yield, and this process may hinder the interaction of apoA-I with lipids and ABCA1, two key steps in reverse cholesterol transport. Lysine 0-3 apolipoprotein A1 Homo sapiens 135-141 20378541-10 2010 Taken together, our observations indicate that MDA damages apoA-I by a pathway that generates lysine adducts at specific sites on the protein. Lysine 94-100 apolipoprotein A1 Homo sapiens 59-65 16497665-5 2006 Using site-directed mutagenesis, we now demonstrate that lysine residues direct tyrosine chlorination in apoA-I. Lysine 57-63 apolipoprotein A1 Homo sapiens 105-111 17216278-4 2007 Glycation of apoA-I was quantified as the reduction in detectable arginine, lysine and tryptophan residues. Lysine 76-82 apolipoprotein A1 Homo sapiens 13-19 17216278-9 2007 RESULTS: Methylglyoxal-mediated modifications of the arginine, lysine and tryptophan residues in lipid-free and lipid-associated apoA-I were time- and concentration-dependent. Lysine 63-69 apolipoprotein A1 Homo sapiens 129-135 16774039-7 2006 Analysis of mutated forms of apoA-I has implicated lysine residues in the regiospecific chlorination of tyrosine. Lysine 51-57 apolipoprotein A1 Homo sapiens 29-35 18688016-3 2008 METHODS AND RESULTS: Mass spectrometry detected the presence of tryptophan, methionine, tyrosine, and lysine oxidation in apoAI recovered from human atheroma. Lysine 102-108 apolipoprotein A1 Homo sapiens 122-127 16495141-3 2006 Acetylation of lysine residues lowered the isoelectric point of apoAI, altered its secondary and tertiary structure, and led to a 40% decrease in cholesterol acceptor activity, while maintaining 93% of its lipid binding activity. Lysine 15-21 apolipoprotein A1 Homo sapiens 64-69 16495141-4 2006 Exhaustive lysine acetoacetylation lowered apoAI"s isoelectric point, profoundly disrupted its secondary and tertiary structure, and led to 90% and 82% reductions in cholesterol acceptor and lipid binding activities, respectively. Lysine 11-17 apolipoprotein A1 Homo sapiens 43-48 16495141-0 2006 Apolipoprotein A-I lysine modification: effects on helical content, lipid binding and cholesterol acceptor activity. Lysine 19-25 apolipoprotein A1 Homo sapiens 0-18 16495141-1 2006 We examined the role of the positively charged lysine residues in apoAI by chemical modification. Lysine 47-53 apolipoprotein A1 Homo sapiens 66-71 16495141-5 2006 The dose-dependent acetoacetylation of an increasing proportion of apoAI lysine residues demonstrated that cholesterol acceptor activity was more sensitive to this modification than lipid binding activity, suggesting that apoAI lysine positive charges play an important role in ABCA1 mediated lipid efflux beyond the role needed to maintain alpha-helical content and lipid binding activity. Lysine 73-79 apolipoprotein A1 Homo sapiens 67-72 16495141-5 2006 The dose-dependent acetoacetylation of an increasing proportion of apoAI lysine residues demonstrated that cholesterol acceptor activity was more sensitive to this modification than lipid binding activity, suggesting that apoAI lysine positive charges play an important role in ABCA1 mediated lipid efflux beyond the role needed to maintain alpha-helical content and lipid binding activity. Lysine 73-79 apolipoprotein A1 Homo sapiens 222-227 16495141-5 2006 The dose-dependent acetoacetylation of an increasing proportion of apoAI lysine residues demonstrated that cholesterol acceptor activity was more sensitive to this modification than lipid binding activity, suggesting that apoAI lysine positive charges play an important role in ABCA1 mediated lipid efflux beyond the role needed to maintain alpha-helical content and lipid binding activity. Lysine 228-234 apolipoprotein A1 Homo sapiens 67-72 16495141-5 2006 The dose-dependent acetoacetylation of an increasing proportion of apoAI lysine residues demonstrated that cholesterol acceptor activity was more sensitive to this modification than lipid binding activity, suggesting that apoAI lysine positive charges play an important role in ABCA1 mediated lipid efflux beyond the role needed to maintain alpha-helical content and lipid binding activity. Lysine 228-234 apolipoprotein A1 Homo sapiens 222-227 14660678-0 2004 Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein. Lysine 0-6 apolipoprotein A1 Homo sapiens 71-89 16126721-4 2005 Tandem mass spectrometric analysis demonstrated that lysine 226, located near the center of helix 10 in apoA-I, was the major site modified by acrolein. Lysine 53-59 apolipoprotein A1 Homo sapiens 104-110 16126721-7 2005 In the crystal structure of truncated apoA-I, Glu-234 lies adjacent to Lys-226, suggesting that negatively charged residues might direct the modification of specific lysine residues in proteins. Lysine 71-74 apolipoprotein A1 Homo sapiens 38-44 16126721-7 2005 In the crystal structure of truncated apoA-I, Glu-234 lies adjacent to Lys-226, suggesting that negatively charged residues might direct the modification of specific lysine residues in proteins. Lysine 166-172 apolipoprotein A1 Homo sapiens 38-44 16037261-5 2005 Tandem mass spectrometric analysis demonstrated that lysine residues were the only amino acids in apoA-I that were modified by acrolein. Lysine 53-59 apolipoprotein A1 Homo sapiens 98-104 15723520-5 2005 The 21 lysine residues within apoA-I were treated with homo bifunctional chemical cross-linkers capable of covalently bridging two lysine residues residing within a defined spacer arm length. Lysine 7-13 apolipoprotein A1 Homo sapiens 30-36 15723520-5 2005 The 21 lysine residues within apoA-I were treated with homo bifunctional chemical cross-linkers capable of covalently bridging two lysine residues residing within a defined spacer arm length. Lysine 131-137 apolipoprotein A1 Homo sapiens 30-36 15723520-8 2005 Using the cross-linker spacer arm length as a constraint for identified Lys pairs, a molecular model was built for the lipid-free apoA-I monomer based on homology with proteins of similar sequence and known three-dimensional structures. Lysine 72-75 apolipoprotein A1 Homo sapiens 130-136 14660678-11 2004 Molecular modeling of the YXXK motif in apolipoprotein A-I demonstrated that these tyrosine and lysine residues are adjacent on the same face of an amphipathic alpha-helix. Lysine 96-102 apolipoprotein A1 Homo sapiens 40-58 11369801-7 2001 Cleavage in the middle of apoA-I occurs at distinct sites in 7.8-nm (Lys(118)) and 12.7-nm (Arg(123)) rHDL, indicating a different conformation in small and large rHDL particles. Lysine 69-72 apolipoprotein A1 Homo sapiens 26-32 12270762-6 2002 RESULTS: There were no sequence abnormalities in LCAT, but we found that he was a heterozygote for a novel APOA1 mutation in codon 107 (AAG->TGG), which predicted the replacement of lysine by tryptophan (K107W). Lysine 185-191 apolipoprotein A1 Homo sapiens 107-112 11689210-1 2001 In the present study apoA-I (Lys 107del), a naturally occurring human apoA-I variant with a deletion of Lys 107, was expressed in E. coli to examine the effect of this mutation on lipid binding, cholesterol efflux and lecithin:cholesterol acyltranferase (LCAT) activation. Lysine 29-32 apolipoprotein A1 Homo sapiens 21-27 11689210-1 2001 In the present study apoA-I (Lys 107del), a naturally occurring human apoA-I variant with a deletion of Lys 107, was expressed in E. coli to examine the effect of this mutation on lipid binding, cholesterol efflux and lecithin:cholesterol acyltranferase (LCAT) activation. Lysine 29-32 apolipoprotein A1 Homo sapiens 70-76 11689210-1 2001 In the present study apoA-I (Lys 107del), a naturally occurring human apoA-I variant with a deletion of Lys 107, was expressed in E. coli to examine the effect of this mutation on lipid binding, cholesterol efflux and lecithin:cholesterol acyltranferase (LCAT) activation. Lysine 104-107 apolipoprotein A1 Homo sapiens 21-27 9464251-5 1998 One case of exceptionally severe atherosclerosis combined with extensive intimal amyloid deposits showed an apoA1 deletion corresponding to Lys 107. Lysine 140-143 apolipoprotein A1 Homo sapiens 108-113 10202375-4 1999 MATERIALS AND METHODS: Apo A-I variants from heterozygous carriers of Lys-107-->0, Lys-107-->Met, Pro-3-->Arg, Pro-4-->Arg, Pro-165-->Arg and Glu-198-->Lys and the corresponding normal apo A-I were purified and then radioiodinated with 131I and 125I. Lysine 86-89 apolipoprotein A1 Homo sapiens 23-30 10202375-4 1999 MATERIALS AND METHODS: Apo A-I variants from heterozygous carriers of Lys-107-->0, Lys-107-->Met, Pro-3-->Arg, Pro-4-->Arg, Pro-165-->Arg and Glu-198-->Lys and the corresponding normal apo A-I were purified and then radioiodinated with 131I and 125I. Lysine 70-73 apolipoprotein A1 Homo sapiens 23-30 10202375-4 1999 MATERIALS AND METHODS: Apo A-I variants from heterozygous carriers of Lys-107-->0, Lys-107-->Met, Pro-3-->Arg, Pro-4-->Arg, Pro-165-->Arg and Glu-198-->Lys and the corresponding normal apo A-I were purified and then radioiodinated with 131I and 125I. Lysine 86-89 apolipoprotein A1 Homo sapiens 23-30 9211897-3 1997 HDL and dimyristoyl phosphatidylcholine binding assays using the variant apoA-I forms have shown that replacement of specific carboxyl-terminal hydrophobic residues Leu222, Phe225, and Phe229 with lysines, as well as replacement of Leu211, Leu214, Leu218, and Leu219 with valines, diminished the ability of apoA-I to bind to HDL and to lyse dimyristoyl phosphatidylcholine liposomes. Lysine 197-204 apolipoprotein A1 Homo sapiens 73-79 7890036-3 1995 In the present study, we labeled the Lys residues of apo AI with 13C by reductive methylation and used 13C NMR to confirm the formation of a native-like structure of apo AI in this environment. Lysine 37-40 apolipoprotein A1 Homo sapiens 53-59 7758222-14 1995 It could, however, be explained by glycation of lysine residues in apolipoprotein A-I, which is the most potent activator of LCAT. Lysine 48-54 apolipoprotein A1 Homo sapiens 67-85 7890036-3 1995 In the present study, we labeled the Lys residues of apo AI with 13C by reductive methylation and used 13C NMR to confirm the formation of a native-like structure of apo AI in this environment. Lysine 37-40 apolipoprotein A1 Homo sapiens 166-172 35304099-0 2022 The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta. Lysine 34-40 apolipoprotein A1 Homo sapiens 15-33 8226847-7 1993 The titration behavior of apoA-I Lys residues is generally similar in the presence and absence of cholesterol, except that 4 Lys residues titrate at a significantly higher pH in the presence of cholesterol. Lysine 33-36 apolipoprotein A1 Homo sapiens 26-32 8226847-7 1993 The titration behavior of apoA-I Lys residues is generally similar in the presence and absence of cholesterol, except that 4 Lys residues titrate at a significantly higher pH in the presence of cholesterol. Lysine 125-128 apolipoprotein A1 Homo sapiens 26-32 1464597-11 1992 The titration behavior of apoA-I Lys residues is the same in small and large spherical particles, indicating that apoA-I conformation is similar on the two particles. Lysine 33-36 apolipoprotein A1 Homo sapiens 26-32 2123232-0 1990 Comparison of deuterated leucine, valine, and lysine in the measurement of human apolipoprotein A-I and B-100 kinetics. Lysine 46-52 apolipoprotein A1 Homo sapiens 81-109 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. Lysine 132-138 apolipoprotein A1 Homo sapiens 59-65 8467951-2 1993 To investigate whether a direct protein-protein interaction between apoA-I and lecithin:cholesterol acyltransferase (LCAT) is necessary for the activation of the enzyme, apoA-I was labelled with N-methylisatoic anhydride at lysine residues. Lysine 224-230 apolipoprotein A1 Homo sapiens 68-74 34904415-5 2021 Mechanistically, our ChIP-seq data showed that ERalpha directly binds to the estrogen response element (ERE) site within the ApoA-I gene and establishes an acetylation of histone 3 lysine 27 (H3K27ac)-enriched chromatin microenvironment. Lysine 181-187 apolipoprotein A1 Homo sapiens 125-131 3723016-5 1986 64: 380-383), represents a mutation in apoA-I in which a single amino acid substitution of lysine for glutamic acid has taken place at residue 136. Lysine 91-97 apolipoprotein A1 Homo sapiens 39-45 2986587-7 1985 Assuming a single receptor model, we found that 2.9 x 10(15) receptors/mg membrane protein bound with an affinity KD = 3.5 x 10(-7) M at 0 to 4 degrees C and KD = 1.9 x 10(-7) M at 37 degrees C. The binding was effectively competed with intact HDL3, with HDL3 that had undergone selective arginine and lysine residue modification, and with antibodies to apolipoproteins A-I and A-II. Lysine 302-308 apolipoprotein A1 Homo sapiens 354-382 35304099-8 2022 Our results suggest that lysine residues within proximity of the known MPO binding sites on HDL are preferentially targeted by the enzymatic (MPO) carbamylation pathway, whereas the non-enzymatic pathway leads to nearly uniform distribution of carbamylated lysine residues along the apoA-I polypeptide chain. Lysine 25-31 apolipoprotein A1 Homo sapiens 283-289 3929832-5 1985 These results, together with kinetic data at variable complex concentrations or at variable temperatures, indicate that specific lysine residues of apolipoprotein A-I are not involved in the lecithin:cholesterol acyltransferase activation process; instead, charge interactions and structural changes are responsible for the observed decrease in activating capacity. Lysine 129-135 apolipoprotein A1 Homo sapiens 148-166 6432779-0 1984 Abnormal lecithin:cholesterol acyltransferase activation by a human apolipoprotein A-I variant in which a single lysine residue is deleted. Lysine 113-119 apolipoprotein A1 Homo sapiens 68-86 6432779-3 1984 The evidence suggests that a single amino acid, lysine 107, has been deleted in the variant apo-A-I of all affected individuals studied from these families, with the remainder of the variant apo-A-I sequence being unaffected. Lysine 48-54 apolipoprotein A1 Homo sapiens 92-99 6432779-3 1984 The evidence suggests that a single amino acid, lysine 107, has been deleted in the variant apo-A-I of all affected individuals studied from these families, with the remainder of the variant apo-A-I sequence being unaffected. Lysine 48-54 apolipoprotein A1 Homo sapiens 92-97