PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17363723-0 2007 Association between IgM against an aldehyde-modified peptide in apolipoprotein B-100 and progression of carotid disease. Aldehydes 35-43 apolipoprotein B Homo sapiens 64-84 18483467-4 2008 Furthermore, the adduction of aldehydes to apolipoprotein B in low-density lipoproteins (LDL) has been strongly implicated in the mechanism by which LDL is converted to an atherogenic form that is taken up by macrophages, leading to the formation of foam cells. Aldehydes 30-39 apolipoprotein B Homo sapiens 43-59 19393338-0 2009 Lipid aldehyde-mediated cross-linking of apolipoprotein B-100 inhibits secretion from HepG2 cells. Aldehydes 6-14 apolipoprotein B Homo sapiens 41-61 19150065-4 2009 METHODS: In the present study, we screened a panel of 25 carotid plaques associated with clinical symptoms and 26 clinically silent plaques obtained at surgery for presence of the aldehyde-modified apoB-100 peptide defined by the 2D03 antibody and compared the expression of this epitope with other plaque constituents, plasma lipoproteins levels, plasma oxidized LDL and autoantibodies against apoB-100 peptides. Aldehydes 180-188 apolipoprotein B Homo sapiens 198-206 19150065-4 2009 METHODS: In the present study, we screened a panel of 25 carotid plaques associated with clinical symptoms and 26 clinically silent plaques obtained at surgery for presence of the aldehyde-modified apoB-100 peptide defined by the 2D03 antibody and compared the expression of this epitope with other plaque constituents, plasma lipoproteins levels, plasma oxidized LDL and autoantibodies against apoB-100 peptides. Aldehydes 180-188 apolipoprotein B Homo sapiens 395-403 17363723-2 2007 The aim of this study was to evaluate the relationship between the immune response against one defined oxidized low-density lipoprotein antigen, the aldehyde-modified peptide corresponding amino acids 3136 and 3155 (MDA-p210) in apolipoprotein (apo) B-100, and progression of carotid intima media thickness (IMT). Aldehydes 149-157 apolipoprotein B Homo sapiens 229-255 17363723-9 2007 CONCLUSIONS: IgM against the aldehyde-modified peptide corresponding amino acids 3136 and 3155 in apo B-100 is common in subjects with asymptomatic carotid disease, and high levels are associated with a more rapid progression of carotid IMT. Aldehydes 29-37 apolipoprotein B Homo sapiens 98-107 12919321-8 2003 It has been shown that these agents modify Arg, Lys and Trp residues of the apoB protein of LDL, with the extent of modification induced by the two aldehydes being more rapid than with glucose. Aldehydes 148-157 apolipoprotein B Homo sapiens 76-80 17364956-1 2007 OBJECTIVES: The goal of our study was to investigate the associations of oxidized LDL (apoB100 aldehyde-modified form) and acute phase proteins (fibrinogen, CRP) with acute ischemic stroke severity and outcome. Aldehydes 95-103 apolipoprotein B Homo sapiens 87-94 17364956-8 2007 Our data refer to possibility that there may exist some links between the LAA subtype of stroke and elevated oxLDL (apoB100 aldehyde-modified form). Aldehydes 124-132 apolipoprotein B Homo sapiens 116-123 16677655-8 2007 CONCLUSIONS: Treatment with antibodies against aldehyde-modified apoB-100 dramatically reduces atherosclerosis and inhibits restrictive vascular remodelling in mice expressing human apoB-100. Aldehydes 47-55 apolipoprotein B Homo sapiens 182-190 15831809-2 2005 The aim of this study was to investigate if humoral immune response against specific oxidized LDL antigens, such as aldehyde-modified peptide sequences of apolipoprotein B-100, reflects disease activity and structure of atherosclerotic plaques. Aldehydes 116-124 apolipoprotein B Homo sapiens 155-175 15831809-4 2005 Plasma levels of IgG and IgM against aldehyde-modified apolipoprotein B-100 amino acid sequences 661 to 680, 3136 to 3155 (peptide 210), and 3661 to 3680 (peptide 240) were determined by enzyme-linked immunosorbent assay. Aldehydes 37-45 apolipoprotein B Homo sapiens 55-75 14670006-1 2003 Damage to apoB100 on low density lipoprotein (LDL) has usually been described in terms of lipid aldehyde derivatisation or fragmentation. Aldehydes 96-104 apolipoprotein B Homo sapiens 10-17 15451805-0 2004 Recombinant human antibodies against aldehyde-modified apolipoprotein B-100 peptide sequences inhibit atherosclerosis. Aldehydes 37-45 apolipoprotein B Homo sapiens 55-75 15451805-3 2004 Aldehyde-modified peptide sequences in apolipoprotein B-100 (apoB-100) are major targets for these immune responses. Aldehydes 0-8 apolipoprotein B Homo sapiens 39-59 15451805-3 2004 Aldehyde-modified peptide sequences in apolipoprotein B-100 (apoB-100) are major targets for these immune responses. Aldehydes 0-8 apolipoprotein B Homo sapiens 61-69 15529550-3 2004 Lipid oxidation results in the generation of aldehydes that substitute lysine residues in the apolipoprotein B-100 moiety. Aldehydes 45-54 apolipoprotein B Homo sapiens 94-114 12649091-0 2003 Identification of immune responses against aldehyde-modified peptide sequences in apoB associated with cardiovascular disease. Aldehydes 43-51 apolipoprotein B Homo sapiens 82-86 12663661-7 2003 The reduction of the core aldehyde levels was accompanied by (i) the formation of free 7-ketocholesterol and 7-ketocholesteryl ester core aldehydes and (ii) an increase in the amounts of apoB-bound cholesterol and 7-ketocholesterol, suggesting that the cholesteryl ester core aldehydes were further converted to their 7-ketocholesterol- and apoB-bound derivatives. Aldehydes 26-34 apolipoprotein B Homo sapiens 187-191 12663661-7 2003 The reduction of the core aldehyde levels was accompanied by (i) the formation of free 7-ketocholesterol and 7-ketocholesteryl ester core aldehydes and (ii) an increase in the amounts of apoB-bound cholesterol and 7-ketocholesterol, suggesting that the cholesteryl ester core aldehydes were further converted to their 7-ketocholesterol- and apoB-bound derivatives. Aldehydes 26-34 apolipoprotein B Homo sapiens 341-345 12663661-7 2003 The reduction of the core aldehyde levels was accompanied by (i) the formation of free 7-ketocholesterol and 7-ketocholesteryl ester core aldehydes and (ii) an increase in the amounts of apoB-bound cholesterol and 7-ketocholesterol, suggesting that the cholesteryl ester core aldehydes were further converted to their 7-ketocholesterol- and apoB-bound derivatives. Aldehydes 276-285 apolipoprotein B Homo sapiens 187-191 12649091-2 2003 METHODS AND RESULTS: Using a library of polypeptides covering the complete sequence of apoB-100, the only major protein of LDL, we have identified over 100 different human antibodies reacting against aldehyde-modified apoB-100 sequences. Aldehydes 200-208 apolipoprotein B Homo sapiens 87-95 12649091-2 2003 METHODS AND RESULTS: Using a library of polypeptides covering the complete sequence of apoB-100, the only major protein of LDL, we have identified over 100 different human antibodies reacting against aldehyde-modified apoB-100 sequences. Aldehydes 200-208 apolipoprotein B Homo sapiens 218-226 12649091-5 2003 In prospective clinical studies, antibody levels against several aldehyde-modified apoB-100 sites were associated with cardiovascular disease in this age group. Aldehydes 65-73 apolipoprotein B Homo sapiens 83-91 7692957-2 1993 Because oxidation of lipoproteins could be a key event in atherogenesis, an antibody against apolipoprotein B (apoB) from low-density lipoprotein (LDL) modified with the lipid peroxidation-specific aldehyde, 4-hydroxynonenal (4-HNE) (anti-4-HNE-apoB), was raised in rabbits. Aldehydes 198-206 apolipoprotein B Homo sapiens 93-109 12146975-8 2002 The nonproteasomal apoB100 degradative pathway was nonlysosomal and resistant to E64d, DTT, and peptide aldehydes such as MG132 or ALLN but was partially sensitive to the serine protease inhibitor APMSF. Aldehydes 104-113 apolipoprotein B Homo sapiens 19-26 10608719-3 1999 It results in the generation of aldehydes, which substitute lysine residues in the apolipoprotein B-100 moiety and thus in the generation of oxidized LDL. Aldehydes 32-41 apolipoprotein B Homo sapiens 83-103 8697069-2 1995 To explore the relationship between these aldehydes-derived epitopes on apolipoprotein B (apo B) and coronary heart disease (CHD), we used both antibody against 4-hydroxynonenal (HNE)-derived epitopes and antibody against apo B to establish a sandwich enzyme-linked immunoassay (ELISA). Aldehydes 42-51 apolipoprotein B Homo sapiens 72-88 8697069-2 1995 To explore the relationship between these aldehydes-derived epitopes on apolipoprotein B (apo B) and coronary heart disease (CHD), we used both antibody against 4-hydroxynonenal (HNE)-derived epitopes and antibody against apo B to establish a sandwich enzyme-linked immunoassay (ELISA). Aldehydes 42-51 apolipoprotein B Homo sapiens 90-95 15992113-7 1999 Prostaglandin synthesis by endothelial cells under oxidative stress and platelet activation are associated with the release of aldehydes; these induce the oxidative modification of the apolipoprotein B-100 moiety of LDL in the absence of lipid peroxidation, and thus generate MDA-modified LDL. Aldehydes 127-136 apolipoprotein B Homo sapiens 185-205 9890615-3 1999 The antigenic epitopes recognized by these antibodies were generated rather late in the process of copper-mediated LDL oxidation, concomitantly with the formation of fluorescent adducts between reactive aldehydes (including MDA) and apo B100. Aldehydes 203-212 apolipoprotein B Homo sapiens 233-241 9922802-2 1998 Peroxidation of lipids in LDL, either initiated by radicals or catalysed by myeloperoxidase, results in the generation of aldehydes which substitute lysine residues in the apolipoprotein B-100 moiety and thus in the generation of oxidised LDL. Aldehydes 122-131 apolipoprotein B Homo sapiens 172-192 7692957-2 1993 Because oxidation of lipoproteins could be a key event in atherogenesis, an antibody against apolipoprotein B (apoB) from low-density lipoprotein (LDL) modified with the lipid peroxidation-specific aldehyde, 4-hydroxynonenal (4-HNE) (anti-4-HNE-apoB), was raised in rabbits. Aldehydes 198-206 apolipoprotein B Homo sapiens 111-115 7692957-2 1993 Because oxidation of lipoproteins could be a key event in atherogenesis, an antibody against apolipoprotein B (apoB) from low-density lipoprotein (LDL) modified with the lipid peroxidation-specific aldehyde, 4-hydroxynonenal (4-HNE) (anti-4-HNE-apoB), was raised in rabbits. Aldehydes 198-206 apolipoprotein B Homo sapiens 245-249 8299218-2 1993 Oxidation of LDLs, especially derivatization by aldehydes originating from peroxidation of fatty acids and fragmentation of apolipoprotein (apo) B-100 which is their major apolipoprotein, probably occurs extravascularly and the presence of oxidized LDLs in the circulation is not well documented. Aldehydes 48-57 apolipoprotein B Homo sapiens 124-150 25968950-4 2015 These aldehydes generated during the peroxidation of LDL exhibit a facile reactivity with proteins, generating a variety of intra- and intermolecular covalent adducts on the apolipoprotein B-100 particle in LDL. Aldehydes 6-15 apolipoprotein B Homo sapiens 174-194 8221023-3 1993 Aldehyde-modified apoB protein has altered receptor affinity, causing it to be scavenged by macrophages in an uncontrolled manner with the development of foam cells and the initiation of the atherosclerotic lesion. Aldehydes 0-8 apolipoprotein B Homo sapiens 18-22 34532909-6 2022 METHODS: IgM and IgG against native and aldehyde-modified apoB100 peptides 210 (p210) and 45 were analyzed by ELISA in 5169 individuals from the Malmo Diet and Cancer cohort. Aldehydes 40-48 apolipoprotein B Homo sapiens 58-65 26425439-2 2015 Apolipoprotein B100 (ApoB100)-derived peptide fragments generated by proteolytic degradation and aldehyde modification are the major antigens in oxLDL, and so the present work was undertaken to detect circulating IgG for Apo-B100-derived peptide antigens. Aldehydes 97-105 apolipoprotein B Homo sapiens 21-28 1450582-12 1992 It is suggested that binding of aldehydes to free amino groups of Apo B is the reason for macrophage uptake. Aldehydes 32-41 apolipoprotein B Homo sapiens 66-71 9562653-2 1997 The oxidation involves the degradation of polyunsaturated fatty acids, the formation of lysolecithin, oxysterols and aldehyde modification of lysine residues on Apo B100. Aldehydes 117-125 apolipoprotein B Homo sapiens 161-169