PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11165196-1 2001 The atherogenic lipoprotein Lp(a) consists of an LDL-like core and apo(a), linked to apoB via a thiol bridge. Sulfhydryl Compounds 96-101 apolipoprotein B Homo sapiens 85-89 9026538-2 1996 The mechanism of VLDL assembly was explored by perturbing apoB folding in HepG2 cells with the thiol reducing agent dithiothreitol (DTT). Sulfhydryl Compounds 95-100 apolipoprotein B Homo sapiens 58-62 9169017-0 1997 The mechanism of apolipoprotein B-100 thiol depletion during oxidative modification of low-density lipoprotein. Sulfhydryl Compounds 38-43 apolipoprotein B Homo sapiens 17-37 9169017-3 1997 In this report, we have evaluated the antioxidant potential of apolipoprotein B-100 (apo-B) thiols during LDL oxidation. Sulfhydryl Compounds 92-98 apolipoprotein B Homo sapiens 63-83 9169017-3 1997 In this report, we have evaluated the antioxidant potential of apolipoprotein B-100 (apo-B) thiols during LDL oxidation. Sulfhydryl Compounds 92-98 apolipoprotein B Homo sapiens 85-90 9169017-6 1997 Blocking apo-B thiols with sulfhydryl modifying agents increased the oxidizability of LDL. Sulfhydryl Compounds 15-21 apolipoprotein B Homo sapiens 9-14 9169017-6 1997 Blocking apo-B thiols with sulfhydryl modifying agents increased the oxidizability of LDL. Sulfhydryl Compounds 27-37 apolipoprotein B Homo sapiens 9-14 9169017-7 1997 As with Cu2+, peroxynitrite also caused depletion of apo-B thiols, and again thiol depletion was inhibited by PBN but not by POBN. Sulfhydryl Compounds 59-65 apolipoprotein B Homo sapiens 53-58 9169017-7 1997 As with Cu2+, peroxynitrite also caused depletion of apo-B thiols, and again thiol depletion was inhibited by PBN but not by POBN. Sulfhydryl Compounds 59-64 apolipoprotein B Homo sapiens 53-58 9169017-9 1997 We conclude that apo-B thiol depletion is mediated by lipid peroxidation, prior to the onset of the propagation phase of LDL oxidation. Sulfhydryl Compounds 23-28 apolipoprotein B Homo sapiens 17-22 9169017-10 1997 The implications of apo-B thiols an intrinsic antioxidants of LDL are discussed. Sulfhydryl Compounds 26-32 apolipoprotein B Homo sapiens 20-25 11054653-1 2000 A novel thiol-specific spin labeling procedure for the protein component (apoprotein B, apoB) of low density lipoproteins (LDLs) is presented. Sulfhydryl Compounds 8-13 apolipoprotein B Homo sapiens 88-92 11054653-4 2000 The suitability of thiol-specific labeling for the study of the stability and conformation of apoB was demonstrated in experiments with denaturing agents. Sulfhydryl Compounds 19-24 apolipoprotein B Homo sapiens 94-98 9692913-13 1998 Our results suggest that oxidized thiols on apoB may be essential for the induction of apoptosis by oxidized LDL in human macrophages. Sulfhydryl Compounds 34-40 apolipoprotein B Homo sapiens 44-48 8187250-4 1994 Using high-performance liquid chromatographic techniques, we have identified sulfhydryl and disulfide groups of apoB-100 from LDL. Sulfhydryl Compounds 77-87 apolipoprotein B Homo sapiens 112-120 8301226-5 1993 Thiol- and Cu(2+)-modified LDL underwent lipid peroxidation and exhibited a number of properties of cell-modified LDL, including increased mobility on agarose gel electrophoresis and fragmentation of apolipoprotein B-100. Sulfhydryl Compounds 0-5 apolipoprotein B Homo sapiens 200-220 1366419-1 1990 Intramolecular thiolester bonds in apolipoprotein B (ApoB) were studied using [14C]methylamine (MA) to cleave the thiolester and [3H]- or [14C]iodoacetate (IA) to titrate the newly generated sulfhydryls. Sulfhydryl Compounds 191-202 apolipoprotein B Homo sapiens 35-51 1366419-1 1990 Intramolecular thiolester bonds in apolipoprotein B (ApoB) were studied using [14C]methylamine (MA) to cleave the thiolester and [3H]- or [14C]iodoacetate (IA) to titrate the newly generated sulfhydryls. Sulfhydryl Compounds 191-202 apolipoprotein B Homo sapiens 53-57 3365394-2 1988 The reduced and carboxymethylated apolipoprotein B was incubated with 50 mM [14C]methylamine at pH 8.5 at 30 degrees C. Covalent incorporation of [14C]methylamine was observed with concomitant generation of new sulfhydryl groups, which could be blocked with [3H]- or [14C]iodoacetic acid. Sulfhydryl Compounds 211-221 apolipoprotein B Homo sapiens 34-50 16631150-3 2006 The approach was based on the combination of (1)H NMR (600 MHz) spectroscopy with thiol-specific spin labeling of the protein (apoB). Sulfhydryl Compounds 82-87 apolipoprotein B Homo sapiens 127-131 16631150-4 2006 It is shown that the spectral peaks assigned to the methyl head groups of phosphatidylcholine and sphingomyelin in the (1)H spectra of LDL exhibit line broadening when otherwise free thiol groups of apoB are covalently modified by methanethiosulfonate spin label. Sulfhydryl Compounds 183-188 apolipoprotein B Homo sapiens 199-203 12668175-8 2003 The results indicate that nine thiol groups in apoB are distributed in different domains of LDL: two are more exposed, two are buried deeply in the lipid matrix of the particle and the rest are located in hydrophobic parts of this extremely complex protein-lipid assembly. Sulfhydryl Compounds 31-36 apolipoprotein B Homo sapiens 47-51 2294968-1 1990 Using the fluorescent sulfhydryl probe, 5-iodoacetamidofluoresceine, to label the free sulfhydryl of low-density lipoprotein, the positions of two cysteine residues in apolipoprotein B were located. Sulfhydryl Compounds 22-32 apolipoprotein B Homo sapiens 168-184 20470939-8 2010 It was verified that the thiols groups were inversely correlated with apolipoprotein B and positively correlated with apolipoprotein A-I. Sulfhydryl Compounds 25-31 apolipoprotein B Homo sapiens 70-86 16990421-6 2006 Pearson correlation showed that among all thiols, only total plasma Hcy is related to apoB-Hcy concentrations. Sulfhydryl Compounds 42-48 apolipoprotein B Homo sapiens 86-90 16817161-4 2006 The increased sensitivity was obtained by drying released apoB thiols after reduction treatment, dissolving them directly in a low volume of derivatization buffer and decreasing the dilution factor of derivatized sample before CE injection. Sulfhydryl Compounds 63-69 apolipoprotein B Homo sapiens 58-62 16631159-5 2006 Based on recent observations with several anti-inflammatory and thiol-containing drugs, the present study was designed to test the hypothesis that anti-hypertensive agents from the angiotensin converting enzyme (ACE) inhibitors group inhibit the oxidative modifications of Apo B-100 caused by MPO. Sulfhydryl Compounds 64-69 apolipoprotein B Homo sapiens 273-282