<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Annangudi SP</submitter><funding>NEI NIH HHS</funding><funding>NHLBI NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>1384-95</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2646868</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(7)</volume><pubmed_abstract>( E)-4-Hydroxynon-2-enal (HNE), an electrophilic bifunctional cytotoxic lipid peroxidation product, forms covalent adducts with nucleophilic side chains of amino acid residues. HNE-derived adducts have been implicated in many pathophysiological processes including atherosclerosis, diabetes, and Alzheimer's disease. Tritium- and deuterium-labeled HNE ( d 4-HNE) were used orthogonally to study adduction with proteins and individual nucleophilic groups of histidyl, lysyl, and cysteine residues. Using tritium-labeled HNE, we detected the binding of 486 molecules of HNE per low-density lipoprotein (LDL) particle, significantly more than the total number of all reactive nucleophiles in the LDL particle. This suggests the formation of adducts that incorporate multiple molecules of HNE with some n</pubmed_abstract><journal>Chemical research in toxicology</journal><pubmed_title>Low-density lipoprotein has an enormous capacity to bind (E)-4-hydroxynon-2-enal (HNE): detection and characterization of lysyl and histidyl adducts containing multiple molecules of HNE.</pubmed_title><pmcid>PMC2646868</pmcid><funding_grant_id>R01 EY014239</funding_grant_id><funding_grant_id>R01 GM021249</funding_grant_id><funding_grant_id>EY 014239</funding_grant_id><funding_grant_id>R01 HL053315</funding_grant_id><funding_grant_id>HL53315</funding_grant_id><funding_grant_id>GM 21249</funding_grant_id><pubmed_authors>Zhang W</pubmed_authors><pubmed_authors>Annangudi SP</pubmed_authors><pubmed_authors>Gu X</pubmed_authors><pubmed_authors>Salomon RG</pubmed_authors><pubmed_authors>Crabb JW</pubmed_authors><pubmed_authors>Deng Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Low-density lipoprotein has an enormous capacity to bind (E)-4-hydroxynon-2-enal (HNE): detection and characterization of lysyl and histidyl adducts containing multiple molecules of HNE.</name><description>( E)-4-Hydroxynon-2-enal (HNE), an electrophilic bifunctional cytotoxic lipid peroxidation product, forms covalent adducts with nucleophilic side chains of amino acid residues. HNE-derived adducts have been implicated in many pathophysiological processes including atherosclerosis, diabetes, and Alzheimer's disease. Tritium- and deuterium-labeled HNE ( d 4-HNE) were used orthogonally to study adduction with proteins and individual nucleophilic groups of histidyl, lysyl, and cysteine residues. Using tritium-labeled HNE, we detected the binding of 486 molecules of HNE per low-density lipoprotein (LDL) particle, significantly more than the total number of all reactive nucleophiles in the LDL particle. This suggests the formation of adducts that incorporate multiple molecules of HNE with some n</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Jul</publication><modification>2026-03-16T16:28:57.415Z</modification><creation>2019-03-27T00:20:52Z</creation></dates><accession>S-EPMC2646868</accession><cross_references><pubmed>18570390</pubmed><doi>10.1021/tx8000303</doi></cross_references></HashMap>