Oxidative Stress and Covalent Modification of Protein with Bioactive Aldehydes
The term “oxidative stress” links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates...
Saved in:
| Published in | The Journal of biological chemistry Vol. 283; no. 32; pp. 21837 - 21841 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
08.08.2008
American Society for Biochemistry and Molecular Biology |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | The term “oxidative stress” links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as “protein carbonylation.” Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. |
|---|---|
| AbstractList | The term âoxidative stressâ links the production of reactive oxygen species to a variety of metabolic outcomes, including
insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or
aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads
to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject
to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as âprotein carbonylation.â
Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification
leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein
carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of alpha,beta-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of alpha,beta-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of alpha,beta-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. The term “oxidative stress” links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as “protein carbonylation.” Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes. |
| Author | Xie, Hongwei Grimsrud, Paul A. Bernlohr, David A. Griffin, Timothy J. |
| AuthorAffiliation | Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455 |
| AuthorAffiliation_xml | – name: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455 |
| Author_xml | – sequence: 1 givenname: Paul A. surname: Grimsrud fullname: Grimsrud, Paul A. – sequence: 2 givenname: Hongwei surname: Xie fullname: Xie, Hongwei – sequence: 3 givenname: Timothy J. surname: Griffin fullname: Griffin, Timothy J. – sequence: 4 givenname: David A. surname: Bernlohr fullname: Bernlohr, David A. email: Bernl001@umn.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18445586$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFkUtvEzEUhS1URNPAliXMArFL8GtmPBukEvGSCkWUSuyuHPtO5laTcWtPUvrvcZtSHlLFyov7naPjcw7Y3hAGZOyp4HPBa_3qbOnmX2vOuWgk5w_YRHCjZqoU3_fYhHMpZo0szT47SOksU1w34hHbF0brsjTVhH0-_kHejrTF4mSMmFJhB18swtb2OIzFp-CpJZeBMBShLb7EMCINxSWNXfGGgnU30sPeY3flMT1mD1vbJ3xy-07Z6bu33xYfZkfH7z8uDo9mrpRinJm6Vc6ryrcmx_OlbQRWtapVpayRDr0puVPKai61k5U0TtaoK9tWYqn90qgpe73zPd8s1-hdzhptD-eR1jZeQbAEf18G6mAVtiB1oxulssHLW4MYLjaYRlhTctj3dsCwSVA16roj_V9Q17XIpTYZfPZnpLssv7rOgN4BLoaUIrbgaLxpNiekHgSH60khTwq_J82y-T-yO-f7BC92go5W3SVFhCUF1-EapFGgJEhhctVT9nyHtTaAXUVKcHoiuVCc5-8YKTJhdgTmJbeEEZIjHPI82dSN4APdl-En2oHLHg |
| CitedBy_id | crossref_primary_10_1039_C5RA04993H crossref_primary_10_1002_iub_1643 crossref_primary_10_1074_jbc_RA118_003469 crossref_primary_10_1016_j_biortech_2020_123707 crossref_primary_10_3390_nu16132004 crossref_primary_10_3390_antiox8030072 crossref_primary_10_1002_oby_24150 crossref_primary_10_2174_2666939001666230718142652 crossref_primary_10_1016_j_freeradbiomed_2016_10_490 crossref_primary_10_1016_j_sjbs_2016_05_015 crossref_primary_10_1007_s00232_012_9429_3 crossref_primary_10_1007_s40618_015_0283_x crossref_primary_10_1016_j_jaci_2023_08_025 crossref_primary_10_1155_2017_6501046 crossref_primary_10_1089_ars_2009_2743 crossref_primary_10_3390_molecules23051005 crossref_primary_10_1016_j_abb_2010_05_003 crossref_primary_10_18311_jnr_2023_29451 crossref_primary_10_3109_10715762_2013_864761 crossref_primary_10_3390_ani11123599 crossref_primary_10_1016_j_freeradbiomed_2017_04_364 crossref_primary_10_1021_acschembio_6b00269 crossref_primary_10_1021_tx500332y crossref_primary_10_3390_ijms222413181 crossref_primary_10_1016_j_jprot_2017_07_006 crossref_primary_10_1016_j_biochi_2019_03_010 crossref_primary_10_1016_j_cbi_2010_07_004 crossref_primary_10_1039_D1NA00631B crossref_primary_10_1371_journal_pone_0237851 crossref_primary_10_1002_jcla_21560 crossref_primary_10_1016_j_ecoenv_2018_07_125 crossref_primary_10_1038_s41423_022_00858_1 crossref_primary_10_1093_ndt_gfv048 crossref_primary_10_1016_j_envpol_2023_122132 crossref_primary_10_1038_s41598_021_98605_5 crossref_primary_10_3389_fmicb_2014_00576 crossref_primary_10_1002_1873_3468_14995 crossref_primary_10_1016_j_freeradbiomed_2013_05_030 crossref_primary_10_3390_molecules24081454 crossref_primary_10_1093_ajcn_nqx012 crossref_primary_10_1089_ars_2023_0245 crossref_primary_10_1271_bbb_130186 crossref_primary_10_1007_s00216_012_6235_9 crossref_primary_10_1016_j_ejim_2016_02_019 crossref_primary_10_1126_scisignal_290re7 crossref_primary_10_3390_microorganisms10050924 crossref_primary_10_1667_RADE_20_00147_1 crossref_primary_10_1021_bc200415v crossref_primary_10_1016_j_jchromb_2015_02_036 crossref_primary_10_1016_j_jdermsci_2016_09_016 crossref_primary_10_1016_j_jdiacomp_2017_11_007 crossref_primary_10_1002_chem_201601918 crossref_primary_10_1016_j_jchromb_2015_11_052 crossref_primary_10_31797_vetbio_839675 crossref_primary_10_1093_eurheartj_ehv126 crossref_primary_10_1016_j_jchromb_2024_124208 crossref_primary_10_3390_toxics9120345 crossref_primary_10_1007_s12649_024_02766_z crossref_primary_10_1007_s11095_014_1496_y crossref_primary_10_1016_j_chemosphere_2018_02_135 crossref_primary_10_1089_ars_2012_4599 crossref_primary_10_1016_j_jpba_2018_03_068 crossref_primary_10_29328_journal_jccm_1001025 crossref_primary_10_1038_cdd_2017_149 crossref_primary_10_1016_j_jpba_2018_02_012 crossref_primary_10_1016_j_meatsci_2010_04_025 crossref_primary_10_1016_j_tiv_2019_104651 crossref_primary_10_1002_rcm_4863 crossref_primary_10_3389_fcimb_2022_1029111 crossref_primary_10_1016_j_cbpa_2023_111470 crossref_primary_10_1038_s41598_021_86366_0 crossref_primary_10_5851_kosfa_2019_e79 crossref_primary_10_1371_journal_pone_0028777 crossref_primary_10_1111_j_1872_034X_2011_00934_x crossref_primary_10_1002_mnfr_201300412 crossref_primary_10_1016_j_jtemb_2014_12_012 crossref_primary_10_3389_fcimb_2024_1368019 crossref_primary_10_1186_s13068_021_01918_w crossref_primary_10_1021_acssuschemeng_0c01086 crossref_primary_10_1038_srep08221 crossref_primary_10_1089_ars_2023_0314 crossref_primary_10_1021_tx900087z crossref_primary_10_18097_pbmc20115706624 crossref_primary_10_1007_s00726_015_1967_4 crossref_primary_10_1016_j_spinee_2013_04_004 crossref_primary_10_1111_j_1432_2277_2010_01214_x crossref_primary_10_1128_IAI_00738_19 crossref_primary_10_1021_ac902786q crossref_primary_10_1073_pnas_2415039122 crossref_primary_10_1016_j_chnaes_2017_05_002 crossref_primary_10_1080_00071668_2012_740615 crossref_primary_10_1053_j_seminhematol_2013_06_011 crossref_primary_10_1021_tx200169n crossref_primary_10_1155_2010_364823 crossref_primary_10_3390_cancers13246377 crossref_primary_10_1155_2013_156562 crossref_primary_10_3390_antiox13020172 crossref_primary_10_1371_journal_pone_0077786 crossref_primary_10_1016_j_bcp_2016_09_027 crossref_primary_10_1038_srep07589 crossref_primary_10_3390_oxygen2040030 crossref_primary_10_17816_PAVLOVJ2013144_48 crossref_primary_10_1371_journal_pone_0074050 crossref_primary_10_1089_ars_2009_2887 crossref_primary_10_1042_EBC20190058 crossref_primary_10_1248_yakushi_13_00176 crossref_primary_10_3168_jds_2015_10481 crossref_primary_10_3390_antiox13010127 crossref_primary_10_1017_S0007114517002112 crossref_primary_10_3390_antiox7070095 crossref_primary_10_1021_acs_chemrestox_9b00013 crossref_primary_10_3389_fneur_2019_00642 crossref_primary_10_1016_j_jasms_2010_03_029 crossref_primary_10_1002_prot_26571 crossref_primary_10_1002_elps_201600134 crossref_primary_10_1093_toxsci_kfq287 crossref_primary_10_3923_ijbc_2015_92_109 crossref_primary_10_3892_etm_2018_6419 crossref_primary_10_1016_j_freeradbiomed_2018_12_017 crossref_primary_10_1016_j_jpba_2025_116681 crossref_primary_10_1039_c2cc30985h crossref_primary_10_1016_j_bbabio_2016_10_003 crossref_primary_10_1021_acsbiomaterials_5c00125 crossref_primary_10_1111_exd_13822 crossref_primary_10_2119_molmed_2011_00085 crossref_primary_10_1016_j_jff_2020_104233 crossref_primary_10_1007_s12020_012_9849_y crossref_primary_10_1016_j_bbrc_2010_01_080 crossref_primary_10_1371_journal_pone_0035841 crossref_primary_10_2174_1381612825666190705192902 crossref_primary_10_1042_CS20130039 crossref_primary_10_1016_j_freeradbiomed_2009_08_002 crossref_primary_10_3109_15376516_2012_657258 crossref_primary_10_1021_cr300073p crossref_primary_10_1051_ocl_2021038 crossref_primary_10_3897_biorisk_17_77320 crossref_primary_10_1016_j_steroids_2022_109032 crossref_primary_10_3390_cells1030631 crossref_primary_10_1111_jcmm_13581 crossref_primary_10_1007_s11033_020_05328_3 crossref_primary_10_1093_femsyr_fow007 crossref_primary_10_1016_j_bbrc_2009_12_161 crossref_primary_10_1186_s12859_020_3505_y crossref_primary_10_15407_ubj86_04_158 crossref_primary_10_1021_tx5002095 crossref_primary_10_1074_jbc_R118_003214 crossref_primary_10_1016_j_jprot_2011_03_031 crossref_primary_10_1088_1752_7163_ab1fc4 crossref_primary_10_1016_j_exger_2012_04_012 crossref_primary_10_1111_jcmm_12107 crossref_primary_10_1021_acs_biochem_7b01119 crossref_primary_10_1513_AnnalsATS_201503_176AW crossref_primary_10_1007_s00702_010_0470_z crossref_primary_10_1097_MD_0000000000015664 crossref_primary_10_1002_elps_202000208 crossref_primary_10_1016_j_jprot_2013_05_008 crossref_primary_10_1016_j_saa_2021_119640 crossref_primary_10_2337_db11_1091 crossref_primary_10_1021_acs_chemrestox_9b00176 crossref_primary_10_1111_jpn_12516 crossref_primary_10_1080_10715760903137101 crossref_primary_10_3390_biom12081087 crossref_primary_10_2144_000114402 crossref_primary_10_20538_1682_0363_2014_3_84_90 crossref_primary_10_1186_1752_0509_5_51 crossref_primary_10_3390_biom11101401 crossref_primary_10_1016_j_arr_2013_12_005 crossref_primary_10_1080_07391102_2015_1086958 crossref_primary_10_1016_j_meatsci_2017_09_002 crossref_primary_10_1007_s11064_016_2140_5 crossref_primary_10_7554_eLife_14601 crossref_primary_10_1016_j_fob_2015_04_004 crossref_primary_10_1038_s41467_019_11169_x crossref_primary_10_1039_C9RA08532G crossref_primary_10_1016_j_taap_2017_08_009 crossref_primary_10_1093_ijfood_vvae020 crossref_primary_10_1007_s10930_011_9307_3 crossref_primary_10_1111_jsr_12271 crossref_primary_10_1373_clinchem_2010_145201 crossref_primary_10_3109_19396368_2016_1148798 crossref_primary_10_1016_j_jprot_2013_05_040 crossref_primary_10_3390_foods10061322 crossref_primary_10_4103_pm_pm_169_19 crossref_primary_10_1016_j_pharmthera_2015_08_005 crossref_primary_10_1016_j_isci_2022_103739 crossref_primary_10_1016_j_phymed_2012_06_011 crossref_primary_10_1097_MJT_0000000000000290 crossref_primary_10_1016_j_jpba_2021_114359 crossref_primary_10_3390_life12030403 crossref_primary_10_3390_foods11111634 crossref_primary_10_1007_s11356_023_30439_2 crossref_primary_10_1016_j_jbc_2022_101582 crossref_primary_10_1016_j_etap_2012_12_014 crossref_primary_10_1021_acs_chemrev_6b00084 crossref_primary_10_1007_s00403_017_1729_0 crossref_primary_10_1016_j_bbalip_2015_12_009 crossref_primary_10_1016_j_tox_2019_02_005 crossref_primary_10_1155_2014_527518 crossref_primary_10_1016_j_saa_2022_121098 crossref_primary_10_1371_journal_pone_0164739 crossref_primary_10_1016_j_jprot_2013_04_002 crossref_primary_10_1007_s11356_019_06370_w crossref_primary_10_1371_journal_pone_0013545 crossref_primary_10_1080_10715762_2019_1629586 crossref_primary_10_1016_j_phytochem_2009_05_018 crossref_primary_10_24326_asphc_2021_1_10 crossref_primary_10_3390_biom5042987 crossref_primary_10_1016_j_marenvres_2019_06_002 crossref_primary_10_1016_j_fbio_2021_101030 crossref_primary_10_1177_09612033221115628 crossref_primary_10_1007_s00216_013_7022_y crossref_primary_10_1007_s13311_020_00954_y crossref_primary_10_1128_AEM_03319_14 crossref_primary_10_1183_13993003_00009_2022 crossref_primary_10_1007_s11010_019_03558_z crossref_primary_10_1074_jbc_M110_202937 crossref_primary_10_1007_s00706_011_0472_z crossref_primary_10_1016_j_cbi_2010_03_003 crossref_primary_10_3389_fpubh_2021_730369 crossref_primary_10_1152_ajprenal_00188_2015 crossref_primary_10_1161_ATVBAHA_110_221747 crossref_primary_10_1016_j_cbi_2018_11_024 crossref_primary_10_1007_s00296_011_1977_9 crossref_primary_10_1016_j_bbagrm_2015_09_003 crossref_primary_10_1165_rcmb_2016_0342OC crossref_primary_10_1155_2018_9620684 crossref_primary_10_1021_acs_est_7b01987 crossref_primary_10_1080_00071668_2012_736609 crossref_primary_10_1074_jbc_M112_400663 crossref_primary_10_1051_medsci_20173302013 crossref_primary_10_1016_j_bbr_2016_07_054 crossref_primary_10_25040_aml2018_03_037 crossref_primary_10_1002_mas_21375 crossref_primary_10_1016_j_tetlet_2012_02_046 crossref_primary_10_3390_cells10092301 crossref_primary_10_4137_NMI_S29531 crossref_primary_10_1016_j_jprot_2011_07_009 crossref_primary_10_1016_j_cbpa_2024_102425 crossref_primary_10_1038_aps_2011_143 crossref_primary_10_1007_s00232_016_9870_9 crossref_primary_10_1089_ars_2010_3474 crossref_primary_10_3390_proteomes4020018 crossref_primary_10_1021_jf202268q crossref_primary_10_1016_j_freeradbiomed_2017_01_023 crossref_primary_10_1016_j_ymben_2018_05_018 crossref_primary_10_1016_j_freeradbiomed_2013_08_174 crossref_primary_10_1016_j_tim_2021_12_011 crossref_primary_10_1016_j_yexmp_2012_01_004 crossref_primary_10_1007_s11011_018_0234_2 crossref_primary_10_1007_s10741_013_9384_9 crossref_primary_10_1016_j_jdermsci_2015_11_005 crossref_primary_10_1186_s13065_018_0402_9 crossref_primary_10_1088_0022_3727_49_8_084004 crossref_primary_10_1093_toxsci_kfw192 crossref_primary_10_1002_art_27442 crossref_primary_10_1371_journal_pone_0091129 crossref_primary_10_1021_jf301770p crossref_primary_10_1093_toxsci_kfab071 crossref_primary_10_1289_ehp_1205432 crossref_primary_10_1021_acsnano_8b02037 crossref_primary_10_1016_j_crtox_2024_100153 crossref_primary_10_1089_ars_2020_8238 crossref_primary_10_1586_14789450_2016_1149470 crossref_primary_10_1016_j_cmet_2012_01_004 crossref_primary_10_1016_j_freeradbiomed_2018_11_036 crossref_primary_10_1080_07391102_2022_2098820 crossref_primary_10_1016_j_cbi_2015_06_029 crossref_primary_10_1016_j_freeradbiomed_2019_05_029 crossref_primary_10_1021_mp300075u crossref_primary_10_1016_j_jsbmb_2023_106345 crossref_primary_10_1016_j_freeradbiomed_2011_10_441 crossref_primary_10_1016_j_micpath_2017_08_015 crossref_primary_10_1017_S1461145711001416 crossref_primary_10_1039_D2RA00009A crossref_primary_10_3390_antiox10091461 crossref_primary_10_3389_fcvm_2019_00068 crossref_primary_10_1016_j_prostaglandins_2020_106500 crossref_primary_10_1139_cjpp_2021_0531 crossref_primary_10_1002_rcm_7577 crossref_primary_10_1134_S1990750812020151 crossref_primary_10_3390_foods10010040 crossref_primary_10_1016_j_pbiomolbio_2024_07_001 crossref_primary_10_4168_aair_2020_12_3_523 crossref_primary_10_1016_j_taap_2015_10_006 crossref_primary_10_1016_j_taap_2025_117293 crossref_primary_10_1016_j_biochi_2018_03_009 crossref_primary_10_1021_pr100555v crossref_primary_10_1039_D2QM00960A crossref_primary_10_1155_2020_1356893 crossref_primary_10_1007_s00253_020_10742_5 crossref_primary_10_1016_j_jsbmb_2016_02_024 crossref_primary_10_1038_s41522_018_0072_3 crossref_primary_10_1007_s11696_023_03197_1 crossref_primary_10_1111_jfs_12746 crossref_primary_10_1016_j_cellsig_2011_07_015 crossref_primary_10_1016_j_freeradbiomed_2011_05_039 crossref_primary_10_1002_cbic_201402193 crossref_primary_10_3166_phyto_2018_0070 crossref_primary_10_1002_mnfr_202400630 crossref_primary_10_1002_rcm_6587 crossref_primary_10_1111_j_1530_0277_2011_01607_x crossref_primary_10_2174_1381612825666190319114641 crossref_primary_10_1016_j_ijrobp_2015_05_009 crossref_primary_10_1016_j_freeradbiomed_2014_01_017 crossref_primary_10_1016_j_jprot_2013_02_004 crossref_primary_10_1371_journal_pone_0125209 crossref_primary_10_1080_07391102_2023_2208234 crossref_primary_10_1016_j_foodchem_2020_126789 crossref_primary_10_1111_febs_12224 crossref_primary_10_1016_j_jtemb_2023_127272 crossref_primary_10_1097_01_EWX_0000482792_76474_f3 crossref_primary_10_3389_fphys_2019_01638 crossref_primary_10_1002_pmic_201500301 crossref_primary_10_1016_j_freeradbiomed_2016_12_011 crossref_primary_10_1021_tx900147g crossref_primary_10_1016_j_jprot_2013_02_015 crossref_primary_10_1016_j_cbi_2018_01_012 crossref_primary_10_1016_j_jprot_2016_12_019 crossref_primary_10_31857_S0026898423060101 crossref_primary_10_1002_pro_495 crossref_primary_10_1016_j_neuroscience_2012_03_058 crossref_primary_10_1093_pcp_pcu072 crossref_primary_10_1002_jcla_22118 crossref_primary_10_1016_j_bcab_2017_10_003 crossref_primary_10_1128_mSystems_00163_19 crossref_primary_10_1016_j_freeradbiomed_2010_12_005 crossref_primary_10_1177_0192623312467399 crossref_primary_10_1021_bi3006169 crossref_primary_10_1074_mcp_M111_007658 crossref_primary_10_1007_s11356_020_12152_6 crossref_primary_10_1007_s12603_014_0518_0 crossref_primary_10_1074_mcp_M900321_MCP200 crossref_primary_10_1093_plphys_kiaa033 crossref_primary_10_3390_antiox4010134 crossref_primary_10_1021_tx100228q crossref_primary_10_1021_jf1010897 crossref_primary_10_1021_acs_jafc_5b03126 crossref_primary_10_1111_jvim_15732 crossref_primary_10_1007_s00216_017_0567_4 crossref_primary_10_3390_antiox5010007 crossref_primary_10_1074_jbc_REV119_006217 crossref_primary_10_1155_2012_329635 crossref_primary_10_1016_j_freeradbiomed_2017_09_015 crossref_primary_10_1080_10253890_2016_1174848 crossref_primary_10_2337_db09_1105 crossref_primary_10_1002_prca_201300068 crossref_primary_10_3390_ijms23031534 crossref_primary_10_3389_fphar_2023_1275388 crossref_primary_10_1016_j_plaphy_2012_03_010 crossref_primary_10_3109_10715762_2013_789136 crossref_primary_10_1016_j_freeradbiomed_2013_09_005 crossref_primary_10_1016_j_ccr_2015_06_001 crossref_primary_10_71336_jabs_1002 crossref_primary_10_1016_j_ejca_2013_08_017 crossref_primary_10_1016_S1773_035X_20_30162_3 crossref_primary_10_1021_ac500810r crossref_primary_10_2460_javma_253_10_1328 crossref_primary_10_1016_j_chembiol_2014_08_009 crossref_primary_10_1016_j_jnutbio_2016_03_003 crossref_primary_10_1016_j_jid_2021_04_037 crossref_primary_10_1016_j_toxlet_2013_09_010 crossref_primary_10_1134_S0026893323060092 crossref_primary_10_15171_bi_2018_13 crossref_primary_10_1007_s12010_017_2573_6 crossref_primary_10_1093_jleuko_qiae107 crossref_primary_10_1016_j_ijbiomac_2020_09_096 crossref_primary_10_1096_fj_09_151308 crossref_primary_10_1007_s10863_012_9456_x crossref_primary_10_1021_acs_jproteome_9b00586 crossref_primary_10_1002_bit_26285 crossref_primary_10_4103_jdmimsu_jdmimsu_13_21 crossref_primary_10_1155_2011_690848 crossref_primary_10_1016_j_neuropharm_2013_11_016 crossref_primary_10_14336_AD_2019_0604 crossref_primary_10_1074_jbc_M109_089250 crossref_primary_10_25040_ecpb2018_04_048 crossref_primary_10_1007_s10545_017_0104_9 crossref_primary_10_1016_j_freeradbiomed_2023_08_014 crossref_primary_10_1007_s12011_019_01937_7 crossref_primary_10_1152_physrev_00004_2012 crossref_primary_10_1016_j_freeradbiomed_2025_03_029 crossref_primary_10_1016_j_crohns_2013_02_010 crossref_primary_10_3109_10715762_2015_1009053 crossref_primary_10_1016_j_etap_2022_103960 crossref_primary_10_1007_s12035_018_1051_7 crossref_primary_10_1002_pro_427 crossref_primary_10_1155_2012_859231 crossref_primary_10_1016_j_amjms_2023_09_002 crossref_primary_10_1186_s12951_023_02058_z crossref_primary_10_1016_j_chemphyslip_2017_04_002 crossref_primary_10_3109_10715762_2012_727209 crossref_primary_10_3390_ijms23137424 crossref_primary_10_15407_ubj93_03_068 crossref_primary_10_1016_j_freeradbiomed_2014_03_001 crossref_primary_10_1016_j_ddstr_2013_11_003 crossref_primary_10_1089_ars_2009_2805 crossref_primary_10_3390_ijms23158466 crossref_primary_10_1016_j_neuint_2019_104484 crossref_primary_10_1177_2045894018794000 crossref_primary_10_1039_D2TB02661A crossref_primary_10_1371_journal_pone_0061380 crossref_primary_10_3390_ijms18102220 crossref_primary_10_1155_2018_9719584 |
| Cites_doi | 10.1016/S0039-6257(00)00140-5 10.1002/med.20117 10.1242/jcs.112.14.2409 10.1023/B:PHAM.0000003366.25263.78 10.1016/S0098-2997(03)00014-1 10.2174/0929867013372922 10.1042/bj20031049 10.1080/10715760310001657712 10.1124/jpet.105.088088 10.1021/ac0514220 10.1021/ac0617971 10.1021/tx050078z 10.1016/0098-2997(93)90008-2 10.1074/jbc.M209493200 10.1124/mol.106.029686 10.1016/S0076-6879(94)33040-9 10.1016/j.exer.2005.11.017 10.1016/j.freeradbiomed.2004.08.027 10.1080/1071576021000041005 10.1002/pmic.200600450 10.1074/jbc.M101266200 10.1093/carcin/bgl111 10.1016/j.freeradbiomed.2005.05.010 10.1016/j.bbrc.2004.12.104 10.1016/S0891-5849(02)00914-0 10.1021/ac062262a 10.1080/10715760600918142 10.1080/03602530600959508 10.1016/j.febslet.2004.11.003 10.1074/jbc.M101821200 10.1002/elps.200405890 10.1006/jmbi.1999.2697 10.1016/S0021-9258(19)47359-6 10.1021/tx00046a009 10.1523/JNEUROSCI.17-03-01046.1997 10.1111/j.1471-4159.2004.02892.x 10.1021/ja057358l 10.1016/S0098-2997(03)00017-7 10.1074/jbc.M509723200 10.1074/mcp.M400129-MCP200 10.1021/tx050080q 10.1093/carcin/15.7.1359 10.1021/tx020105a 10.1021/ac0607257 10.1021/tx600270f 10.1021/tx600289r 10.1152/japplphysiol.01145.2006 10.1248/bpb.26.1652 10.1016/0891-5849(91)90192-6 10.1016/j.chroma.2006.08.096 10.1016/j.chroma.2006.11.009 10.1002/mas.10076 10.1016/j.febslet.2007.06.044 10.1021/ac0484373 10.1042/bj3550237 10.1016/j.taap.2003.10.001 10.1074/mcp.M600120-MCP200 10.1074/jbc.M308167200 10.1124/mol.58.3.535 10.1016/j.freeradbiomed.2004.07.016 10.1016/S0891-5849(01)00480-4 10.18388/abp.2003_3689 10.1021/ac0303822 10.1046/j.1471-4159.2002.01103.x 10.1038/nmeth725 10.1002/pmic.200500876 10.1038/47520 |
| ContentType | Journal Article |
| Copyright | 2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc. |
| Copyright_xml | – notice: 2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. – notice: Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc. |
| DBID | 6I. AAFTH FBQ AAYXX CITATION CGR CUY CVF ECM EIF NPM 7S9 L.6 7X8 5PM |
| DOI | 10.1074/jbc.R700019200 |
| DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access AGRIS CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed AGRICOLA AGRICOLA - Academic MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) AGRICOLA AGRICOLA - Academic MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE AGRICOLA |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1083-351X |
| EndPage | 21841 |
| ExternalDocumentID | PMC2494933 18445586 10_1074_jbc_R700019200 283_32_21837 US201300919821 S0021925820661725 |
| Genre | Review Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: Eli Lilly and Co. – fundername: Minnesota Obesity Center – fundername: National Institutes of Health grantid: AG25371; T32 HL07741 – fundername: Minnesota Agricultural Experiment Station – fundername: NHLBI grantid: DK053189 – fundername: NIDDK NIH HHS grantid: DK053189 – fundername: NIDDK NIH HHS grantid: R01 DK084669 – fundername: NIA NIH HHS grantid: AG25371 – fundername: NHLBI NIH HHS grantid: T32 HL07741 |
| GroupedDBID | --- -DZ -ET -~X .55 0SF 186 18M 29J 2WC 34G 39C 4.4 53G 5BI 5GY 5RE 5VS 6I. 79B 85S AAEDW AAFTH AAFWJ AARDX AAXUO ABDNZ ABOCM ABPPZ ABRJW ACGFO ACNCT ADBBV ADIYS ADNWM AENEX AEXQZ AFFNX AFMIJ AFOSN AFPKN ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS BAWUL BTFSW C1A CJ0 CS3 DIK DU5 E3Z EBS EJD F20 F5P FDB FRP GROUPED_DOAJ GX1 HH5 HYE IH2 KQ8 L7B MVM N9A OHT OK1 P-O P0W P2P R.V RHF RHI RNS ROL RPM SJN TBC TN5 TR2 UHB UKR UPT UQL VQA W8F WH7 WOQ X7M XFK XSW Y6R YQT YSK YWH YZZ ZA5 ZE2 ~02 ~KM .GJ 3O- 41~ 6TJ AAYJJ AAYOK ABFSI ABPTK ABTAH ACSFO ACYGS AEQTP AFDAS AI. E.L FA8 FBQ J5H NHB QZG VH1 WHG XJT YYP ZGI ZY4 - 02 55 AAWZA ABFLS ABUFD ABZEH ADACO ADCOW AEILP AIZTS DL DZ ET FH7 H13 KM LI LI0 MYA O0- X XHC .7T 0R~ AALRI AAYWO AAYXX ACVFH ADCNI ADVLN ADXHL AEUPX AFPUW AIGII AITUG AKBMS AKRWK AKYEP CITATION CGR CUY CVF ECM EIF NPM PKN Z5M 7S9 L.6 7X8 5PM |
| ID | FETCH-LOGICAL-c521t-87f3cd36df8925d5a91e6737363a82ced850c33a4024c2628c27e46af61b4db83 |
| ISSN | 0021-9258 |
| IngestDate | Thu Aug 21 18:41:41 EDT 2025 Fri Jul 11 01:29:17 EDT 2025 Fri Jul 11 08:26:39 EDT 2025 Wed Feb 19 02:29:26 EST 2025 Thu Apr 24 23:11:10 EDT 2025 Tue Jul 01 02:13:35 EDT 2025 Tue Jan 05 14:52:02 EST 2021 Wed Dec 27 19:11:51 EST 2023 Fri Feb 23 02:47:15 EST 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 32 |
| Language | English |
| License | This is an open access article under the CC BY license. http://creativecommons.org/licenses/by/4.0 https://www.elsevier.com/tdm/userlicense/1.0 |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c521t-87f3cd36df8925d5a91e6737363a82ced850c33a4024c2628c27e46af61b4db83 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Review-3 The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1. To whom correspondence should be addressed. E-mail: Bernl001@umn.edu. This work was supported, in whole or in part, by National Institutes of Health Grant AG25371 (to T. J. G.), Grant T32 HL07741 from NHLBI (to P. A. G.), and Grant DK053189 (to D. A. B.). This work was also supported by an award from Eli Lilly and Co. (to T. J. G.) and by the Minnesota Agricultural Experiment Station and the Minnesota Obesity Center (to D. A. B.). This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009. |
| OpenAccessLink | https://dx.doi.org/10.1074/jbc.R700019200 |
| PMID | 18445586 |
| PQID | 47714919 |
| PQPubID | 24069 |
| PageCount | 5 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_2494933 proquest_miscellaneous_69384454 proquest_miscellaneous_47714919 pubmed_primary_18445586 crossref_citationtrail_10_1074_jbc_R700019200 crossref_primary_10_1074_jbc_R700019200 highwire_biochem_283_32_21837 fao_agris_US201300919821 elsevier_sciencedirect_doi_10_1074_jbc_R700019200 |
| ProviderPackageCode | RHF RHI CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2008-08-08 |
| PublicationDateYYYYMMDD | 2008-08-08 |
| PublicationDate_xml | – month: 08 year: 2008 text: 2008-08-08 day: 08 |
| PublicationDecade | 2000 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | The Journal of biological chemistry |
| PublicationTitleAlternate | J Biol Chem |
| PublicationYear | 2008 |
| Publisher | Elsevier Inc American Society for Biochemistry and Molecular Biology |
| Publisher_xml | – name: Elsevier Inc – name: American Society for Biochemistry and Molecular Biology |
| References | Ferrington, Kapphahn (bib39) 2004; 578 Ji, Kozak, Marnett (bib44) 2001; 276 Zhang, Liu, Xu, Yuan, Sayre (bib14) 2003; 16 Castegna, Aksenov, Thongboonkerd, Klein, Pierce, Booze, Markesbery, Butterfield (bib51) 2002; 82 Bennaars-Eiden, Higgins, Hertzel, Kapphahn, Ferrington, Bernlohr (bib29) 2002; 277 Williams, Wishnok, Tannenbaum (bib15) 2007; 20 Thomas, Soreghan, Nistor, Sarsoza, Head, Yang (bib58) 2005; 92 Eriksson (bib5) 2007; 581 Sampey, Carbone, Doorn, Drechsel, Petersen (bib42) 2007; 71 Yang, Sharma, Sharma, Awasthi, Awasthi (bib17) 2003; 50 Tidball, Wehling-Henricks (bib4) 2007; 102 Sayre, Smith, Perry (bib1) 2001; 8 Castegna, Aksenov, Aksenova, Thongboonkerd, Klein, Pierce, Booze, Markesbery, Butterfield (bib52) 2002; 33 Lin, Lee, Liu, Perry, Smith, Sayre (bib12) 2005; 18 Grune, Davies (bib37) 2003; 24 Carbone, Doorn, Kiebler, Ickes, Petersen (bib35) 2005; 315 Fazio, Rinaldi, Ciafre, Barrera, Farace (bib26) 1993; 14 Bruns, Hubatsch, Ridderstrom, Mannervik, Tainer (bib22) 1999; 288 Yoo, Regnier (bib53) 2004; 25 Mirzaei, Regnier (bib62) 2006; 78 Levonen, Landar, Ramachandran, Ceaser, Dickinson, Zanoni, Morrow, Darley-Usmar (bib40) 2004; 378 Park, Koh, Takahashi, Miyamoto, Suzuki, Dohmae, Takio, Honke, Taniguchi (bib34) 2003; 37 Sayre, Lin, Yuan, Zhu, Tang (bib10) 2006; 38 Roe, Xie, Bandhakavi, Griffin (bib63) 2007; 79 Grimsrud, Picklo, Griffin, Bernlohr (bib24) 2007; 6 Soreghan, Yang, Thomas, Hsu, Yang (bib55) 2003; 20 Stadtman, Berlett (bib7) 1991; 266 Bruenner, Jones, German (bib16) 1995; 8 Awasthi, Sharma, Cheng, Yang, Sharma, Singhal, Awasthi (bib25) 2003; 24 Wagner, Mullally, Fitzpatrick (bib43) 2006; 281 Cassidy, Edes, Nelson, Parsawar, Fitzpatrick, Moos (bib32) 2006; 27 Liu, Akhand, Kato, Yokoyama, Miyata, Kurokawa, Uchida, Nakashima (bib47) 1999; 112 Fenaille, Tabet, Guy (bib61) 2004; 76 Meany, Xie, Thompson, Arriaga, Griffin (bib60) 2007; 7 Levine, Williams, Stadtman, Shacter (bib65) 1994; 233 Oe, Arora, Lee, Blair (bib13) 2003; 278 Leonarduzzi, Robbesyn, Poli (bib41) 2004; 37 Schafer, Buettner (bib2) 2001; 30 Mirzaei, Regnier (bib56) 2005; 77 Miyake, Kadoya, Ohyashiki (bib27) 2003; 26 Beatty, Koh, Phil, Henson, Boulton (bib3) 2000; 45 Mirzaei, Regnier (bib66) 2006; 1134 Schneider, Tallman, Porter, Brash (bib8) 2001; 276 Hiratsuka, Tobita, Saito, Sakamoto, Nakano, Ogura, Nishiyama, Watabe (bib23) 2001; 355 Yang, Yang, Park (bib30) 2004; 38 Carbone, Doorn, Petersen (bib38) 2004; 37 Chavez, Wu, Han, Chung, Maier (bib64) 2006; 78 Yuan, Zhu, Sayre (bib9) 2007; 20 Poli, Schaur, Siems, Leonarduzzi (bib20) 2008; 28 Esterbauer, Schaur, Zollner (bib11) 1991; 11 Honzatko, Brichac, Murphy, Reberg, Kubatova, Smoliakova, Picklo (bib18) 2005; 39 Sadygov, Cociorva, Yates (bib49) 2004; 1 Fang, Holmgren (bib31) 2006; 128 Canuto, Ferro, Muzio, Bassi, Leonarduzzi, Maggiora, Adamo, Poli, Lindahl (bib19) 1994; 15 Mirzaei, Regnier (bib57) 2007; 1141 Stadtman (bib6) 2006; 40 Park, Misonou, Fujiwara, Takahashi, Miyamoto, Koh, Suzuki, Taniguchi (bib33) 2005; 327 Soh, Jeong, Lee, Bae, Kim, Song (bib46) 2000; 58 Han, Stevens, Maier (bib67) 2007; 79 Mark, Pang, Geddes, Uchida, Mattson (bib28) 1997; 17 Roe, Griffin (bib54) 2006; 6 Rossi, Kapahi, Natoli, Takahashi, Chen, Karin, Santoro (bib45) 2000; 403 Ross, Huang, Marchese, Williamson, Parker, Hattan, Khainovski, Pillai, Dey, Daniels, Purkayastha, Juhasz, Martin, Bartlet-Jones, He, Jacobson, Pappin (bib59) 2004; 3 Carbone, Doorn, Kiebler, Petersen (bib36) 2005; 18 Engle, Singh, Czernik, Gaddy, Montague, Ceci, Yang, Awasthi, Awasthi, Zimniak (bib21) 2004; 194 Kapphahn, Giwa, Berg, Roehrich, Feng, Olsen, Ferrington (bib50) 2006; 83 Carini, Aldini, Facino (bib48) 2004; 23 Fang (10.1074/jbc.R700019200_bib31) 2006; 128 Grune (10.1074/jbc.R700019200_bib37) 2003; 24 Kapphahn (10.1074/jbc.R700019200_bib50) 2006; 83 Ferrington (10.1074/jbc.R700019200_bib39) 2004; 578 Eriksson (10.1074/jbc.R700019200_bib5) 2007; 581 Liu (10.1074/jbc.R700019200_bib47) 1999; 112 Castegna (10.1074/jbc.R700019200_bib51) 2002; 82 Carbone (10.1074/jbc.R700019200_bib36) 2005; 18 Mirzaei (10.1074/jbc.R700019200_bib66) 2006; 1134 Canuto (10.1074/jbc.R700019200_bib19) 1994; 15 Yang (10.1074/jbc.R700019200_bib30) 2004; 38 Stadtman (10.1074/jbc.R700019200_bib6) 2006; 40 Miyake (10.1074/jbc.R700019200_bib27) 2003; 26 Mirzaei (10.1074/jbc.R700019200_bib62) 2006; 78 Soh (10.1074/jbc.R700019200_bib46) 2000; 58 Carbone (10.1074/jbc.R700019200_bib38) 2004; 37 Bennaars-Eiden (10.1074/jbc.R700019200_bib29) 2002; 277 Mirzaei (10.1074/jbc.R700019200_bib57) 2007; 1141 Soreghan (10.1074/jbc.R700019200_bib55) 2003; 20 Meany (10.1074/jbc.R700019200_bib60) 2007; 7 Yang (10.1074/jbc.R700019200_bib17) 2003; 50 Bruns (10.1074/jbc.R700019200_bib22) 1999; 288 Roe (10.1074/jbc.R700019200_bib63) 2007; 79 Grimsrud (10.1074/jbc.R700019200_bib24) 2007; 6 Levine (10.1074/jbc.R700019200_bib65) 1994; 233 Beatty (10.1074/jbc.R700019200_bib3) 2000; 45 Stadtman (10.1074/jbc.R700019200_bib7) 1991; 266 Hiratsuka (10.1074/jbc.R700019200_bib23) 2001; 355 Wagner (10.1074/jbc.R700019200_bib43) 2006; 281 Han (10.1074/jbc.R700019200_bib67) 2007; 79 Thomas (10.1074/jbc.R700019200_bib58) 2005; 92 Schafer (10.1074/jbc.R700019200_bib2) 2001; 30 Ross (10.1074/jbc.R700019200_bib59) 2004; 3 Rossi (10.1074/jbc.R700019200_bib45) 2000; 403 Mark (10.1074/jbc.R700019200_bib28) 1997; 17 Carbone (10.1074/jbc.R700019200_bib35) 2005; 315 Sadygov (10.1074/jbc.R700019200_bib49) 2004; 1 Fenaille (10.1074/jbc.R700019200_bib61) 2004; 76 Castegna (10.1074/jbc.R700019200_bib52) 2002; 33 Mirzaei (10.1074/jbc.R700019200_bib56) 2005; 77 Yoo (10.1074/jbc.R700019200_bib53) 2004; 25 Schneider (10.1074/jbc.R700019200_bib8) 2001; 276 Williams (10.1074/jbc.R700019200_bib15) 2007; 20 Awasthi (10.1074/jbc.R700019200_bib25) 2003; 24 Esterbauer (10.1074/jbc.R700019200_bib11) 1991; 11 Bruenner (10.1074/jbc.R700019200_bib16) 1995; 8 Leonarduzzi (10.1074/jbc.R700019200_bib41) 2004; 37 Yuan (10.1074/jbc.R700019200_bib9) 2007; 20 Poli (10.1074/jbc.R700019200_bib20) 2008; 28 Honzatko (10.1074/jbc.R700019200_bib18) 2005; 39 Carini (10.1074/jbc.R700019200_bib48) 2004; 23 Tidball (10.1074/jbc.R700019200_bib4) 2007; 102 Levonen (10.1074/jbc.R700019200_bib40) 2004; 378 Sayre (10.1074/jbc.R700019200_bib10) 2006; 38 Zhang (10.1074/jbc.R700019200_bib14) 2003; 16 Park (10.1074/jbc.R700019200_bib34) 2003; 37 Engle (10.1074/jbc.R700019200_bib21) 2004; 194 Oe (10.1074/jbc.R700019200_bib13) 2003; 278 Sampey (10.1074/jbc.R700019200_bib42) 2007; 71 Park (10.1074/jbc.R700019200_bib33) 2005; 327 Roe (10.1074/jbc.R700019200_bib54) 2006; 6 Fazio (10.1074/jbc.R700019200_bib26) 1993; 14 Ji (10.1074/jbc.R700019200_bib44) 2001; 276 Lin (10.1074/jbc.R700019200_bib12) 2005; 18 Chavez (10.1074/jbc.R700019200_bib64) 2006; 78 Sayre (10.1074/jbc.R700019200_bib1) 2001; 8 Cassidy (10.1074/jbc.R700019200_bib32) 2006; 27 |
| References_xml | – volume: 33 start-page: 562 year: 2002 end-page: 571 ident: bib52 publication-title: Free Radic. Biol. Med. – volume: 78 start-page: 770 year: 2006 end-page: 778 ident: bib62 publication-title: Anal. Chem. – volume: 58 start-page: 535 year: 2000 end-page: 541 ident: bib46 publication-title: Mol. Pharmacol. – volume: 194 start-page: 296 year: 2004 end-page: 308 ident: bib21 publication-title: Toxicol. Appl. Pharmacol. – volume: 40 start-page: 1250 year: 2006 end-page: 1258 ident: bib6 publication-title: Free Radic. Res. – volume: 278 start-page: 42098 year: 2003 end-page: 42105 ident: bib13 publication-title: J. Biol. Chem. – volume: 79 start-page: 3342 year: 2007 end-page: 3354 ident: bib67 publication-title: Anal. Chem. – volume: 128 start-page: 1879 year: 2006 end-page: 1885 ident: bib31 publication-title: J. Am. Chem. Soc. – volume: 1134 start-page: 122 year: 2006 end-page: 133 ident: bib66 publication-title: J. Chromatogr. A – volume: 11 start-page: 81 year: 1991 end-page: 128 ident: bib11 publication-title: Free Radic. Biol. Med. – volume: 281 start-page: 2598 year: 2006 end-page: 2604 ident: bib43 publication-title: J. Biol. Chem. – volume: 82 start-page: 1524 year: 2002 end-page: 1532 ident: bib51 publication-title: J. Neurochem. – volume: 288 start-page: 427 year: 1999 end-page: 439 ident: bib22 publication-title: J. Mol. Biol. – volume: 355 start-page: 237 year: 2001 end-page: 244 ident: bib23 publication-title: Biochem. J. – volume: 378 start-page: 373 year: 2004 end-page: 382 ident: bib40 publication-title: Biochem. J. – volume: 38 start-page: 241 year: 2004 end-page: 249 ident: bib30 publication-title: Free Radic. Res. – volume: 277 start-page: 50693 year: 2002 end-page: 50702 ident: bib29 publication-title: J. Biol. Chem. – volume: 24 start-page: 219 year: 2003 end-page: 230 ident: bib25 publication-title: Mol. Aspects Med. – volume: 71 start-page: 871 year: 2007 end-page: 883 ident: bib42 publication-title: Mol. Pharmacol. – volume: 7 start-page: 1150 year: 2007 end-page: 1163 ident: bib60 publication-title: Proteomics – volume: 18 start-page: 1324 year: 2005 end-page: 1331 ident: bib36 publication-title: Chem. Res. Toxicol. – volume: 79 start-page: 3747 year: 2007 end-page: 3756 ident: bib63 publication-title: Anal. Chem. – volume: 20 start-page: 129 year: 2007 end-page: 139 ident: bib9 publication-title: Chem. Res. Toxicol. – volume: 83 start-page: 165 year: 2006 end-page: 175 ident: bib50 publication-title: Exp. Eye Res. – volume: 38 start-page: 651 year: 2006 end-page: 675 ident: bib10 publication-title: Drug Metab. Rev. – volume: 3 start-page: 1154 year: 2004 end-page: 1169 ident: bib59 publication-title: Mol. Cell. Proteomics – volume: 327 start-page: 1058 year: 2005 end-page: 1065 ident: bib33 publication-title: Biochem. Biophys. Res. Commun. – volume: 15 start-page: 1359 year: 1994 end-page: 1364 ident: bib19 publication-title: Carcinogenesis – volume: 403 start-page: 103 year: 2000 end-page: 108 ident: bib45 publication-title: Nature – volume: 25 start-page: 1334 year: 2004 end-page: 1341 ident: bib53 publication-title: Electrophoresis – volume: 37 start-page: 205 year: 2003 end-page: 211 ident: bib34 publication-title: Free Radic. Res. – volume: 8 start-page: 552 year: 1995 end-page: 559 ident: bib16 publication-title: Chem. Res. Toxicol. – volume: 20 start-page: 1713 year: 2003 end-page: 1720 ident: bib55 publication-title: Pharm. Res. (N. Y.) – volume: 20 start-page: 767 year: 2007 end-page: 775 ident: bib15 publication-title: Chem. Res. Toxicol. – volume: 6 start-page: 624 year: 2007 end-page: 637 ident: bib24 publication-title: Mol. Cell. Proteomics – volume: 266 start-page: 17201 year: 1991 end-page: 17211 ident: bib7 publication-title: J. Biol. Chem. – volume: 76 start-page: 867 year: 2004 end-page: 873 ident: bib61 publication-title: Anal. Chem. – volume: 37 start-page: 1694 year: 2004 end-page: 1702 ident: bib41 publication-title: Free Radic. Biol. Med. – volume: 112 start-page: 2409 year: 1999 end-page: 2417 ident: bib47 publication-title: J. Cell Sci. – volume: 18 start-page: 1219 year: 2005 end-page: 1231 ident: bib12 publication-title: Chem. Res. Toxicol. – volume: 6 start-page: 4678 year: 2006 end-page: 4687 ident: bib54 publication-title: Proteomics – volume: 39 start-page: 913 year: 2005 end-page: 924 ident: bib18 publication-title: Free Radic. Biol. Med. – volume: 102 start-page: 1677 year: 2007 end-page: 1686 ident: bib4 publication-title: J. Appl. Physiol. – volume: 14 start-page: 217 year: 1993 end-page: 228 ident: bib26 publication-title: Mol. Aspects Med. – volume: 23 start-page: 281 year: 2004 end-page: 305 ident: bib48 publication-title: Mass Spectrom. Rev. – volume: 77 start-page: 2386 year: 2005 end-page: 2392 ident: bib56 publication-title: Anal. Chem. – volume: 276 start-page: 20831 year: 2001 end-page: 20838 ident: bib8 publication-title: J. Biol. Chem. – volume: 233 start-page: 346 year: 1994 end-page: 357 ident: bib65 publication-title: Methods Enzymol. – volume: 315 start-page: 8 year: 2005 end-page: 15 ident: bib35 publication-title: J. Pharmacol. Exp. Ther. – volume: 30 start-page: 1191 year: 2001 end-page: 1212 ident: bib2 publication-title: Free Radic. Biol. Med. – volume: 24 start-page: 195 year: 2003 end-page: 204 ident: bib37 publication-title: Mol. Aspects Med. – volume: 50 start-page: 319 year: 2003 end-page: 336 ident: bib17 publication-title: Acta Biochim. Pol. – volume: 17 start-page: 1046 year: 1997 end-page: 1054 ident: bib28 publication-title: J. Neurosci. – volume: 581 start-page: 3734 year: 2007 end-page: 3742 ident: bib5 publication-title: FEBS Lett. – volume: 578 start-page: 217 year: 2004 end-page: 223 ident: bib39 publication-title: FEBS Lett. – volume: 27 start-page: 2538 year: 2006 end-page: 2549 ident: bib32 publication-title: Carcinogenesis – volume: 276 start-page: 18223 year: 2001 end-page: 18228 ident: bib44 publication-title: J. Biol. Chem. – volume: 28 start-page: 569 year: 2008 end-page: 631 ident: bib20 publication-title: Med. Res. Rev. – volume: 1141 start-page: 22 year: 2007 end-page: 31 ident: bib57 publication-title: J. Chromatogr. A – volume: 8 start-page: 721 year: 2001 end-page: 738 ident: bib1 publication-title: Curr. Med. Chem. – volume: 26 start-page: 1652 year: 2003 end-page: 1656 ident: bib27 publication-title: Biol. Pharm. Bull. – volume: 45 start-page: 115 year: 2000 end-page: 134 ident: bib3 publication-title: Surv. Ophthalmol. – volume: 37 start-page: 1430 year: 2004 end-page: 1439 ident: bib38 publication-title: Free Radic. Biol. Med. – volume: 16 start-page: 512 year: 2003 end-page: 523 ident: bib14 publication-title: Chem. Res. Toxicol. – volume: 92 start-page: 705 year: 2005 end-page: 717 ident: bib58 publication-title: J. Neurochem. – volume: 1 start-page: 195 year: 2004 end-page: 202 ident: bib49 publication-title: Nat. Methods – volume: 78 start-page: 6847 year: 2006 end-page: 6854 ident: bib64 publication-title: Anal. Chem. – volume: 45 start-page: 115 year: 2000 ident: 10.1074/jbc.R700019200_bib3 publication-title: Surv. Ophthalmol. doi: 10.1016/S0039-6257(00)00140-5 – volume: 28 start-page: 569 year: 2008 ident: 10.1074/jbc.R700019200_bib20 publication-title: Med. Res. Rev. doi: 10.1002/med.20117 – volume: 112 start-page: 2409 year: 1999 ident: 10.1074/jbc.R700019200_bib47 publication-title: J. Cell Sci. doi: 10.1242/jcs.112.14.2409 – volume: 20 start-page: 1713 year: 2003 ident: 10.1074/jbc.R700019200_bib55 publication-title: Pharm. Res. (N. Y.) doi: 10.1023/B:PHAM.0000003366.25263.78 – volume: 24 start-page: 195 year: 2003 ident: 10.1074/jbc.R700019200_bib37 publication-title: Mol. Aspects Med. doi: 10.1016/S0098-2997(03)00014-1 – volume: 8 start-page: 721 year: 2001 ident: 10.1074/jbc.R700019200_bib1 publication-title: Curr. Med. Chem. doi: 10.2174/0929867013372922 – volume: 378 start-page: 373 year: 2004 ident: 10.1074/jbc.R700019200_bib40 publication-title: Biochem. J. doi: 10.1042/bj20031049 – volume: 38 start-page: 241 year: 2004 ident: 10.1074/jbc.R700019200_bib30 publication-title: Free Radic. Res. doi: 10.1080/10715760310001657712 – volume: 315 start-page: 8 year: 2005 ident: 10.1074/jbc.R700019200_bib35 publication-title: J. Pharmacol. Exp. Ther. doi: 10.1124/jpet.105.088088 – volume: 78 start-page: 770 year: 2006 ident: 10.1074/jbc.R700019200_bib62 publication-title: Anal. Chem. doi: 10.1021/ac0514220 – volume: 79 start-page: 3747 year: 2007 ident: 10.1074/jbc.R700019200_bib63 publication-title: Anal. Chem. doi: 10.1021/ac0617971 – volume: 18 start-page: 1324 year: 2005 ident: 10.1074/jbc.R700019200_bib36 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx050078z – volume: 14 start-page: 217 year: 1993 ident: 10.1074/jbc.R700019200_bib26 publication-title: Mol. Aspects Med. doi: 10.1016/0098-2997(93)90008-2 – volume: 277 start-page: 50693 year: 2002 ident: 10.1074/jbc.R700019200_bib29 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M209493200 – volume: 71 start-page: 871 year: 2007 ident: 10.1074/jbc.R700019200_bib42 publication-title: Mol. Pharmacol. doi: 10.1124/mol.106.029686 – volume: 233 start-page: 346 year: 1994 ident: 10.1074/jbc.R700019200_bib65 publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(94)33040-9 – volume: 83 start-page: 165 year: 2006 ident: 10.1074/jbc.R700019200_bib50 publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2005.11.017 – volume: 37 start-page: 1694 year: 2004 ident: 10.1074/jbc.R700019200_bib41 publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2004.08.027 – volume: 37 start-page: 205 year: 2003 ident: 10.1074/jbc.R700019200_bib34 publication-title: Free Radic. Res. doi: 10.1080/1071576021000041005 – volume: 7 start-page: 1150 year: 2007 ident: 10.1074/jbc.R700019200_bib60 publication-title: Proteomics doi: 10.1002/pmic.200600450 – volume: 276 start-page: 18223 year: 2001 ident: 10.1074/jbc.R700019200_bib44 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M101266200 – volume: 27 start-page: 2538 year: 2006 ident: 10.1074/jbc.R700019200_bib32 publication-title: Carcinogenesis doi: 10.1093/carcin/bgl111 – volume: 39 start-page: 913 year: 2005 ident: 10.1074/jbc.R700019200_bib18 publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2005.05.010 – volume: 327 start-page: 1058 year: 2005 ident: 10.1074/jbc.R700019200_bib33 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2004.12.104 – volume: 33 start-page: 562 year: 2002 ident: 10.1074/jbc.R700019200_bib52 publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(02)00914-0 – volume: 79 start-page: 3342 year: 2007 ident: 10.1074/jbc.R700019200_bib67 publication-title: Anal. Chem. doi: 10.1021/ac062262a – volume: 40 start-page: 1250 year: 2006 ident: 10.1074/jbc.R700019200_bib6 publication-title: Free Radic. Res. doi: 10.1080/10715760600918142 – volume: 38 start-page: 651 year: 2006 ident: 10.1074/jbc.R700019200_bib10 publication-title: Drug Metab. Rev. doi: 10.1080/03602530600959508 – volume: 578 start-page: 217 year: 2004 ident: 10.1074/jbc.R700019200_bib39 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2004.11.003 – volume: 276 start-page: 20831 year: 2001 ident: 10.1074/jbc.R700019200_bib8 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M101821200 – volume: 25 start-page: 1334 year: 2004 ident: 10.1074/jbc.R700019200_bib53 publication-title: Electrophoresis doi: 10.1002/elps.200405890 – volume: 288 start-page: 427 year: 1999 ident: 10.1074/jbc.R700019200_bib22 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.2697 – volume: 266 start-page: 17201 year: 1991 ident: 10.1074/jbc.R700019200_bib7 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)47359-6 – volume: 8 start-page: 552 year: 1995 ident: 10.1074/jbc.R700019200_bib16 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx00046a009 – volume: 17 start-page: 1046 year: 1997 ident: 10.1074/jbc.R700019200_bib28 publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.17-03-01046.1997 – volume: 92 start-page: 705 year: 2005 ident: 10.1074/jbc.R700019200_bib58 publication-title: J. Neurochem. doi: 10.1111/j.1471-4159.2004.02892.x – volume: 128 start-page: 1879 year: 2006 ident: 10.1074/jbc.R700019200_bib31 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja057358l – volume: 24 start-page: 219 year: 2003 ident: 10.1074/jbc.R700019200_bib25 publication-title: Mol. Aspects Med. doi: 10.1016/S0098-2997(03)00017-7 – volume: 281 start-page: 2598 year: 2006 ident: 10.1074/jbc.R700019200_bib43 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M509723200 – volume: 3 start-page: 1154 year: 2004 ident: 10.1074/jbc.R700019200_bib59 publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M400129-MCP200 – volume: 18 start-page: 1219 year: 2005 ident: 10.1074/jbc.R700019200_bib12 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx050080q – volume: 15 start-page: 1359 year: 1994 ident: 10.1074/jbc.R700019200_bib19 publication-title: Carcinogenesis doi: 10.1093/carcin/15.7.1359 – volume: 16 start-page: 512 year: 2003 ident: 10.1074/jbc.R700019200_bib14 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx020105a – volume: 78 start-page: 6847 year: 2006 ident: 10.1074/jbc.R700019200_bib64 publication-title: Anal. Chem. doi: 10.1021/ac0607257 – volume: 20 start-page: 129 year: 2007 ident: 10.1074/jbc.R700019200_bib9 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx600270f – volume: 20 start-page: 767 year: 2007 ident: 10.1074/jbc.R700019200_bib15 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx600289r – volume: 102 start-page: 1677 year: 2007 ident: 10.1074/jbc.R700019200_bib4 publication-title: J. Appl. Physiol. doi: 10.1152/japplphysiol.01145.2006 – volume: 26 start-page: 1652 year: 2003 ident: 10.1074/jbc.R700019200_bib27 publication-title: Biol. Pharm. Bull. doi: 10.1248/bpb.26.1652 – volume: 11 start-page: 81 year: 1991 ident: 10.1074/jbc.R700019200_bib11 publication-title: Free Radic. Biol. Med. doi: 10.1016/0891-5849(91)90192-6 – volume: 1134 start-page: 122 year: 2006 ident: 10.1074/jbc.R700019200_bib66 publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2006.08.096 – volume: 1141 start-page: 22 year: 2007 ident: 10.1074/jbc.R700019200_bib57 publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2006.11.009 – volume: 23 start-page: 281 year: 2004 ident: 10.1074/jbc.R700019200_bib48 publication-title: Mass Spectrom. Rev. doi: 10.1002/mas.10076 – volume: 581 start-page: 3734 year: 2007 ident: 10.1074/jbc.R700019200_bib5 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2007.06.044 – volume: 77 start-page: 2386 year: 2005 ident: 10.1074/jbc.R700019200_bib56 publication-title: Anal. Chem. doi: 10.1021/ac0484373 – volume: 355 start-page: 237 year: 2001 ident: 10.1074/jbc.R700019200_bib23 publication-title: Biochem. J. doi: 10.1042/bj3550237 – volume: 194 start-page: 296 year: 2004 ident: 10.1074/jbc.R700019200_bib21 publication-title: Toxicol. Appl. Pharmacol. doi: 10.1016/j.taap.2003.10.001 – volume: 6 start-page: 624 year: 2007 ident: 10.1074/jbc.R700019200_bib24 publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M600120-MCP200 – volume: 278 start-page: 42098 year: 2003 ident: 10.1074/jbc.R700019200_bib13 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M308167200 – volume: 58 start-page: 535 year: 2000 ident: 10.1074/jbc.R700019200_bib46 publication-title: Mol. Pharmacol. doi: 10.1124/mol.58.3.535 – volume: 37 start-page: 1430 year: 2004 ident: 10.1074/jbc.R700019200_bib38 publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2004.07.016 – volume: 30 start-page: 1191 year: 2001 ident: 10.1074/jbc.R700019200_bib2 publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(01)00480-4 – volume: 50 start-page: 319 year: 2003 ident: 10.1074/jbc.R700019200_bib17 publication-title: Acta Biochim. Pol. doi: 10.18388/abp.2003_3689 – volume: 76 start-page: 867 year: 2004 ident: 10.1074/jbc.R700019200_bib61 publication-title: Anal. Chem. doi: 10.1021/ac0303822 – volume: 82 start-page: 1524 year: 2002 ident: 10.1074/jbc.R700019200_bib51 publication-title: J. Neurochem. doi: 10.1046/j.1471-4159.2002.01103.x – volume: 1 start-page: 195 year: 2004 ident: 10.1074/jbc.R700019200_bib49 publication-title: Nat. Methods doi: 10.1038/nmeth725 – volume: 6 start-page: 4678 year: 2006 ident: 10.1074/jbc.R700019200_bib54 publication-title: Proteomics doi: 10.1002/pmic.200500876 – volume: 403 start-page: 103 year: 2000 ident: 10.1074/jbc.R700019200_bib45 publication-title: Nature doi: 10.1038/47520 |
| SSID | ssj0000491 |
| Score | 2.4714327 |
| SecondaryResourceType | review_article |
| Snippet | The term “oxidative stress” links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune... The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune... The term âoxidative stressâ links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune... The term “oxidative stress” links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune... |
| SourceID | pubmedcentral proquest pubmed crossref highwire fao elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 21837 |
| SubjectTerms | Aldehydes - metabolism Animals Electrophoresis, Gel, Two-Dimensional Humans Mass Spectrometry Minireviews Oxidative Stress Protein Carbonylation Proteins - chemistry Proteins - metabolism Proteomics Reactive Oxygen Species - metabolism |
| Title | Oxidative Stress and Covalent Modification of Protein with Bioactive Aldehydes |
| URI | https://dx.doi.org/10.1074/jbc.R700019200 http://www.jbc.org/content/283/32/21837.abstract https://www.ncbi.nlm.nih.gov/pubmed/18445586 https://www.proquest.com/docview/47714919 https://www.proquest.com/docview/69384454 https://pubmed.ncbi.nlm.nih.gov/PMC2494933 |
| Volume | 283 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Bb9MwFLa6cYALgg1YgIEPCA5VShM7iXssFaga6hhslXqzkthZO7XJ1LWC8S_5RzzHdpJOrQS7RFVix02-L8_P9vP3EHpHZFdpqPRcIYLApSz0XOaplGGBjBhJUkFjNTUwOg2HY3oyCSat1p9G1NJ6lXTS31v3ldwHVTgHuKpdsv-BbHVTOAG_AV84AsJw_CeMv_2aCS3cfa63fKhZ8EEBTagV_lEhVBxQ5ROeKUmGmd62rXJQxqWpa_fnQk5vhYklvKrZ0_BVtVSTFhOxGeLqyJ3Z4ma5FjbOsN3v2EsTvfgxLPLLn3LWqJBlWrrAMKV9UlX5JJf5vJguq3h7ezs7M8HKuDhWc8kuOTXjT-Hpqv-pQ0lsFmCTfLNpAMvwEV9Lu3ekNtDgMqrdB5OmBfd1LhxDVTNfag0y06IypndXI1pva9cBvpTqOpK08yPSnm8pobpq8Oh6URIJbkGD4K6Cd-kTnI0GvtL7IWQPPfBh5KKSanz9XgvYw4BMJ3E0j2Z1RCP6cbNppWZr2tnlMu1lcdHQtd42Rrob6tvwnS6eoMeGSLivGfwUtWR-gA77ebwqFrf4PS7DkEtYDtDDgQXuEJ1WBMea4BiwxJbguElwXGTYEBwrguOK4Lgi-DM0_vL5YjB0TQIQN1V5NqCnzkgqSCgyBu9KBHHPkyqvEglJzPxUChZ0U0JiCo5m6oc-S_1I0jDOQi-hImHkOdrPi1weIRwFaUIZzbww7lJB_TgCE5olEjxYtdQfOMi175inRh1fJWmZ8zJKI6Ic4OE1PA76UJW_1rowO0t6FjJuvFrtrXJg3s46R4Atjy-ho-fjc1-FF4Bj32O-56BjCzhP9MfEgf-c-LzkuoPeWhZwQEst_8W5LNY3nEaRB-zr7S4R9oiiHHXQC82a-tEMFR0UbfCpKqBU6jev5LNpqVZvvoeX9675Cj2qrctrtL9aruUxjARWyZvy2_oLAQkIQg |
| linkProvider | Colorado Alliance of Research Libraries |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Oxidative+Stress+and+Covalent+Modification+of+Protein+with+Bioactive+Aldehydes&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=Grimsrud%2C+Paul+A.&rft.au=Xie%2C+Hongwei&rft.au=Griffin%2C+Timothy+J.&rft.au=Bernlohr%2C+David+A.&rft.date=2008-08-08&rft.pub=American+Society+for+Biochemistry+and+Molecular+Biology&rft.issn=0021-9258&rft.eissn=1083-351X&rft.volume=283&rft.issue=32&rft.spage=21837&rft.epage=21841&rft_id=info:doi/10.1074%2Fjbc.R700019200&rft_id=info%3Apmid%2F18445586&rft.externalDocID=PMC2494933 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon |