{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Doulias PT"],"funding":["NIDA NIH HHS","NIA NIH HHS","NIMH NIH HHS","NINDS NIH HHS","National Institutes of Health"],"pagination":["367-378"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8477648"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(3)"],"pubmed_abstract":["In the brain, both HIV-1 and methamphetamine (meth) use result in increases in oxidative and nitrosative stress. This redox stress is thought to contribute to the pathogenesis of HIV-associated neurocognitive disorder (HAND) and further worsening cognitive activity in the setting of drug abuse. One consequence of such redox stress is aberrant protein S-nitrosylation, derived from nitric oxide, which may disrupt normal protein activity. Here, we report an improved, mass spectrometry-based technique to assess S-nitrosylated protein in human postmortem brains using selective enrichment of S-nitrosocysteine residues with an organomercury resin. The data show increasing S-nitrosylation of tricarboxylic acid (TCA) enzymes in the setting of HAND and HAND/meth use compared with HIV+ control brains"],"journal":["Journal of neurovirology"],"pubmed_title":["TCA cycle metabolic compromise due to an aberrant S-nitrosoproteome in HIV-associated neurocognitive disorder with methamphetamine use."],"pmcid":["PMC8477648"],"funding_grant_id":["R01 AG056259","U24 MH100928","RF1 AG057409","R01 AG061845","DP1 DA041722","R01 NS086890"],"pubmed_authors":["Scott H","Ischiropoulos H","McKercher SR","Albertolle M","Lipton SA","Doulias PT","Nakamura T","Deal A","Sultan A"],"additional_accession":[]},"is_claimable":false,"name":"TCA cycle metabolic compromise due to an aberrant S-nitrosoproteome in HIV-associated neurocognitive disorder with methamphetamine use.","description":"In the brain, both HIV-1 and methamphetamine (meth) use result in increases in oxidative and nitrosative stress. This redox stress is thought to contribute to the pathogenesis of HIV-associated neurocognitive disorder (HAND) and further worsening cognitive activity in the setting of drug abuse. One consequence of such redox stress is aberrant protein S-nitrosylation, derived from nitric oxide, which may disrupt normal protein activity. Here, we report an improved, mass spectrometry-based technique to assess S-nitrosylated protein in human postmortem brains using selective enrichment of S-nitrosocysteine residues with an organomercury resin. The data show increasing S-nitrosylation of tricarboxylic acid (TCA) enzymes in the setting of HAND and HAND/meth use compared with HIV+ control brains","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2025-04-19T18:16:57.651Z","creation":"2025-02-18T23:35:48.12Z"},"accession":"S-EPMC8477648","cross_references":{"pubmed":["33876414"],"doi":["10.1007/s13365-021-00970-4"]}}