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- Author:
- Xing, Longsheng; Ding, Tianbo; Huang, Cong; Xi, Yu; Wu, Qiang; Qian, Wanqiang; Wan, Fanghao; Zhang, Bin
- Source:
- Journal of proteomics 2019 v.207 pp. 103465
- ISSN:
- 1874-3919
- Subject:
- Thrips tabaci; acetylation; aerobiosis; amino acid metabolism; antibodies; bioinformatics; carbohydrate metabolism; enzymes; fatty acid metabolism; genes; insect pests; insecticide resistance; lysine; oxidative phosphorylation; peptides; pesticides; post-translational modification; protein-protein interactions; proteins; proteomics; ribosomes; surveys; tandem mass spectrometry; transcription (genetics)
- Abstract:
- ... Protein lysine acetylation is a reversible posttranslational modification and plays a pivotal role in a broad array of physiological functions. In our study, a strategy combining immunoaffinity enrichment of acetylated peptides based on anti-acetyllysine antibody with high-resolution tandem mass spectrometry was employed for a systemic survey of acetylation sites in a polyphagous pest insect Thrip ...
- DOI:
- 10.1016/j.jprot.2019.103465
-
https://dx.doi.org/10.1016/j.jprot.2019.103465
- Author:
- Jiang, Shengwang; Liu, Yisong; Shen, Zhenglei; Zhou, Bing; Shen, Qingwu W.
- Source:
- Journal of proteomics 2019 v.205 pp. 103412
- ISSN:
- 1874-3919
- Subject:
- acetylation; apoptosis; bioinformatics; calcium signaling; color; flavor; flavor compounds; gene expression; glucose; glycolysis; inosine monophosphate; lysine; meat; meat quality; mitochondria; muscle contraction; muscle protein; muscles; pH; post-translational modification; proteins; proteolysis; proteomics; quality control; raw meat; rigor mortis; swine; tenderizing
- Abstract:
- ... Protein lysine acetylation is an post-translational modification that regulates gene expression, metabolism, cell signaling, and diseases, but its implication in the postmortem (PM) meat quality development is basically unclear. In the present study, a quantitative proteomic analysis was conducted to profile acetylome in porcine muscle within 24 h PM. In total 595 acetylation sites assigned to 163 ...
- DOI:
- 10.1016/j.jprot.2019.103412
-
https://dx.doi.org/10.1016/j.jprot.2019.103412
- Author:
- Wang, Yangbo; Wang, Feifei; Bao, Xingyue; Fu, Linglin
- Source:
- Journal of proteomics 2019 v.205 pp. 103419
- ISSN:
- 1874-3919
- Subject:
- Shewanella baltica; acetylation; aminoacyl transfer RNA; biosynthesis; cold; cold shock proteins; data collection; databases; enzymes; eukaryotic cells; fatty acid metabolism; lysine; nutrients; post-translational modification; prokaryotic cells; proteins; putrescine; quorum sensing; ribosomes; seafoods; spoilage; storage temperature; surveys; unsaturated fatty acids
- Abstract:
- ... Protein lysine acetylation is a major post-translational modification and plays a critical regulatory role in almost every aspect in both eukaryotes and prokaryotes, yet there have been no data on Shewanella baltica, which is one of the specific spoilage organism (SSO) of aquatic products. Here, we performed the first global acetylproteome analysis of S. baltica. 2929 lysine acetylation sites were ...
- DOI:
- 10.1016/j.jprot.2019.103419
-
https://dx.doi.org/10.1016/j.jprot.2019.103419
- Author:
- Finamore, Francesco; Reny, Jean-Luc; Malacarne, Sarah; Fontana, Pierre; Sanchez, Jean-Charles
- Source:
- Journal of proteomics 2019 v.192 pp. 258-266
- ISSN:
- 1874-3919
- Subject:
- acetylation; aspirin; blood platelets; cardiovascular diseases; diabetes; glucose; glycation; hyperglycemia; mass spectrometry; patients; prostaglandin synthase; proteins; risk factors; serine
- Abstract:
- ... Diabetes is a major risk factor for cardiovascular diseases. Although aspirin is considered a cornerstone of the prevention and treatment of atherothrombotic-related ischemic events, this antiplatelet drug appears to be less effective in patients with poorly controlled diabetes. It has been suggested that the glycation of platelet proteins plays a pivotal role in poor responsiveness to aspirin. Ho ...
- DOI:
- 10.1016/j.jprot.2018.09.007
-
https://dx.doi.org/10.1016/j.jprot.2018.09.007