Data on multiple post-translational modifications in Alzheimer's disease

Q4 Neuroscience Neuroscience Research Notes Pub Date : 2022-06-10 DOI:10.31117/neuroscirn.v5i2.153
Sayali Chandrashekhar Deolankar, Shashanka G Koyangana, Arun H. Patil, Yashwanth Subbannayya, P. K. Modi, T. Prasad
{"title":"Data on multiple post-translational modifications in Alzheimer's disease","authors":"Sayali Chandrashekhar Deolankar, Shashanka G Koyangana, Arun H. Patil, Yashwanth Subbannayya, P. K. Modi, T. Prasad","doi":"10.31117/neuroscirn.v5i2.153","DOIUrl":null,"url":null,"abstract":"This article describes the data obtained for global post-translational modifications (PTMs) profiled for Alzheimer's Disease (AD) from two distinct human brain regions and one cerebrospinal fluid (CSF) sample. The PTM profiling was performed to identify phosphorylation, O-GluNAcetylation, methylation, acetylation and citrullination using three publicly available LC-MS/MS raw data sets (PRIDE ID: PXD004010, PXD002516, PXD004863). A total of 1,857 PTM harbouring proteins with 4,961 unique post-translationally modified peptides were identified. Among the modified peptides, 75 corresponded uniquely to proteins identified from CSF samples. The data is related to the research article \"Dissecting Alzheimer's disease molecular substrates by proteomics and discovery of novel post-translational modifications (PTMs)\".","PeriodicalId":36108,"journal":{"name":"Neuroscience Research Notes","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Neuroscience Research Notes","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.31117/neuroscirn.v5i2.153","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Neuroscience","Score":null,"Total":0}
引用次数: 0

Abstract

This article describes the data obtained for global post-translational modifications (PTMs) profiled for Alzheimer's Disease (AD) from two distinct human brain regions and one cerebrospinal fluid (CSF) sample. The PTM profiling was performed to identify phosphorylation, O-GluNAcetylation, methylation, acetylation and citrullination using three publicly available LC-MS/MS raw data sets (PRIDE ID: PXD004010, PXD002516, PXD004863). A total of 1,857 PTM harbouring proteins with 4,961 unique post-translationally modified peptides were identified. Among the modified peptides, 75 corresponded uniquely to proteins identified from CSF samples. The data is related to the research article "Dissecting Alzheimer's disease molecular substrates by proteomics and discovery of novel post-translational modifications (PTMs)".
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
阿尔茨海默病中多种翻译后修饰的数据
本文描述了从两个不同的人脑区域和一个脑脊液样本中获得的阿尔茨海默病(AD)的全局翻译后修饰(PTM)数据。使用三个公开可用的LC-MS/MS原始数据集(PRIDE ID:PXD004010、PXD002516、PXD004863)进行PTM分析以鉴定磷酸化、O-谷氨酸乙酰化、甲基化、乙酰化和瓜氨酸化。共鉴定出1857个含有蛋白质的PTM和4961个独特的翻译后修饰肽。在修饰的肽中,75个与从CSF样品中鉴定的蛋白质唯一对应。这些数据与研究文章“通过蛋白质组学解析阿尔茨海默病分子底物和发现新的翻译后修饰(PTM)”有关。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Neuroscience Research Notes
Neuroscience Research Notes Neuroscience-Neurology
CiteScore
1.00
自引率
0.00%
发文量
21
期刊最新文献
Comparative retrospective analysis: exploring the quality of life of people with epilepsy in two cohorts Default mode network perturbations in Alzheimer's disease: an fMRI study in Klang Valley, Malaysia Gene expression analysis in plasma of patients with Alzheimer's disease Psychological science in Mongolia: Its history, development, and future prospects Neuroinflammation-induced neurodegeneration and associated microglia activation in Parkinson’s disease: a novel neurotherapeutic avenue
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1