Proteomics

Dataset Information

0

Hs_U1snRNP_AD

ABSTRACT: U1 Small Nuclear Ribonucleoprotein Complex and RNA Splicing Alterations in Alzheimer Disease

REANALYSIS of: PXD000067

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

SUBMITTER: Bai B, et al. 

PROVIDER: PAe005157 | PeptideAtlas | 2013-12-31

REPOSITORIES: PeptideAtlas

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Publications

U1 small nuclear ribonucleoprotein complex and RNA splicing alterations in Alzheimer's disease.

Bai Bing B   Hales Chadwick M CM   Chen Ping-Chung PC   Gozal Yair Y   Dammer Eric B EB   Fritz Jason J JJ   Wang Xusheng X   Xia Qiangwei Q   Duong Duc M DM   Street Craig C   Cantero Gloria G   Cheng Dongmei D   Jones Drew R DR   Wu Zhiping Z   Li Yuxin Y   Diner Ian I   Heilman Craig J CJ   Rees Howard D HD   Wu Hao H   Lin Li L   Szulwach Keith E KE   Gearing Marla M   Mufson Elliott J EJ   Bennett David A DA   Montine Thomas J TJ   Seyfried Nicholas T NT   Wingo Thomas S TS   Sun Yi E YE   Jin Peng P   Hanfelt John J   Willcock Donna M DM   Levey Allan A   Lah James J JJ   Peng Junmin J  

Proceedings of the National Academy of Sciences of the United States of America 20130910 41

Deposition of insoluble protein aggregates is a hallmark of neurodegenerative diseases. The universal presence of β-amyloid and tau in Alzheimer's disease (AD) has facilitated advancement of the amyloid cascade and tau hypotheses that have dominated AD pathogenesis research and therapeutic development. However, the underlying etiology of the disease remains to be fully elucidated. Here we report a comprehensive study of the human brain-insoluble proteome in AD by mass spectrometry. We identify 4  ...[more]

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