Quantitative phosphoproteomic analysis of RIP3-dependent protein phosphorylation in the course of TNF-induced necroptosis
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Title
Quantitative phosphoproteomic analysis of RIP3-dependent protein phosphorylation in the course of TNF-induced necroptosis
Authors
Keywords
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Journal
PROTEOMICS
Volume 14, Issue 6, Pages 713-724
Publisher
Wiley
Online
2014-01-23
DOI
10.1002/pmic.201300326
References
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Related references
Note: Only part of the references are listed.- Diverse Sequence Determinants Control Human and Mouse Receptor Interacting Protein 3 (RIP3) and Mixed Lineage Kinase domain-Like (MLKL) Interaction in Necroptotic Signaling
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- Identification of Mechanism That Couples Multisite Phosphorylation of Yes-associated Protein (YAP) with Transcriptional Coactivation and Regulation of Apoptosis
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- Quantitative Phosphoproteomic Analysis of Soybean Root Hairs Inoculated withBradyrhizobium japonicum
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- (2009) YoungSik Cho et al. CELL
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- (2009) Sudan He et al. CELL
- Universal sample preparation method for proteome analysis
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- Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
- (2009) Da Wei Huang et al. Nature Protocols
- RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
- (2009) D.-W. Zhang et al. SCIENCE
- Nonlinear Fitting Method for Determining Local False Discovery Rates from Decoy Database Searches
- (2008) Wilfred H. Tang et al. JOURNAL OF PROTEOME RESEARCH
- Protein Profilings in Mouse Liver Regeneration after Partial Hepatectomy Using iTRAQ Technology
- (2008) Hui-Chu Hsieh et al. JOURNAL OF PROTEOME RESEARCH
- Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
- (2008) Da Wei Huang et al. NUCLEIC ACIDS RESEARCH
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