Titlebook: Current Proteomic Approaches Applied to Brain Function; Enrique Santamaría,Joaquín Fernández-Irigoyen Book 2017 Springer Science+Business

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Characterization of the Phosphoproteome and Sialoproteome in Brain Tissues by Mass Spectrometryientists to investigate a large proportion of the proteome in the brain in only short analysis time. Yet, a detailed functional investigation of the intrinsic biochemical processes of the brain by evaluation of the post-translational modifications in proteins is still missing. Phosphorylation and N-

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S-Nitrosylation in Alzheimer’s Disease Using Oxidized Cysteine-Selective cPILOTing apoptotic pathways. In Alzheimer’s disease (AD), SNO can exhibit neuroprotective effects through the inhibition of detrimental enzyme activity. However, in AD SNO is also implicated in mitochondrial dysfunction, neuronal loss, impaired metabolism, and protein misfolding and aggregation. In order

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Applications of Amine-Reactive Tandem Mass Tags (TMT) in Human Neuroproteomicsd, and analyzed by LC-MS/MS. The multiplexing allows different designs and comparisons between the samples. Therefore the method is highly recommendable for, e.g., biomarker discovery in the neuroproteomic field. In this chapter the TMT 10-plex method will be detailed for use with three different br

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Methods for Human Olfactory Bulb Tissue Studies Using Peptide/Protein MALDI-TOF Imaging Mass Spectrohe molecular histology. The peptide/protein MALDI-IMS studies of neural structures such as OB are hampered by its very soft consistency and large amounts of lipids in these tissues. In this chapter, we describe how to analyze OB protein/peptide signals employing the MALDI-IMS. To circumvent the limi

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Neuroproteomics Using Short GeLC-SWATH: From the Evaluation of Proteome Changes to the Clarificationon, namely, its high efficiency and compatibility, in a very reproducible method that proves to be particularly advantageous for quantitative mass spectrometry analyses. Moreover, the short GeLC approach combined with SWATH acquisition has been revealed as a promising method for reliable quantitativ

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Characterization of the Phosphoproteome and Sialoproteome in Brain Tissues by Mass Spectrometryly enrich these low abundant protein modifications from the high abundant nonmodified peptides and from the very lipid-rich brain material..Here, we describe how a highly selective, sensitive, low hands-on-time and cost-effective simultaneous enrichment of phosphorylated peptides, sialylated N-linke

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