Proteomics

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Deep chemoproteomic analysis of LPS-stimulated RAW264.7 cell proteome

ABSTRACT: Unanticipated regulatory protein modifications can be discovered from the unbiased comprehensive analysis of biological systems using SAMPEI. To explore this idea, we sought to map protein modifications induced during mammalian cell differentiation, modeled by the response of mouse RAW264.7 macrophage cells to lipopolysaccharide (LPS), a potent inducer of macrophage activation and differentiation that involves extensive protein and metabolic signaling.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Suspension Culture, Macrophage

SUBMITTER: Alex Kentsis  

LAB HEAD: Alex Kentsis

PROVIDER: PXD019853 | Pride | 2021-07-22

REPOSITORIES: pride

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MS205975QEHF_Alex_Kentsis_RAW264p7_LPS_tryp_SCX_F1.raw Raw
MS205975QEHF_Alex_Kentsis_RAW264p7_LPS_tryp_SCX_F10.raw Raw
MS205975QEHF_Alex_Kentsis_RAW264p7_LPS_tryp_SCX_F10_20191112053440.raw Raw
MS205975QEHF_Alex_Kentsis_RAW264p7_LPS_tryp_SCX_F11.raw Raw
MS205975QEHF_Alex_Kentsis_RAW264p7_LPS_tryp_SCX_F12.raw Raw
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Publications

Discovery of Protein Modifications Using Differential Tandem Mass Spectrometry Proteomics.

Cifani Paolo P   Li Zhi Z   Luo Danmeng D   Grivainis Mark M   Intlekofer Andrew M AM   Fenyö David D   Kentsis Alex A  

Journal of proteome research 20210322 4

Recent studies have revealed diverse amino acid, post-translational, and noncanonical modifications of proteins in diverse organisms and tissues. However, their unbiased detection and analysis remain hindered by technical limitations. Here, we present a spectral alignment method for the identification of protein modifications using high-resolution mass spectrometry proteomics. Termed SAMPEI for spectral alignment-based modified peptide identification, this open-source algorithm is designed for t  ...[more]

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