Proteomics

Dataset Information

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Thermal proteome profiling of cell cycle

ABSTRACT: We combined quantitative mass spectrometry with thermal profiling to systematically analyze the thermal stability and solubility of proteins during the eukaryotic cell cycle on a proteome-wide scale.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Andre Mateus  

LAB HEAD: Mikhail M. Savitski

PROVIDER: PXD008646 | Pride | 2018-05-02

REPOSITORIES: Pride

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160815_S075_IB_Cycle_rep2_37_R1_F1.raw Raw
160815_S075_IB_Cycle_rep2_37_R1_F10.raw Raw
160815_S075_IB_Cycle_rep2_37_R1_F11.raw Raw
160815_S075_IB_Cycle_rep2_37_R1_F12.raw Raw
160815_S075_IB_Cycle_rep2_37_R1_F2.raw Raw
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Publications

Quantitative mass spectrometry has established proteome-wide regulation of protein abundance and post-translational modifications in various biological processes. Here, we used quantitative mass spectrometry to systematically analyze the thermal stability and solubility of proteins on a proteome-wide scale during the eukaryotic cell cycle. We demonstrate pervasive variation of these biophysical parameters with most changes occurring in mitosis and G1. Various cellular pathways and components var  ...[more]

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