Proteomics

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Thermal proteome profiling in of CA-074me

ABSTRACT: We performed thermal proteome profiling (TPP) to study changes to protein thermal stability and abundance of CA-074me (cathepsin inhibitor) in RAW264.7 macrophages after Salmonella typhimurium infection.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Salmonella Typhimurium (strain Lt2 / Sgsc1412 / Atcc 700720) Mus Musculus (mouse)

TISSUE(S): Macrophage

SUBMITTER: Andre Mateus  

LAB HEAD: Athanasios Typas

PROVIDER: PXD016086 | Pride | 2020-02-07

REPOSITORIES: Pride

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Bert_S1652_AM_JS_2DTPP_cathepsin_inh_T1T2_n1_R1_F1.raw Raw
Bert_S1652_AM_JS_2DTPP_cathepsin_inh_T1T2_n1_R1_F10.raw Raw
Bert_S1652_AM_JS_2DTPP_cathepsin_inh_T1T2_n1_R1_F11.raw Raw
Bert_S1652_AM_JS_2DTPP_cathepsin_inh_T1T2_n1_R1_F12.raw Raw
Bert_S1652_AM_JS_2DTPP_cathepsin_inh_T1T2_n1_R1_F2.raw Raw
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Publications

The interplay between host and pathogen relies heavily on rapid protein synthesis and accurate protein targeting to ensure pathogen destruction. To gain insight into this dynamic interface, we combined Click chemistry with pulsed stable isotope labelling of amino acids in cell culture to quantify the host proteome response during macrophage infection with the intracellular bacterial pathogen Salmonella enterica Typhimurium. We monitored newly synthesized proteins across different host cell compa  ...[more]

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