Dataset Information

Mammalian proteome changes during oxidative stress and stress of the endoplasmic reticulum

ABSTRACT: Stress due to protein misfolding in the endoplasmic reticulum affects transcription and translation, RNA and protein degradation. By integrating several large-scale datasets, we quantified transcription, translation, RNA-protein binding events, and protein levels for several thousands of genes in HeLa cells. Here, we deposit the TMT-based, quantitative proteomics data consisting of two replicates with four measured time points collected for two stress treatments, i.e. tunicamycin and hydrogen peroxide.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Shuvadeep Maity

LAB HEAD: Christine Vogel

PROVIDER: PXD008575 | Pride | 2018-10-11

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	080416_Q_jrc_Vogel_TMT01.raw	Raw
	080416_Q_jrc_Vogel_TMT02.raw	Raw
	080416_Q_jrc_Vogel_TMT03.raw	Raw
	080416_Q_jrc_Vogel_TMT04.raw	Raw
	080416_Q_jrc_Vogel_TMT05.raw	Raw

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Publications

New insights into the cellular temporal response to proteostatic stress.

Rendleman Justin J Cheng Zhe Z Maity Shuvadeep S Kastelic Nicolai N Munschauer Mathias M Allgoewer Kristina K Teo Guoshou G Zhang Yun Bin Matteo YBM Lei Amy A Parker Brian B Parker Brian B Landthaler Markus M Freeberg Lindsay L Kuersten Scott S Choi Hyungwon H Vogel Christine C

eLife 20181012

Maintaining a healthy proteome involves all layers of gene expression regulation. By quantifying temporal changes of the transcriptome, translatome, proteome, and RNA-protein interactome in cervical cancer cells, we systematically characterize the molecular landscape in response to proteostatic challenges. We identify shared and specific responses to misfolded proteins and to oxidative stress, two conditions that are tightly linked. We reveal new aspects of the unfolded protein response, includi ...[more]

PMID: 30272558

Dataset Information

Mammalian proteome changes during oxidative stress and stress of the endoplasmic reticulum

Dataset's files

Publications

New insights into the cellular temporal response to proteostatic stress.

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