Proteomics

Dataset Information

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Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as new regulators of cytosolic dsRNA-induced innate immune response


ABSTRACT: In this study, we have used global phosphoproteomic analysis to define phosphorylation-dependent signaling events regulated during RLR stimulation in human keratinocytes. In addition, we used quantitative 14-3-3-affinity capture to identify major target molecules of 14-3-3 regulation.

INSTRUMENT(S): QSTAR

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Keratinocyte

SUBMITTER: Tuula Nyman  

LAB HEAD: Tuula Nyman

PROVIDER: PXD000670 | Pride | 2014-07-08

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
110623hacat_case_emphasis.xml Xml
110623hacat_ctr1.wiff Wiff
110623hacat_ctr1.wiff.scan Wiff
110623hacat_ctr2.wiff Wiff
110623hacat_ctr2.wiff.scan Wiff
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Publications

Phosphoproteomics combined with quantitative 14-3-3-affinity capture identifies SIRT1 and RAI as novel regulators of cytosolic double-stranded RNA recognition pathway.

Öhman Tiina T   Söderholm Sandra S   Hintsanen Petteri P   Välimäki Elina E   Lietzén Niina N   MacKintosh Carol C   Aittokallio Tero T   Matikainen Sampsa S   Nyman Tuula A TA  

Molecular & cellular proteomics : MCP 20140705 10


Viral double-stranded RNA (dsRNA) is the most important viral structure recognized by cytosolic pattern-recognition receptors of the innate immune system, and its recognition results in the activation of signaling cascades that stimulate the production of antiviral cytokines and apoptosis of infected cells. 14-3-3 proteins are ubiquitously expressed regulatory molecules that participate in a variety of cellular processes, and 14-3-3 protein-mediated signaling pathways are activated by cytoplasmi  ...[more]

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