MassIVE MSV000080772

Imported Reanalysis Dataset Public PXD003514

SILAC-based quantitative Nox4-Co-immunoprecipitation

Description

Within the family of NADPH oxidases, Nox4 is unique as it is predominantly localized in the endoplasmic reticulum, has constitutive activity and generates H2O2. We hypothesize that these features are consequences of a so far unidentified Nox4-interacting protein. Interacting proteins were screened by quantitative SILAC-Co-immunoprecipitation in HEK293 cells stably overexpressing Nox4. By this technique, several interacting proteins were identified with calnexin showing the most robust interaction. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: SILAC ; LC-MSMS ; macromolecular complexes ; Co-immunoprecipitation

Contact

Principal Investigators:
(in alphabetical order)
Ralf Brandes, Institut f�r Kardiovaskul�re Physiologie, Goethe-Universit�t, Frankfurt am Main, Germany, N/A
Submitting User: ccms

Publications

Prior KK, Wittig I, Leisegang MS, Groenendyk J, Weissmann N, Michalak M, Jansen-Dürr P, Shah AM, Brandes RP.
The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein.
J. Biol. Chem. 2016 Mar 25;291(13):7045-59. Epub 2016 Mar 9.

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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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This dataset may not contain all raw spectra data as originally deposited in PRIDE. It has been imported to MassIVE for reanalysis purposes, so its spectra data here may consist solely of processed peak lists suitable for reanalysis with most software.