Issue 8, 2010
From the journal:

Molecular BioSystems

Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry†

Sarah Pelletier,ab   Karianne G. Schuurman,c   Celia R. Berkers,bc   Huib Ovaa,bc   Albert J. R. Heck*ab  and  Reinout Raijmakers*ab  

* Corresponding authors

a Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands
E-mail: r.raijmakers@uu.nl, a.j.r.heck@uu.nl

b Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, The Netherlands

c Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX, Amsterdam, The Netherlands

Abstract

The composition of 20S mouse proteasome complexes isolated from mice heart, kidney, liver, lung, thymus and spleen was compared using quantitative mass spectrometry. Significant variety was observed in hybrid classes of immunoproteasomes which may have implications for the use of proteasome targeted inhibitors.

Graphical abstract: Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry

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Article information

DOI
https://doi.org/10.1039/C004989A
Article type
Communication
Submitted
09 Apr 2010
Accepted
13 May 2010
First published
24 May 2010

Mol. BioSyst., 2010,6, 1450-1453

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Quantifying cross-tissue diversity in proteasome complexes by mass spectrometry

S. Pelletier, K. G. Schuurman, C. R. Berkers, H. Ovaa, A. J. R. Heck and R. Raijmakers, Mol. BioSyst., 2010, 6, 1450 DOI: 10.1039/C004989A

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