Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/93878
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Type: Journal article
Title: Comprehensive identification of proteins from MALDI imaging
Author: Maier, S.
Hahne, H.
Gholami, A.
Balluff, B.
Meding, S.
Schoene, C.
Walch, A.
Kuster, B.
Citation: Molecular and Cellular Proteomics, 2013; 12(10):2901-2910
Publisher: American Society for Biochemistry and Molecular Biology
Issue Date: 2013
ISSN: 1535-9476
1535-9484
Statement of
Responsibility: 
Stefan K. Maier, Hannes Hahne, Amin Moghaddas Gholami, Benjamin Balluff, Stephan Meding, Cedrik Schoene, Axel K. Walch, and Bernhard Kuster
Abstract: Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) is a powerful tool for the visualization of proteins in tissues and has demonstrated considerable diagnostic and prognostic value. One main challenge is that the molecular identity of such potential biomarkers mostly remains unknown. We introduce a generic method that removes this issue by systematically identifying the proteins embedded in the MALDI matrix using a combination of bottom-up and top-down proteomics. The analyses of ten human tissues lead to the identification of 1400 abundant and soluble proteins constituting the set of proteins detectable by MALDI IMS including >90% of all IMS biomarkers reported in the literature. Top-down analysis of the matrix proteome identified 124 mostly N- and C-terminally fragmented proteins indicating considerable protein processing activity in tissues. All protein identification data from this study as well as the IMS literature has been deposited into MaTisse, a new publically available database, which we anticipate will become a valuable resource for the IMS community.
Keywords: Proteomics
Rights: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
RMID: 0030028655
DOI: 10.1074/mcp.M113.027599
Appears in Collections:Molecular and Biomedical Science publications

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