MALDI-TOF and nESI Orbitrap MS/MS identify orthogonal parts of the phosphoproteome-Reference-Cited by-同舟云学术

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MALDI-TOF and nESI Orbitrap MS/MS identify orthogonal parts of the phosphoproteome

Published:2016-05 Issue:10 Volume:16 Page:1447-1456
ISSN:1615-9853
Container-title:PROTEOMICS
language:en
Short-container-title:Proteomics

Author:

Ruprecht Benjamin¹²,Roesli Christoph³⁴,Lemeer Simone¹²,Kuster Bernhard¹²⁴⁵⁶

Affiliation:

1. Chair of Proteomics and Bioanalytics; Technische Universität München; Freising Germany

2. Center for Protein Science Munich (CIPSM); Freising Germany

3. HI-STEM - Heidelberg; Institute for Stem Cell Technology and Experimental Medicine gemeinnützige GmbH; Heidelberg Germany

4. German Cancer Research Center (DKFZ); Heidelberg Germany

5. German Cancer Consortium (DKTK); Heidelberg Germany

6. Bavarian Biomolecular Mass Spectrometry Center; Technische Universität München; Freising Germany

Funder

for integrated Protein Research Munich (CiPSM)

German Cancer Consortium (DKTK)

German Cancer Research Center (DKFZ)

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference45 articles.

1. SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma;Fernández-Sáiz;Nat. Cell Biol.,2013

2. Proteomic analysis of phosphorylation in cancer;Ruprecht;Expert Rev. Proteomics,2014

3. Mass-spectrometry-based draft of the human proteome;Wilhelm;Nature,2014

4. Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling;Sharma;Cell Rep.,2014

5. Status of large-scale analysis of post-translational modifications by mass spectrometry;Olsen;Mol. Cell. Proteomics,2013

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