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Biochemical and mass spectrometry-based approaches to profile SUMOylation in human cells

Abstract:

Posttranslational modification of proteins with the small ubiquitin-like modifier (SUMO) regulates protein function in the context of cell cycle and DNA repair. The occurrence of SUMOylation is less frequent as compared to protein modification with ubiquitin, and appears to be controlled by a smaller pool of conjugating and deconjugating enzymes. Mass spectrometry has been instrumental in defining specific as well as proteome-wide views of SUMO-dependent biological processes, and several meth...

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Publication status:
In press
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Target Discovery Institute
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Target Discovery Institute
Role:
Author

Contributors

Role:
Editor
Role:
Editor
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Funding agency for:
Kessler, B
Grant:
097813/Z/11/Z
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Funding agency for:
Kessler, B
Grant:
097813/Z/11/Z
More from this funder
Funding agency for:
Kessler, B
Grant:
097813/Z/11/Z
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Funding agency for:
Bursomanno, S
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Publisher:
Springer New York Publisher's website
Volume:
1491
Pages:
131-144
Series:
Methods in Molecular Biology
Host title:
Methods in Molecular Biology
Publication date:
2017-01-01
DOI:
ISSN:
1064-3745
Source identifiers:
656777
ISBN:
9781493964390
Language:
English
Keywords:
Pubs id:
pubs:656777
UUID:
uuid:8a4dfeff-dc0c-4435-90a0-4f9ad082537d
Local pid:
pubs:656777
Deposit date:
2016-11-05

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