Advances in characterizing ubiquitylation sites by mass spectrometry

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Advances in characterizing ubiquitylation sites by mass spectrometry. / Sylvestersen, K.B.; Young, C.; Nielsen, M.L.

In: Current Opinion in Chemical Biology, Vol. 17, No. 1, 05.01.2013, p. 49-58.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sylvestersen, KB, Young, C & Nielsen, ML 2013, 'Advances in characterizing ubiquitylation sites by mass spectrometry', Current Opinion in Chemical Biology, vol. 17, no. 1, pp. 49-58. https://doi.org/10.1016/j.cbpa.2012.12.009

APA

Sylvestersen, K. B., Young, C., & Nielsen, M. L. (2013). Advances in characterizing ubiquitylation sites by mass spectrometry. Current Opinion in Chemical Biology, 17(1), 49-58. https://doi.org/10.1016/j.cbpa.2012.12.009

Vancouver

Sylvestersen KB, Young C, Nielsen ML. Advances in characterizing ubiquitylation sites by mass spectrometry. Current Opinion in Chemical Biology. 2013 Jan 5;17(1):49-58. https://doi.org/10.1016/j.cbpa.2012.12.009

Author

Sylvestersen, K.B. ; Young, C. ; Nielsen, M.L. / Advances in characterizing ubiquitylation sites by mass spectrometry. In: Current Opinion in Chemical Biology. 2013 ; Vol. 17, No. 1. pp. 49-58.

Bibtex

@article{f1cf1810f6644141b02831364b2e9996,
title = "Advances in characterizing ubiquitylation sites by mass spectrometry",
abstract = "The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a two-fold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.",
author = "K.B. Sylvestersen and C. Young and M.L. Nielsen",
year = "2013",
month = jan,
day = "5",
doi = "10.1016/j.cbpa.2012.12.009",
language = "English",
volume = "17",
pages = "49--58",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",
publisher = "Elsevier Ltd. * Current Opinion Journals",
number = "1",

}

RIS

TY - JOUR

T1 - Advances in characterizing ubiquitylation sites by mass spectrometry

AU - Sylvestersen, K.B.

AU - Young, C.

AU - Nielsen, M.L.

PY - 2013/1/5

Y1 - 2013/1/5

N2 - The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a two-fold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.

AB - The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a two-fold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.

UR - http://www.scopus.com/inward/record.url?scp=84875252687&partnerID=8YFLogxK

U2 - 10.1016/j.cbpa.2012.12.009

DO - 10.1016/j.cbpa.2012.12.009

M3 - Journal article

AN - SCOPUS:84875252687

VL - 17

SP - 49

EP - 58

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

SN - 1367-5931

IS - 1

ER -

ID: 46438909