Large-Scale Identification of the Arginine Methylome by Mass Spectrometry

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Large-Scale Identification of the Arginine Methylome by Mass Spectrometry. / Sylvestersen, Kathrine B; Nielsen, Michael L.

Current Protocols in Protein Science. Vol. 82 2015. (Current Protocols in Protein Science).

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearchpeer-review

Harvard

Sylvestersen, KB & Nielsen, ML 2015, Large-Scale Identification of the Arginine Methylome by Mass Spectrometry. in Current Protocols in Protein Science. vol. 82, Current Protocols in Protein Science. https://doi.org/10.1002/0471140864.ps2407s82

APA

Sylvestersen, K. B., & Nielsen, M. L. (2015). Large-Scale Identification of the Arginine Methylome by Mass Spectrometry. In Current Protocols in Protein Science (Vol. 82). Current Protocols in Protein Science https://doi.org/10.1002/0471140864.ps2407s82

Vancouver

Sylvestersen KB, Nielsen ML. Large-Scale Identification of the Arginine Methylome by Mass Spectrometry. In Current Protocols in Protein Science. Vol. 82. 2015. (Current Protocols in Protein Science). https://doi.org/10.1002/0471140864.ps2407s82

Author

Sylvestersen, Kathrine B ; Nielsen, Michael L. / Large-Scale Identification of the Arginine Methylome by Mass Spectrometry. Current Protocols in Protein Science. Vol. 82 2015. (Current Protocols in Protein Science).

Bibtex

@inbook{0f5b59dde65349aa929df71c8a1989d2,
title = "Large-Scale Identification of the Arginine Methylome by Mass Spectrometry",
abstract = "The attachment of one or more methylation groups to the side chain of arginine residues is a regulatory mechanism for cellular proteins. Recent advances in mass spectrometry-based characterization allow comprehensive identification of arginine methylation sites by peptide-level enrichment strategies. Described in this unit is a 4-day protocol for enrichment of arginine-methylated peptides and subsequent identification of thousands of distinct sites by mass spectrometry. Specifically, the protocol explains step-by-step sample preparation, enrichment using commercially available antibodies, prefractionation using strong cation exchange, and identification using liquid chromatography coupled to tandem mass spectrometry. A strategy for relative quantification is described using stable isotope labeling by amino acids in cell culture (SILAC). Approaches for analysis of arginine methylation site occupancy are also discussed. Collectively, the unit describes the essential parameters required for a successful and comprehensive experiment detailing the arginine methylome. {\circledC} 2015 by John Wiley & Sons, Inc.",
author = "Sylvestersen, {Kathrine B} and Nielsen, {Michael L}",
note = "Copyright {\circledC} 2015 John Wiley & Sons, Inc.",
year = "2015",
month = "11",
day = "2",
doi = "10.1002/0471140864.ps2407s82",
language = "English",
volume = "82",
series = "Current Protocols in Protein Science",
publisher = "JohnWiley & Sons, Inc.",
booktitle = "Current Protocols in Protein Science",

}

RIS

TY - CHAP

T1 - Large-Scale Identification of the Arginine Methylome by Mass Spectrometry

AU - Sylvestersen, Kathrine B

AU - Nielsen, Michael L

N1 - Copyright © 2015 John Wiley & Sons, Inc.

PY - 2015/11/2

Y1 - 2015/11/2

N2 - The attachment of one or more methylation groups to the side chain of arginine residues is a regulatory mechanism for cellular proteins. Recent advances in mass spectrometry-based characterization allow comprehensive identification of arginine methylation sites by peptide-level enrichment strategies. Described in this unit is a 4-day protocol for enrichment of arginine-methylated peptides and subsequent identification of thousands of distinct sites by mass spectrometry. Specifically, the protocol explains step-by-step sample preparation, enrichment using commercially available antibodies, prefractionation using strong cation exchange, and identification using liquid chromatography coupled to tandem mass spectrometry. A strategy for relative quantification is described using stable isotope labeling by amino acids in cell culture (SILAC). Approaches for analysis of arginine methylation site occupancy are also discussed. Collectively, the unit describes the essential parameters required for a successful and comprehensive experiment detailing the arginine methylome. © 2015 by John Wiley & Sons, Inc.

AB - The attachment of one or more methylation groups to the side chain of arginine residues is a regulatory mechanism for cellular proteins. Recent advances in mass spectrometry-based characterization allow comprehensive identification of arginine methylation sites by peptide-level enrichment strategies. Described in this unit is a 4-day protocol for enrichment of arginine-methylated peptides and subsequent identification of thousands of distinct sites by mass spectrometry. Specifically, the protocol explains step-by-step sample preparation, enrichment using commercially available antibodies, prefractionation using strong cation exchange, and identification using liquid chromatography coupled to tandem mass spectrometry. A strategy for relative quantification is described using stable isotope labeling by amino acids in cell culture (SILAC). Approaches for analysis of arginine methylation site occupancy are also discussed. Collectively, the unit describes the essential parameters required for a successful and comprehensive experiment detailing the arginine methylome. © 2015 by John Wiley & Sons, Inc.

U2 - 10.1002/0471140864.ps2407s82

DO - 10.1002/0471140864.ps2407s82

M3 - Book chapter

C2 - 26521714

VL - 82

T3 - Current Protocols in Protein Science

BT - Current Protocols in Protein Science

ER -

ID: 176889772