The characterization of protein post-translational modifications by mass spectrometry

Claire Eyers; Rebecca E. Schweppe; Claire E. Haydon; Timothy S. Lewis; Katheryn A. Resing; Natalie G. Ahn

doi:10.1021/ar020143l

The characterization of protein post-translational modifications by mass spectrometry

Claire Eyers, Rebecca E. Schweppe, Claire E. Haydon, Timothy S. Lewis, Katheryn A. Resing, Natalie G. Ahn

Research output: Contribution to journal › Article › peer-review

Abstract

Most biological processes are regulated by post-translational modifications of proteins, and conditions that disrupt the regulation of such events can lead to disease, In the past decade, the identification and characterization of covalent modifications have been driven by advances in mass spectrometry. Here, we discuss current mass spectrometric and proteomic approaches for the identification of proteins and their covalent modifications, and we highlight high-throughput strategies for comprehensive analysis of cell proteomes.

Original language	English
Pages (from-to)	453-461
Number of pages	8
Journal	Accounts of Chemical Research
Volume	36
Issue number	6
DOIs	https://doi.org/10.1021/ar020143l
Publication status	Published - 1 Jun 2003

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title = "The characterization of protein post-translational modifications by mass spectrometry",

abstract = "Most biological processes are regulated by post-translational modifications of proteins, and conditions that disrupt the regulation of such events can lead to disease, In the past decade, the identification and characterization of covalent modifications have been driven by advances in mass spectrometry. Here, we discuss current mass spectrometric and proteomic approaches for the identification of proteins and their covalent modifications, and we highlight high-throughput strategies for comprehensive analysis of cell proteomes.",

author = "Claire Eyers and Schweppe, {Rebecca E.} and Haydon, {Claire E.} and Lewis, {Timothy S.} and Resing, {Katheryn A.} and Ahn, {Natalie G.}",

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AU - Schweppe, Rebecca E.

AU - Haydon, Claire E.

AU - Lewis, Timothy S.

AU - Resing, Katheryn A.

AU - Ahn, Natalie G.

PY - 2003/6/1

Y1 - 2003/6/1

N2 - Most biological processes are regulated by post-translational modifications of proteins, and conditions that disrupt the regulation of such events can lead to disease, In the past decade, the identification and characterization of covalent modifications have been driven by advances in mass spectrometry. Here, we discuss current mass spectrometric and proteomic approaches for the identification of proteins and their covalent modifications, and we highlight high-throughput strategies for comprehensive analysis of cell proteomes.

AB - Most biological processes are regulated by post-translational modifications of proteins, and conditions that disrupt the regulation of such events can lead to disease, In the past decade, the identification and characterization of covalent modifications have been driven by advances in mass spectrometry. Here, we discuss current mass spectrometric and proteomic approaches for the identification of proteins and their covalent modifications, and we highlight high-throughput strategies for comprehensive analysis of cell proteomes.

U2 - 10.1021/ar020143l

DO - 10.1021/ar020143l

M3 - Article

SN - 0001-4842

VL - 36

SP - 453

EP - 461

JO - Accounts of Chemical Research

JF - Accounts of Chemical Research

IS - 6

ER -

The characterization of protein post-translational modifications by mass spectrometry

Abstract

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