Journal home
Advance online publication
Current issue
Archive
Press releases
Methagora
Focuses
Guide to authors
Online submissionOnline submission
Permissions
For referees
Free online issue
Contact the journal
Subscribe
naturejobs
For Advertisers
work@npg
naturereprints
About this site
For librarians
Application notes
 
NPG Resources
Nature
Nature Biotechnology
Nature Protocols
Nature Genetics
Nature Chemical Biology
Nature Cell Biology
Nature Neuroscience
Nature Reviews Genetics
Nature Reviews Molecular Cell Biology
Nature Reviews Drug Discovery
Nature Conferences
NPG Subject areas
Biotechnology
Cancer
Chemistry
Clinical Medicine
Dentistry
Development
Drug Discovery
Earth Sciences
Evolution & Ecology
Genetics
Immunology
Materials Science
Medical Research
Microbiology
Molecular Cell Biology
Neuroscience
Pharmacology
Physics
Browse all publications
Review
Focus on RNA interference - A user�s guide
Contents Foreword Commentaries Reviews
Perspectives Glossary NPG Library Feedback


Nature Methods - 4, 798 - 806 (2007)
Published online: 27 September 2007; | doi:10.1038/nmeth1100

Mapping protein post-translational modifications with mass spectrometry

Eric S Witze1, 3, William M Old1, 3, Katheryn A Resing1 & Natalie G Ahn1, 2

1  Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA.

2  Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA.

3  These authors contributed equally to this work.

Correspondence should be addressed to Natalie G Ahn natalie.ahn@colorado.edu

Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry–based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.

MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

NEWS AND VIEWS

Phosphoproteomics finds its timing

Nature Biotechnology News and Views (01 Sep 2004)

Toward the phosphoproteome

Nature Biotechnology Research News (01 Apr 2001)

See all 3 matches for News And Views
 Top
Abstract
Previous | Next
Table of contents
Full textFull text
Download PDFDownload PDF
Send to a friendSend to a friend
rights and permissionsRights and permissions
Order commercial reprintsOrder commercial reprints
CrossRef lists 290 articles citing this articleCrossRef lists 290 articles citing this article
Save this linkSave this link
Figures & Tables
Export citation

naturejobs

natureevents

natureproducts

Search buyers guide:

ADVERTISEMENT

 
Nature Methods
ISSN: 1548-7091
EISSN: 1548-7105
Journal home | Current issue | Archive | Press releases |
Nature Publishing Group, publisher of Nature, and other science journals and reference works©2007 Nature Publishing Group | Privacy policy