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Protein Acetylation

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Cover of 'Protein Acetylation'

Table of Contents

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    Book Overview
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    Chapter 1 Validation of Protein Acetylation by Mass Spectrometry
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    Chapter 2 Protein Acetylation
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    Chapter 3 Application of the MIDAS Approach for Analysis of Lysine Acetylation Sites.
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    Chapter 4 Application of high content biology to yield quantitative spatial proteomic information on protein acetylations.
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    Chapter 5 Towards the N-Terminal Acetylome: An N-Terminal Acetylated Peptide Enrichment Method Using CNBr-Activated Sepharose Resin
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    Chapter 6 Identification and Analysis of O -Acetylated Sialoglycoproteins
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    Chapter 7 HPLC-Based Quantification of In Vitro N-Terminal Acetylation
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    Chapter 8 Separation and Purification of Multiply Acetylated Proteins Using Cation-Exchange Chromatography
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    Chapter 9 In-Gel N-Acetylation for the Quantification of the Degree of Protein In Vivo N-Terminal Acetylation
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    Chapter 10 Computational Prediction of Lysine Acetylation Proteome-Wide
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    Chapter 11 Generation and Characterization of Pan-Specific Anti-acetyllysine Antibody
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    Chapter 12 Using Functional Proteome Microarrays to Study Protein Lysine Acetylation
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    Chapter 13 Quantitation of Nucleosome Acetylation and Other Histone Posttranslational Modifications Using Microscale NU-ELISA
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    Chapter 14 Preparing Semisynthetic and Fully Synthetic Histones H3 and H4 to Modify the Nucleosome Core
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    Chapter 15 Production of Amino-Terminally Acetylated Recombinant Proteins in E. coli
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    Chapter 16 Identification of Lysine Acetyltransferase Substrates Using Bioorthogonal Chemical Proteomics
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    Chapter 17 Nonradioactive In Vitro Assays for Histone Deacetylases
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    Chapter 18 The Fluorescence-Based Acetylation Assay Using Thiol-Sensitive Probes
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    Chapter 19 Analysis of Protein Acetyltransferase Structure–Function Relation by Surface-Enhanced Raman Scattering (SERS): A Tool to Screen and Characterize Small Molecule Modulators
Attention for Chapter 12: Using Functional Proteome Microarrays to Study Protein Lysine Acetylation
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Chapter title
Using Functional Proteome Microarrays to Study Protein Lysine Acetylation
Chapter number 12
Book title
Protein Acetylation
Published in
Methods in molecular biology, January 2013
DOI 10.1007/978-1-62703-305-3_12
Pubmed ID
Book ISBNs
978-1-62703-304-6, 978-1-62703-305-3
Authors

Jin-ying Lu, Yu-yi Lin, Jef D. Boeke, Heng Zhu

Abstract

Emergence of proteome microarray provides a versatile platform to globally explore biological functions of broad significance. In the past decade, researchers have successfully fabricated functional proteome microarrays by printing individually purified proteins at a high-throughput, proteome-wide scale on one single slide. These arrays have been used to profile protein posttranslational modifications, including phosphorylation, ubiquitylation, acetylation, and nitrosylation. In this chapter, we summarize our work of using the yeast proteome microarrays to connect protein lysine acetylation substrates to their upstream modifying enzyme, the nucleosome acetyltransferase of H4 (NuA4), which is the only essential acetyltransferase in yeast. We further prove that the reversible acetylation on critical cell metabolism-related enzymes controls life span in yeast. Our studies represent a paradigm shift for the functional dissection of a crucial acetylation enzyme affecting aging and longevity pathways.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 17%
Unknown 5 83%

Demographic breakdown

Readers by professional status Count As %
Professor 2 33%
Researcher 2 33%
Student > Ph. D. Student 1 17%
Unknown 1 17%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 33%
Biochemistry, Genetics and Molecular Biology 1 17%
Chemistry 1 17%
Medicine and Dentistry 1 17%
Unknown 1 17%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 08 March 2013.
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#18,331,227
of 22,699,621 outputs
Outputs from Methods in molecular biology
#7,845
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Outputs of similar age
#217,982
of 280,695 outputs
Outputs of similar age from Methods in molecular biology
#220
of 340 outputs
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