Protein Acetylation Methods and Protocols
The book focuses on the regulation of protein function and biological activity by the post-translational modification known as acetylation. Chapters detail a wide range of topics in protein acetylation dealing with pathways relevant to cellular homeostasi
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Robert M. Brosh, Jr. Editor
Protein Acetylation Methods and Protocols
Methods
in
M o l e c u l a r B i o lo g y
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Protein Acetylation Methods and Protocols
Edited by
Robert M. Brosh, Jr. NIH Biomedical Research Center, National Institute on Aging, National Institutes of Health, Baltimore, MD, USA
Editor Robert M. Brosh, Jr. NIH Biomedical Research Center National Institute on Aging National Institutes of Health Baltimore, MD, USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-9433-5 ISBN 978-1-4939-9434-2 (eBook) https://doi.org/10.1007/978-1-4939-9434-2 © Springer Science+Business Media, LLC, part of Springer Nature 2019 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors, and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. Cover caption: Detection of acetylated histones on newly replicated DNA using Click-It reaction to attach biotin molecules to EdU bases in DNA, and Proximity Ligation Assay to generate fluorescent signal at sites where EdU bases and acetylated histones are close to each other. This Humana Press imprint is published by the registered company Springer Science+Business Media, LLC, part of Springer Nature. The registered company address is: 233 Spring Street, New York, NY 10013, U.S.A.
Preface Over the past several decades, modulation of protein function by posttranslational modifications has attracted great interest in multiple areas of biology. The covalent and enzymatic modification of proteins post their biosynthesis provides an often reversible and acute means of regulating vital processes in cells. The functional roles of proteins can be modulated by various covalent modifications including phosphorylation, sumoylation, ubiquitination, glycosylati
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