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Protein Arginylation

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Cover of 'Protein Arginylation'

Table of Contents

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    Book Overview
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    Chapter 1 Protein Arginylation: Over 50 Years of Discovery.
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    Chapter 2 Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase.
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    Chapter 3 Arginyltransferase: A Personal and Historical Perspective.
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    Chapter 4 Arginylation in a Partially Purified Fraction of 150k × g Supernatants of Axoplasm and Injured Vertebrate Nerves.
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    Chapter 5 Preparation of ATE1 Enzyme from Native Mammalian Tissues.
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    Chapter 6 Protein Arginylation
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    Chapter 7 Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.
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    Chapter 8 Assaying ATE1 Activity in Yeast by β-Gal Degradation.
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    Chapter 9 Bacterial Expression and Purification of Recombinant Arginyltransferase (ATE1) and Arg-tRNA Synthetase (RRS) for Arginylation Assays.
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    Chapter 10 Assaying ATE1 Activity In Vitro.
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    Chapter 11 High-Throughput Arginylation Assay in Microplate Format.
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    Chapter 12 Assay of Arginyltransferase Activity by a Fluorescent HPLC Method.
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    Chapter 13 Identification of Arginylated Proteins by Mass Spectrometry.
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    Chapter 14 Analysis of Arginylated Peptides by Subtractive Edman Degradation.
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    Chapter 15 Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles.
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    Chapter 16 Applying Arginylation for Bottom-Up Proteomics.
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    Chapter 17 Development of New Tools for the Studies of Protein Arginylation.
Attention for Chapter 2: Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase.
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Chapter title
Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase.
Chapter number 2
Book title
Protein Arginylation
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2935-1_2
Pubmed ID
26285875
Book ISBNs
978-1-4939-2934-4, 978-1-4939-2935-1
Authors

Hideko Kaji, Akira Kaji

Editors

Anna S. Kashina

Abstract

Protein arginylation has been discovered in 1963 as a soluble activity in cell extracts that mediates addition of amino acids to proteins. This discovery was nearly accidental, but due to the persistence of the research team, it has been followed through and led to the emergence of a new field of research. This chapter describes the original discovery of arginylation and the first methods used to demonstrate the existence of this important biological process.

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Mendeley readers

The data shown below were compiled from readership statistics for 2 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 2 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 1 50%
Lecturer 1 50%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 100%

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