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Protein Arginylation

Overview of attention for book
Cover of 'Protein Arginylation'

Table of Contents

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    Book Overview
  2. Altmetric Badge
    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 10: Assaying ATE1 Activity In Vitro.
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Chapter title
Assaying ATE1 Activity In Vitro.
Chapter number 10
Book title
Protein Arginylation
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2935-1_10
Pubmed ID
Book ISBNs
978-1-4939-2934-4, 978-1-4939-2935-1
Authors

Junling Wang, Anna S. Kashina

Editors

Anna S. Kashina

Abstract

Here we describe a standard arginyltransferase assay in vitro using bacterially expressed purified ATE1 in a system with minimal number of components (Arg, tRNA, Arg-tRNA synthetase, and arginylation substrate). Assays of this type have first been developed in the 1980s using crude ATE1 preparations from cells and tissues and then perfected recently for the use with bacterially expressed recombinant protein. This assay represents a simple and efficient way to measure ATE1 activity.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 4 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 4 100%

Demographic breakdown

Readers by professional status Count As %
Professor 1 25%
Student > Ph. D. Student 1 25%
Lecturer 1 25%
Unknown 1 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 50%
Agricultural and Biological Sciences 1 25%
Unknown 1 25%