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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 15: Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles.
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Chapter title
Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles.
Chapter number 15
Book title
Protein Arginylation
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2935-1_15
Pubmed ID
Book ISBNs
978-1-4939-2934-4, 978-1-4939-2935-1
Authors

Anne M. Wagner, John B. Warner, Haviva E. Garrett, Christopher R. Walters, E. James Petersson

Editors

Anna S. Kashina

Abstract

The E. coli aminoacyl transferase (AaT) can be used to transfer a variety of unnatural amino acids, including those with azide or alkyne groups, to the α-amine of a protein with an N-terminal Lys or Arg. Subsequent functionalization through either copper-catalyzed or strain-promoted click reactions can be used to label the protein with fluorophores or biotin. This method can be used to directly detect AaT substrates or in a two-step protocol to detect substrates of the mammalian ATE1 transferase.

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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 %
Student > Ph. D. Student 1 50%
Lecturer 1 50%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 100%