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Protein Arginylation

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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 16: Applying Arginylation for Bottom-Up Proteomics.
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Chapter title
Applying Arginylation for Bottom-Up Proteomics.
Chapter number 16
Book title
Protein Arginylation
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2935-1_16
Pubmed ID
Book ISBNs
978-1-4939-2934-4, 978-1-4939-2935-1
Authors

H. Alexander Ebhardt

Editors

Anna S. Kashina

Abstract

Arginylation is an enzymatic reaction in which arginyl-tRNA protein transferase 1 (ATE1, EC 2.3.2.8) conjugates a single arginyl moiety from aminoacylated tRNA(Arg) onto a target polypeptide. We established arginylation for in vitro labeling of peptides with N-terminal acidic amino acids. Consistent with prior knowledge, arginylated peptides flanked by basic amino acids result in rich redundant MS/MS fragment spectra using various precursor fragmentation modes. Arginylation carried out by ATE1 is a fast method for labeling peptides. Sequence-specific proteolytic digest of proteins is best carried out using a double digest of proteins by Lys-C and Asp-N to generate peptides with a basic amino acid on the C-terminus and an acidic amino acid on the N-terminus. Under these conditions, arginylation is specific for N-terminal acidic amino acids and results in a near 2× sequence coverage in the MS/MS spectrum are achieved.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 3 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 1 33%
Lecturer 1 33%
Student > Postgraduate 1 33%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 67%
Agricultural and Biological Sciences 1 33%
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 25 May 2016.
All research outputs
#20,328,845
of 22,873,031 outputs
Outputs from Methods in molecular biology
#9,915
of 13,130 outputs
Outputs of similar age
#296,036
of 353,317 outputs
Outputs of similar age from Methods in molecular biology
#636
of 997 outputs
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