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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 17: Development of New Tools for the Studies of Protein Arginylation.
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Chapter title
Development of New Tools for the Studies of Protein Arginylation.
Chapter number 17
Book title
Protein Arginylation
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2935-1_17
Pubmed ID
Book ISBNs
978-1-4939-2934-4, 978-1-4939-2935-1
Authors

Kashina, Anna S, Anna S. Kashina

Editors

Anna S. Kashina

Abstract

Studies of posttranslational modifications present many unique challenges, stemming from their role as the major drivers of biological complexity. Perhaps the most immediate challenge to researchers working on virtually any posttranslational modification is the shortage of reliable easy-to-use tools that can enable massive identification and characterization of posttranslationally modified proteins, as well as their functional modulation in vitro and in vivo. In the case of protein arginylation, which utilizes charged Arg-tRNA that is also used by the ribosomes, detection and labeling of arginylated proteins are especially difficult, because of the necessity of distinguishing these proteins from the products of conventional translation. As of now, this difficulty remains the major obstacle to new researchers entering the field. This chapter discusses some of the strategies for developing antibodies for arginylation detection, as well as some general considerations for development of other tools for the studies of arginylation.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
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%
Researcher 1 25%
Lecturer 1 25%
Lecturer > Senior Lecturer 1 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 50%
Agricultural and Biological Sciences 2 50%
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 20 August 2015.
All research outputs
#15,344,095
of 22,824,164 outputs
Outputs from Methods in molecular biology
#5,343
of 13,124 outputs
Outputs of similar age
#209,005
of 353,117 outputs
Outputs of similar age from Methods in molecular biology
#346
of 997 outputs
Altmetric has tracked 22,824,164 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,124 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 44th percentile – i.e., 44% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 353,117 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 31st percentile – i.e., 31% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 997 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 56% of its contemporaries.