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Split Inteins

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Cover of 'Split Inteins'

Table of Contents

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    Book Overview
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    Chapter 1 Affinity Purification of Proteins in Tag-Free Form: Split Intein-Mediated Ultrarapid Purification (SIRP)
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    Chapter 2 Purification of Microbially Expressed Recombinant Proteins via a Dual ELP Split Intein System
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    Chapter 3 Intracellular Production of Cyclic Peptide Libraries with SICLOPPS
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    Chapter 4 Recombinant Expression of Cyclotides Using Split Inteins
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    Chapter 5 Ribosomal Synthesis of Thioether-Bridged Bicyclic Peptides
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    Chapter 6 Preparation of Semisynthetic Peptide Macrocycles Using Split Inteins
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    Chapter 7 Semisynthesis of Membrane-Attached Proteins Using Split Inteins
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    Chapter 8 Protein Chemical Modification Inside Living Cells Using Split Inteins
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    Chapter 9 Segmental Isotopic Labeling of Proteins for NMR Study Using Intein Technology
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    Chapter 10 Segmental Isotope Labeling of Insoluble Proteins for Solid-State NMR by Protein Trans-Splicing
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    Chapter 11 Split-Intein Triggered Protein Hydrogels
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    Chapter 12 A Recessive Pollination Control System for Wheat Based on Intein-Mediated Protein Splicing
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    Chapter 13 Conditional Toxin Splicing Using a Split Intein System
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    Chapter 14 Photocontrol of the Src Kinase in Mammalian Cells with a Photocaged Intein
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    Chapter 15 LOV2-Controlled Photoactivation of Protein Trans -Splicing
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    Chapter 16 A Cassette Approach for the Identification of Intein Insertion Sites
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    Chapter 17 Computational Prediction of New Intein Split Sites
Attention for Chapter 2: Purification of Microbially Expressed Recombinant Proteins via a Dual ELP Split Intein System
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Chapter title
Purification of Microbially Expressed Recombinant Proteins via a Dual ELP Split Intein System
Chapter number 2
Book title
Split Inteins
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-6451-2_2
Pubmed ID
Book ISBNs
978-1-4939-6449-9, 978-1-4939-6451-2
Authors

Changhua Shi, Tzu-Chiang Han, David W. Wood, Shi, Changhua, Han, Tzu-Chiang, Wood, David W.

Abstract

Fusions of elastin-like peptide (ELP) purification tags and self-cleaving inteins provide a powerful platform for purifying tagless recombinant proteins without the need for conventional packed-bed columns. A drawback to this method has been premature cleaving of the ELP tag during expression, before the purification procedure can take place. Here we demonstrate a split-intein method, where the self-cleaving intein is divided into two inactive segments during expression and purification. Spontaneous assembly of the purified intein segments then restores self-cleaving activity to deliver the tagless target protein.

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Mendeley readers

The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 5 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 2 40%
Student > Bachelor 1 20%
Student > Doctoral Student 1 20%
Unknown 1 20%
Readers by discipline Count As %
Chemical Engineering 1 20%
Biochemistry, Genetics and Molecular Biology 1 20%
Agricultural and Biological Sciences 1 20%
Unknown 2 40%