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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 15: LOV2-Controlled Photoactivation of Protein Trans -Splicing
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Chapter title
LOV2-Controlled Photoactivation of Protein Trans -Splicing
Chapter number 15
Book title
Split Inteins
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-6451-2_15
Pubmed ID
Book ISBNs
978-1-4939-6449-9, 978-1-4939-6451-2
Authors

Anam Qudrat, Abdullah Mosabbir, Kevin Truong, Qudrat, Anam, Mosabbir, Abdullah, Truong, Kevin

Abstract

Protein trans-splicing is a posttranslational modification that joins two protein fragments together via a peptide a bond in a process that does not require exogenous cofactors. Towards achieving cellular control, synthetically engineered systems have used a variety of stimuli such as small molecules and light. Recently, split inteins have been engineered to be photoactive by the LOV2 domain (named LOVInC). Herein, we discuss (1) designing of LOV2-activated target proteins (e.g., inteins), (2) selecting feasible splice sites for the extein, and (3) imaging cells that express LOVInC-based target exteins.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 11 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 11 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 36%
Researcher 1 9%
Lecturer > Senior Lecturer 1 9%
Student > Master 1 9%
Unknown 4 36%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 36%
Chemistry 2 18%
Medicine and Dentistry 1 9%
Unknown 4 36%