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Innate DNA and RNA Recognition

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Cover of 'Innate DNA and RNA Recognition'

Table of Contents

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    Book Overview
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    Chapter 1 Detection of RNA modifications by HPLC analysis and competitive ELISA.
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    Chapter 2 Enzymatic Synthesis and Purification of a Defined RIG-I Ligand.
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    Chapter 3 Crystallization of Mouse RIG-I ATPase Domain: In Situ Proteolysis.
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    Chapter 4 Isolation of RIG-I-Associated RNAs from Virus-Infected Cells.
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    Chapter 5 Structure modeling of toll-like receptors.
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    Chapter 6 Nucleic Acid recognition in dendritic cells.
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    Chapter 7 Viral nucleic Acid recognition in human nonimmune cells: in vitro systems.
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    Chapter 8 Analysis of nucleic Acid-induced nonimmune cell death in vitro.
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    Chapter 9 In vitro analysis of nucleic Acid recognition in B lymphocytes.
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    Chapter 10 Mapping of optimal CD8 T cell epitopes.
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    Chapter 11 A Modular Approach to Suppression Assays: TLR Ligands, Conditioned Medium, and Viral Infection.
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    Chapter 12 MicroRNA Methodology: Advances in miRNA Technologies.
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    Chapter 13 Expression Profiling by Real-Time Quantitative Polymerase Chain Reaction (RT-qPCR)
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    Chapter 14 Evaluating the role of nucleic Acid antigens in murine models of systemic lupus erythematosus.
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    Chapter 15 Induction and analysis of nephrotoxic serum nephritis in mice.
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    Chapter 16 Isolation of Intratumoral Leukocytes of TLR-Stimulated Tumor-Bearing Mice.
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    Chapter 17 Bifunctional siRNAs for Tumor Therapy.
Attention for Chapter 3: Crystallization of Mouse RIG-I ATPase Domain: In Situ Proteolysis.
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Chapter title
Crystallization of Mouse RIG-I ATPase Domain: In Situ Proteolysis.
Chapter number 3
Book title
Innate DNA and RNA Recognition
Published in
Methods in molecular biology, May 2014
DOI 10.1007/978-1-4939-0882-0_3
Pubmed ID
Book ISBNs
978-1-4939-0881-3, 978-1-4939-0882-0
Authors

Civril F, Hopfner KP, Filiz Civril, Karl-Peter Hopfner

Editors

Hans-Joachim Anders, Adriana Migliorini

Abstract

RIG-I is a key pattern recognition receptor that recognizes cytoplasmic viral RNA. Upon ligand binding, it undergoes a conformational change that induces an active signaling conformation. However, the details of this conformational change remain elusive until high-resolution crystal structures of different functional conformations are available. X-ray crystallography is a powerful tool to study structure-function relationships, but crystallization is often the limiting step of the method. Here, we describe the in situ in-drop proteolysis of RIG-I that yielded crystals of the ATPase domain of mouse RIG-I suitable for structure determination.

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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 %
Professor 1 33%
Student > Bachelor 1 33%
Researcher 1 33%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 67%
Chemistry 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 05 February 2015.
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#20,257,230
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Outputs of similar age from Methods in molecular biology
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