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NLR Proteins

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Cover of 'NLR Proteins'

Table of Contents

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    Book Overview
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    Chapter 1 NLR Proteins
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    Chapter 2 Atypical Inflammasomes.
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    Chapter 3 NLR Proteins
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    Chapter 4 Investigating IL-1β Secretion Using Real-Time Single-Cell Imaging.
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    Chapter 5 NLR Proteins
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    Chapter 6 Measuring IL-1β Processing by Bioluminescence Sensors II: The iGLuc System.
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    Chapter 7 Assessing Extracellular ATP as Danger Signal In Vivo: The pmeLuc System.
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    Chapter 8 Measuring NLR Oligomerization I: Size Exclusion Chromatography, Co-immunoprecipitation, and Cross-Linking.
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    Chapter 9 NLR Proteins
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    Chapter 10 NLR Proteins
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    Chapter 11 Measuring NLR Oligomerization IV: Using Förster Resonance Energy Transfer (FRET)-Fluorescence Lifetime Imaging Microscopy (FLIM) to Determine the Close Proximity of Inflammasome Components.
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    Chapter 12 Measuring NLR Oligomerization V: In Situ Proximity Ligation Assay.
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    Chapter 13 Assessing Caspase-1 Activation.
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    Chapter 14 Cell-Free Assay for Inflammasome Activation.
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    Chapter 15 Functional Reconstruction of NLRs in HEK293 Cells.
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    Chapter 16 Method to Measure Ubiquitination of NLRs.
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    Chapter 17 Cytofluorometric Quantification of Cell Death Elicited by NLR Proteins.
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    Chapter 18 NLR in Human Diseases: Role and Laboratory Findings.
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    Chapter 19 Erratum to: Measuring NLR Oligomerization II: Detection of ASC Speck Formation by Confocal Microscopy and Immunofluorescence
Attention for Chapter 11: Measuring NLR Oligomerization IV: Using Förster Resonance Energy Transfer (FRET)-Fluorescence Lifetime Imaging Microscopy (FLIM) to Determine the Close Proximity of Inflammasome Components.
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Chapter title
Measuring NLR Oligomerization IV: Using Förster Resonance Energy Transfer (FRET)-Fluorescence Lifetime Imaging Microscopy (FLIM) to Determine the Close Proximity of Inflammasome Components.
Chapter number 11
Book title
NLR Proteins
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3566-6_11
Pubmed ID
Book ISBNs
978-1-4939-3564-2, 978-1-4939-3566-6
Authors

Catrin Youssif, Bárbara Flix, Olivia Belbin, Mònica Comalada

Editors

Francesco Di Virgilio, Pablo Pelegrín

Abstract

Intracellular signaling and cellular activation have been demonstrated to reside on multi-protein complexes rather than in isolated proteins. Consequently, techniques to resolve these complexes have gained much attention over the last few years. Förster Resonance Energy Transfer (FRET) coupled with Fluorescence Lifetime Imaging Microscopy (FLIM) is a powerful tool to discriminate direct interactions between two proteins within a multi-protein complex. Here, we present the use of FRET-FLIM as an experimental tool for the interpretation of the inflammasome composition. We also introduce some considerations required for the correct use of this technique and the control experiments that should be implemented.

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 %
Professor > Associate Professor 3 27%
Researcher 3 27%
Student > Ph. D. Student 2 18%
Student > Doctoral Student 1 9%
Student > Master 1 9%
Other 0 0%
Unknown 1 9%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 18%
Neuroscience 2 18%
Agricultural and Biological Sciences 2 18%
Business, Management and Accounting 1 9%
Medicine and Dentistry 1 9%
Other 1 9%
Unknown 2 18%