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SUMO

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Cover of 'SUMO'

Table of Contents

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    Book Overview
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    Chapter 1 SUMO
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    Chapter 2 SUMO
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    Chapter 3 Reconstitution of the Recombinant RanBP2 SUMO E3 Ligase Complex.
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    Chapter 4 Production and Purification of Recombinant SUMOylated Proteins Using Engineered Bacteria.
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    Chapter 5 A Fluorescent In Vitro Assay to Investigate Paralog-Specific SUMO Conjugation.
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    Chapter 6 SUMO
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    Chapter 7 Real-Time Surface Plasmon Resonance (SPR) for the Analysis of Interactions Between SUMO Traps and Mono- or PolySUMO Moieties.
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    Chapter 8 SUMO
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    Chapter 9 SUMO
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    Chapter 10 Detection of Protein SUMOylation In Situ by Proximity Ligation Assays.
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    Chapter 11 In Situ SUMOylation and DeSUMOylation Assays: Fluorescent Methods to Visualize SUMOylation and DeSUMOylation in Permeabilized Cells.
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    Chapter 12 SUMO
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    Chapter 13 Label-Free Identification and Quantification of SUMO Target Proteins.
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    Chapter 14 The Use of Multimeric Protein Scaffolds for Identifying Multi-SUMO Binding Proteins.
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    Chapter 15 SUMO
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    Chapter 16 SUMO
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    Chapter 17 SUMO
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    Chapter 18 SUMO
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    Chapter 19 SUMO
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    Chapter 20 Systematic Localization and Identification of SUMOylation Substrates in Knock-In Mice Expressing Affinity-Tagged SUMO1.
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    Chapter 21 Erratum
Attention for Chapter 7: Real-Time Surface Plasmon Resonance (SPR) for the Analysis of Interactions Between SUMO Traps and Mono- or PolySUMO Moieties.
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Chapter title
Real-Time Surface Plasmon Resonance (SPR) for the Analysis of Interactions Between SUMO Traps and Mono- or PolySUMO Moieties.
Chapter number 7
Book title
SUMO
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-6358-4_7
Pubmed ID
Book ISBNs
978-1-4939-6356-0, 978-1-4939-6358-4
Authors

Wendy Xolalpa, Manuel S. Rodriguez, Patrick England

Editors

Manuel S. Rodriguez

Abstract

Isolating endogenous SUMOylated proteins is a challenging task due to the high reversibility of this posttranslational modification. We have shown that SUMO traps are useful tools for the enrichment and isolation of proteins modified by SUMO in vitro and in vivo. To characterize the affinity and specificity of different SUMO chains for these traps, that are based on SUMO-interacting motifs, we have used real-time surface plasmon resonance (SPR), which allows a label-free analysis of protein/protein interactions. Here, a protocol to determine the affinities of multivalent SUMO traps for polySUMO chains or mono-SUMO molecules by SPR is presented.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 8 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 4 50%
Student > Ph. D. Student 1 13%
Lecturer > Senior Lecturer 1 13%
Unknown 2 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 5 63%
Agricultural and Biological Sciences 1 13%
Unknown 2 25%