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SUMO

Overview of attention for book
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 18: SUMO
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Chapter title
SUMO
Chapter number 18
Book title
SUMO
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-6358-4_18
Pubmed ID
27631811
Book ISBNs
978-1-4939-6356-0, 978-1-4939-6358-4
Authors

Rytz, Thérèse C, Miller, Marcus J, Vierstra, Richard D, Thérèse C. Rytz, Marcus J. Miller, Richard D. Vierstra

Editors

Manuel S. Rodriguez

Abstract

The posttranslational modification of proteins with small ubiquitin-related modifier (SUMO) is a rapid, robust, and reversible mechanism that impacts a host of eukaryotic processes important to both normal cellular functions and survival during various abiotic and biotic challenges. Essential to defining the breadth of events impacted by SUMOylation is the development of full catalogues of protein targets. Here, we describe a stringent affinity method to purify native SUMO conjugates from the model plant Arabidopsis thaliana based on the expression of modified SUMOs bearing epitope tags. When combined with standard and quantitative mass spectrometric methods, deep datasets of SUMOylated proteins can be acquired. Functional analysis of these lists links SUMO to numerous regulatory events, with an emphasis on those associated with transcription, DNA replication and repair, and chromatin assembly/accessibility.

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X Demographics

The data shown below were collected from the profiles of 2 X users who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 14 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Austria 1 7%
Unknown 13 93%

Demographic breakdown

Readers by professional status Count As %
Researcher 6 43%
Student > Ph. D. Student 2 14%
Student > Doctoral Student 1 7%
Lecturer > Senior Lecturer 1 7%
Professor > Associate Professor 1 7%
Other 0 0%
Unknown 3 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 57%
Agricultural and Biological Sciences 2 14%
Medicine and Dentistry 1 7%
Unknown 3 21%
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 20 June 2017.
All research outputs
#17,816,222
of 22,888,307 outputs
Outputs from Methods in molecular biology
#7,244
of 13,132 outputs
Outputs of similar age
#267,809
of 393,716 outputs
Outputs of similar age from Methods in molecular biology
#752
of 1,471 outputs
Altmetric has tracked 22,888,307 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,132 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 39th percentile – i.e., 39% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 393,716 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 27th percentile – i.e., 27% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 1,471 others from the same source and published within six weeks on either side of this one. This one is in the 42nd percentile – i.e., 42% of its contemporaries scored the same or lower than it.

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