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Ubiquitin Family Modifiers and the Proteasome

Overview of attention for book
Cover of 'Ubiquitin Family Modifiers and the Proteasome'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Three decades of studies to understand the functions of the ubiquitin family.
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    Chapter 2 Structure and evolution of ubiquitin and ubiquitin-related domains.
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    Chapter 3 Deciphering tissue-specific ubiquitylation by mass spectrometry.
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    Chapter 4 Analysis of Cellular SUMO and SUMO-Ubiquitin Hybrid Conjugates.
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    Chapter 5 Recombinant reconstitution of sumoylation reactions in vitro.
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    Chapter 6 Reconstitution of SUMO-Dependent Ubiquitylation In Vitro.
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    Chapter 7 Detection and Analysis of FAT10 Modification.
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    Chapter 8 Isolation of NEDDylated Proteins in Human Cells.
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    Chapter 9 The ISG15 Conjugation System.
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    Chapter 10 Pupylation: proteasomal targeting by a protein modifier in bacteria.
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    Chapter 11 Role of UbL Family Modifiers and Their Binding Proteins in Cell Signaling.
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    Chapter 12 Ubiquitin Family Modifiers and the Proteasome
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    Chapter 13 Using linkage-specific monoclonal antibodies to analyze cellular ubiquitylation.
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    Chapter 14 Measuring rates of ubiquitin chain formation as a functional readout of ligase activity.
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    Chapter 15 Synthesis and analysis of k11-linked ubiquitin chains.
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    Chapter 16 Synthesis and analysis of linear ubiquitin chains.
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    Chapter 17 Detection and Quantitation of SUMO Chains by Mass Spectrometry
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    Chapter 18 Bioinformatical Detection of Recognition Factors for Ubiquitin and SUMO.
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    Chapter 19 Surface Plasmon Resonance to Measure Interactions of UbFs with Their Binding Partners.
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    Chapter 20 Identifying and studying ubiquitin receptors by NMR.
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    Chapter 21 Exploring the Role of p97 and Its UBX-Domain Cofactors Through Identification of Their Interacting Proteins.
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    Chapter 22 Assembly and function of the proteasome.
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    Chapter 23 Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes.
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    Chapter 24 Disulfide engineering to map subunit interactions in the proteasome and other macromolecular complexes.
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    Chapter 25 Using DNA damage sensitivity phenotypes to characterize mutations affecting proteasome function.
  27. Altmetric Badge
    Chapter 26 Analysing properties of proteasome inhibitors using kinetic and x-ray crystallographic studies.
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    Chapter 27 Immunoproteasome-specific inhibitors and their application.
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    Chapter 28 Binding of ubiquitin conjugates to proteasomes as visualized with native gels.
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    Chapter 29 Affinity Purification of Mammalian 26S Proteasomes Using an Ubiquitin-Like Domain.
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    Chapter 30 Using siRNA Techniques to Dissect Proteasome Assembly Pathways in Mammalian Cells.
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    Chapter 31 Reconstitution of PA700, the 19S Regulatory Particle, from Purified Precursor Complexes.
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    Chapter 32 Cellular responses to misfolded proteins and protein aggregates.
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    Chapter 33 Live-cell imaging of ubiquitin-proteasome system function.
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    Chapter 34 Analysis of chaperone-assisted ubiquitylation.
  36. Altmetric Badge
    Chapter 35 Use of CPY* and Its Derivatives to Study Protein Quality Control in Various Cell Compartments.
  37. Altmetric Badge
    Chapter 36 Assays to Measure ER-Associated Degradation in Yeast.
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    Chapter 37 SDS-PAGE Techniques to Study Ubiquitin-Like Conjugation Systems in Yeast Autophagy.
  39. Altmetric Badge
    Chapter 38 Analysis of Ubiquitin-Dependent Proteolysis in Caenorhabditis elegans.
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    Chapter 39 Structural insights into functional modes of proteins involved in ubiquitin family pathways.
  41. Altmetric Badge
    Chapter 40 Ubiquitin Family Modifiers and the Proteasome
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    Chapter 41 Ubiquitin Family Modifiers and the Proteasome
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    Chapter 42 Synthesis of atypical diubiquitin chains.
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    Chapter 43 TIPI: TEV Protease-Mediated Induction of Protein Instability.
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    Chapter 44 PROTAC-Induced Proteolytic Targeting
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    Chapter 45 Formation of nondegradable forked ubiquitin conjugates by ring-finger ligases and its prevention by s5a.
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    Chapter 46 S5a/Rpn10, a UIM-Protein, as a Universal Substrate for Ubiquitination.
Attention for Chapter 27: Immunoproteasome-specific inhibitors and their application.
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Chapter title
Immunoproteasome-specific inhibitors and their application.
Chapter number 27
Book title
Ubiquitin Family Modifiers and the Proteasome
Published in
Methods in molecular biology, January 2012
DOI 10.1007/978-1-61779-474-2_27
Pubmed ID
22350900
Book ISBNs
978-1-61779-473-5, 978-1-61779-474-2
Authors

Basler M, Groettrup M, Michael Basler, Marcus Groettrup

Editors

R. Jürgen Dohmen, Martin Scheffner

Abstract

Immunoproteasomes (IPs) containing the interferon-inducible subunits β1i (LMP2), β2i (MECL-1), and β5i (LMP7) alter proteasomal cleavage preference, optimise the generation of peptide ligands of MHC class I molecules, alter cytokine profile, influence T-helper cell differentiation, and play a role in T-cell survival. Small molecule inhibitors are useful tools for probing the role of the immunoproteasome in immune functions. Here, we describe different methods to characterise immunoproteasome-selective inhibitors. Thereby, we provide the methodology to analyse the specificity and cell permeability of immunoproteasome inhibitors, as well as to functionally investigate immunoproteasome inhibitors in antigen presentation.

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X Demographics

The data shown below were collected from the profile of 1 X user 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 %
Russia 1 7%
Unknown 13 93%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 5 36%
Researcher 3 21%
Student > Bachelor 2 14%
Professor 1 7%
Professor > Associate Professor 1 7%
Other 1 7%
Unknown 1 7%
Readers by discipline Count As %
Agricultural and Biological Sciences 8 57%
Biochemistry, Genetics and Molecular Biology 2 14%
Medicine and Dentistry 2 14%
Chemistry 1 7%
Unknown 1 7%
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 01 March 2012.
All research outputs
#18,304,874
of 22,663,150 outputs
Outputs from Methods in molecular biology
#7,811
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Outputs of similar age
#194,815
of 243,381 outputs
Outputs of similar age from Methods in molecular biology
#324
of 475 outputs
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So far Altmetric has tracked 13,021 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 24th percentile – i.e., 24% of its peers scored the same or lower than it.
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We're also able to compare this research output to 475 others from the same source and published within six weeks on either side of this one. This one is in the 10th percentile – i.e., 10% of its contemporaries scored the same or lower than it.

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