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Proteases and Cancer

Overview of attention for book
Cover of 'Proteases and Cancer'

Table of Contents

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    Book Overview
  2. Altmetric Badge
    Chapter 1 Dissecting Degradomes: Analysis of Protease-Coding Genes
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    Chapter 2 Identification of Protease Cleavage Sites and Substrates in Cancer by Carboxy-TAILS (C-TAILS)
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    Chapter 3 Identification of Proteolytic Cleavage Sites of EphA2 by Membrane Type 1 Matrix Metalloproteinase on the Surface of Cancer Cells
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    Chapter 4 Biotin-Chasing Assay to Evaluate uPAR Stability and Cleavage on the Surface of Cells
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    Chapter 5 Determination of Aconitase Activity: A Substrate of the Mitochondrial Lon Protease
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    Chapter 6 A Simple Cell-Based Assay for the Detection of Surface Protein Shedding by Rhomboid Proteases
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    Chapter 7 Functional Production of Catalytic Domains of Human MMPs in Escherichia coli Periplasm
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    Chapter 8 Autophagy and Proteases: Basic Study of the Autophagic Flux by Western Blot
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    Chapter 9 Gel-Based Gelatin Zymography to Examine Matrix Metalloproteinase Activity in Cell Culture
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    Chapter 10 Analysis of Enzymatic Activity of Matrix Metalloproteinase (MMP) by Collagen Zymography in Melanoma
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    Chapter 11 Measurement of Protease Activities Using Fluorogenic Substrates
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    Chapter 12 Targeting the Expression of Cathepsin B Using CRISPR/Cas9 System in Mammalian Cancer Cells
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    Chapter 13 Assessing the Influence of a Protease in Cell Migration Using the Barrier-Migration Assay
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    Chapter 14 Analysis of Invasive Activity of CAF Spheroids into Three Dimensional (3D) Collagen Matrices
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    Chapter 15 Beyond the Proteolytic Activity: Examining the Functional Relevance of the Ancillary Domains Using Tri-Dimensional (3D) Spheroid Invasion Assay
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    Chapter 16 Analyzing the Type II Transmembrane Serine Protease Hepsin-Dependent Basement Membrane Remodeling in 3D Cell Culture
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    Chapter 17 Evaluation of Tumor Vasculature Using a Syngeneic Tumor Model in Wild-Type and Genetically Modified Mice
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    Chapter 18 3D Image Analysis of the Microvasculature in Healthy and Diseased Tissues
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    Chapter 19 Human Tumor Tissue-Based 3D In Vitro Invasion Assays
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    Chapter 20 Ear Sponge Assay: A Method to Investigate Angiogenesis and Lymphangiogenesis in Mice
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    Chapter 21 Cancer Susceptibility Models in Protease-Deficient Mice
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    Chapter 22 Imaging Proteolytic Activities in Mouse Models of Cancer
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    Chapter 23 Protease Silencing to Explore the Molecular Mechanisms of Cancer and Aging
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    Chapter 24 Analysis of Somatic DNA Methylation Alterations of Genes Encoding Cell Surface Metallopeptidases in Colorectal Cancer
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    Chapter 25 Targeting Deubiquitinases in Cancer
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    Chapter 26 Generation of Highly Selective MMP Antibody Inhibitors
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    Chapter 27 Strategies to Target Matrix Metalloproteinases as Therapeutic Approach in Cancer
Attention for Chapter 5: Determination of Aconitase Activity: A Substrate of the Mitochondrial Lon Protease
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Chapter title
Determination of Aconitase Activity: A Substrate of the Mitochondrial Lon Protease
Chapter number 5
Book title
Proteases and Cancer
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7595-2_5
Pubmed ID
Book ISBNs
978-1-4939-7594-5, 978-1-4939-7595-2
Authors

Pedro M. Quirós

Abstract

Mitochondrial aconitase is a reversible enzyme that catalyzes the conversion of citrate to isocitrate in the tricarboxylic acid cycle. Mitochondrial aconitase is very sensitive to oxidative inactivation and can aggregate and accumulate in the mitochondrial matrix causing mitochondrial dysfunction. Lon protease, one of the major quality control proteases in mitochondria, degrades oxidized aconitase maintaining mitochondrial homeostasis. This chapter describes a step-by-step protocol for a simple and reliable measurement of mitochondrial aconitase, as well as citrate synthase activity, using isolated mitochondria from cells. The protocol is simple and fast, and it is optimized for a 96-well plate using a microplate reader.

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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 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 22 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 18%
Student > Master 4 18%
Professor > Associate Professor 3 14%
Student > Bachelor 2 9%
Researcher 2 9%
Other 5 23%
Unknown 2 9%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 36%
Chemistry 3 14%
Medicine and Dentistry 2 9%
Pharmacology, Toxicology and Pharmaceutical Science 1 5%
Immunology and Microbiology 1 5%
Other 3 14%
Unknown 4 18%
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 11 January 2018.
All research outputs
#20,458,307
of 23,015,156 outputs
Outputs from Methods in molecular biology
#9,945
of 13,165 outputs
Outputs of similar age
#378,187
of 442,344 outputs
Outputs of similar age from Methods in molecular biology
#1,193
of 1,498 outputs
Altmetric has tracked 23,015,156 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,165 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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We're also able to compare this research output to 1,498 others from the same source and published within six weeks on either side of this one. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.