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AMPK

Overview of attention for book
Cover of 'AMPK'

Table of Contents

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    Book Overview
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    Chapter 1 Production and Crystallization of Full-Length Human AMP-Activated Protein Kinase (α1β1γ1)
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    Chapter 2 Visualizing AMPK Drug Binding Sites Through Crystallization of Full-Length Phosphorylated α2β1γ1 Heterotrimer
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    Chapter 3 Biophysical Interactions of Direct AMPK Activators
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    Chapter 4 Biochemical Measurement of Glycogen: Method to Investigate the AMPK-Glycogen Relationship
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    Chapter 5 Cell-Free Assays to Measure Effects of Regulatory Ligands on AMPK
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    Chapter 6 Applications of NMR and ITC for the Study of the Kinetics of Carbohydrate Binding by AMPK β-Subunit Carbohydrate-Binding Modules
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    Chapter 7 Bioinformatics Approach to Identify Novel AMPK Targets
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    Chapter 8 Studying AMPK in an Evolutionary Context
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    Chapter 9 AMPK Protein Interaction Analyses by Yeast Two-Hybrid
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    Chapter 10 Transient Expression of AMPK Heterotrimer Complexes in Mammalian Cells
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    Chapter 11 Knockdown of Human AMPK Using the CRISPR/Cas9 Genome-Editing System
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    Chapter 12 Compound C/Dorsomorphin: Its Use and Misuse as an AMPK Inhibitor
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    Chapter 13 Identifying the Heterotrimeric Complex Stoichiometry of AMPK in Skeletal Muscle by Immunoprecipitation
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    Chapter 14 Kinase Activity Determination of Specific AMPK Complexes/Heterotrimers in the Skeletal Muscle
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    Chapter 15 Determination of Adenine Nucleotide Concentrations in Cells and Tissues by High-Performance Liquid Chromatography
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    Chapter 16 Intact Cell Assays to Monitor AMPK and Determine the Contribution of the AMP-Binding or ADaM Sites to Activation
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    Chapter 17 Cellular Application of Genetically Encoded Sensors and Impeders of AMPK
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    Chapter 18 Assessing Mitochondrial Bioenergetics by Respirometry in Cells or Isolated Organelles
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    Chapter 19 Study of AMPK-Regulated Metabolic Fluxes in Neurons Using the Seahorse XFe Analyzer
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    Chapter 20 Investigating the Role of AMPK in Inflammation
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    Chapter 21 Studying the Role of AMPK in Cardiac Hypertrophy and Protein Synthesis
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    Chapter 22 Assessment of AMPK-Stimulated Cellular Long-Chain Fatty Acid and Glucose Uptake
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    Chapter 23 Measurement of AMPK-Induced Inhibition of Lipid Synthesis Flux in Cultured Cells
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    Chapter 24 Studying the Role of AMPK in Autophagy
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    Chapter 25 Determining AMPK Activation via the Lysosomal v-ATPase-Ragulator-AXIN/LKB1 Axis
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    Chapter 26 Manipulation and Measurement of AMPK Activity in Pancreatic Islets
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    Chapter 27 Analyzing AMPK Function in the Hypothalamus
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    Chapter 28 Using Ex Vivo Kidney Slices to Study AMPK Effects on Kidney Proteins
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    Chapter 29 A Flow Cytometry-Based Protocol to Measure Lymphocyte Viability Upon Metabolic Stress
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    Chapter 30 Methods to Evaluate AMPK Regulation of Macrophage Cholesterol Homeostasis
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    Chapter 31 Modulation of Vascular Function by AMPK: Assessment of NO Bioavailability and Surrogates of Oxidative Stress
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    Chapter 32 Measurement of Reactive Oxygen Species (ROS) and Mitochondrial ROS in AMPK Knockout Mice Blood Vessels
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    Chapter 33 Studying the Role of AMPK in Angiogenesis
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    Chapter 34 Analysis of Muscle Stem Cell Fate Through Modulation of AMPK Activity
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    Chapter 35 Evaluating the Role of Host AMPK in Leishmania Burden
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    Chapter 36 Analysis of Transgenerational Phenotypes Following Acute Starvation in AMPK-Deficient C. elegans
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    Chapter 37 Human γ2-AMPK Mutations
Attention for Chapter 2: Visualizing AMPK Drug Binding Sites Through Crystallization of Full-Length Phosphorylated α2β1γ1 Heterotrimer
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Chapter title
Visualizing AMPK Drug Binding Sites Through Crystallization of Full-Length Phosphorylated α2β1γ1 Heterotrimer
Chapter number 2
Book title
AMPK
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7598-3_2
Pubmed ID
Book ISBNs
978-1-4939-7597-6, 978-1-4939-7598-3
Authors

Christopher G. Langendorf, Jonathan S. Oakhill, Bruce E. Kemp

Abstract

Here, we describe the crystallization protocol for AMPK, including protein production and purification. AMPK can be readily crystallized in the presence of PEG to give diffracting crystals to a resolution of between 2.5 and 3.5 Å using synchrotron radiation. This method allows for visualization of drugs or small molecules that bind to the ADaM site, CBS sites, ATP binding site, and the newly identified C2 binding sites in the γ-subunit via co-crystallization with phosphorylated AMPK (pT172) α2β1γ1 isoform or α2/1β1γ1 chimera. Drugs with binding affinities above 500 nM fail to co-crystallize with AMPK using these parameters.

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Mendeley readers

The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 3 100%

Demographic breakdown

Readers by professional status Count As %
Professor 1 33%
Librarian 1 33%
Unknown 1 33%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 1 33%
Earth and Planetary Sciences 1 33%
Unknown 1 33%