ArticleStructure (London, England : 1993)2013
Activation of AMP-activated protein kinase revealed by hydrogen/deuterium exchange mass spectrometry.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- RAB5A regulates cell proliferation and lipid metabolism by modulating mitochondrial ROS via AMPK signaling pathway in ovarian granulosa cells.Redox biology · 2026Article
- The metabolic sensor AMPK: Twelve enzymes in one.Molecular metabolism · 2024Review
- Proteoglycan Extracted fromACS omega · 2023Article
- The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis.Foods (Basel, Switzerland) · 2023Article
- Structure of an AMPK complex in an inactive, ATP-bound state.Science (New York, N.Y.) · 2021Article
- AMPK inhibits Smad3-mediated autoinduction of TGF-β1 in gastric cancer cells.Journal of cellular and molecular medicine · 2021Article
- Molecular Basis of the Mechanisms Controlling MASTL.Molecular & cellular proteomics : MCP · 2020Article
- Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism.Nature communications · 2019Article
- 3-Acetyl-oleanolic acid ameliorates non-alcoholic fatty liver disease in high fat diet-treated rats by activating AMPK-related pathways.Acta pharmacologica Sinica · 2018Article
- Whole-protein alanine-scanning mutagenesis of allostery: A large percentage of a protein can contribute to mechanism.Human mutation · 2017Article
- Caspase-6 Undergoes a Distinct Helix-Strand Interconversion upon Substrate Binding.The Journal of biological chemistry · 2017Article
- β-subunit myristoylation functions as an energy sensor by modulating the dynamics of AMP-activated Protein Kinase.Scientific reports · 2016Article
- Probing the enzyme kinetics, allosteric modulation and activation of α1- and α2-subunit-containing AMP-activated protein kinase (AMPK) heterotrimeric complexes by pharmacological and physiological activators.The Biochemical journal · 2016Article
- Comprehensive Characterization of AMP-Activated Protein Kinase Catalytic Domain by Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Differential isotopic enrichment to facilitate characterization of asymmetric multimeric proteins using hydrogen/deuterium exchange mass spectrometry.Analytical chemistry · 2015Article
- Integration of G protein α (Gα) signaling by the regulator of G protein signaling 14 (RGS14).The Journal of biological chemistry · 2015Article
- Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- HDX-MS guided drug discovery: small molecules and biopharmaceuticals.Current opinion in structural biology · 2014Review
- Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry.Structure (London, England : 1993) · 2014Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
AMP-activated protein kinase (AMPK) monitors cellular energy, regulates genes involved in ATP synthesis and consumption, and is allosterically activated by nucleotides and synthetic ligands. Analysis of the intact enzyme with hydrogen/deuterium exchange mass spectrometry reveals conformational perturbations of AMPK in response to binding of nucleotides, cyclodextrin, and a synthetic small molecule activator, A769662. Results from this analysis clearly show that binding of AMP leads to conformational changes primarily in the γ subunit of AMPK and subtle changes in the α and β subunits. In contrast, A769662 causes profound conformational changes in the glycogen binding module of the β subunit and in the kinase domain of the α subunit, suggesting that the molecular binding site of the latter resides between the α and β subunits. The distinct short- and long-range perturbations induced upon binding of AMP and A769662 suggest fundamentally different molecular mechanisms for activation of AMPK by these two ligands.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.