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Mechanism of Action of an EPAC1-Selective Competitive Partial Agonist

https://doi.org/10.1021/acs.jmedchem.9b02151

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Epac1 knockdown inhibits the proliferation of ovarian cancer cells by inactivating AKT/Cyclin D1/CDK4 pathway in vitro and in vivo

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An exact mathematical expression for describing competitive binding of two different ligands to a protein molecule

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The novel exchange protein activated by cyclic AMP 1 (EPAC1) agonist, I942, regulates inflammatory gene expression in human umbilical vascular endothelial cells (HUVECs)

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The (R)-enantiomer of CE3F4 is a preferential inhibitor of human exchange protein directly activated by cyclic AMP isoform 1 (Epac1)

inferredcites →https://doi.org/10.1016/j.bpj.2011.12.030openalex-snapshot

The Projection Analysis of NMR Chemical Shifts Reveals Extended EPAC Autoinhibition Determinants

inferredcites →https://doi.org/10.1016/j.canlet.2008.09.008openalex-snapshot

The inhibitory effect of norepinephrine on the migration of ES-2 ovarian carcinoma cells involves a Rap1-dependent pathway

inferredcites →https://doi.org/10.1016/j.neuron.2012.02.003openalex-snapshot

EPAC Null Mutation Impairs Learning and Social Interactions via Aberrant Regulation of miR-124 and Zif268 Translation

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Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms

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Epac proteins: multi-purpose cAMP targets

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Structure?Activity Relationship Studies with Tetrahydroquinoline Analogs as EPAC Inhibitors

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Group Epitope Mapping by Saturation Transfer Difference NMR To Identify Segments of a Ligand in Direct Contact with a Protein Receptor

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Understanding cAMP-Dependent Allostery by NMR Spectroscopy: Comparative Analysis of the EPAC1 cAMP-Binding Domain in Its Apo and cAMP-Bound States

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Mechanism of Selective Enzyme Inhibition through Uncompetitive Regulation of an Allosteric Agonist

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Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP

inferredcites →https://doi.org/10.1038/ijo.2016.208openalex-snapshot

Epac2a-null mice exhibit obesity-prone nature more susceptible to leptin resistance

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The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways

inferredcites →https://doi.org/10.1038/nature04468openalex-snapshot

Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state

inferredcites →https://doi.org/10.1038/nature07187openalex-snapshot

Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B

inferredcites →https://doi.org/10.1038/ncb874openalex-snapshot

A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK

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The role of dynamic conformational ensembles in biomolecular recognition

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Cyclic nucleotide analogs as probes of signaling pathways

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Structure and regulation of the cAMP-binding domains of Epac2

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Identification of a Novel, Small Molecule Partial Agonist for the Cyclic AMP Sensor, EPAC1

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Exchange protein directly activated by cAMP plays a critical role in bacterial invasion during fatal rickettsioses

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inferredcites →https://doi.org/10.1074/jbc.m111.277723openalex-snapshot

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inferredcites →https://doi.org/10.1074/jbc.m112.422956openalex-snapshot

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inferredcites →https://doi.org/10.1074/jbc.m114.569319openalex-snapshot

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inferredcites →https://doi.org/10.1074/jbc.m115.685305openalex-snapshot

Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG)

inferredcites →https://doi.org/10.1074/jbc.m302179200openalex-snapshot

cAMP Analog Mapping of Epac1 and cAMP Kinase

inferredcites →https://doi.org/10.1074/jbc.m306292200openalex-snapshot

Ligand-mediated Activation of the cAMP-responsive Guanine Nucleotide Exchange Factor Epac

inferredcites →https://doi.org/10.1074/jbc.m802164200openalex-snapshot

Entropy-driven cAMP-dependent Allosteric Control of Inhibitory Interactions in Exchange Proteins Directly Activated by cAMP

inferredcites →https://doi.org/10.1083/jcb.200209105openalex-snapshot

Cyclic AMP induces integrin-mediated cell adhesion through Epac and Rap1 upon stimulation of the β2-adrenergic receptor

inferredcites →https://doi.org/10.1093/abbs/gmx045openalex-snapshot

Lithium and an EPAC-specific inhibitor ESI-09 synergistically suppress pancreatic cancer cell proliferation and survival

inferredcites →https://doi.org/10.1093/bioinformatics/bth078openalex-snapshot

Open source clustering software

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Exchange protein directly activated by cAMP 1 promotes autophagy during cardiomyocyte hypertrophy

inferredcites →https://doi.org/10.1093/cvr/cvz076openalex-snapshot

Identification of a pharmacological inhibitor of Epac1 that protects the heart against acute and chronic models of cardiac stress

inferredcites →https://doi.org/10.1124/mol.112.080689openalex-snapshot

A Novel EPAC-Specific Inhibitor Suppresses Pancreatic Cancer Cell Migration and Invasion

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inferredcites →https://doi.org/10.1124/pr.110.003707openalex-snapshot

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inferredcites →https://doi.org/10.1126/science.282.5397.2275openalex-snapshot

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inferredcites →https://doi.org/10.1128/jvi.03001-13openalex-snapshot

Blocking of Exchange Proteins Directly Activated by cAMP Leads to Reduced Replication of Middle East Respiratory Syndrome Coronavirus

inferredcites →https://doi.org/10.1128/mcb.01034-15openalex-snapshot

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inferredcites →https://doi.org/10.1128/mcb.01227-12openalex-snapshot

Enhanced Leptin Sensitivity, Reduced Adiposity, and Improved Glucose Homeostasis in Mice Lacking Exchange Protein Directly Activated by Cyclic AMP Isoform 1

inferredcites →https://doi.org/10.1146/annurev.biochem.76.060305.150444openalex-snapshot

Biochemistry and Physiology of Cyclic Nucleotide Phosphodiesterases: Essential Components in Cyclic Nucleotide Signaling

inferredcites →https://doi.org/10.1152/physrev.00025.2017openalex-snapshot

Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development

inferredcites →https://doi.org/10.1161/01.res.0000194325.31359.86openalex-snapshot

cAMP-Binding Protein Epac Induces Cardiomyocyte Hypertrophy

inferredcites →https://doi.org/10.1161/circresaha.107.164947openalex-snapshot

Epac Mediates β-Adrenergic Receptor–Induced Cardiomyocyte Hypertrophy

inferredcites →https://doi.org/10.1161/circresaha.116.309859openalex-snapshot

Multifunctional Mitochondrial Epac1 Controls Myocardial Cell Death

inferredcites →https://doi.org/10.1172/jci66241openalex-snapshot

Balancing GRK2 and EPAC1 levels prevents and relieves chronic pain

inferredcites →https://doi.org/10.1371/journal.pone.0030441openalex-snapshot

A Fluorescence-Based High-Throughput Assay for the Discovery of Exchange Protein Directly Activated by Cyclic AMP (EPAC) Antagonists

inferredcites →https://doi.org/10.1371/journal.pone.0107359openalex-snapshot

Activation of Exchange Protein Activated by cAMP in the Rat Basolateral Amygdala Impairs Reconsolidation of a Memory Associated with Self-Administered Cocaine

inferredcites →https://doi.org/10.1371/journal.ppat.1004520openalex-snapshot

The Central Role of cAMP in Regulating Plasmodium falciparum Merozoite Invasion of Human Erythrocytes

inferredcites →https://doi.org/10.1523/jneurosci.0999-04.2004openalex-snapshot

Presynaptic Mechanism Underlying cAMP-Dependent Synaptic Potentiation

inferredcites →https://doi.org/10.3390/cells8111462openalex-snapshot

Recent Advances in EPAC-Targeted Therapies: A Biophysical Perspective

inferredcites →https://doi.org/10.3390/jcdd4040022openalex-snapshot

The Potential of a Novel Class of EPAC-Selective Agonists to Combat Cardiovascular Inflammation

inferredcites →https://doi.org/10.7554/elife.02777openalex-snapshot

Structure of a low-population intermediate state in the release of an enzyme product

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Divergent Allostery Reveals Critical Differences between Structurally Homologous Regulatory Domains of Plasmodium Falciparum and Human Protein Kinase G

inferred← citeshttps://doi.org/10.1002/1873-3468.14610openalex-snapshot

An NMR portrait of functional and dysfunctional allosteric cooperativity in cAMP ‐dependent protein kinase A

inferred← citeshttps://doi.org/10.1016/j.biocel.2026.106944openalex-snapshot

“EPAC1: Molecular architecture, physiological regulation, and therapeutic implications in diseases”

inferred← citeshttps://doi.org/10.1016/j.bpj.2020.07.038openalex-snapshot

Allosteric Mechanisms of Nonadditive Substituent Contributions to Protein-Ligand Binding

inferred← citeshttps://doi.org/10.1016/j.csbj.2020.10.026openalex-snapshot

Allosteric inhibition explained through conformational ensembles sampling distinct “mixed” states

inferred← citeshttps://doi.org/10.1016/j.jbc.2022.101691openalex-snapshot

Divergent allostery reveals critical differences between structurally homologous regulatory domains of Plasmodium falciparum and human protein kinase G

inferred← citeshttps://doi.org/10.1016/j.pharmr.2025.100078openalex-snapshot

Role of exchange proteins directly activated by cAMP signaling in vascular remodeling

inferred← citeshttps://doi.org/10.1016/j.sbi.2021.06.002openalex-snapshot

Making the invisible visible: Toward structural characterization of allosteric states, interaction networks, and allosteric regulatory mechanisms in protein kinases

inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5c02974openalex-snapshot

Development and Evaluation of Benzofuran Oxoacetic Acid Compounds as EPAC1 Activators

inferred← citeshttps://doi.org/10.1021/acs.jmedchem.9b02094openalex-snapshot

Synthesis and Biochemical Evaluation of Noncyclic Nucleotide Exchange Proteins Directly Activated by cAMP 1 (EPAC1) Regulators

inferred← citeshttps://doi.org/10.1021/acs.jpcb.1c03622openalex-snapshot

Dynamical Basis of Allosteric Activation for the Plasmodium falciparum Protein Kinase G

inferred← citeshttps://doi.org/10.1038/s41598-022-20607-8openalex-snapshot

Protein interaction, cytotoxic, transcriptomic and proteomic responses to structurally distinct EPAC1 activators in HUVECs

inferred← citeshttps://doi.org/10.1039/d2cb00106copenalex-snapshot

QSAR models reveal new EPAC-selective allosteric modulators

inferred← citeshttps://doi.org/10.1039/d5sc02112jopenalex-snapshot

Elucidation of the mechanism of partial activation of EPAC1 allosteric modulators by Markov state modelling

inferred← citeshttps://doi.org/10.1080/21623945.2025.2603605openalex-snapshot

cAMP–PKA/EPAC signaling pathways: crucial regulators of lipid homeostasis

inferred← citeshttps://doi.org/10.1093/bioinformatics/btaa781openalex-snapshot

CHESPA/CHESCA-SPARKY: automated NMR data analysis plugins for SPARKY to map protein allostery

inferred← citeshttps://doi.org/10.1139/cjc-2021-0359openalex-snapshot

Allosteric regulation of cyclic nucleotide-dependent protein kinases

inferred← citeshttps://doi.org/10.3389/fphar.2022.929152openalex-snapshot

Epac: A Promising Therapeutic Target for Vascular Diseases: A Review

inferred← citeshttps://doi.org/10.3390/cells9091954openalex-snapshot

Role of EPAC1 Signalosomes in Cell Fate: Friends or Foes?

inferred← citeshttps://doi.org/10.3390/pathogens10101307openalex-snapshot

Host EPAC1 Modulates Rickettsial Adhesion to Vascular Endothelial Cells via Regulation of ANXA2 Y23 Phosphorylation

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