ArticleStructure (London, England : 1993)2007
Structural and functional characterization of the human protein kinase ASK1.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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Who cites it
53 citing papers in PubMed.
- Mitogen-activated protein kinase kinase 4 (MKK4) as a promising therapeutic target in liver diseases: a review.Journal of enzyme inhibition and medicinal chemistry · 2026Review
- c-Jun in neurodegeneration: A key transcriptional regulator with therapeutic implications.Molecular therapy. Nucleic acids · 2026Review
- The GATA3-RFPL3-ASK1 axis suppresses breast cancer growth and lung metastasis.Apoptosis : an international journal on programmed cell death · 2026Article
- In silico analysis of MALAT1 and H19 lncRNA interactions with the diabetes-related proteins ASK1 and YAP1.In silico pharmacology · 2026Article
- Updated insights on ASK1 signaling: mechanisms, regulation, and therapeutic potential in diseases.Molecular and cellular biochemistry · 2025Review
- Targeting ASK1 signaling in neurodegeneration: molecular insights and therapeutic promise.Apoptosis : an international journal on programmed cell death · 2025Review
- Reactive oxygen species activate the Drosophila TNF receptor Wengen for damage-induced regeneration.The EMBO journal · 2024Article
- The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1.eLife · 2024Article
- Article
- The Function of ASK1 in Sepsis and Stress-Induced Disorders.International journal of molecular sciences · 2023Review
- Targeted therapeutics and novel signaling pathways in non-alcohol-associated fatty liver/steatohepatitis (NAFL/NASH).Signal transduction and targeted therapy · 2022Review
- Intrinsic disorder in proteins associated with oxidative stress-induced JNK signaling.Cellular and molecular life sciences : CMLS · 2022Article
- Crystallographic mining of ASK1 regulators to unravel the intricate PPI interfaces for the discovery of small molecule.Computational and structural biotechnology journal · 2022Review
- The sooner, the better: ROS, kinases and nutrients at the onset of the damage response inFrontiers in cell and developmental biology · 2022Review
- Structural Insights Support Targeting ASK1 Kinase for Therapeutic Interventions.International journal of molecular sciences · 2021Review
- ASKA technology-based pull-down method reveals a suppressive effect of ASK1 on the inflammatory NOD-RIPK2 pathway in brown adipocytes.Scientific reports · 2021Article
- Prdx1 Interacts with ASK1 upon Exposure to HAntioxidants (Basel, Switzerland) · 2021Article
- WNKs are potassium-sensitive kinases.American journal of physiology. Cell physiology · 2021Article
- Cells recognize osmotic stress through liquid-liquid phase separation lubricated with poly(ADP-ribose).Nature communications · 2021Article
- Demystifying Chronic Kidney Disease of Unknown Etiology (CKDu): Computational Interaction Analysis of Pesticides and Metabolites with Vital Renal Enzymes.Biomolecules · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Apoptosis signal-regulating kinase 1 (ASK1) plays an essential role in stress and immune response and has been linked to the development of several diseases. Here, we present the structure of the human ASK1 catalytic domain in complex with staurosporine. Analytical ultracentrifugation (AUC) and crystallographic analysis showed that ASK1 forms a tight dimer (K(d) approximately 0.2 microM) interacting in a head-to-tail fashion. We found that the ASK1 phosphorylation motifs differ from known ASK1 phosphorylation sites but correspond well to autophosphorylation sites identified by mass spectrometry. Reporter gene assays showed that all three identified in vitro autophosphorylation sites (Thr813, Thr838, Thr842) regulate ASK1 signaling, but site-directed mutants showed catalytic activities similar to wild-type ASK1, suggesting a regulatory mechanism independent of ASK1 kinase activity. The determined high-resolution structure of ASK1 and identified ATP mimetic inhibitors will provide a first starting point for the further development of selective inhibitors.
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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.