ArticleProtein science : a publication of the Protein Society2018
Crystal structure of the human dual specificity phosphatase 1 catalytic domain.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.
- Rare variant analysis in eczema identifies exonic variants in DUSP1, NOTCH4 and SLC9A4.Nature communications · 2021Pooled it
- Review
- Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms.Journal of microbiology (Seoul, Korea) · 2025Review
- p38α MAPK Regulation of Energy Metabolism in Skeletal Muscle Offers a Therapeutic Path for Type 2 Diabetes.Cells · 2025Review
- Genome-wide characterization and comparative expression profiling ofFrontiers in immunology · 2024Article
- Monobodies as enabling tools for structural and mechanistic biology.Current opinion in structural biology · 2020Review
- Improving Obesity and Insulin Resistance by Targeting Skeletal Muscle MKP-1.Journal of cellular signaling · 2020Article
- MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.Acta crystallographica. Section F, Structural biology communications · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 Å resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain.
Indexed as
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What OpenQuestion holds
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.