ArticleActa crystallographica. Section D, Biological crystallography2011
Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- 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
- A Review of DUSP26: Structure, Regulation and Relevance in Human Disease.International journal of molecular sciences · 2021Review
- Molecular Architecture of the Inositol Phosphatase Siw14.Biochemistry · 2019Article
- Structural mechanisms of plant glucan phosphatases in starch metabolism.The FEBS journal · 2016Review
- Structural Insight into the Critical Role of the N-Terminal Region in the Catalytic Activity of Dual-Specificity Phosphatase 26.PloS one · 2016Article
- Global gene expression patterns of grass carp following compensatory growth.BMC genomics · 2015Article
- Article
- Structure of human PIR1, an atypical dual-specificity phosphatase.Biochemistry · 2014Article
- Impaired embryonic motility in dusp27 mutants reveals a developmental defect in myofibril structure.Disease models & mechanisms · 2014Article
- Article
- Structure and catalytic mechanism of human protein tyrosine phosphatome.BMB reports · 2012Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
There are over 100 genes in the human genome that encode protein tyrosine phosphatases (PTPs) and approximately 60 of these are classified as dual-specificity phosphatases (DUSPs). Although many dual-specificity phosphatases are still not well characterized, novel functions have been discovered for some of them that have led to new insights into a variety of biological processes and the molecular basis for certain diseases. Indeed, as the functions of DUSPs continue to be elucidated, a growing number of them are emerging as potential therapeutic targets for diseases such as cancer, diabetes and inflammatory disorders. Here, the overexpression, purification and structure determination of DUSP27 at 2.38 Å resolution are presented.
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