Blog
About

0
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Approaches to Study Phosphatases

      1 , 1 , 1

      ACS Chemical Biology

      American Chemical Society (ACS)

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Phosphatases play key roles in normal physiology and diseases. Studying phosphatases has been both essential and challenging, and the application of conventional genetic and biochemical methods has led to crucial but still limited understanding of their mechanisms, substrates, and exclusive functions within highly intricate networks. With the advances in technologies such as cellular imaging and molecular and chemical biology in terms of sensitive tools and methods, the phosphatase field has thrived in the past years and has set new insights for cell signaling studies and for therapeutic development. In this review, we give an overview of the existing interdisciplinary tools for phosphatases, give examples on how they have been applied to increase our understanding of these enzymes, and suggest how they-and other tools yet barely used in the phosphatase field-might be adapted to address future questions and challenges.

          Related collections

          Author and article information

          Journal
          ACS Chemical Biology
          ACS Chem. Biol.
          American Chemical Society (ACS)
          1554-8929
          1554-8937
          October 12 2016
          November 18 2016
          October 04 2016
          November 18 2016
          : 11
          : 11
          : 2944-2961
          Affiliations
          [1 ]European Molecular Biology Laboratory, Genome Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany
          Article
          10.1021/acschembio.6b00570
          27700050
          © 2016

          Comments

          Comment on this article