Structural basis for the preference of the Arabidopsis thaliana phosphatase RLPH2 for tyrosine-phosphorylated substrates
Author:
Affiliation:
1. Department of Biological Sciences, University of Calgary, 2500 University Drive Northwest, Calgary, Alberta T2N 1N4, Canada.
2. Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2R3, Canada.
Abstract
Funder
NSERC
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. Preface
2. Ultradeep Human Phosphoproteome Reveals a Distinct Regulatory Nature of Tyr and Ser/Thr-Based Signaling
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5. Insight into the redox regulation of the phosphoglucan phosphatase SEX4 involved in starch degradation
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1. Phospho-proteomics identifies D-group MAP kinases as substrates of the Arabidopsis tyrosine phosphatase RLPH2;2024-08-26
2. Importance of tyrosine phosphorylation for transmembrane signaling in plants;Biochemical Journal;2021-07-23
3. Origin of the Phosphoprotein Phosphatase (PPP) sequence family in Bacteria: Critical ancestral sequence changes, radiation patterns and substrate binding features;BBA Advances;2021
4. Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism;Frontiers in Plant Science;2018-07-17
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