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2 documents found
1: Title: Phosphorylated TandeMBP: A unique protein substrate for protein phosphatase assay.
Authors: Sugiyama, Yasunori, et.al. .
Journal: Analytical biochemistry (Anal Biochem), Vol. 513, 2016 .
Snippet: Moreover, P-TandeMBP served as an efficient substrate for PPM family phosphatases (PPM1A, PPM1B, PPM1D, PPM1F, PPM1G, PPM1H, PPM1K, and PPM1M) and PPP family phosphatase PP5.
Affiliation: Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa 761-0795, Japan. Electronic address: sugiyama@ag.kagawa-u.ac.jp. Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa 761-0795, Japan. Department of Life Sciences, Faculty of Agriculture, Kagawa University, Kagawa 761-0795, Japan; Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki 305-8566, Japan. Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo 135-0064, Japan. Health Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Osaka 563-8577, Japan. .
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2: Title: The modulation of phosphatase expression impacts the proliferation efficiency of HSV-1 in infected astrocytes.
Authors: Yue, Lei, et.al. .
Journal: PloS one, Vol. 8 (11): e79648, 2013 .
Snippet: The results showed that the downregulation of five phosphatase genes (PNKP, SNAP23, PTPRU, LOC714621 and PPM1M) significantly inhibited HSV-1 infection, suggesting that these phosphatases were needed in HSV-1 replication in rhesus astrocytes.
Affiliation: Institute of Medical Biology, Chinese Academy of Medicine Science & Peking Union Medical College, Kunming, People's Republic of China. .
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