Fred L. Robinson
Affiliations: | Vollum Institute | Oregon Health and Science University, Portland, OR |
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| Mammel AE, Delgado KC, Chin AL, et al. (2021) Distinct roles for the Charcot-Marie-tooth disease-causing endosomal regulators Mtmr5 and Mtmr13 in axon radial sorting and Schwann cell myelination. Human Molecular Genetics |
| Robinson DC, Mammel AE, Logan AM, et al. (2018) An In Vitro Model of Charcot-Marie-Tooth Disease Type 4B2 Provides Insight Into the Roles of MTMR13 and MTMR2 in Schwann Cell Myelination. Asn Neuro. 10: 1759091418803282 |
| Logan AM, Mammel AE, Robinson DC, et al. (2017) Schwann cell-specific deletion of the endosomal PI 3-kinase Vps34 leads to delayed radial sorting of axons, arrested myelination, and abnormal ErbB2-ErbB3 tyrosine kinase signaling. Glia |
| Ng AA, Logan AM, Schmidt EJ, et al. (2013) The CMT4B disease-causing phosphatases Mtmr2 and Mtmr13 localize to the Schwann cell cytoplasm and endomembrane compartments, where they depend upon each other to achieve wild-type levels of protein expression. Human Molecular Genetics. 22: 1493-506 |
| Jean S, Cox S, Schmidt EJ, et al. (2012) Sbf/MTMR13 coordinates PI(3)P and Rab21 regulation in endocytic control of cellular remodeling. Molecular Biology of the Cell. 23: 2723-40 |
| Robinson FL, Niesman IR, Beiswenger KK, et al. (2008) Loss of the inactive myotubularin-related phosphatase Mtmr13 leads to a Charcot-Marie-Tooth 4B2-like peripheral neuropathy in mice. Proceedings of the National Academy of Sciences of the United States of America. 105: 4916-21 |
| Robinson FL, Dixon JE. (2006) Myotubularin phosphatases: policing 3-phosphoinositides. Trends in Cell Biology. 16: 403-12 |
| Robinson FL, Dixon JE. (2005) The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease. The Journal of Biological Chemistry. 280: 31699-707 |
| Whitehurst AW, Robinson FL, Moore MS, et al. (2004) The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions. The Journal of Biological Chemistry. 279: 12840-7 |
| Robinson FL, Whitehurst AW, Raman M, et al. (2002) Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1. The Journal of Biological Chemistry. 277: 14844-52 |