Philip E. Ryan
National Institutes of Health
12 Papers
80 Citations
Philip E. Ryan is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Proto-Oncogene Proteins c-cbl & Ubiquitin ligase. The author has an hindex of 8, co-authored 12 publications. Previous affiliations of Philip E. Ryan include University of California, Davis.
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Papers
•Journal Article
Characterization of a Novel Androgen Receptor Mutation in a Relapsed CWR22 Prostate Cancer Xenograft and Cell Line
Clifford G. Tepper,David L. Boucher,Philip E. Ryan,Ai Hong Ma,Liang Xia,Liang Xia,Li Fen Lee,Thomas G. Pretlow,Hsing Jien Kung +8 more
TL;DR: The CWR22Rv1 cell line displays both androgens-responsive and androgen-insensitive features due, at least in part, to a novel insertional mutation of the AR.
301
Cbl and human myeloid neoplasms: the Cbl oncogene comes of age.
TL;DR: The recent data begin to reconcile this paradox as the loss of ubiquitin ligase function ( the tumor suppressor function) is coupled to the maintenance of the positive signaling function (the oncogene function) and provide insight into potential therapeutic approaches to myeloid disorders harboring Cbl mutations.
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Profiling of gene expression changes caused by p53 gain-of-function mutant alleles in prostate cancer cells.
Clifford G. Tepper,Jeffrey P. Gregg,Xu Bao Shi,Ruth Louise Vinall,Colin A. Baron,Philip E. Ryan,Pierre Yves Desprez,Hsing Jien Kung,Ralph W deVere White +8 more
TL;DR: In this article, gene expression profiling was performed using Affymetrix HG-U95Av2 arrays followed by hierarchical clustering to identify expression patterns associated with particular molecular alterations.
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The N Terminus of Cbl-c Regulates Ubiquitin Ligase Activity by Modulating Affinity for the Ubiquitin-conjugating Enzyme
TL;DR: It is shown for the first time that phosphorylation of Tyr-341 or the Y341E mutation leads to a decrease in affinity for the ubiquitin-conjugating enzyme (E2), UbcH5b and that the decreased affinity of the Y 341E mutant Cbl-c for Ubch5b results in a more rapid turnover of bound Ubc H5b coincident with the increased E3 activity.
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Cbl interacts with multiple E2s in vitro and in cells.
Mariya S. Liyasova,Ke Ma,Donna Voeller,Philip E. Ryan,Jinqiu Chen,Rachel E. Klevit,Stanley Lipkowitz +6 more
TL;DR: It is suggested that multiple E2s can interact with Cbl and modulate its E3 activity in vitro and in cells, and that the Ube2d family, U be2e family, and Ube 2n/2v1 contributed to EGFR ubiquitination.
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