R
Richard G. MacDonald
Researcher at University of Nebraska Medical Center
Publications - 53
Citations - 1726
Richard G. MacDonald is an academic researcher from University of Nebraska Medical Center. The author has contributed to research in topics: Receptor & Mannose 6-phosphate. The author has an hindex of 23, co-authored 53 publications receiving 1669 citations. Previous affiliations of Richard G. MacDonald include Eppley Institute for Research in Cancer and Allied Diseases.
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Journal ArticleDOI
M6P/IGF2R imprinting evolution in mammals.
J. Keith Killian,James C. Byrd,James V Jirtle,BL Munday,Michael K. Stoskopf,Richard G. MacDonald,Randy L. Jirtle +6 more
TL;DR: It is shown that M6P/IGF2R is not imprinted in monotremes and does not encode for a receptor that binds IGF2, and invasive placentation and gestational fetal growth are not required for imprinted genes to evolve.
Journal ArticleDOI
Disruption of Ligand Binding to the Insulin-like Growth Factor II/Mannose 6-Phosphate Receptor by Cancer-associated Missense Mutations
TL;DR: Four of the five cancer-associated mutants analyzed demonstrated altered ligand binding, providing further evidence that loss of IGF2R function is characteristic of certain cancers.
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Insulin-sensitive phosphorylation of serine 1293/1294 on the human insulin receptor by a tightly associated serine kinase.
TL;DR: Analysis of the serine phosphate incorporated into partially purified or highly purified insulin receptor suggests that an insulin-sensitive serine kinase (IRSK) copurifies with the insulin receptor, and HPLC and two-dimensional separation indicate that the same phosphopeptide is obtained when affinity-purified insulin receptors are phosphorylated by IRSK.
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Single Transmembrane Domain Insulin-Like Growth Factor-II/Mannose-6-Phosphate Receptor Regulates Central Cholinergic Function by Activating a G-Protein-Sensitive, Protein Kinase C-Dependent Pathway
Cheryl A. Hawkes,Jack H. Jhamandas,Kim H. Harris,Wen Fu,Richard G. MacDonald,Satyabrata Kar,Satyabrata Kar +6 more
TL;DR: It is reported for the first time that the single transmembrane domain IGF-II/M6P receptor expressed in the rat brain is G-protein coupled and is involved in the regulation of central cholinergic function via the activation of specific intracellular signaling cascades.
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An Insulin-Like Growth Factor II (IGF-II) Affinity-Enhancing Domain Localized within Extracytoplasmic Repeat 13 of the IGF-II/Mannose 6-Phosphate Receptor
TL;DR: It is revealed that two independent receptor domains are involved in the formation of a high-affinity binding site for IGF-II, and that a complete repeat 13 is required for high-Affinity IGF- II binding.