M
Margaret P. Price
Researcher at Roy J. and Lucille A. Carver College of Medicine
Publications - 52
Citations - 9030
Margaret P. Price is an academic researcher from Roy J. and Lucille A. Carver College of Medicine. The author has contributed to research in topics: Acid-sensing ion channel & Mechanosensation. The author has an hindex of 38, co-authored 51 publications receiving 8508 citations. Previous affiliations of Margaret P. Price include University of Iowa & Howard Hughes Medical Institute.
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Journal ArticleDOI
Biochemical Basis of Touch Perception: Mechanosensory Function of Degenerin/Epithelial Na+ Channels
TL;DR: In insights into how DEG/ENaC channels may contribute to mechanosensation are reviewed, including the core of a multiprotein ion channel complex that opens in response to mechanical stimulation.
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Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel).
TL;DR: Using the yeast two-hybrid assay, it is found that the PDZ domain-containing protein PICK1 interacts specifically with the C-termini of BNC1 and ASIC, but not DRASIC or the related aENaC or b ENaC.
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ASIC3 and ASIC1 mediate FMRFamide-related peptide enhancement of H+-gated currents in cultured dorsal root ganglion neurons.
Jinghui Xie,Margaret P. Price,John A. Wemmie,John A. Wemmie,Candice C. Askwith,Michael J. Welsh +5 more
TL;DR: The results suggest that FMRFamide-related peptides, including the newly identified RFRPs, modulate H(+)-gated DRG currents through ASIC1 and ASIC3 and that ASIC3 plays the major role.
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DRASIC Contributes to pH-Gated Currents in Large Dorsal Root Ganglion Sensory Neurons by Forming Heteromultimeric Channels
TL;DR: The data indicate that the DRASIC subunit makes an important contribution to H+-gated currents in large DRG sensory neurons, and suggests that related acid-activated DEG/ENaC channel subunits contribute with DRASic to form heteromultimeric acid- activated channels.
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cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1
A. Soren Leonard,Olena Yermolaieva,Alesia Hruska-Hageman,Candice C. Askwith,Margaret P. Price,John A. Wemmie,Michael J. Welsh +6 more
TL;DR: The acid-sensing ion channel-1 (ASIC1) contributes to synaptic plasticity and may influence the response to cerebral ischemia and acidosis and regulation of this interaction by phosphorylation provides a mechanism to control the cellular localization of ASIC1.