O
Owen P. Hamill
Researcher at University of Texas Medical Branch
Publications - 82
Citations - 24210
Owen P. Hamill is an academic researcher from University of Texas Medical Branch. The author has contributed to research in topics: Mechanosensitive channels & Ion channel. The author has an hindex of 32, co-authored 82 publications receiving 23913 citations. Previous affiliations of Owen P. Hamill include University of Texas System & Max Planck Society.
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Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches.
TL;DR: The extracellular patch clamp method, which first allowed the detection of single channel currents in biological membranes, has been further refined to enable higher current resolution, direct membrane patch potential control, and physical isolation of membrane patches.
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Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones.
TL;DR: The ion‐selective and ion transport properties of glycine receptor and gamma‐aminobutyric acid receptor channels in the soma membrane of mouse spinal cord neurones were investigated using the whole‐cell, cell‐attached and outside‐out patch versions of the patch‐clamp technique, indicating that GlyR and GABAR channels are multi‐conductance‐state channels.
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Molecular basis of mechanotransduction in living cells
Owen P. Hamill,Boris Martinac +1 more
TL;DR: The simplest cell-like structure, the lipid bilayer vesicle, can respond to mechanical deformation by elastic membrane dilation/thinning and curvature changes and changes in local membrane curvature may shift the equilibrium between channel conformations.
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TRPC1 forms the stretch-activated cation channel in vertebrate cells
TL;DR: A membrane-protein fraction that reconstituted high MscCa activity and showed an abundance of a protein that had a relative molecular mass of 80,000 (Mr 80K) indicate that TRPC1 is a component of the vertebrate MSCCa, which is gated by tension developed in the lipid bilayer, as is the case in various prokaryotic mechanosensitive (Ms) channels.
Journal Article
The pharmacology of mechanogated membrane ion channels.
Owen P. Hamill,Don W. McBride +1 more
TL;DR: The observation that MG channels can be chemically blocked and/or activated by a wide range of compounds requires revision of the long-standing conclusion of Paintal that mechanotransduction is a process that has a low susceptibility to chemical influence.