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Paul Blount
Researcher at University of Texas Southwestern Medical Center
Publications - 90
Citations - 6035
Paul Blount is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Mechanosensitive channels & Ion channel. The author has an hindex of 38, co-authored 87 publications receiving 5627 citations. Previous affiliations of Paul Blount include University of Wisconsin-Madison & Laboratory of Molecular Biology.
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Journal ArticleDOI
A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
Sergei Sukharev,Paul Blount,Boris Martinac,Boris Martinac,Frederick R. Blattner,Ching Kung,Ching Kung +6 more
TL;DR: The mscL nucleotide sequence predicts a unique protein of only 136 amino acids, with a highly hydrophobic core and very different from porins or other known proteins.
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Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities.
TL;DR: A 2.5-ns mechanosensitive conductance in giant E. coli spheroplasts is discovered and several residues, which when deleted or substituted, affect channel kinetics or mechanosensitivity are identified.
Journal ArticleDOI
Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
Paul Blount,John P. Merlie +1 more
TL;DR: Data support a model of two nonequivalent binding sites within the AChR and imply that the basis for this nonequivalence is the association of the alpha subunit with the gamma or delta subunit.
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ACh receptor-rich membrane domains organized in fibroblasts by recombinant 43-kildalton protein.
William D. Phillips,Carrie Kopta,Paul Blount,Paul D. Gardner,Joe Henry Steinbach,John P. Merlie +5 more
TL;DR: The mechanism of clustering was analyzed with fibroblast cell lines that were stably transfected with mouse muscle nicotinic acetylcholine receptors and it was suggested that 43-kilodalton protein can induce A ChR clustering and that cluster induction involves direct contact between AChR and 43- KilodAlton protein.
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One face of a transmembrane helix is crucial in mechanosensitive channel gating
TL;DR: The data suggest that the slowed or no-growth phenotype is caused by solute loss because of inappropriate gating of the channel, and most of the mutations mapped to the first transmembrane domain.