Daniel H. Cox
Tufts University
22 Papers
231 Citations
Daniel H. Cox is an academic researcher from Tufts University. The author has contributed to research in topics: Chemistry & Ligand-gated ion channel. The author has an hindex of 16, co-authored 22 publications. Previous affiliations of Daniel H. Cox include Howard Hughes Medical Institute & Stanford University.
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Papers
Abnormal Vascular Function and Hypertension in Mice Deficient in Estrogen Receptor β
Yan Zhu,Zhao Bian,Ping Lu,Richard H. Karas,Lin Bao,Daniel H. Cox,Jeffrey B. Hodgin,Philip W. Shaul,Peter Thorén,Oliver Smithies,Jan-Åke Gustafsson,Michael E. Mendelsohn +11 more
TL;DR: An essential role for ERβ in the regulation of vascular function and blood pressure is supported by show that vascular smooth muscle cells and blood vessels from estrogen receptor β (ERβ)–deficient mice exhibit multiple functional abnormalities.
519
Elimination of the BKCa Channel's High-Affinity Ca2+ Sensitivity
TL;DR: It is argued that the BKCa channel contains three types of Ca2+ binding sites, one of low affinity that is Mg2+ sensitive (as has been suggested previously) and two of higher affinity that have similar binding characteristics and contribute approximately equally to the power of Ca 2+ to influence channel opening.
124
Mapping the BKCa Channel's “Ca2+ Bowl”: Side-chains Essential for Ca2+ Sensing
TL;DR: Much of the data supports the conclusion that Ca2+ binds to the BKCa channel's intracellular domain, and acidic residues, D898 and D900, are found to be essential, and they define theCa2+ bowl's essential Ca2-sensing motif.
115
Pharmacological discrimination of N-type from L-type calcium current and its selective modulation by transmitters
Daniel H. Cox,Kathleen Dunlap +1 more
TL;DR: Both GABA and norepinephrine modulate the N- type component as evidenced by their lack of effect on the pure L-type tail current, prolonged by a dihydropyridine calcium channel agonist.
113
Measurements of the BKCa channel's high-affinity Ca2+ binding constants: effects of membrane voltage.
Tara-Beth Sweet,Daniel H. Cox +1 more
TL;DR: Ca2+ dose–response curves of channel activity at constant voltage for the wild-type mSlo channel and for channels that have had one or the other Ca2+ binding site disabled via mutation indicate that at −80 mV the Ca 2+ bowl has higher affinity for Ca2- than does the RCK1 site in both the opened and closed conformations of the channel.