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Federico Sesti

Researcher at Rutgers University

Publications -  61
Citations -  4334

Federico Sesti is an academic researcher from Rutgers University. The author has contributed to research in topics: Potassium channel & Caenorhabditis elegans. The author has an hindex of 28, co-authored 55 publications receiving 4110 citations. Previous affiliations of Federico Sesti include University of Genoa & Yale University.

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MiRP1 Forms IKr Potassium Channels with HERG and Is Associated with Cardiac Arrhythmia

TL;DR: A mechanism for acquired arrhythmia is revealed: genetically based reduction in potassium currents that remains clinically silent until combined with additional stressors.
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A common polymorphism associated with antibiotic-induced cardiac arrhythmia

TL;DR: It is concluded that allelic variants of MiRP1 contribute to a significant fraction of cases of drug-induced LQTS through multiple mechanisms and that common sequence variations that increase the risk of life-threatening drug reactions can be clinically silent before drug exposure.
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Single-walled Carbon Nanotubes Are a New Class of Ion Channel Blockers

TL;DR: A novel class of biological membrane ion channel blockers called single-walled carbon nanotubes (SWNTs) are identified and postulate new uses for SWNTs in biological applications and provide unexpected insights into the current view of mechanisms governing the interaction of ion channels with blocking molecules.
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The Native Rat Olfactory Cyclic Nucleotide-Gated Channel Is Composed of Three Distinct Subunits

TL;DR: It is concluded that the native CNG channel in OSNs is composed of all three subunits, and that CNG channels in both rod photoreceptors and olfactory sensory neurons result from coassembly of specific α subunits with various forms of an alternatively spliced β subunit.
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A 240 kDa protein represents the complete β subunit of the cyclic nucleotide-gated channel from rod photoreceptor

TL;DR: It is demonstrated by peptide sequencing and by cloning and functional expression of cDNA that the 240 kDa protein represents the complete beta subunit with an unusual bipartite structure.