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Stephen B. Long
Researcher at Memorial Sloan Kettering Cancer Center
Publications - 36
Citations - 7098
Stephen B. Long is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Ion channel & Gating. The author has an hindex of 20, co-authored 34 publications receiving 6529 citations. Previous affiliations of Stephen B. Long include Duke University & Howard Hughes Medical Institute.
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Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel
TL;DR: In this paper, the authors reported the crystal structure of a mammalian voltage-dependent potassium ion (K+) channel, Kv1.2, which is a member of the Shaker K+ channel family.
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Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
TL;DR: The detailed structure of a chimaeric voltage-dependent K+ channel, which the authors call the ‘paddle-chimaera channel’, is described, which explains charge stabilization within the membrane and suggests a mechanism for voltage-sensor movements and pore gating.
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Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling
TL;DR: The x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing the investigation of the mechanism by which these channels sense cell membrane voltage.
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Crystal structure of the calcium release-activated calcium channel Orai.
TL;DR: The crystal structure of Orai from Drosophila melanogaster, determined at 3.35 angstrom resolution, reveals that the calcium channel is composed of a hexameric assembly of ORAi subunits arranged around a central ion pore, which regulates the flow of calcium into cells.
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Merlin/NF2 Suppresses Tumorigenesis by Inhibiting the E3 Ubiquitin Ligase CRL4DCAF1 in the Nucleus
Wei Li,Liru You,Jonathan Cooper,Jonathan Cooper,Gaia Schiavon,Angela Pepe-Caprio,Lu Zhou,Ryohei Ishii,Marco Giovannini,C. Oliver Hanemann,Stephen B. Long,Hediye Erdjument-Bromage,Pengbo Zhou,Paul Tempst,Filippo G. Giancotti +14 more
TL;DR: It is shown that the closed, growth-inhibitory form of Merlin accumulates in the nucleus, binds to the E3 ubiquitin ligase CRL4(DCAF1), and suppresses its activity.