Notes in Channels (Grover)

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Published	08/07/2024	There are significantly more {{c1::Kv}} α subunits than {{c1::Nav}}
Published	08/07/2024	{{c1::HVA}} channels are activated by a {{c2::large}} change in membrane potential.
Published	08/07/2024	{{c1::LVA}} channels activate with a {{c2::smaller}} change in membrane potential.
Published	08/07/2024	High voltage activated ({{c1::HVA}}) channels need a large change in membrane {{c2::potential}}.
Published	08/07/2024	Low voltage activated ({{c1::LVA}}) channels respond to {{c2::smaller}} changes in membrane potential.
Published	08/07/2024	Drugs may selectively target specific CaV subunits, including some {{c1::antihypertensive}} and {{c2::antiepileptic}} drugs.
Published	08/07/2024	CaV channels can be categorized by the {{c1::magnitude of membrane potential}} required to activate them: HVA (high voltage activated) or {{c2::LVA}} …
Published	08/07/2024	The α subunit family of CaV channels includes three families: {{c1::CaV1}}, {{c2::CaV2}}, and CaV3.
Published	08/07/2024	The older naming system for CaV channels includes alphabetical names such as {{c1::L-type}}, {{c2::N-type}}, P/Q-type, and R-type.
Published	08/07/2024	Leak channels are often described as lacking a {{c1::gating mechanism}}, and thus are {{c2::always open}} in the cell membrane.
Published	08/07/2024	Like other ion channels, leak channels are {{c1::selectively permeable}}.
Published	08/07/2024	Leak potassium channels, such as {{c1::KIR}} and {{c2::K2P}}, are selectively permeable to potassium ions.
Published	08/07/2024	The sodium-selective leak channel {{c1::NaVi2.1}} is permeable to sodium ions.
Published	08/07/2024	Leak channels play a crucial role in determining the {{c1::resting membrane potential}} of cells.
Published	08/07/2024	Inward rectifying potassium ({{c1::KIR}}) channels are more permeable to potassium flowing in an {{c2::inward}} direction.
Published	08/07/2024	KIR channels are composed of 4 {{c1::α}} subunits, each with 2 transmembrane segments and {{c2::1 pore}} loop.
Published	08/07/2024	The KIR channel does not have a {{c1::voltage-sensor}}, so it is not gated by membrane potential.
Published	08/07/2024	Two pore-domain potassium ({{c1::K2P}}) channels have a structure with 2 P-loops and {{c2::4 transmembrane}} segments.
Published	08/07/2024	K2P channels are composed of 2 {{c1::α}} subunits and are {{c2::dimers}}.
Published	08/07/2024	K2P channels, like KIR channels, do not have a {{c1::voltage-sensor}} and do not require membrane depolarization to {{c2::open}}.
Published	08/07/2024	KIR channels are regulated by {{c1::neurotransmitters}} through G protein-coupled receptors.
Published	08/07/2024	NaVi2.1 channels are structurally related to the {{c1::NaV1}} family but are not {{c2::voltage-sensitive}}.
Published	08/07/2024	The S4 segment in NaVi2.1 channels has fewer {{c1::positively charged}} amino acids compared to NaV1 channels.
Published	08/07/2024	NaVi2.1 channels do not exhibit {{c1::fast inactivation}}.
Published	08/07/2024	NaVi2.1 channels are formed from a single {{c1::α}} subunit with {{c2::4 domains}}.
Published	08/07/2024	None of the 6 {{c1::transmembrane segments}} in NaVi2.1 channels functions as a voltage-sensor.
Published	08/07/2024	Other NaV channelopathies affect the movement of the {{c1::S4 voltage-sensor}}, altering the process of {{c2::activation}}.
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