TY - JOUR
T1 - Molecular biology of the voltage-gated sodium channel
AU - Salkoff, Lawrence
AU - Butler, Alice
AU - Wei, Aguan
AU - Scavarda, Nancy
AU - Baker, Keith
AU - Pauron, David
AU - Smith, Cynthia
N1 - Funding Information:
Supported by NIH grant I R01 NS24785-01, NSF grant BNS-8311024, and a grant from the EstherA . and Joseph Klingenstein Fund (L.5.), an NIH training grant 5-T32- NS07057-08 (A. W.), and grant NIHRSA 6M07200 from the NIGM5 (K.B. and C.S.).
PY - 1987/12
Y1 - 1987/12
N2 - The integral membrane protein composing the voltage-sensitive sodium channel is a bagel-like structure (Fig. 1) with a central pore that is highly selective for sodium ions. When the electric field across a cell's membrane becomes depolarized, the pore of the channel opens to allow sodium ions to flow down their electrochemical gradient into the cell1. Voltage-gating, a common feature of all voltage-activated channels, is an essential functional property that is only now being understood in terms of the structural features of the protein.
AB - The integral membrane protein composing the voltage-sensitive sodium channel is a bagel-like structure (Fig. 1) with a central pore that is highly selective for sodium ions. When the electric field across a cell's membrane becomes depolarized, the pore of the channel opens to allow sodium ions to flow down their electrochemical gradient into the cell1. Voltage-gating, a common feature of all voltage-activated channels, is an essential functional property that is only now being understood in terms of the structural features of the protein.
UR - http://www.scopus.com/inward/record.url?scp=45949115923&partnerID=8YFLogxK
U2 - 10.1016/0166-2236(87)90134-2
DO - 10.1016/0166-2236(87)90134-2
M3 - Review article
AN - SCOPUS:45949115923
SN - 0166-2236
VL - 10
SP - 522
EP - 527
JO - Trends in Neurosciences
JF - Trends in Neurosciences
IS - 12
ER -