BIOMAT Database Logo BIOMAT Database Logo

Polypeptide toxins as tools to study voltage-sensitive Na+ channels. 1986

M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne

UI MeSH Term Description Entries
D007473 Ion Channels Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS. Membrane Channels,Ion Channel,Ionic Channel,Ionic Channels,Membrane Channel,Channel, Ion,Channel, Ionic,Channel, Membrane,Channels, Ion,Channels, Ionic,Channels, Membrane
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008564 Membrane Potentials The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization). Resting Potentials,Transmembrane Potentials,Delta Psi,Resting Membrane Potential,Transmembrane Electrical Potential Difference,Transmembrane Potential Difference,Difference, Transmembrane Potential,Differences, Transmembrane Potential,Membrane Potential,Membrane Potential, Resting,Membrane Potentials, Resting,Potential Difference, Transmembrane,Potential Differences, Transmembrane,Potential, Membrane,Potential, Resting,Potential, Transmembrane,Potentials, Membrane,Potentials, Resting,Potentials, Transmembrane,Resting Membrane Potentials,Resting Potential,Transmembrane Potential,Transmembrane Potential Differences
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D009498 Neurotoxins Toxic substances from microorganisms, plants or animals that interfere with the functions of the nervous system. Most venoms contain neurotoxic substances. Myotoxins are included in this concept. Alpha-Neurotoxin,Excitatory Neurotoxin,Excitotoxins,Myotoxin,Myotoxins,Neurotoxin,Alpha-Neurotoxins,Excitatory Neurotoxins,Excitotoxin,Alpha Neurotoxin,Alpha Neurotoxins,Neurotoxin, Excitatory,Neurotoxins, Excitatory
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011950 Receptors, Cholinergic Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology. ACh Receptor,Acetylcholine Receptor,Acetylcholine Receptors,Cholinergic Receptor,Cholinergic Receptors,Cholinoceptive Sites,Cholinoceptor,Cholinoceptors,Receptors, Acetylcholine,ACh Receptors,Receptors, ACh,Receptor, ACh,Receptor, Acetylcholine,Receptor, Cholinergic,Sites, Cholinoceptive
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Voltage-sensitive Na+ channels in mammalian peripheral nerves detected using scorpion toxins.
December 1990, Journal of neurocytology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Overview of toxins and drugs as tools to study excitable membrane ion channels: I. Voltage-activated channels.
January 1992, Methods in enzymology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Molecular diversity of voltage-sensitive Na channels.
January 1989, Annual review of physiology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Voltage-dependent blockade of muscle Na+ channels by guanidinium toxins.
November 1984, The Journal of general physiology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Voltage-sensitive Na+ channels: motifs, modes and modulation.
August 1991, Current opinion in cell biology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Voltage-Gated K+/Na+ Channels and Scorpion Venom Toxins in Cancer.
January 2020, Frontiers in pharmacology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Scorpion toxins as tools for studying potassium channels.
January 1999, Methods in enzymology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Two new scorpion toxins that target voltage-gated Ca2+ and Na+ channels.
December 2002, Biochemical and biophysical research communications,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Postnatal development of voltage-sensitive Na+ channels in rat brain.
July 1994, The Journal of comparative neurology,
M Lazdunski, and C Frelin, and J Barhanin, and A Lombet, and H Meiri, and D Pauron, and G Romey, and A Schmid, and H Schweitz, and P Vigne
Overview of toxins and drugs as tools to study excitable membrane ion channels: II. Transmitter-activated channels.
January 1992, Methods in enzymology,
Copied contents to your clipboard!