ELK Promotion

The S100 proteins are a family of low-molecular-weight proteins found in vertebrates and characterized by two calcium-binding sites that have helix-loop-helix ("EF-hand type") conformation.

Despite their relatively small size (8-12 kDa) and uncomplicated architecture, S100 proteins regulate a variety of cellular processes such as cell growth and motility, cell cycle progression, transcription, and differentiation.

Estrogen receptors are a group of proteins found inside cells. Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains.

Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry a evolutionarily conserved domain called the prohibitin homology domain. May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.

Bcl-xL prevents apoptosis through two different mechanisms: heterodimerization with an apoptotic protein inhibits its apoptotic effect and formation of mitochondrial outer membrane pores help maintain a normal membrane state under stressful conditions.

Nuclear factor (erythroid-derived 2)-like 2, also known as NFE2L2 or Nrf2, is a transcription factor that in humans is encoded by the NFE2L2 gene. Small amounts of constitutive nuclear NRF2 maintain cellular homeostasis through regulation of basal expression of antioxidant response genes.

Amiloride-sensitive cation channel 2, neuronal is a protein that in humans is encoded by the ACCN2 gene.

Brain-specific angiogenesis inhibitor 1 is a protein that in humans is encoded by the BAI1 gene.It is a member of the adhesion-GPCR family of receptors.

Bestrophins were first found by genetic linkage of human-Bestrophin-1 (hBest1) to a juvenile form of macular degeneration called Best vitelliform macular dystrophy (BVMD). Forms calcium-sensitive chloride channels.

Bombesin receptor 2 (BB2) is a member of a family of receptors that binds the 14 amino acid peptide, bombesin.

Calcium binding proteins are an important component of calcium mediated cellular signal transduction. It has two EF hand motifs and is expressed in neuronal cells in such areas as hippocampus, habenular nucleus of the epithalamus, Purkinje cell layer of the cerebellum, and the amacrine cells and cone bipolar cells of the retina.

Glutamate receptor 1 is a protein that in humans is encoded by the GRIA1 gene. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist.

This gene belongs to a subfamily of calcium binding proteins that share similarity to calmodulin. Like calmodulin, these family members can likely stimulate calmodulin-dependent kinase II and the protein phosphatase calcineurin.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel.

Receptor for gastrin and cholecystokinin. The CKK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity.

Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.

Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.

CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.

CXCR4 is a chemokine receptor that belongs to the G protein-coupled receptor family. The main function of CXCR4 is the mediation of the homing of progenitor cells in the bone marrow and their recruitment to sites of injury.

The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands.

Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.

GALR2 Receptor for the hormone galanin and for GALP. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).

Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP).

The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents. Activated by arachidonic acid and other naturally occurring unsaturated free fatty acids.

KCNK4 belongs to the two pore domain potassium channel family and is an outward rectifying potassium channel. This channel produces rapidly activating and non-inactivating outward rectifier K(+) currents.

KCNK9 or TASK-3 (TWIK-related Acid sensitive K+ channel) is a member of the potassium channel family of proteins that contain two-pore domain and four transmembrane domains. These channels are characterized as leak K+ channels that are sensitive to changes in the extracellular pH.

Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system.

Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization.

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization.

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization.

Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells.

Human K(v) channel interacting protein 1 (KCHIP1) is a new member of the neural calcium binding protein superfamily. Members of the KCNIP family are small calcium binding proteins. They all have EF-hand-like domains, and differ from each other in the N-terminus. They are integral subunit components of native Kv4 channel complexes. They may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. KChIP1 is a neuronal calcium sensor protein that is predominantly expressed at GABAergic synapses and it has been related with modulation of K(+) channels, GABAergic transmission and cell death.