Results 41 to 50 of about 2,309 (187)
Investigating role of ASIC2 in synaptic and behavioral responses to drugs of abuse
Drugs of abuse produce rearrangements at glutamatergic synapses thought to contribute to drug-reinforced behaviors. Acid-Sensing Ion Channels (ASICs) have been suggested to oppose these effects, largely due to observations in mice lacking the ASIC1A ...
Margaret J. Fuller +22 more
doaj +1 more source
Effects of acid-sensing ion channel-1A (ASIC1A) on cocaine-induced synaptic adaptations
Chronic drug abuse is thought to induce synaptic changes in nucleus accumbens medium spiny neurons (MSNs) that promote subsequent craving and drug-seeking behavior. Accumulating data suggest acid-sensing ion channels (ASICs) may play a critical role.
Subhash C. Gupta +17 more
doaj +1 more source
Channel Dysfunction as the Basis for Comorbidities in Multiple Sclerosis and Depression. [PDF]
Ion channel remodelling induced by neuroinflammation in multiple sclerosis alters neuronal excitability and immune signalling, creating shared molecular pathways that link multiple sclerosis pathology to depression and reveal novel pharmacological targets.
Rychlik N +4 more
europepmc +2 more sources
Opening the Pore of ASIC1a [PDF]
Acid-sensing ion channels (ASICs) are voltage-independent proton-gated ion channels expressed throughout neurons of the mammalian central and peripheral nervous systems. These channels are organized as homo- or hetero-trimers. Each subunit has two transmembrane segments (TMs) connected by a large extracellular region with the N- and C- termini on the ...
Tolino, Lindsey A. +3 more
openaire +1 more source
A Gating Mutation in the Internal Pore of ASIC1a [PDF]
Using a substituted cysteine accessibility scan, we have investigated the structures that form the internal pore of the acid-sensing ion channel 1a. We have identified the amino acid residues Ala-22, Ile-33, and Phe-34 in the amino terminus and Arg-43 in the first transmembrane helix, which when mutated into cysteine, were modified by intracellular ...
Pfister Y +5 more
openaire +3 more sources
Diminazene Interaction with ASIC1A Channels [PDF]
Diaryldiamidines, a class of DNA minor groove binders used clinically since the 1940s in the treatment of tropical parasitoses such as trypanosomiasis, leishmaniasis, pneumocystis pneumonia and babesiosis, have been recently found to exert specific blocking effects on acid-sensing ion channels (ASIC), raising hopes to develop new small molecule ...
Amuzescu, Bogdan P. +4 more
openaire +1 more source
Signaling Pathways in Proton and Non-proton ASIC1a Activation [PDF]
Acid-sensing ion channels (ASICs) regulate synaptic activities and play important roles in neurodegenerative diseases as well as pain conditions. Classically, ASICs are described as transiently activated by a reduced pH, followed by desensitization; the activation allows sodium influx, and in the case of ASIC1a-composed channels, also calcium to some ...
Libia Catalina Salinas Castellanos +2 more
openaire +4 more sources
Characteristics of ASIC1a, ASIC1a/ASIC2a and ASIC1a/ASIC2b channels.
A, Peak current ratios (pH6.6/pH5.0) obtained from whole-cell patch-clamp experiments performed in HEK293 cells transfected with either ASIC1a alone, ASIC1a+ASIC2a or ASIC1a+ASIC2b (n = 7–25, One-way ANOVA followed by a Tukey’s post hoc test with ****pB,
Ludivine Pidoux (12871781) +9 more
core +1 more source
CaM/CaMKII mediates activation and proliferation of hepatic stellate cells regulated by ASIC1a
The activation of hepatic stellate cells (HSCs) is closely related to hepatic fibrosis and plays a key role in its occurrence and development. In the damaged liver, inhibition of the activation, proliferation, and clearance of HSCs is an important ...
Hui Liu +30 more
doaj +1 more source
Light-dependent activation of ASIC1a.
A, Structural image of the ASIC1a trimer showing its domain organization; transmembrane (red), thumb (green), palm (yellow), β-ball (orange), finger (purple), and knuckle (cyan; human ASIC1a model based on chicken ASIC1a structure).
Stephan Kellenberger (5042927) +1 more
core +1 more source

