Results 21 to 30 of about 230,640 (243)

Effects of NR1 splicing on NR1/NR3B-type excitatory glycine receptors [PDF]

open access: yes, 2009
BACKGROUND: N-methyl-D-aspartate receptors (NMDARs) are the most complex of ionotropic glutamate receptors (iGluRs). Subunits of this subfamily assemble into heteromers, which – depending on the subunit combination – may display very different ...
Angela Orth   +2 more
core   +2 more sources

Differential Actions of Ethanol and Trichloroethanol at Sites in the M3 and M4 Domains of the NMDA Receptor GluN2A (NR2A) Subunit [PDF]

open access: yes, 2009
Background and purpose:  Alcohol produces its behavioural effects in part due to inhibition of N-methyl-d-aspartate (NMDA) receptors in the CNS. Previous studies have identified amino acid residues in membrane-associated domains 3 (M3) and 4 (M4) of the ...
Hu, Xiang-Qun   +5 more
core   +3 more sources

Different Sites of Alcohol Action in the NMDA Receptor GluN2A and GluN2B Subunits [PDF]

open access: yes, 2015
The NMDA receptor is a major target of alcohol action in the CNS, and recent behavioral and cellular studies have pointed to the importance of the GluN2B subunit in alcohol action.
Allgaier   +68 more
core   +2 more sources

Novel Modulators of Glycine Receptors [PDF]

open access: yesBiophysical Journal, 2016
Inhibitory glycine receptors (GlyRs) are pentameric ligand-gated ion channels, found primarily in the spinal cord, and are important targets for neuroactive drugs. Δ9-tetrahydrocannabinol (THC) potentiates the glycine receptor by interacting with residue S296 in GlyR-α1 and S307 in GlyR-α3 subunits, directly contributing to cannabis-induced analgesia ...
Pei Tang   +3 more
openaire   +2 more sources

Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits [PDF]

open access: yes, 2003
The subunits that compose eukaryotic glutamate ion channel receptors have three transmembrane domains (TMs) and terminate with intracellular tails that are important for controlling channel expression and localization.
Colquhoun, D., Schorge, S.
core   +1 more source

Glycine and glycine receptor immunoreactivity in brain and spinal cord [PDF]

open access: yesThe Journal of Neuroscience, 1988
To study the distribution of glycine immunoreactive neurons in the spinal cord and brain, antisera were raised against glycine conjugated to protein carriers. High-titer rabbit glycine antiserum was purified by affinity chromatography. Testing against other amino acids and peptides with immuno dot blots and ELISA assays showed little apparent cross ...
AN van den Pol, T Gorcs
openaire   +3 more sources

C-Terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors [PDF]

open access: yes, 2000
NMDA receptors interact via the extended intracellular C-terminal domain of the NR2 subunits with constituents of the postsynaptic density for purposes of retention, clustering, and functional regulation at central excitatory synapses.
Kennedy, Mary B.   +5 more
core   +1 more source

Ion channel function of polycystin‐2/polycystin‐1 heteromer revealed by structure‐guided mutagenesis

open access: yesFEBS Letters, EarlyView.
Mutations in polycystin‐1 (PC1) or polycystin‐2 (PC2) cause autosomal‐dominant polycystic kidney disease (ADPKD). We generated a novel gain‐of‐function PC2/PC1 heteromeric ion channel by mutating pore‐blocking residues. Moreover, we demonstrated that PC2 will preferentially assemble with PC1 to form heteromeric complexes when PC1 is co‐expressed ...
Tobias Staudner   +7 more
wiley   +1 more source

Autophagy in cancer and protein conformational disorders

open access: yesFEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

Single-channel behavior of heteromeric α1β glycine receptors: an attempt to detect a conformational change before the channel opens [PDF]

open access: yes, 2004
The α1β heteromeric receptors are likely to be the predominant synaptic form of glycine receptors in the adult. Their activation mechanism was investigated by fitting putative mechanisms to single-channel recordings obtained at four glycine ...
Beato, M.   +4 more
core  

Home - About - Disclaimer - Privacy