Results 51 to 60 of about 175,721 (299)

A glycine receptor is involved in the organization of swimming movements in an invertebrate chordate

open access: yesBMC Neuroscience, 2010
Background Rhythmic motor patterns for locomotion in vertebrates are generated in spinal cord neural networks known as spinal Central Pattern Generators (CPGs).
Okamura Yasushi   +3 more
doaj   +1 more source

Chameleon sequences reveal structural effects in proteins representing micelle‐like distribution of hydrophobicity

open access: yesFEBS Open Bio, EarlyView.
Amino acids sequence of two different proteins with the same sequence (chameleon sequence—black boxes) represent in 3D structure of the proteins different secondary structures: HHHH—helical and BBB—Beta‐structural. The chains folded in water environment adopt different III‐order structures in which the chameleon fragments appear to adopt similar status
Irena Roterman   +4 more
wiley   +1 more source

Matrix metalloproteinase‐9 regulates cell adhesion and membrane protrusive activity of ovarian cancer cells

open access: yesFEBS Open Bio, EarlyView.
Matrix metalloproteinase‐9 (MMP9) drives ovarian cancer progression. Using MMP9‐null cells (M9‐KO) created from ovarian cancer cells, we found MMP9 loss did not block Epidermal Growth Factor (EGF)‐driven E‐cadherin dissolution or EMT but delayed and reduced EGF‐driven membrane protrusions. Transient MMP9 re‐expression drove membrane protrusion.
Claire Strauel   +8 more
wiley   +1 more source

Glycine Receptors in Spinal Nociceptive Control—An Update

open access: yesBiomolecules, 2021
Diminished inhibitory control of spinal nociception is one of the major culprits of chronic pain states. Restoring proper synaptic inhibition is a well-established rational therapeutic approach explored by several pharmaceutical companies.
Hanns Ulrich Zeilhofer   +3 more
doaj   +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 ...
A N, van den Pol, T, Gorcs
openaire   +2 more sources

Glycine Transporters and Its Coupling with NMDA Receptors

open access: yes, 2017
Glycine plays two roles in neurotransmission. In caudal areas like the spinal cord and the brainstem, it acts as an inhibitory neurotransmitter, but in all regions of the CNS, it also works as a co-agonist with L-glutamate at N-methyl-D-aspartate ...
Ibáñez, Ignacio   +11 more
core   +1 more source

Identifying transcription factors controlling the basal expression of human MRP4 highlights a substantial role for Sp1

open access: yesFEBS Open Bio, EarlyView.
The MRP4 transporter exports several drugs and signaling molecules. Here, we identified key promoter elements regulating basal MRP4 expression. Using reporter assays, we defined a conserved region with essential Sp1 and contributory Ets sites, which controlled basal MRP4 expression.
Debora Singer   +7 more
wiley   +1 more source

Structures, Diversity and Pharmacology of Glycine Receptors and Transporters

open access: yes, 2001
The amino acid glycine is highly concentrated in the ventral and dorsal horns of the spinal cord, in many brain stem nuclei, and in sensory relay stations such as the cochlear nucleus and the retina.
H. Betz   +5 more
core   +1 more source

Gephyrin, the enigmatic organizer at GABAergic synapses

open access: yesFrontiers in Cellular Neuroscience, 2012
GABAA receptors are clustered at synaptic sites to achieve a high density of postsynaptic receptors opposite the input axonal terminals. This allows an efficient propagation of GABA mediated signals, which mostly result in neuronal inhibition.
Verena Eva Tretter   +5 more
doaj   +1 more source

Molecular dynamics simulations of positively selected codons in FcγRI reveal novel biochemical binding properties

open access: yesFEBS Open Bio, EarlyView.
Evolutionary analysis across 32 placental mammals identified positive selection at residues H148 and W149 in the immune receptor FcγR1. Ancestral reconstruction combined with molecular dynamics simulations reveals how these mutations may influence receptor structure and dynamics, providing insight into the evolution of antibody recognition and immune ...
David A. Young   +7 more
wiley   +1 more source

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