scholarly journals Three Arginines in the GABAA Receptor Binding Pocket Have Distinct Roles in the Formation and Stability of Agonist- versus Antagonist-Bound Complexes

2011 ◽  
Vol 80 (4) ◽  
pp. 647-656 ◽  
Author(s):  
Marcel P. Goldschen-Ohm ◽  
David A. Wagner ◽  
Mathew V. Jones
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Binding Pocket

Subchronic phencyclidine in rats: alterations in locomotor activity, maze performance, and GABAA receptor binding

2010 ◽  
Vol 21 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Richard J. Beninger ◽  
Jonathan Beuk ◽  
Tomek J. Banasikowski ◽  
Michael van Adel ◽  
Gregory A. Boivin ◽  
...  
Keyword(s):  
Locomotor Activity ◽  
Gabaa Receptor ◽  
Receptor Binding ◽  
Maze Performance

Celecoxib does not induce convulsions nor does it affect GABAA receptor binding activity in the presence of new quinolones in mice

2005 ◽  
Vol 507 (1-3) ◽  
pp. 69-76 ◽  
Author(s):  
Taiji Yoshino ◽  
Masahiro Noguchi ◽  
Hiroko Okutsu ◽  
Aishi Kimoto ◽  
Masao Sasamata ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Binding Activity ◽  
Receptor Binding Activity ◽  
New Quinolones

Measurement of GABAA receptor binding in vivo with [11C]Flumazenil: A test–retest study in healthy subjects

NeuroImage ◽  
2008 ◽  
Vol 41 (2) ◽  
pp. 260-269 ◽  
Author(s):  
Elina Salmi ◽  
Sargo Aalto ◽  
Jussi Hirvonen ◽  
Jaakko W. Långsjö ◽  
Anu T. Maksimow ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Healthy Subjects

Effect of synthetic steroids on GABAA receptor binding in rat brain

Neuroscience ◽  
2015 ◽  
Vol 290 ◽  
pp. 138-146 ◽  
Author(s):  
M. Rey ◽  
A.S. Veleiro ◽  
A.A. Ghini ◽  
M.S. Kruse ◽  
G. Burton ◽  
...  
Keyword(s):  
Rat Brain ◽  
Gabaa Receptor ◽  
Receptor Binding ◽  
Synthetic Steroids

Focus on GABAA receptor function

2014 ◽  
Vol 53 (06) ◽  
pp. 227-337 ◽  
Author(s):  
H. Hautzel ◽  
H.-W. Müller ◽  
S. Nikolaus
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Temporal Cortex ◽  
Primary Diagnosis ◽  
Receptor Function ◽  
Healthy Individuals ◽  
Major Depressive ◽  
Neuropsychiatric Diseases ◽  
Pubmed Search

SummaryImpairment of GABAA receptor function is increasingly recognized to play a major role in the pathophysiology of neuropsychiatric diseases including anxiety disorder (AD), major depressive disorder (MDD) and schizophrenia (SZ). Patients, method: We conducted a PUBMED search, which provided a total of 23 in vivo investigations with PET and SPECT, in which GABAA receptor binding in patients with the primary diagnosis of AD (n = 14, 160 patients, 172 controls), MDD (n = 2, 24 patients, 28 controls) or SZ (n = 6, 77 patients, 90 controls) was compared to healthy individuals. Results: A retrospective analysis revealed that AD, MDD and SZ differed as to both site(s) and extent(s) of GABAergic impairment. Additionally, it may be stated that, while the decline of GABAA receptor binding AD involved the whole mesolimbocortical system, in SZ it was confined to the frontal and temporal cortex. Conclusion: As GABA is known to inhibit dopamine and serotonin, GABAergic dysfunction may be associated with the disturbances of dopaminergic and serotonergic neurotransmission in neuropsychiatric disorders.

A Comprehensive Ligand Based Mapping of the σ2 Receptor Binding Pocket

2013 ◽  
Vol 10 (1) ◽  
pp. 98-121 ◽  
Author(s):  
Derek Rhoades ◽  
David Kinder ◽  
Tarek Mahfouz
Keyword(s):  
Receptor Binding ◽  
Binding Pocket

scholarly journals GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity

1993 ◽  
Vol 122 (6) ◽  
pp. 1253-1265 ◽  
Author(s):  
GW Kemble ◽  
YI Henis ◽  
JM White
Keyword(s):  
Cell Surface ◽  
Receptor Binding ◽  
Conformational Changes ◽  
Binding Pocket ◽  
Binding Activity ◽  
Great Distance ◽  
Fusion Peptides ◽  
Wild Type ◽  
Influenza Hemagglutinin ◽  
Receptor Binding Activity

We investigated the influence of a glycosylphosphatidylinositol (GPI) anchor on the ectodomain of the influenza hemagglutinin (HA) by replacing the wild type (wt) transmembrane and cytoplasmic domains with a GPI lipid anchor. GPI-anchored HA (GPI-HA) was transported to the cell surface with equal efficiency and at the same rate as wt-HA. Like wt-HA, cell surface GPI-HA, and its ectodomain released with the enzyme PI-phospholipase C (PI-PLC), were 9S trimers. Compared to wt-HA, the GPI-HA ectodomain underwent additional terminal oligosaccharide modifications; some of these occurred near the receptor binding pocket and completely inhibited the ability of GPI-HA to bind erythrocytes. Growth of GPI-HA-expressing cells in the presence of the mannosidase I inhibitor deoxymannojirimycin (dMM) abrogated the differences in carbohydrate modification and restored the ability of GPI-HA to bind erythrocytes. The ectodomain of GPI-HA produced from cells grown in the presence or absence of dMM underwent characteristic low pH-induced conformational changes (it released its fusion peptides and became hydrophobic and proteinase sensitive) but at 0.2 and 0.4 pH units higher than wt-HA, respectively. These results demonstrate that although GPI-HA forms a stable trimer with characteristics of the wt, its structure is altered such that its receptor binding activity is abolished. Our results show that transmembrane and GPI-anchored forms of the same ectodomain can exhibit functionally important differences in structure at a great distance from the bilayer.

scholarly journals Structural Studies of GABAA Receptor Binding Sites: Which Experimental Structure Tells us What?

2016 ◽  
Vol 9 ◽  
Author(s):  
Roshan Puthenkalam ◽  
Marcel Hieckel ◽  
Xenia Simeone ◽  
Chonticha Suwattanasophon ◽  
Roman V. Feldbauer ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Binding Sites ◽  
Structural Studies ◽  
Experimental Structure
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