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Epitope tagging of the human hâ†1 histamine receptorScott, Alison January 2000 (has links)
No description available.
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Studies on the Dâ†2 and Dâ†3 dopamine receptors expressed in insect cells using the baculovirus expression vector systemWoodcock, Christine January 1994 (has links)
No description available.
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Regulation of #beta#-adrenoceptor function : a study of the three subtypesKennedy, Fiona Ruth January 1996 (has links)
No description available.
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Regulation of stress-activated protein kinases (SAPKs) mediated by proteinase-activated receptor-2 (PAR-2)Kanke, Toru January 2002 (has links)
No description available.
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Characterizing the Role of RGS5 in the Regulation of Vascular Smooth Muscle Cell FunctionTirgari, Sam 16 February 2010 (has links)
Regulators of G-protein signaling (RGS) modulate G-protein coupled receptor (GPCR) activity in vascular smooth muscle cells (VSMCs). One such protein, RGS5, has been shown to have selective expression in VSMCs and pericytes, and can inhibit signaling from Gαq and Gαi subunits. Using an RGS5 knockout model, we assessed the functional effect of RGS5 in the constriction and dilation of resistance arterioles. Furthermore, we examined the intracellular lipid interaction of RGS proteins to identify the determinants regulating the biologic function of RGS5. Surprisingly, loss of RGS5 function in mesenteric arterioles had no effect on constriction and dilation of resistance arterioles. Cultured VSMCs showed increased basal ERK1/2 phosphorylation and increased VASP signaling in response to SNP treatment in RGS5KO VSMCs as compared to wild type controls, with no effect on cell proliferation. These data suggest RGS5 may integrate multiple intracellular pathways with competing effects on VSMC contraction.
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Characterizing the Role of RGS5 in the Regulation of Vascular Smooth Muscle Cell FunctionTirgari, Sam 16 February 2010 (has links)
Regulators of G-protein signaling (RGS) modulate G-protein coupled receptor (GPCR) activity in vascular smooth muscle cells (VSMCs). One such protein, RGS5, has been shown to have selective expression in VSMCs and pericytes, and can inhibit signaling from Gαq and Gαi subunits. Using an RGS5 knockout model, we assessed the functional effect of RGS5 in the constriction and dilation of resistance arterioles. Furthermore, we examined the intracellular lipid interaction of RGS proteins to identify the determinants regulating the biologic function of RGS5. Surprisingly, loss of RGS5 function in mesenteric arterioles had no effect on constriction and dilation of resistance arterioles. Cultured VSMCs showed increased basal ERK1/2 phosphorylation and increased VASP signaling in response to SNP treatment in RGS5KO VSMCs as compared to wild type controls, with no effect on cell proliferation. These data suggest RGS5 may integrate multiple intracellular pathways with competing effects on VSMC contraction.
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G protein-coupled receptors; discovery of new human members and analyses of the entire repertoires in human, mouse and rat /Gloriam, David E., January 2006 (has links)
Diss. (sammanfattning) Uppsala : Uppsala universitet, 2006. / Härtill 6 uppsatser. Med sammanfattning på svenska.
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Dissecting the molecular basis of neurotransmitter signaling modulation by GINIPLuebbers, Alex 25 January 2024 (has links)
G protein-coupled receptors (GPCRs) activate heterotrimeric G proteins (Gαβγ), which together form one of the most important signaling axes found in the cell. Because GPCRs are very common targets for therapeutic drugs, the mechanisms underlying their regulation are of high biomedical importance. Downstream of GPCR activation, there are many cytoplasmic proteins that regulate the activity of G proteins, providing an opportunity for therapeutic intervention. The neuronal protein GINIP binds directly to Gαi and is believed to play a role in modulating GPCR-mediated neurotransmission, an exquisitely-balanced process whereby dysregulation leads to neurological disorders including chronic pain and epilepsy. However, the molecular and structural determinants of GINIP underlying and required for proper regulation of G protein signaling downstream of GPCRs are unclear. In the studies presented here, we dissect the molecular and structural basis by which GINIP regulates G proteins after receptor activation and contributes to the fine-tuning of neurotransmitter responses in the nervous system. First, we revealed a new paradigm of G protein regulation by GINIP whereby it biases GPCR responses favoring Gβγ-mediated signaling to the detriment of Gα-mediated signaling. Second, we demonstrated that GINIP uses specific residues in the first loop of the PHD domain to physically engage Gαi by adopting a binding mode similar to that of G protein effectors like adenylyl cyclase, which is in turn required for the subsequent modulation of G protein signaling. Together, these insights advance our understanding of how GPCR signaling is fine-tuned by GINIP to set the tone of neurotransmission. Characterizing this layer of G protein regulation after receptor activation is crucial for developing novel therapeutic approaches to target diseases that arise from dysregulated GPCR signaling.
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The conformation of the β-ionone ring region of the chromophore of rhodopsin, in the dark and meta-I photostatesSharples, Jonathan M. January 2003 (has links)
No description available.
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Preparing, measuring and capturing G-protein coupled receptor (GPCR) signalling complexes for future development of cell-free assay technologiesBucco, Olgatina, olgatina@gmail.com January 2006 (has links)
G-protein coupled receptors (GPCRs) are integral membrane proteins which
represent primary cellular targets for intracellular signalling. Many of these receptors
are altered in disease states and hence are the target for over 50% of marketed drugs.
Despite their physiological importance, high-throughput, cell-free assays which
measure functional or signalling activity are only recently being investigated. The
current approach by the pharmaceutical industry to initially screen compounds for
functionality is to use heterologous cell-based assay formats. The aim of this work
was to reconstitute a cell-free GPCR signalling system on an appropriate platform
(surface) as a prototype for future rapid drug screening and other applications. The
proof-of-concept approach involved using the �2A-adrenergic receptor (�2A-AR)
containing cell membrane preparations as the model GPCR, reconstituted with a set
of heterotrimeric G-proteins; G�i1 and �1�2 (the signal transducing complex being
termed a �transductosome�). However, other receptors and G-proteins were also
investigated. Receptors were initially obtained from natural (tissue) sources, however
in the later stages they were expressed in a heterologous system (insect or
mammalian expression system). G-proteins were expressed in Spodoptera
frugiperida (Sf9) insect cells using the baculovirus expression system. Receptor
expression was verified by radioligand binding assays and endogenous G-proteins
were removed from membrane preparations using the chaotropic agent urea to allow
for reconstitution with purified G-proteins. Signal transduction through the
transductosome was measured using the [35S]GTP�S binding assay. Receptor
activated [35S]GTP�S binding was used to determine functional reconstitution and to
validate that the system was working in the normal physiological manner both on and
off a surface (with surface attachment being via histidine attachment on the G�i1
(6xHIS) subunit). Using the captured (surface-attached) transductosomes, the IC50 values for Rauwolscine, Yohimbine (potent �2-AR antagonists), Prazosin (potent �1-
AR antagonist) and Propranolol (�-AR antagonist) displayed the appropriate rank
order for this class of receptor. This cell-free, surface-attached signalling complex
prototype may have use in the future development of drug screening and discovery
assay technologies as well as other applications as an alternative to cell-based assays
which are not readily amendable to miniaturisation, long term storage and therefore
stable robust microarray formats.
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