Search results for "Homomeric"

showing 6 items of 6 documents

Altered atypical coupling of γ-aminobutyrate type A receptor agonist and convulsant binding sites in subunit-deficient mouse lines

2001

We searched for subunit correlations for GABA(A) receptor-associated atypically GABA-insensitive [35S]TBPS binding. The homomeric beta3 subunit receptors could be excluded, as GABA-insensitive [35S]TBPS binding was present in beta3-/- mice. Localization of GABA-insensitive [35S]TBPS binding correlated best with those of delta, alpha4 and alpha6 subunit mRNAs. The amounts of GABA-insensitive [35S]TBPS binding components were increased in delta-/- mice, but dramatically reduced in alpha6-/- mice, suggesting a role for alpha6 but excluding delta subunits.

Agonistmedicine.medical_specialtymedicine.drug_classProtein subunitMolecular Sequence DataConvulsantsBiologySulfur Radioisotopesmedicine.disease_causeMiceRadioligand AssayCellular and Molecular NeuroscienceInternal medicinemedicineAnimalsHomomericRNA MessengerBinding siteReceptorGABA AgonistsMolecular BiologyBrain ChemistryMice KnockoutMutationBinding SitesGABAA receptorBridged Bicyclo Compounds HeterocyclicReceptors GABA-AMolecular biologyEndocrinologynervous systemConvulsantMolecular Brain Research
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Dynamics of homomeric polypeptides studied with neutron scattering, dielectric spectroscopy and calorimetry

2012

Dynamics of homomeric polypeptides protein dynamical transition
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Expression of p11 and Heteromeric TASK Channels in Rat Carotid Body Glomus Cells and Nerve Growth Factor–differentiated PC12 Cells

2020

Psychological stress activates the hypothalamus, augments the sympathetic nervous output, and elevates blood pressure via excitation of the ventral medullary cardiovascular regions. However, anatomical and functional connectivity from the hypothalamus to the ventral medullary cardiovascular regions has not been fully elucidated. We investigated this issue by tract-tracing and functional imaging in rats. Retrograde tracing revealed the rostral ventrolateral medulla was innervated by neurons in the ipsilateral dorsomedial hypothalamus (DMH). Anterograde tracing showed DMH neurons projected to the ventral medullary cardiovascular regions with axon terminals in contiguity with tyrosine hydroxyl…

MaleHistologyNerve Tissue ProteinsProximity ligation assayPC12 Cells03 medical and health sciencesPotassium Channels Tandem Pore Domain0302 clinical medicineGlomus cellmedicineAnimalsHomomericRats WistarAnnexin A2030304 developmental biologyCarotid Body0303 health sciencesChemistryEndoplasmic reticulumS100 ProteinsfungiArticlesImmunohistochemistryRatsCell biologymedicine.anatomical_structureNerve growth factorCytoplasmCarotid bodyAnatomySignal transduction030217 neurology & neurosurgeryJournal of Histochemistry & Cytochemistry
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Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors.

2010

AMPA receptors (AMPARs) are tetrameric ion channels that mediate rapid glutamate signaling in neurons and many non-neuronal cell types. Endoplasmic reticulum (ER) quality control mechanisms permit only correctly folded functional receptors to be delivered to the cell surface. We analyzed the biosynthetic maturation and transport of all 12 GluA1–4 subunit splice variants as homomeric receptors and observed robust isoform-dependent differences in ER exit competence and surface expression. In contrast to inefficient ER exit of both GluA3 splice forms and the flop variants of GluA1 and GluA4, prominent plasma membrane expression was observed for the other AMPAR isoforms. Surprisingly, deletion …

Models MolecularProtein ConformationImmunoblottingMolecular Sequence DataAMPA receptorBiologymedicine.disease_causeEndoplasmic ReticulumLigandsBiochemistryCell membrane03 medical and health sciences0302 clinical medicineNeurobiologyProtein targetingChlorocebus aethiopsmedicineHomomericAnimalsHumansProtein IsoformsAmino Acid SequenceReceptors AMPAReceptorMolecular BiologyIon channel030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidEndoplasmic reticulumCell MembraneCell BiologyCell biologyTransport proteinProtein Structure TertiaryAlternative SplicingProtein SubunitsProtein Transportmedicine.anatomical_structureHEK293 CellsMicroscopy FluorescenceCOS CellsProtein Multimerization030217 neurology & neurosurgeryThe Journal of biological chemistry
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Neuronal Nicotinic Receptors in the Locust Locusta migratoria

1998

We have identified five cDNA clones that encode nicotinic acetylcholine receptor (nAChR) subunits expressed in the nervous system of the locust Locusta migratoria. Four of the subunits are ligand-binding α subunits, and the other is a structural β subunit. The existence of at least one more nAChR gene, probably encoding a β subunit, is indicated. Based on Northern analysis and in situ hybridization, the five subunit genes are expressed. locα1, locα3, andlocβ1 are the most abundant subunits and are expressed in similar areas of the head ganglia and retina of the adult locust. Because Locα3 binds α-bungarotoxin with high affinity, it may form a homomeric nAChR subtype such as the mammalian α7…

Nervous systemGene isoformmedicine.medical_specialtyanimal structuresbiologyProtein subunitCell BiologyIn situ hybridizationbiology.organism_classificationBiochemistryCell biologyNicotinic acetylcholine receptormedicine.anatomical_structureEndocrinologynervous systemInternal medicineMushroom bodiesmedicineHomomericsense organsMolecular BiologyLocustJournal of Biological Chemistry
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Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides

2012

Neutron scattering reveals a complex dynamics in polypeptide chains, with two main onsets of anharmonicity whose physical origin and biological role are still debated. In this study the dynamics of strategically selected homomeric polypeptides is investigated with elastic neutron scattering using different energy resolutions and compared with that of a real protein. Our data spotlight the dependence of anharmonic transition temperatures and fluctuation amplitudes on energy resolution, which we quantitatively explain in terms of a two-site model for the protein-hydration water energy landscape. Experimental data strongly suggest that the protein dynamical transition is not a mere resolution …

PhysicsQuantitative Biology::BiomoleculesfluctuationsResolution (electron density)AnharmonicityProtein dynamical transitionProteinsGeneral Physics and AstronomyNeutron scatteringMolecular physicsPhase TransitionSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Neutron DiffractionComplex dynamicsAmplitudeModels ChemicalBiophysicsHomomericProtein dynamicConnection (algebraic framework)PeptidesEnergy (signal processing)
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