Search results for "binding"

showing 10 items of 3896 documents

Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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A novel arousal-based individual screening reveals susceptibility and resilience to PTSD-like phenotypes in mice

2021

Translational animal models for studying post-traumatic stress disorder (PTSD) are valuable for elucidating the poorly understood neurobiology of this neuropsychiatric disorder. These models should encompass crucial features, including persistence of PTSD-like phenotypes triggered after exposure to a single traumatic event, trauma susceptibility/resilience and predictive validity. Here we propose a novel arousal-based individual screening (AIS) model that recapitulates all these features. The AIS model was designed by coupling the traumatization (24 h restraint) of C57BL/6 J mice with a novel individual screening. This screening consists of z-normalization of post-trauma changes in startle …

Physiology5-trial SM 5-trial social memoryBiochemistryFight-or-flight responseFST forced swim test0302 clinical medicineEndocrinologySSRIs selective serotonin reuptake inhibitorsDSM-5 Diagnostic and Statistical Manual of Mental DisordersOriginal Research ArticleFear conditioningmedia_commonHT hypothalamusAIS arousal-based individual screeningQP351-495ParoxetinePhenotypeHPA hypothalamic–pituitary–adrenalBST basal synaptic transmissionHIP hippocampusPTSD post-traumatic stress disorder[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Psychological resilienceAmy amygdalaRC321-571medicine.drugNeurophysiology and neuropsychologymedia_common.quotation_subjectBDNF brain derived neurotropic factorFear conditioningNeurosciences. Biological psychiatry. NeuropsychiatryBiologyStressArousal03 medical and health sciencesCellular and Molecular NeuroscienceAnimal model Fear conditioning Resilience Stress Susceptibility Z-scoreAnimal modelCORT corticosteroneOF open fieldTE trauma-exposedBiological neural networkmedicineAnimal model[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]C controlfEPSPs field excitatory post-synaptic potentialsSGK1 serum/glucocorticoid-regulated kinase 1RC346-429Molecular BiologyResilienceEndocrine and Autonomic SystemsZ-scoremPFC medial prefrontal cortexFKBP5 FK506 binding protein 5FDA Food and Drug AdministrationASR acoustic startle reactivityEPM elevated plus maze030227 psychiatrySusceptibilityAnimal model; Fear conditioning; Resilience; Stress; Susceptibility; Z-scoreNeurology. Diseases of the nervous systemNeuroscience030217 neurology & neurosurgeryNeurobiology of Stress
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Effects of alpha-melanotropin C-terminal tripeptide analogues on macrophage NO production.

2003

The C-terminal tripeptide of melanocyte-stimulating hormone, MSH (11-13) (Lys-Pro-Val), possesses strong anti-inflammatory actions, which are mediated via mechanisms that are not fully understood. To shed more light into these mechanisms we have here synthesised and evaluated the activities of L- and D-Val substituted cyclic modifications of MSH (11-13) on nitric oxide (NO) in macrophage RAW 264.7 cells, as well as on binding to melanocortin receptors (MCRs) in B16-F1 and MCR expressing insect cells, and for effects on cAMP. MSH (11-13) and its analogues did neither bind to MCRs nor stimulate cAMP in RAW 264.7 and B16-F1 cells, except H-, which showed a tendency to increase cAMP at high (10…

PhysiologyAnti-Inflammatory AgentsTripeptideBiologyNitric OxideBiochemistryNitric oxideCellular and Molecular Neurosciencechemistry.chemical_compoundMiceEndocrinologyCell Line TumorCyclic AMPStructure–activity relationshipAnimalsMelanocyte-Stimulating HormonesBinding siteReceptorBinding SitesMacrophagesStereoisomerismPeptide FragmentschemistryBiochemistryCell cultureMelanocortinSignal transductionSignal TransductionPeptides
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Cops and robbers: putative evolution of copper oxygen-binding proteins.

2000

Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs).

PhysiologyCopper proteinCopper metabolismchemistry.chemical_elementAquatic ScienceEvolution MolecularPrimary immune responseAnimalsBinding siteMolecular BiologyEcology Evolution Behavior and SystematicsBinding SitesbiologyMonophenol MonooxygenaseOxygen transportActive siteCopperOxygenchemistryBiochemistryInsect ScienceHemocyaninsbiology.proteinAnimal Science and ZoologyOxygen bindingCopperThe Journal of experimental biology
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Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus.

2000

When Astacus leptodactylus were kept at various temperatures for several weeks, different ratios between di-hexameric and hexameric hemocyanins were observed in their hemolymph. The higher the temperature the more hexamers were present. This long-term adaptation to different temperatures or/and to temperature-induced pH-shifts as observed in the hemolymph has different effects on the expression of subunit types building up hexamers and those which covalently link two hexamers within the di-hexamers. The oxygen binding behaviour of di-hexameric hemocyanins from cold and warm adapted animals do not show differences with respect to affinity, Bohr effect and cooperativity.

PhysiologyEcologymedicine.medical_treatmentProtein subunitTemperatureCooperativityHemocyaninBohr effectmacromolecular substancesBiologyHydrogen-Ion ConcentrationAstacus leptodactylusbiology.organism_classificationBiochemistryAdaptation PhysiologicalCrustaceaHemolymphHemocyaninsmedicineBiophysicsAnimalsElectrophoresis Polyacrylamide GelAdaptationMolecular BiologyOxygen bindingComparative biochemistry and physiology. Part A, Molecularintegrative physiology
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Coupled transport of Arabidopsis p24 proteins at the ER–Golgi interface

2012

p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)–p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in…

PhysiologyMolecular Sequence DataArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic Reticulumcoat protein (COP) IIcoat protein (COP) Isymbols.namesakeAmino Acid SequenceER–Golgi transportCOPIISecretory pathwayArabidopsis ProteinsVesicular-tubular clusterEndoplasmic reticulumMembrane ProteinsCOPIGolgi apparatussecretory pathwayTransport proteinCell biologyProtein TransportSecretory proteinp24 proteinssymbolsProtein BindingResearch PaperJournal of Experimental Botany
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Thermostability of Two Cyanobacterial GrpE Thermosensors

2011

GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle i…

PhysiologyMolecular Sequence DataProtein domainPlant SciencePlasma protein bindingCyanobacteriaProtein structureBacterial ProteinsHeat shock proteinEscherichia coliAmino Acid SequencePeptide sequenceHeat-Shock ProteinsThermostabilitySequence Homology Amino AcidbiologyProtein StabilityChemistryCircular DichroismGenetic Complementation TestSynechocystisSynechocystisTemperatureCell BiologyGeneral Medicinebiology.organism_classificationProtein Structure TertiaryCross-Linking ReagentsChaperone (protein)Biophysicsbiology.proteinbacteriaProtein MultimerizationProtein BindingPlant and Cell Physiology
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Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.

2010

In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…

Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein BindingPlantcell physiology
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Physostigmine and Neuromuscular Transmission

1993

Single channel studies carried out in cultured rat myoballs and cultured hippocampal neurons, and ion flux studies performed on Torpedo electrocyte membrane vesicles, showed that physostigmine (Phy), a well-established acetylcholinesterase inhibitor, interacts directly with nicotinic acetylcholine receptors (nAChR). Low concentrations (0.1 microM) of Phy activate the receptor integral channel, whereas higher concentrations blocked the channel in its opened state. In contrast to channel activation by acetylcholine (ACh) and classical cholinergic agonists, however, Phy was capable of activating the nAChR channel even when the ACh binding sites were blocked by competitive antagonists, such as …

PhysostigmineMolecular Sequence DataNeuromuscular JunctionNeuromuscular transmissionIn Vitro TechniquesReceptors NicotinicTorpedoHippocampusSynaptic TransmissionGeneral Biochemistry Genetics and Molecular BiologyNeuromuscular junctionHistory and Philosophy of SciencemedicineAnimalsAmino Acid SequencePatch clampBinding siteCells CulturedAcetylcholine receptorBinding SitesChemistryGeneral NeuroscienceAcetylcholineRatsQuaternary Ammonium CompoundsNicotinic agonistmedicine.anatomical_structureBiophysicsCholinergicIon Channel GatingNeuroscienceAcetylcholinemedicine.drugAnnals of the New York Academy of Sciences
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Photoaffinity labeling of Torpedo acetylcholine receptor by physostigmine.

1993

The plant alkaloid physostigmine, an established anti-cholinesterase agent of the carbamate type, has recently been shown to bind to the nicotinic acetylcholine receptor from Torpedo marmorata electrocytes [Okonjo, K. O., Kuhlmann, J.Maelicke, A. (1991) Eur. J. Biochem. 200, 671-677]. Pharmacological studies of physostigmine-induced ion flux into nicotinic-acetylcholine-receptor-rich membrane vesicles, indicated distinct binding sites for physostigmine and acetylcholine. As shown in this study by photoaffinity labeling with [phenyl-(n)-3H](-)physostigmine, the physostigmine-binding site is located within the same subunit (alpha polypeptide) of the receptor as the acetylcholine-binding site.…

PhysostigmineStereochemistryPhotochemistryUltraviolet RaysPhysostigmineMolecular Sequence DataReceptors NicotinicTorpedoTritiumBiochemistrylaw.inventionlawmedicineAnimalsAmino Acid SequenceAcetylcholine receptorBinding SitesPhotoaffinity labelingChemistryAffinity LabelsBungarotoxinLigand (biochemistry)Nicotinic acetylcholine receptorBiochemistryTorpedoAcetylcholinemedicine.drugEuropean journal of biochemistry
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