Search results for "Protein S"

showing 10 items of 1431 documents

The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling.

2013

14 pages; International audience; In corals, biocalcification is a major function that may be drastically affected by ocean acidification (OA). Scleractinian corals grow by building up aragonitic exoskeletons that provide support and protection for soft tissues. Although this process has been extensively studied, the molecular basis of biocalcification is poorly understood. Notably lacking is a comprehensive catalog of the skeleton-occluded proteins-the skeletal organic matrix proteins (SOMPs) that are thought to regulate the mineral deposition. Using a combination of proteomics and transcriptomics, we report the first survey of such proteins in the staghorn coral Acropora millepora. The or…

0106 biological sciencesProteomeCoralMolecular Sequence Datacalcium carbonate skeletonProteomics010603 evolutionary biology01 natural sciencesMass SpectrometryCalcium CarbonateEvolution Molecular03 medical and health sciencesAcropora milleporaCalcification PhysiologicproteomicsPhylogeneticsAnthozoa[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionGeneticsAnimals14. Life underwaterAmino Acid Sequencescleractinian[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyEcology Evolution Behavior and SystematicsDiscoveriesPhylogeny030304 developmental biologyStaghorn coral0303 health sciencesbiologySequence Homology Amino AcidEcologyMolecular Sequence Annotationbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsAnthozoabiomineralizationExtracellular MatrixProtein Structure TertiaryEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeSequence AlignmentFunction (biology)
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There's More to the Picture Than Meets the Eye: Nitric Oxide Cross Talk with Ca2+ Signaling

2013

Abstract Calcium and nitric oxide (NO) are two important biological messengers. Increasing evidence indicates that Ca2+ and NO work together in mediating responses to pathogenic microorganisms and microbe-associated molecular patterns. Ca2+ fluxes were recognized to account for NO production, whereas evidence gathered from a number of studies highlights that NO is one of the key messengers mediating Ca2+ signaling. Here, we present a concise description of the current understanding of the molecular mechanisms underlying the cross talk between Ca2+ and NO in plant cells exposed to biotic stress. Particular attention will be given to the involvement of cyclic nucleotide-gated ion channels and…

0106 biological sciencescalmodulinCell signalingCalmodulinPhysiology[SDV.SA.AGRO]Life Sciences [q-bio]/Agricultural sciences/AgronomyNanotechnologyPlant ScienceBiology01 natural sciencesNitric oxideTranscriptome03 medical and health scienceschemistry.chemical_compound[ SDV.SA.AGRO ] Life Sciences [q-bio]/Agricultural sciences/Agronomyplant defenseGeneticsPlant defense against herbivoryIon channel030304 developmental biology0303 health sciencescell signallingBiotic stressCell biologychemistryprotein S-nitrosylationgene expressionbiology.proteinplant immunitySignal transduction010606 plant biology & botanyPlant Physiology
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Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D

1991

Resting barley (Hordeum vulgare L.) grains contain acid-proteinase activity. The corresponding enzyme was purified from grain extracts by affinity chromatography on a pepstatin-Sepharose column. The pH optimum of the affinity-purified enzyme was between 3.5 and 3.9 as measured by hemoglobin hydrolysis and the enzymatic activity was completely inhibited by pepstatin a specific inhibitor of aspartic proteinases (EC 3.4.23). Further purification on a Mono S column followed by activity measurements and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the affinity-purified enzyme preparation contained two active heterodimeric aspartic proteinases: a larger 48k Da enzyme, c…

0106 biological scienceschemistry.chemical_classificationGel electrophoresis0303 health sciencesProtein subunitCathepsin DPlant ScienceBiology01 natural sciencesMolecular biologyEndopeptidase03 medical and health scienceschemistry.chemical_compoundEnzymechemistryAffinity chromatographyBiochemistryGeneticsHordeum vulgarePepstatin030304 developmental biology010606 plant biology & botanyPlanta
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2018

ABC (ATP binding cassette) transporters, ubiquitous in all kingdoms of life, carry out essential substrate transport reactions across cell membranes. Their transmembrane domains bind and translocate substrates and are connected to a pair of nucleotide binding domains, which bind and hydrolyze ATP to energize import or export of substrates. Over four decades of investigations into ABC transporters have revealed numerous details from atomic-level structural insights to their functional and physiological roles. Despite all these advances, a comprehensive understanding of the mechanistic principles of ABC transporter function remains elusive. The human multidrug resistance transporter ABCB1, al…

0301 basic medicine030102 biochemistry & molecular biologyIn silicoBiophysicsATP-binding cassette transporterCell BiologyPlasma protein bindingBiologyBiochemistry03 medical and health sciencesTransmembrane domain030104 developmental biologyProtein structureBiochemistryATP hydrolysisFunction (biology)ATP-binding domain of ABC transportersBiochimica et Biophysica Acta (BBA) - Biomembranes
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Hands On: Using Tryptophan Fluorescence Spectroscopy to Study Protein Structure

2019

Fluorescence spectroscopy is well suited to obtain information about the structure and function of proteins. The major advantage of this spectroscopic technique is the pronounced dependence of the fluorescence emission characteristics of fluorophores on their distinct local environment and the rather inexpensive equipment required. In particular, the use of intrinsic tryptophan fluorescence offers the possibility to study structure and function of proteins without the need to modify the protein. While fluorescence spectroscopy is technically not demanding, a number of factors can artificially alter the results. In this article, we systematically describe the most common applications in fluo…

0301 basic medicine030103 biophysicsQuenching (fluorescence)ChemistryTryptophanFluorescenceFluorescence spectroscopy03 medical and health sciences030104 developmental biologyProtein structureTryptophan fluorescenceBiophysicsLocal environmentSpectroscopy
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Techniques to Analyze sRNA Protein Cofactor Self-Assembly In Vitro

2018

Post-transcriptional control of gene expression by small regulatory noncoding RNA (sRNA) needs protein accomplices to occur. Past research mainly focused on the RNA chaperone Hfq as cofactor. Nevertheless, recent studies indicated that other proteins might be involved in sRNA-based regulations. As some of these proteins have been shown to self-assemble, we describe in this chapter protocols to analyze the nano-assemblies formed. Precisely, we focus our analysis on Escherichia coli Hfq as a model, but the protocols presented here can be applied to analyze any polymer of proteins. This chapter thus provides a guideline to develop commonly used approaches to detect prokaryotic protein self-ass…

0301 basic medicine030103 biophysicsbiologyChemistryNoncoding RNA cofactorComputational biologyNon-coding RNAmedicine.disease_causeIn vitroCofactorProtein self-assembly03 medical and health sciences030104 developmental biologyGene expressionTransfer RNARNA chaperoneFunctional amyloidmedicinebiology.proteinEscherichia coli
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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2,3-Dihydrobenzofuran privileged structures as new bioinspired lead compounds for the design of mPGES-1 inhibitors

2016

International audience; 2,3-Dihydrobenzofurans are proposed as privileged structures and used as chemical platform to design small compound libraries. By combining molecular docking calculations and experimental verification of biochemical interference, we selected some potential inhibitors of microsomal prostaglandin E2 synthase (mPGES)-1. Starting from low affinity natural product 1, by our combined approach we identified the compounds 19 and 20 with biological activity in the low micromolar range. Our data suggest that the 2,3-dihydrobenzofuran derivatives might be suitable bioinspired lead compounds for development of new generation mPGES-1 inhibitors with increased affinity.

0301 basic medicine300323-Dihydrobenzofuran privileged structure; Cancer; Inflammation; Molecular docking; mPGES-1 inhibitors; Biochemistry; Clinical Biochemistry; Molecular Biology; Molecular Medicine; Organic Chemistry; Drug Discovery3003 Pharmaceutical Science; 3003Amino Acid MotifsClinical BiochemistryGene ExpressionPharmaceutical Science01 natural sciencesClinical biochemistryBiochemistry[ CHIM ] Chemical SciencesProtein Structure Secondary[ SDV.CAN ] Life Sciences [q-bio]/Cancerchemistry.chemical_compoundLow affinityDrug DiscoveryEnzyme Inhibitors23-Dihydrobenzofuran privileged structure; Molecular docking; mPGES-1 inhibitors; Cancer; InflammationProstaglandin-E SynthasesCancerAnti-Inflammatory Agents Non-SteroidalBiological activityProto-Oncogene Proteins c-metIntramolecular OxidoreductasesMolecular Docking SimulationMolecular dockingMolecular Medicinelipids (amino acids peptides and proteins)Cell SurvivalStereochemistryMolecular Sequence Data2Antineoplastic Agents[SDV.CAN]Life Sciences [q-bio]/Cancer3-Dihydrobenzofuran privileged structureInhibitory Concentration 50Structure-Activity Relationship03 medical and health sciencesCell Line TumorMicrosomesHumans[CHIM]Chemical SciencesMolecular BiologyBenzofuransInflammationNatural product010405 organic chemistryDrug Discovery3003 Pharmaceutical ScienceOrganic ChemistryEpithelial CellsmPGES-1 inhibitorsCombinatorial chemistryCombined approach0104 chemical sciences030104 developmental biologychemistryDrug DesignDrug Screening Assays Antitumor
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Synergistic activation of AMPK prevents from polyglutamine-inducedtoxicity inCaenorhabditis elegans

2020

11 páginas, 4 figuras. Supplementary material related to this article can be found, in the online version, at doi: https://doi.org/10.1016/j.phrs.2020.105105.

0301 basic medicineAMPKProtein subunitMutantEnzyme ActivatorsAMP-Activated Protein KinasesProtein Serine-Threonine KinasesProtein Aggregation PathologicalpolyQ toxicityArticleAnimals Genetically ModifiedProtein Aggregates03 medical and health sciences0302 clinical medicineRNA interferenceAutophagymedicineAnimalsAMPK Caenorhabditis elegans Metformin Salycilate Synergy polyQ toxicityCaenorhabditis elegans ProteinsCaenorhabditis elegansLoss functionCaenorhabditis elegansNeuronsPharmacologybiologyChemistrySalycilateAutophagyAMPKDrug Synergismbiology.organism_classificationSalicylatesMetforminCell biologyMetforminEnzyme ActivationSynergy030104 developmental biology030220 oncology & carcinogenesisMutationProteostasisPeptidesmedicine.drug
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Novel KIAA1033/WASHC4 mutations in three patients with syndromic intellectual disability and a review of the literature.

2019

In 2011, KIAA1033/WASHC4 was associated with autosomal recessive intellectual disability (ARID) in a large consanguineous family comprising seven affected individuals with moderate ID and short stature. Since then, no other cases of KIAA1033 variants have been reported. Here we describe three additional patients (from two unrelated families) with syndromic ID due to compound heterozygous KIAA1033 variants ascertained by exome sequencing (ES). Two sisters, aged 4 and 5.5 years, had a stop-gain and a missense variants, each inherited from one parent (p.(Gln442*) and p.(Asp1048Gly)). Both had learning disabilities, macrocephaly, dysmorphic features, skeletal anomalies, and subependymal heterot…

0301 basic medicineAdultMaleMicrocephaly030105 genetics & heredityCompound heterozygosityShort stature03 medical and health sciencesKIAA0196Intellectual DisabilityIntellectual disabilityGeneticsMedicineMissense mutationHumansGenetics (clinical)Exome sequencingGeneticsbusiness.industryMacrocephalyInfant NewbornIntracellular Signaling Peptides and Proteinsmedicine.diseasePedigreeProtein Subunits030104 developmental biologyPhenotypeChild PreschoolMutationFemalemedicine.symptombusinessAmerican journal of medical genetics. Part AREFERENCES
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