Search results for "Protein S"

showing 10 items of 1431 documents

Sugar moiety has a direct influence on the secondary structure and properties of sturgeon gonadotropin

2009

Sugar moiety has a direct influence on the secondary structure and properties of sturgeon gonadotropin Sturgeon Acipenser güldenstädti Br. gonadotropic hormone (GTH) β-subunit (β-GTH) was selectively chemically deglycosylated (dg) by anhydrous hydrogen fluoride and trifluoromethane sulfonic acid. Two dgβ-GTH molecular forms retaining 35% (dgβ-GTH1) and 13% (dgβ-GTH2) of their initial carbohydrates were obtained. Investigation of the reassociated α-β hybrid dimers (recombinants) α-GTH+dgβ-GTH1 and α-GTH+dgβ-GTH2 showed that the immunoreactivity with antiserum raised against standard GTH dropped by 22.5%. Hybrid dimers were recognised by the standard GTH antibodies, which indicated that the s…

endocrine systemMultidisciplinaryGeneral interestmedicine.drug_classChemistrySciencesecondary structure of the α-βQdeglycosylationdimersturgeon gonadotropic hormoneSturgeonBiochemistrymedicineSugar moietyβ-subunitGonadotropinProtein secondary structurebiological functionProceedings of the Latvian Academy of Sciences. Section B. Natural, Exact, and Applied Sciences.
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2004

Background Arabidopsis thaliana copper metallochaperone CCH is a functional homologue of yeast antioxidant ATX1, involved in cytosolic copper transport. In higher plants, CCH has to be transported to specialised cells through plasmodesmata, being the only metallochaperone reported to date that leaves the cell where it is synthesised. CCH has two different domains, the N-terminal domain conserved among other copper-metallochaperones and a C-terminal domain absent in all the identified non-plant metallochaperones. The aim of the present study was the biochemical and biophysical characterisation of the C-terminal domain of the copper metallochaperone CCH.

endocrine systembiologyfood and beverageschemistry.chemical_elementPlasmodesmabiology.organism_classificationCopperYeastMetallochaperonesCytosolProtein structurechemistryBiochemistryStructural BiologyArabidopsisBiophysicsPeptide sequenceBMC Structural Biology
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Melatonin stimulates the nonamyloidogenic processing ofβAPP through the positive transcriptional regulation of ADAM10 and ADAM17

2014

Melatonin controls many physiological functions including regulation of the circadian rhythm and clearance of free radicals and neuroprotection. Importantly, melatonin levels strongly decrease as we age and patients with Alzheimer's disease (AD) display lower melatonin than age-matched controls. Several studies have reported that melatonin can reduce aggregation and toxicity of amyloid-β peptides that are produced from the β-amyloid precursor protein (βAPP). However, whether melatonin can directly regulate the βAPP-cleaving proteases ('secretases') has not been investigated so far. In this study, we establish that melatonin stimulates the α-secretase cleavage of βAPP in cultured neuronal an…

endocrine systemmedicine.medical_specialtyProteasesADAM10Blotting WesternApoptosisADAM17 ProteinBiologyMelatonin receptorNeuroprotectionMelatoninADAM10 ProteinAmyloid beta-Protein PrecursorTransactivationEndocrinologyInternal medicinemedicineHumansPhosphorylationPromoter Regions GeneticMelatoninMembrane ProteinsADAM ProteinsHEK293 CellsEndocrinologyGene Expression Regulationbiology.proteinPhosphorylationAmyloid Precursor Protein SecretasesAmyloid precursor protein secretasehormones hormone substitutes and hormone antagonistsmedicine.drugJournal of Pineal Research
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SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus.

2006

Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120–140 in the C-terminal part of the protein. We provide evidence that SAP30L induces…

entsyymitvuorovaikutustumajyvänenBiologySAP30Protein Sorting SignalsHistone DeacetylasesArticleCell Line03 medical and health sciencesMice0302 clinical medicineHistone H1Histone H2AGeneticsHistone codeAnimalsHumansGene Silencingnucleolus030304 developmental biologyNuclear receptor co-repressor 2Histone deacetylationGenetics0303 health sciencesgeenitbiokemiaNuclear ProteinsCell biologyRepressor ProteinsProtein TransportSin3 Histone Deacetylase and Corepressor Complextranskriptio (biologia)030220 oncology & carcinogenesisSin-associated proteinsHistone deacetylase complexhistonideasetylaatioHistone deacetylaseproteiinitCorepressorSin-assosioituvat proteiinitCell NucleolusNucleic acids research
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Membrane Protein Complexes: Structure and Function

2018

This edited book contains a compilation of 14 advanced academic chapters dealing with the structure and function of membrane protein complexes. This rapidly advancing important field of study closely parallels those on soluble protein complexes, and viral protein and nucleoprotein complexes.Diverse topics are included in this book, ranging from membrane–bound enzymes to ion channels, proton pumps and photosystems. Data from X-ray crystallography, cryo-electron microscopy and other biophysical and biochemical techniques are presented throughout the book. There is extensive use of colour figures of protein structures. Throughout the book structure and function are closely correlated.The two e…

functionprotein complexesViral proteineducationComputational biologyBiologymedicine.disease_causehumanitiesStructure and functionProtein structureMembrane proteinMembrane proteinsmedicinestructure
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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins.

2015

Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and sta…

guanidiniun chloride0301 basic medicineGuanidinium chlorideSmall AngleCircular dichroismBiophysicsmacromolecular substancesBiochemistryGroELChaperoninScatteringMitochondrial Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsX-Ray DiffractionScattering Small AngleHumansGuanidinebiologyProtein StabilityCircular DichroismOrganic ChemistryTemperatureGroESSAXSChaperonin 60Hsp60GroELSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CDcited By 5enzymes and coenzymes (carbohydrates)Denaturation030104 developmental biologychemistryBiochemistryChaperone (protein)biological sciencesbiology.proteinCD; Denaturation; GroEL; Guanidinium chloride; Hsp60; SAXS; Bacterial Proteins; Chaperonin 60; Circular Dichroism; Humans; Mitochondrial Proteins; Protein Stability; Scattering Small Angle; Temperature; X-Ray DiffractionbacteriaHSP60Guanidinium chlorideBiophysical chemistry
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Chemical and physical characterization of thermal aggregation of model proteins modulated by zinc(II) and copper(II) ions

2016

BACKGROUND: Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies, where the protein deposition occurs, and in the biotechnology field like the food technology where many processes in food manufacturing are based on thermal treatments. OBJECTIVE: The influence of Cu2+ or Zn2+ ions on the thermal aggregation process of Bovine beta-lactoglobulin (BLG) and Bovine Serum Albumin (BSA), two protein models, was studied with the aim of delineating the role of these ions in the protein aggregation kinetics and to clarify the related molecular mechanisms. METHODS: The protein structure changes were monitored by Raman spectroscopy, whereas the aggregate gr…

inorganic chemicals0301 basic medicineMetal ions in aqueous solutionKineticsInorganic chemistryBeta-lactoglobulinchemistry.chemical_elementZincProtein aggregation010402 general chemistry01 natural sciencesBovine Serum Albumin (BSA)Beta-lactoglobulin bovine serum albumin (BSA) copper and zinc ionsRaman spectroscopy dynamic light scatteringMetal03 medical and health sciencesProtein structureDynamic light scatteringcopper and zinc ionRadiology Nuclear Medicine and imagingcopper and zinc ionsBovine serum albuminBeta-lactoglobulin; Bovine Serum Albumin (BSA); copper and zinc ions; Raman spectroscopy; dynamic light scatteringbiologydigestive oral and skin physiologydynamic light scattering0104 chemical sciences030104 developmental biologychemistryvisual_artRaman spectroscopyBiophysicsbiology.proteinvisual_art.visual_art_medium
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Nitrated Fatty Acids Modulate the Physical Properties of Model Membranes and the Structure of Transmembrane Proteins

2017

Nitrated fatty acids (NO2 -FAs) act as anti-inflammatory signal mediators, albeit the molecular mechanisms behind NO2 -FAs' influence on diverse metabolic and signaling pathways in inflamed tissues are essentially elusive. Here, we combine fluorescence measurements with surface-specific sum frequency generation vibrational spectroscopy and coarse-grained computer simulations to demonstrate that NO2 -FAs alter lipid organization by accumulation at the membrane-water interface. As the function of membrane proteins strongly depends on both, protein structure as well as membrane properties, we consecutively follow the structural dynamics of an integral membrane protein in presence of NO2 -FAs. …

inorganic chemicals0301 basic medicineProtein Conformationcomplex mixturesPhase TransitionCatalysisPhysical Phenomena03 medical and health sciences0302 clinical medicineProtein structureJournal ArticleFluorescence Resonance Energy TransferMembrane fluidityComputer SimulationLipid bilayerIntegral membrane proteinNitratesChemistryCircular DichroismCell MembraneFatty AcidsOrganic ChemistryPeripheral membrane proteinMembrane ProteinsGeneral Chemistryrespiratory systemLipidsTransmembrane protein030104 developmental biologyMembraneMembrane proteinBiochemistryBiophysics030217 neurology & neurosurgerySignal TransductionChemistry – A European Journal
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4,4′-bis(dimethylamino)biphenyl containing binding sites. A newfluorescent subunit for cation sensing

2002

The emission behaviour of the 4,4′-bis(dimethylamino)biphenyl subunit covalently attached to aza-crown ethers is studied. Some new ligands have been synthesised in order to test the properties of this new fluorophore. The fluorescence of these new ligands and some other compounds previously described has been studied in acetonitrile in the presence of Ni2+, Cu2+, Zn2+, Hg2+, Pb2+, Cd2+ and also in the presence of some alkali and alkaline-earth cations.

inorganic chemicalsBiphenylFluorophoreStereochemistryProtein subunitGeneral ChemistryAlkali metalFluorescenceMedicinal chemistrychemistry.chemical_compoundchemistryCovalent bondBinding siteAcetonitrile
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