Search results for "Sulfhydryl Compounds"

showing 10 items of 85 documents

The In Vitro Interaction of 12-Oxophytodienoic Acid and Related Conjugated Carbonyl Compounds with Thiol Antioxidants

2021

α,β-unsaturated carbonyls interfere with numerous plant physiological processes. One mechanism of action is their reactivity toward thiols of metabolites like cysteine and glutathione (GSH). This work aimed at better understanding these interactions. Both 12-oxophytodienoic acid (12-OPDA) and abscisic acid (ABA) conjugated with cysteine. It was found that the reactivity of α,β-unsaturated carbonyls with GSH followed the sequence trans-2-hexenal &lt

0106 biological sciences0301 basic medicinecysteine covalent modification570Isomerase activityArabidopsis thalianaArabidopsislcsh:QR1-50201 natural sciencesBiochemistryArticleAntioxidantslcsh:Microbiology03 medical and health scienceschemistry.chemical_compoundThioredoxinsPlant Growth RegulatorsmedicineCysteineSulfhydryl CompoundsMolecular BiologyCyclophilinchemistry.chemical_classificationChemistry<i>Arabidopsis thaliana</i>peroxiredoxinGlutathionethioredoxinphytohormones030104 developmental biologyMechanism of actionBiochemistryprotein–ligand interactioncyclophilinThiolFatty Acids Unsaturatedmedicine.symptomThioredoxinPeroxiredoxinthiol antioxidants010606 plant biology & botanyCysteineBiomolecules
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Prooxidative chain transfer activity by thiol groups in biological systems

2020

Cysteine is arguably the best-studied biological amino acid, whose thiol group frequently participates in catalysis or ligand binding by proteins. Still, cysteine's unusual biological distribution has remained mysterious, being strikingly underrepresented in transmembrane domains and on accessible protein surfaces, particularly in aerobic life forms (“cysteine anomaly”). Noting that lipophilic thiols have been used for decades as radical chain transfer agents in polymer chemistry, we speculated that the rapid formation of thiyl radicals in hydrophobic phases might provide a rationale for the cysteine anomaly. Hence, we have investigated the effects of dodecylthiol and related compounds in i…

0301 basic medicineFree RadicalsDNA damageLipid peroxidationClinical BiochemistryProtein oxidationBiochemistryLipid peroxidation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCysteine oxidationAnimalsHumansCysteineSulfhydryl CompoundsCaenorhabditis eleganslcsh:QH301-705.5chemistry.chemical_classificationlcsh:R5-920Organic ChemistryAmino acidTransmembrane domain030104 developmental biologylcsh:Biology (General)Structural biologychemistryBiochemistryThiyl radicalsThiolRadical propagationlcsh:Medicine (General)Protein oxidation030217 neurology & neurosurgeryResearch PaperCysteineRedox Biology
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Redox signaling in the gastrointestinal tract.

2017

Redox signaling regulates physiological self-renewal, proliferation, migration and differentiation in gastrointestinal epithelium by modulating Wnt/β-catenin and Notch signaling pathways mainly through NADPH oxidases (NOXs). In the intestine, intracellular and extracellular thiol redox status modulates the proliferative potential of epithelial cells. Furthermore, commensal bacteria contribute to intestine epithelial homeostasis through NOX1- and dual oxidase 2-derived reactive oxygen species (ROS). The loss of redox homeostasis is involved in the pathogenesis and development of a wide diversity of gastrointestinal disorders, such as Barrett's esophagus, esophageal adenocarcinoma, peptic ulc…

0301 basic medicineGastrointestinal DiseasesNotch signaling pathwaymedicine.disease_causeBiochemistryGastrointestinal epitheliumSuperoxide dismutase03 medical and health scienceschemistry.chemical_compoundPhysiology (medical)medicineHumansSulfhydryl CompoundsIntestinal MucosaWnt Signaling PathwayCell Proliferationchemistry.chemical_classificationReactive oxygen speciesbiologySuperoxideWnt signaling pathwayNADPH OxidasesDual oxidase 2digestive system diseasesGastrointestinal TractIntestinesOxidative Stress030104 developmental biologychemistryImmunologybiology.proteinCancer researchReactive Oxygen SpeciesOxidation-ReductionOxidative stressFree radical biologymedicine
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Effect of Omega-3 and Vitamins E + C Supplements on the Concentration of Serum B-Vitamins and Plasma Redox Aminothiol Antioxidant Status in Elderly M…

2015

&lt;b&gt;&lt;i&gt;Background:&lt;/i&gt;&lt;/b&gt; Data on redox plasma aminothiol status in individuals on strength training are very limited. Therefore, we studied the effect of omega-3 and vitamins E + C supplementation on the concentration of B-vitamins and redox aminothiol status in elderly men after strength training for 3 months. &lt;b&gt;&lt;i&gt;Methods:&lt;/i&gt;&lt;/b&gt; Healthy men, age 60 ± 6 (mean ± SD) were randomly divided into 3 groups: group I received placebo (n = 17), group II consumed omega-3 (700 mg, n = 17), and group III consumed vitamins E + C (235 mg +1 g, n = 16) daily for 3 months. All participants completed a strength training program for the same period. &lt;b&…

0301 basic medicineMalemedicine.medical_specialtyAntioxidantPyridoxalStrength trainingmedicine.medical_treatmentMedicine (miscellaneous)Ascorbic Acid030204 cardiovascular system & hematologyPlaceboAntioxidants03 medical and health scienceschemistry.chemical_compound0302 clinical medicineFolic AcidInternal medicineFatty Acids Omega-3medicineHumansVitamin ESulfhydryl CompoundsPyridoxalAgedNutrition and DieteticsVitamin EResistance TrainingVitaminsMiddle AgedAscorbic acidUric AcidB vitaminsVitamin B 12030104 developmental biologyEndocrinologyBiochemistrychemistryDietary SupplementsVitamin B ComplexUric acidAnnals of nutritionmetabolism
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Chemoselective Dual Labeling of Native and Recombinant Proteins

2017

The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups. In order to ensure broader applicability of the functionalization strategy, a novel, short peptide sequence that introduces a disulfide bridge was designed and site-selective dual labeling in the presenc…

0301 basic medicineModels MolecularBiomedical EngineeringPharmaceutical ScienceBioengineering010402 general chemistry01 natural scienceslaw.inventionCell LineMaleimides03 medical and health scienceschemistry.chemical_compoundMiceBacterial ProteinslawAnimalsHumansReactivity (chemistry)CysteineSulfhydryl CompoundsSulfonesMaleimidePeptide sequenceDual labelingPharmacologychemistry.chemical_classificationStaining and LabelingCommunicationOrganic ChemistryDisulfide bondProteinsCombinatorial chemistryRecombinant Proteins0104 chemical sciencesAllyl CompoundsLuminescent Proteins030104 developmental biologychemistryThiolRecombinant DNASurface modificationInterleukin-2PeptidesBiotechnologyBioconjugate Chemistry
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Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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Oxidative stress and frailty : a systematic review and synthesis of the best evidence

2017

Objective Oxidative stress (OS) is associated with accelerated aging. Previous studies have suggested a possible relationship between OS and frailty but this association remains unclear. We conducted a systematic review to investigate potential interactions between OS and frailty. Methods A systematic literature search of original reports providing data on ‘OS and antioxidant’ parameters and frailty was carried out across major electronic databases from inception until May 2016. Cross-sectional/case control and longitudinal studies reporting data on the association between frailty and anti-oxidants-OS biomarkers were considered for inclusion. Results were summarized with a synthesis based o…

0301 basic medicineOncologyGerontologyGenetics and Molecular Biology (all)AgingCross-sectional studyalpha-TocopherolAntioxidantesIsoprostanesmedicine.disease_causeBiochemistryAnti-oxidantAntioxidants0302 clinical medicineLongitudinal StudiesAged 80 and overFrailtyGlutathione DisulfideObstetrics and GynecologyGlutathione8-Hydroxy-2'-DeoxyguanosineSystematic searchAnti-oxidant; Frail; Frailty; Oxidative stress; Biochemistry Genetics and Molecular Biology (all); Obstetrics and Gynecologymedicine.medical_specialtyFrail ElderlyGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesFrailInternal medicinemedicineHumansFrail elderlySulfhydryl CompoundsAgedAldehydesbusiness.industryCase-control studyFrailty Frail Oxidative stress Anti-oxidantEstresse OxidativoDeoxyguanosineMean ageOxidized GlutathioneOxidative Stress030104 developmental biologyCross-Sectional Studies1-Alkyl-2-acetylglycerophosphocholine EsteraseBest evidencebusinessReactive Oxygen Species030217 neurology & neurosurgeryOxidative stressBiomarkers
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Plasmin-Induced Activation of Human Platelets Is Modulated by Thrombospondin-1, Bona Fide Misfolded Proteins and Thiol Isomerases

2020

Inflammatory processes are triggered by the fibrinolytic enzyme plasmin. Tissue-type plasminogen activator, which cleaves plasminogen to plasmin, can be activated by the cross-&beta

0301 basic medicineProtein FoldingPlatelet AggregationPlasmin030204 cardiovascular system & hematologyProtein aggregationFibrinogenThrombospondin 10302 clinical medicinePlateletFibrinolysinprotein misfoldingIsomerasesSpectroscopyChemistryfood and beveragesGeneral Medicinethiol-isomerasesComputer Science ApplicationsCell biologyP-Selectinplateletsmedicine.drugcirculatory and respiratory physiologyBlood PlateletsCatalysisArticleInorganic Chemistry03 medical and health sciencesProtein AggregatesThrombospondin 1medicineHumansPlatelet activationSulfhydryl CompoundsPhysical and Theoretical Chemistrythrombospondin-1Molecular BiologyplasminInflammationOrganic ChemistryfungiFibrinogen bindingFibrinogenPlasminogenPlatelet Activation030104 developmental biologyProtein Conformation beta-StrandPeptidesPlasminogen activatorInternational Journal of Molecular Sciences
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A Vastly Increased Chemical Variety of RNA Modifications Containing a Thioacetal Structure

2018

International audience; Recently discovered new chemical entities in RNA modifications have involved surprising functional groups that enlarge the chemical space of RNA. Using LC-MS, we found over 100 signals of RNA constituents that contained a ribose moiety in tRNAs from E. coli. Feeding experiments with variegated stable isotope labeled compounds identified 37 compounds that are new structures of RNA modifications. One structure was elucidated by deuterium exchange and high-resolution mass spectrometry. The structure of msms2 i6 A (2-methylthiomethylenethio-N6-isopentenyl-adenosine) was confirmed by methione-D3 feeding experiments and by synthesis of the nucleobase. The msms2 i6 A contai…

0301 basic medicineStereochemistryThioacetal010402 general chemistry01 natural sciencesCatalysisNucleobaseisotope labelling03 medical and health scienceschemistry.chemical_compoundAcetalsRNA modificationsTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]RiboseEscherichia coliMoietySulfhydryl Compoundschemistry.chemical_classificationChemistrythioacetalsRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyGeneral Chemistryradical-SAM enzymesChemical space0104 chemical sciencesLC-MSRNA Bacterial030104 developmental biologyEnzymeNucleic Acid ConformationHydrogen–deuterium exchangeChromatography Liquid
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Physico-chemical study of the radiopharmaceuticals 99mTc-DMSA, 99mTc-EDTA and 99mTc-DTPA interaction with plasmatic proteins.

1989

This report studies the binding rate of the radiopharmaceuticals 99mTc-DTPA, 99mTc-EDTA and 99mTc-DMSA to plasmatic proteins. The proteins bind to the tested radiopharmaceuticals in the following sequence: 99mTc-DTPA less than 99mTc-DMSA(C1) less than 99mTc-EDTA less than 99mTc-DMSA(C2) where C1 and C2 represent two different Tc-DMSA complexes. The thermodynamic study suggests a quantitative relationship of radiopharmaceutical:protein = 1:1 and an almost nonexistent influence of the temperature, which means that the interacting forces in this process are relatively weak.

99mtc dtpaPentetic acid99mTc-DMSAGeneral Engineeringchemistry.chemical_elementTechnetiumPlasma protein bindingBlood ProteinsOrganotechnetium CompoundsPentetic AcidTechnetiumBlood proteinschemistry.chemical_compoundchemistryBiochemistryTechnetium Tc 99m Dimercaptosuccinic AcidTechnetium Tc 99m PentetateEdetic AcidTechnetium Tc 99m Dimercaptosuccinic AcidSulfhydryl CompoundsSuccimerEdetic AcidProtein BindingInternational journal of radiation applications and instrumentation. Part A, Applied radiation and isotopes
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