Search results for "Thiol"

showing 10 items of 485 documents

Time-course of thiol oxidation of protein phosphatases during cerulein-induced acute pancreatitis

2018

Acute pancreatitis (AP) is an acute inflammatory process of the pancreatic gland. The aim of this work was to evaluate the role of thiol oxidation of key proteins that can be involved in the regulation of the inflammatory process during AP. AP was induced in C57BL/6 mice by 7 hourly subcutaneous injections of cerulein (50 ug/kg bw). Animals were sacrificed after 1, 3, 5 and 7 injections of cerulein. One hour after the first injection, hyperoxidation of peroxiredoxin 1–4 was detected coinciding with a H2O2 peak. Three hours later, a marked up-regulation of mRNA and protein expression of sulfiredoxin, partially mediated by Nrf-2, takes place. The up-regulation of sulfiredoxin seems to be resp…

0301 basic medicineMessenger RNA030102 biochemistry & molecular biologyChemistryp38 mitogen-activated protein kinasesThiol oxidationPhosphataseProtein phosphatase 2Pharmacologymedicine.diseaseBiochemistry03 medical and health sciencesSulfiredoxin0302 clinical medicine030220 oncology & carcinogenesisPhysiology (medical)medicineAcute pancreatitisPeroxiredoxinFree Radical Biology and Medicine
researchProduct

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
researchProduct

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
researchProduct

Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
researchProduct

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
researchProduct

ISG15 Is Upregulated in Respiratory Syncytial Virus Infection and Reduces Virus Growth through Protein ISGylation

2016

ABSTRACT Human respiratory syncytial virus (RSV), for which neither a vaccine nor an effective therapeutic treatment is currently available, is the leading cause of severe lower respiratory tract infections in children. Interferon-stimulated gene 15 (ISG15) is a ubiquitin-like protein that is highly increased during viral infections and has been reported to have an antiviral or a proviral activity, depending on the virus. Previous studies from our laboratory demonstrated strong ISG15 upregulation during RSV infection in vitro . In this study, an in-depth analysis of the role of ISG15 in RSV infection is presented. ISG15 overexpression and small interfering RNA (siRNA)-silencing experiments,…

0301 basic medicineSmall interfering RNAvirusesImmunologyCellular Response to InfectionRespiratory Syncytial Virus InfectionsUbiquitin-Activating EnzymesBiologyMicrobiologyVirus03 medical and health sciencesIn vivoImmunityRNA interferenceVirologyCell Line TumorEndopeptidasesHumansRNA Small InterferingRespiratory Tract InfectionsUbiquitinsInnate immune system030102 biochemistry & molecular biologyRespiratory tract infectionsInfantEpithelial CellsISG15VirologyImmunity Innate030104 developmental biologyInsect ScienceRespiratory Syncytial Virus HumanCytokinesRNA InterferenceUbiquitin ThiolesteraseProtein Processing Post-TranslationalHeLa Cells
researchProduct

Characterization of sulfhydryl oxidase from Aspergillus tubingensis

2017

Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…

0301 basic medicineentsyymitBOVINE-MILKThioredoxin reductaselcsh:Animal biochemistryBiochemistrySubstrate Specificitychemistry.chemical_compoundNonribosomal peptide synthesisEnzyme Stabilitylcsh:QD415-436DisulfidesDISULFIDE BONDSPeptide Synthaseschemistry.chemical_classificationbiologyGliotoxinChemistrynonribosomal peptide synthesisHydrogen-Ion ConcentrationGlutathioneFAMILYSOXSglutathione oxidationhomesienetAspergillusBiochemistrySENSITIVITYsecreted sulfhydryl oxidaseOxidoreductasesResearch ArticleDithiol oxidaseCofactorlcsh:Biochemistry03 medical and health sciencesNonribosomal peptideNATURAL-PRODUCTSoksidoreduktaasitBIOSYNTHESISlcsh:QP501-801Molecular Biologysecondary metabolismPURIFICATIONIDENTIFICATION030102 biochemistry & molecular biologyCXXC-MOTIFGlutathioneNIGERluonnonaineet030104 developmental biologyEnzymedithiol oxidasebiology.protein1182 Biochemistry cell and molecular biologyAspergillus tubingensisSecreted sulfhydryl oxidaseSecondary metabolismGlutathione oxidationCysteineBMC Biochemistry
researchProduct

Ammonium thiolactate and thiolactic acid: important hairdressers' allergens?

2002

030201 allergyAllergyThiolactic acidbusiness.industryDermatologymedicine.diseasemedicine.disease_cause030207 dermatology & venereal diseases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAllergenAmmonium thiolactatechemistryContact allergyImmunopathologyImmunologymedicineImmunology and AllergyOccupational exposurebusinessContact dermatitisContact Dermatitis
researchProduct

Design of new sensitive α,β-unsaturated carbonyl 1,8-naphtalimide fluorescent probes for thiol bioimaging

2017

International audience; We report herein an efficient synthesis of news naphtalimide-based fluorescent derivatives functionalized with an a,(3-unsaturated carbonyl group. Probes were synthesized from reaction of an amino-naphtalimide precursor with maleic anhydride. Photophysical study of fluorescent probes and cells labelling were performed, and showed that the reactive derivatives exhibit rich turn on fluorescence properties in presence of different biological thiol (Glutathione and Cysteine) making these systems a very promising way for thiol bioimaging.

1Biological thiolsThiol probes010402 general chemistryPhotochemistry01 natural sciencesTurn (biochemistry)Turn-on fluorescencechemistry.chemical_compoundMichael's additionLabelling[SDV.IDA]Life Sciences [q-bio]/Food engineeringMaterials ChemistryElectrical and Electronic EngineeringHomocysteineInstrumentationchemistry.chemical_classification010405 organic chemistry[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringMetals and AlloysMaleic anhydrideGlutathioneKetonesCondensed Matter PhysicsBioimagingGlutathioneCarbonyl groupCombinatorial chemistryFluorescence4-addition0104 chemical sciences3. Good healthSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryThiolCysteineSensors and Actuators B: Chemical
researchProduct

CCDC 285998: Experimental Crystal Structure Determination

2006

Related Article: S.Amriou, Changsheng Wang, A.S.Batsanov, M.R.Bryce, D.F.Perepichka, E.Orti, R.Viruela, J.Vidal-Gancedo, C.Rovira|2006|Chem.-Eur.J.|12|3389|doi:10.1002/chem.200501326

27-di-iodo-9-(45-dimethyl-13-dithiol-2-ylidene)fluoreneSpace GroupCrystallographyCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
researchProduct