Search results for "cysteine"

showing 10 items of 550 documents

Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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Candidate Targets for Hepatitis C Virus-Specific Antiviral Therapy

1997

The hepatitis C virus (HCV) was identified as the major causative agent of posttransfusion and community-acquired non-A, non-B hepatitis throughout the world. It is an enveloped virus with a plus-strand RNA genome encoding a polyprotein of about 3,010 amino acids. This polyprotein is cleaved co- and posttranslationally into mature viral proteins by host cell signal peptidases and 2 viral enzymes designated the NS2-3 proteinase and the NS3/4A proteinase complex. It is assumed that virus replication takes place in a membrane-associated complex containing at least 2 viral enzymatic activities: the NS3 nucleoside triphosphatase (NTPase)/helicase and the NS5B RNA-dependent RNA polymerase (RdRp).…

Models MolecularvirusesHepatitis C virusHepacivirusViral Nonstructural ProteinsBiologyVirus Replicationmedicine.disease_causechemistry.chemical_compoundViral life cycleViral envelopeVirologyRNA polymeraseEndopeptidasesmedicineHumansNS5BNS3DNA Helicasesvirus diseasesRNAbiochemical phenomena metabolism and nutritionRNA-Dependent RNA PolymeraseVirologydigestive system diseasesCysteine EndopeptidasesInfectious DiseaseschemistryViral replicationIntervirology
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Cyclometalated Au(III) Complexes for Cysteine Arylation in Zinc Finger Protein Domains: Towards Controlled Reductive Elimination

2019

With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C-atom transfer, the gold-mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCON)Cl2] complex featuring the 2-benzoylpyridine (CCON) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high-resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (Q…

Models Molecularzinc finger proteinProtein DomainPeptidecatalysi010402 general chemistry01 natural sciencesCatalysisReductive eliminationCatalysisThermodynamicOrganogold Compounds[CHIM]Chemical SciencesReactivity (chemistry)CysteineZinc fingerchemistry.chemical_classificationAqueous solutionCoordination Complexe010405 organic chemistryOrganic Chemistryreductive eliminationZinc FingersGeneral ChemistryCombinatorial chemistry0104 chemical sciencescysteine arylationchemistrySettore CHIM/03 - Chimica Generale E Inorganicagold complexeQuantum TheoryGoldCysteine
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Site-specific incorporation of perylene into an N-terminally modified light-harvesting complex II.

2010

Employing the utility of the native chemical ligation, site-specific attachment of an ultrastable perylene dye to a derivative of the major light-harvesting complex (LHCII) was demonstrated. Biochemical analysis of the conjugate indicated that the structure and function of LHCII remain largely unaffected by the N-terminal modification.

Molecular Sequence DataLight-Harvesting Protein Complexes010402 general chemistryPhotochemistry01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundPhysical and Theoretical ChemistryFLUORESCENCEPROTEIN LIGATIONPerylene030304 developmental biologyFluorescent DyesPlant Proteins0303 health sciencesSTABILITYOrganic ChemistryMICROSCOPYPlantsNative chemical ligationFluorescenceLIVE CELLS0104 chemical sciencesStructure and functionchemistryBiophysicsSMALL-MOLECULE PROBESCYSTEINEPeryleneDerivative (chemistry)DYESCysteineConjugateLight harvesting complex IIOrganicbiomolecular chemistry
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Staphylococcus aureus alpha-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine at positions 6…

1993

Staphylococcal alpha-toxin, the prototype of an oligomerizing, pore-forming cytotoxin, is sensitive to biochemical modifications and cannot be labeled with biotin or fluorescein under preservation of its biological activity. In this study, we have used site-directed mutagenesis to introduce cysteine residues at positions 69, 130, and 186. Each mutant was fully and rapidly reactive with several sulfhydryl-specific reagents, indicating superficial location. Coupling of SH-groups with fluorescein-maleimide or biotin-maleimide was tolerated without loss of hemolytic activity at position 130, and the formed hexamers were visible on target cells by fluorescence microscopy and could be detected on…

MutagenesisBiological activityCell BiologyBiochemistrychemistry.chemical_compoundBiotinchemistryBiochemistryFluorescence microscopeSite-directed mutagenesisMolecular BiologyElectroblottingStaphylococcus aureus alpha toxinCysteineJournal of Biological Chemistry
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Redox signaling in acute pancreatitis

2015

Acute pancreatitis is an inflammatory process of the pancreatic gland that eventually may lead to a severe systemic inflammatory response. A key event in pancreatic damage is the intracellular activation of NF-κB and zymogens, involving also calcium, cathepsins, pH disorders, autophagy, and cell death, particularly necrosis. This review focuses on the new role of redox signaling in acute pancreatitis. Oxidative stress and redox status are involved in the onset of acute pancreatitis and also in the development of the systemic inflammatory response, being glutathione depletion, xanthine oxidase activation, and thiol oxidation in proteins critical features of the disease in the pancreas. On th…

NecrosisGSH reduced glutathioneSTAT3 signal transducer and activator of transcription 3ERK extracellular signal-regulated kinasesClinical BiochemistryCCK cholecystokininTRAFs TNF receptor associated factorsReview ArticleIκB kinasePharmacologymedicine.disease_causeBiochemistrySHP small heterodimer partnerSTIM1 stromal interaction molecule 1chemistry.chemical_compoundHATs histone acetyltransferasesMedicineASK1GCL glutamate cysteine ligaseTNF-α tumor necrosis factor alphaIKK IκB kinaseNOS nitric oxide synthaseAcute inflammationHIF hypoxia inducible factorlcsh:QH301-705.5NF-κB nuclear factor kappa BDAMPs damage-associated molecular pattern moleculeslcsh:R5-920biologyGSSG oxidized glutathioneNF-kappa BNLRs nucleotide-binding oligomerization domain (NOD) like receptorsTRADD tumor necrosis factor receptor type 1-associated DEATH domain proteinTRPC3 transient receptor potential channel 3VEGF vascular endothelial growth factorGlutathioneTNFR tumor necrosis factor receptorHMGB1 high-mobility group Box 1 proteinIP3R inositol 145-trisphosphate receptor type 3VCAM-1 Vascular Cell adhesion protein 1Acute DiseaseJNK c-Jun N-terminal kinaseAcute pancreatitisTLRs toll-like receptorsmedicine.symptomlcsh:Medicine (General)Oxidation-ReductionAP-1 activator protein-1Signal TransductionmRNA messenger ribonucleic acidHMGB1ASC apoptosis-associated speck-like protein containing a carboxy-terminal CARDRNS reactive nitrogen speciesPTPs protein tyrosine phosphatasesROS reactive oxygen speciesNADH nicotinamide adenine dinucleotidepHe extracellular pHFAEE fatty acid ethyl estersAP acute pancreatitisHumansXanthine oxidaseCBP CREB-binding proteinRyR endoplasmic reticulum membrane ryanodine receptorsMDA malondialdehydeNO nitric oxideXO xanthine oxidaseASK1 apoptosis signal-regulating kinase-1business.industryOrganic ChemistryAutophagyNADPH nicotinamide adenine dinucleotide phosphateHDACs histone deacetylasesmedicine.diseaseCARS compensatory anti-inflammatory response syndromeXDH xanthine dehydrogenaseIL interleukinIκB inhibitor of kappa BAcute pancreatitisETC Electron transport chainPancreatitisMKPs MAPK phosphatasesSAP severe acute pancreatitischemistrylcsh:Biology (General)DTT dithiothreitolOxidative stressNAC N-acetyl cysteineImmunologybiology.proteinCalciumLysosomesReactive Oxygen SpeciesbusinessMAPK mitogen-activated protein kinaseOxidative stressERCP endoscopic retrograde cholangiopancreatographyRedox Biology
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Verwertbarkeit verschiedener Cysteinderivate bei langfristiger parenteraler Ernährung

1989

Utilization of cysteine derivatives for parenteral nutrition was established by means of nitrogen balance of growing rats. N,N-bis-acetylcystine and bisacetyl-glycyl-cystine were not utilized as substrates. N-acetylcysteine, glutathione disulfide, and L-thiazolidine-(4)-carboxylic acid gave evidence as suitable cysteine sources for parenteral nutrition.

Nitrogen balancechemistry.chemical_compoundParenteral nutritionBiochemistryChemistryMedicine (miscellaneous)Glutathione disulfideBiochemistryNitrogen cycleFood ScienceCysteineZeitschrift für Ernährungswissenschaft
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The putative PAINs nostotrebin 6 and derivatives from Nostoc sp. inhibit the trypanosomal cysteine protease rhodesain

2017

NostocBiochemistryChemical engineeringbiologyChemistryNostotrebin 6biology.organism_classificationCysteine protease65th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA 2017)
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Age-dependent changes in the transcription profile of long-lived Drosophila over-expressing glutamate cysteine ligase

2011

Abstract In our prior studies ( Orr et al., 2005 ) we achieved a 30–50% increase in the life span of Drosophila by manipulating glutathione (GSH) production in neuronal tissues, through over-expression of glutamate-cysteine ligase (GCL), a key enzyme in glutathione biosynthesis. In the present study, we identified gene response patterns from which plausible mechanisms responsible for the observed effects on life span might be inferred. Functional clustering analysis of the transcriptome data revealed that biological processes affected by GCLc in young flies (10 days) were generally related to cell morphogenesis and differentiation, while those in older flies were associated with nucleosome …

Nucleosome organizationAgingGlutamate-Cysteine LigaseLongevityBiologyTranscriptomechemistry.chemical_compoundTranscription (biology)MorphogenesisAnimalsGeneOligonucleotide Array Sequence AnalysisGeneticschemistry.chemical_classificationDNA ligaseCell morphogenesisGene Expression ProfilingfungiCell DifferentiationGlutathioneGlutathioneImmunity HumoralNucleosomesDrosophila melanogasterGCLCchemistryDevelopmental BiologyMechanisms of Ageing and Development
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Determination of total free amino acids with o-phthalaldehyde and N-acetyl-l-cysteine

1990

Abstract A spectrophotometric procedure is proposed for the determination of total free amino acids after reaction with o-phthalaldehyde and N-acetyl- l -cysteine, using isoleucine as the reference. The procedure was applied to the analysis of five samples of widely different composition. Recoveries were 98–105%.

O-PhthalaldehydeStereochemistryChemistryComposition (visual arts)IsoleucineFree aminoSpectroscopyN-acetyl-L-cysteineAnalytical ChemistryCysteineMicrochemical Journal
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