Search results for "Cyst"

showing 10 items of 1960 documents

Interaction of Heparins and Dextran Sulfates with a Mesoscopic Protein Nanopore

2009

A mechanism of how polyanions influence the channel formed by Staphylococcus aureus alpha-hemolysin is described. We demonstrate that the probability of several types of polyanions to block the ion channel depends on the presence of divalent cations and the polyanion molecular weight and concentration. For heparins, a 10-fold increase in molecular weight decreases the half-maximal inhibitory concentration, IC(50), nearly 10(4)-fold. Dextran sulfates were less effective at blocking the channel. The polyanions are significantly more effective at reducing the conductance when added to the trans side of this channel. Lastly, the effectiveness of heparins on the channel conductance correlated wi…

Models MolecularStereochemistryBacterial ToxinsLipid BilayersMolecular ConformationBiophysicsmacromolecular substancesDivalentIonchemistry.chemical_compoundHemolysin ProteinsCysteineChannels and TransportersLipid bilayerIon channelchemistry.chemical_classificationMesoscopic physicsHeparinCell MembraneElectric Conductivitytechnology industry and agricultureConductanceDextransNanostructuresNanoporeDextranchemistryLiposomesMutationBiophysicsPorosityProtein BindingBiophysical Journal
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The Molecular and Crystal Structure of tert-Butyl N.ALPHA.-tert-Butoxycarbonyl-L-(S-trityl)cysteinate and the Conformation-Stabilizing Function of We…

2001

The title compound, C31H37NO4S [systematic name: (R)-tert-butyl-2-[(tert-butoxycarbonyl)amino]-3-(tritylsulfanyl)propanoate] is an L-cysteine derivative with three functions: NH2, COOH and SH, blocked by protecting groups tert-butoxycarbonyl, tert-butyl and trityl, respectively. The main chain of the molecule adopts the extended, nearly all-trans C5 conformation with the intramolecular N-H...O=C hydrogen bond. The urethane group is not involved in any intermolecular hydrogen bonding. Only weak intermolecular hydrogen bonds and hydrophobic contacts are observed in the crystal structure. These are C-H...O hydrogen bonds and CH/pi interactions with donor...acceptor distances, C...O ca. 3.5 A a…

Models MolecularStereochemistryPopulationMolecular ConformationCrystallography X-RayRing (chemistry)chemistry.chemical_compoundSpectroscopy Fourier Transform InfraredDrug DiscoveryMoleculeCysteineC5 conformationWeak hydrogen bondseducationConformational isomerismeducation.field_of_studyS-tritylcysteineChemistryHydrogen bondCrystal structureIntermolecular forceHydrogen BondingGeneral ChemistryGeneral MedicineFTIR spectroscopyIntramolecular forceIndicators and ReagentsGasesAb initio calculationsMethyl groupChemical and Pharmaceutical Bulletin
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Toward very potent, non-covalent organophosphonate inhibitors of cathepsin C and related enzymes by 2-amino-1-hydroxy-alkanephosphonates dipeptides

2013

Cathepsins play an important role in several human disorders and therefore the design and synthesis of their inhibitors attracts considerable interest in current medicinal chemistry approaches. Due to the presence of a strong sulphydryl nucleophile in the active center of the cysteine type cathepsins, most strategies to date have yielded covalent inhibitors. Here we present a series of non-covalent β-amino-α-hydroxyalkanephosphonate dipeptidic inhibitors of cathepsin C, ranking amongst the best low-molecular weight inhibitors of this enzyme. Their binding modes determined by molecular modelling indicate that the hydroxymethyl fragment of the molecule, not the phosphonate moiety, acts as a t…

Models MolecularStereochemistryhydroxyphosphonateBiochemistryCathepsin CCathepsin BCathepsin CInhibitory Concentration 50chemistry.chemical_compoundCathepsin OTransition state analogCathepsin KHumanscysteine proteasePeptide bondcathepsinAminesEnzyme InhibitorsCathepsinDipeptideChemistryMolecular MimicryDipeptidesGeneral MedicineOrganophosphatesEnzyme ActivationinhibitorBiochemistryHydroxy AcidsBiochimie
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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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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Sialolith and adenoid cystic carcinoma in the submandibular gland: a rare case

2011

Salivary calculi occur most frequently in the submandibular gland of the human beings. It is because of the specific anatomy of both the glands and its duct. Presentation typically consists of a painful swelling of the gland at meal times, when the effect of obstruction is most acute. The clinical signs, in most of times, can lead us to the diagnosis easily. The coexistence of sialolith and malignant tumors are very rare. This case report is about a male patient of 45 year with a swelling in the submandibular region for the last eighteen months with an intermittent episode of moderate to severe pain which increased during a mealtime and diagnosed as sialolith on radiograph, but on biopsy pr…

Moderate to severePathologymedicine.medical_specialtymedicine.diagnostic_testAdenoid cystic carcinomabusiness.industrySalivary calculusOdontología:CIENCIAS MÉDICAS [UNESCO]medicine.diseaseSubmandibular glandCiencias de la saludstomatognathic diseasesmedicine.anatomical_structurestomatognathic systemMale patientRare caseBiopsyUNESCO::CIENCIAS MÉDICASmedicineRadiologybusinessGeneral DentistryDuct (anatomy)
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Stafne bone defects radiographic features in panoramic radiographs: Assessment of 91 cases.

2018

Background To evaluate 91 cases of Stafne bone defect (SBD) in panoramic radiographs (PR) to determine the prevalence of different SBD variants, considering age, gender, and side. Additionally, to assess the most frequent imaging features of SBD. Material and Methods Participant data were collected from 91 SBD cases with PR imaging. First, SBDs were classified according to their location, as anterior, posterior, or ramus variant. SBD imaging features were classified according to radiographic imaging findings, assessing margins, degree of internal radiolucency, shape, topographic relationship between the defect and mandibular border, location of the defect according to mandibular teeth, and …

MolarAdultMalePanoramic radiographRadiographic imagingRadiographyRadiodensityMandibular canalMandible03 medical and health sciences0302 clinical medicinestomatognathic systemRadiography PanoramicmedicineBone CystsHumansGeneral DentistryAgedOrthodonticsAged 80 and overOral Medicine and Pathologybusiness.industryResearchMandible030206 dentistryMiddle Aged:CIENCIAS MÉDICAS [UNESCO]medicine.anatomical_structureOtorhinolaryngology030220 oncology & carcinogenesisUNESCO::CIENCIAS MÉDICASSurgeryFemaleDifferential diagnosisbusinessMedicina oral, patologia oral y cirugia bucal
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Comparison of postoperative morbidity between piezoelectric surgery and conventional rotary instruments in mandibular third molar surgery: a split-mo…

2020

Background The extraction of impacted third molar teeth is a common procedure in maxillofacial surgery. The aim of this study was to compare of piezoelectric surgical technique with the one with conventional rotary instruments in terms of edema, trismus and pain, in mandibular third molar surgery. Material and Methods 20 individuals with symmetrically impacted lower mandibular third molars and 40 teeth were included in the study. Third molars on the left side of each patient were removed with piezosurgery, while the counterparts on the right side were removed with conventional rotary instruments. Postoperatively, the same antibiotic, analgesic, and mouthwash were recommended to both groups.…

MolarAdultmedicine.medical_specialtypseudocystpiezosurgeryAnalgesicsinus liftPainMandibleTrismusMandibular third molarmucous retention cystYoung Adultstomatognathic systemEdemadental implantsMedicineEdemaHumansGeneral DentistryPiezosurgeryUNESCO:CIENCIAS MÉDICASPiezoelectric surgeryMouthPain Postoperativebusiness.industryResearchUltrasoundTooth ImpactedMolarimpacted third molarSurgeryOtorhinolaryngologyTooth ExtractionSurgeryMolar ThirdTrismusmedicine.symptommaxillary sinusMorbidityOral SurgerybusinessRemovalMedicina oral, patologia oral y cirugia bucal
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