Search results for "TERT"

showing 10 items of 1210 documents

Strontium/lithium ratio in aragonitic shells of Cerastoderma edule (Bivalvia) — A new potential temperature proxy for brackish environments

2015

Abstract Quantitative reconstruction of water temperature from shells of bivalve mollusks is still a very challenging task. For example, in highly variable environments such as intertidal zones, shell oxygen isotope values can only provide reliable temperature estimates if the δ18Owater signature during the time of growth is known. Furthermore, trace element-to-calcium ratios such as Sr/Ca or Mg/Ca often do not serve as reliable paleothermometers, because their incorporation into bivalve shells is known to be strongly biologically controlled. Here, we present a potential novel temperature proxy which is based on the Sr/Lishell ratio of the intertidal bivalve Cerastoderma edule. Up to 81% of…

Cerastoderma eduleStrontiumbiologyBrackish waterChemistrychemistry.chemical_elementMineralogyIntertidal zoneGeologybiology.organism_classificationBivalviaIsotopes of oxygenGeochemistry and PetrologyGrowth rateBivalve shellChemical Geology
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"Quels beste ce pooit estre" : Merlin et le bestiaire dans trois Suites du Merlin en prose : d'une poétique du personnage à une poétique du roman

2016

One of the most eminent figures of Arthurian literature, renowned in the Middle Ages as in later periods, Merlin remains however a polymorphous and contradictory character. A study focusing on two aspects will allow us to perceive his ambiguities and to form the poetics of the character. Firstly, from a relational perspective, the bestiary, that is to say the literary fauna, constitutes an element of this definition. In Prose Merlin’s retrospective prose sequels (the “Vulgate” Suite, the “Post-Vulgate” Suite and the Livre d’Artus), romances which constitute the apex of thirteenth century Arthurian texts in prose, this relation axis encounters an intertextual perspective. By its extent and i…

CharacterMerlinVita Merlini[SHS.LITT]Humanities and Social Sciences/LiteraturePersonnageBestiarySuites du Merlin en proseProse MerlinRoman de BrutMerlin en prose[ SHS.LITT ] Humanities and Social Sciences/LiteratureIntertextualitéProse Merlin “Suites”[SHS.LITT] Humanities and Social Sciences/LiteratureHistoria Regum BritanniaeBestiaireFictionIntertextuality
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N‐[tert‐Butoxy­carbonyl­glycyl‐(Z)‐α,β‐de­hydro­phenyl­alanyl­glycyl‐(E)‐α,β‐de­hydro­phenyl­alanyl]­glycine methyl ester dihydrate

2006

The title pentapeptide, Boc0—Gly1–ΔZPhe2—Gly3–ΔEPhe4—Gly5—OMe, C30H35N5O8·2H2O, adopts the type I β-turn conformation for the ΔZPhe2—Gly3 residues. It is stabilized by a 4\rightarrow1 intramolecular hydrogen bond between the ΔEPhe4 NH and Gly1 CO groups. All the amino acid residues in the pentapeptide sequence are linked trans to each other. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.

ChemistryHydrogen bondStereochemistryIntramolecular forceIntermolecular forceGlycine methyl esterGeneral Materials ScienceTert-butoxySequence (biology)General ChemistryCrystal structureCondensed Matter PhysicsPentapeptide repeatActa Crystallographica Section E-Structure Reports Online
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Tertiary cytoreduction in the setting of recurrent ovarian cancer (Review)

2013

Ovarian cancer is the most lethal gynecological malignancy, with aggressive surgical debulking and adjuvant chemotherapy as the main treatment modalities. Optimal debulking during the primary surgery is significantly correlated with prolonged survival. As surgical techniques and chemotherapeutic agents improve, more patients with prolonged survival may face secondary and tertiary recurrences. The role of surgical debulking in secondary cytoreduction (SC) is not clearly defined and is based on retrospective series. The treatment of patients with primary or secondary recurrences generally consists of second-line chemotherapy, but may be performed on medically fit patients in certain circumsta…

Chemotherapymedicine.medical_specialtyCancer Researchbusiness.industrymedicine.medical_treatmentOptimal DebulkingCancerArticlesTertiary cytoreductionDebulkingmedicine.diseaseSettore MED/40 - Ginecologia E OstetriciaSurgeryOncologyAscitesmedicineStage (cooking)medicine.symptomRecurrent ovarian cancerOvarian cancerComplicationbusinessTumoral debulking
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Sesterterpenes and macrolide derivatives from the endophytic fungus Aplosporella javeedii.

2020

Abstract Five sesterterpenes (1–5) including two new compounds (1 and 2), as well as a new (6) and a known macrolide (7) were isolated from the endophytic fungus Aplosporella javeedii. The structures of the new compounds were elucidated by analysis of their 1D and 2D NMR and HRMS data as well as by comparison with the literature. Compound 4 and its acetyl derivatives 4a, 4b, 4c which were prepared by acetylation of 4 exhibited moderate cytotoxicity against the mouse lymphoma cell line L5178Y with IC50 values ranging from 6.2 to 12.8 μM, respectively. Moreover, 4a and 4c exhibited also cytotoxicity against human leukemia (Jurkat J16) and lymphoma (Ramos) cell lines. Compound 7 showed strong …

ChinaStaphylococcus aureusSesterterpenesAntineoplastic AgentsApoptosismedicine.disease_cause01 natural sciencesJurkat cellsSesterterpenesMiceStructure-Activity RelationshipAscomycotaCell Line TumorDrug DiscoverymedicineEndophytesAnimalsHumansCytotoxicityPharmacologyMolecular Structure010405 organic chemistryChemistryGeneral MedicineMolecular biology0104 chemical sciencesAnti-Bacterial Agents010404 medicinal & biomolecular chemistryStaphylococcus aureusCell cultureAcetylationBrassicaceaeMacrolidesAntibacterial activityTwo-dimensional nuclear magnetic resonance spectroscopyFitoterapia
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Random mutations directed to transmembrane and loop domains of the light-harvesting chlorophyll a/b protein: impact on pigment binding.

1999

The major light-harvesting complex of photosystem II (LHCII) can be reconstituted in vitro by folding its bacterially expressed apoprotein, Lhcb, in detergent solution in the presence of chlorophylls and carotenoids. To compare the impact of alpha-helical transmembrane domains and hydrophilic loop domains of the apoprotein on complex formation and stability, we introduced random mutations into a segment of the protein comprising the stromal loop, the third (C-proximal) transmembrane helix, and part of the amphipathic helix in the C-terminal domain. The mutant versions of Lhcb were screened for the loss of their ability to form stable LHCII upon reconstitution in vitro. Most steps during the…

Chlorophyll bChlorophyllProtein FoldingPigment bindingMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureChlorophyll bindingAmino Acid SequencePeptide sequencePeasMembrane ProteinsPhotosystem II Protein ComplexCarotenoidsTransmembrane proteinProtein Structure TertiaryTransmembrane domainSpectrometry FluorescencechemistryBiochemistryEnergy TransferMutationMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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Rigid versus Flexible Protein Matrix: Light-Harvesting Complex II Exhibits a Temperature-Dependent Phonon Spectral Density

2018

Dynamics-function correlations are usually inferred when molecular mobility and protein function are simultaneously impaired at characteristic temperatures or hydration levels. In this sense, excitation energy transfer in the photosynthetic light-harvesting complex II (LHC II) is an untypical example because it remains fully functional even at cryogenic temperatures relying mainly on interactions of electronic states with protein vibrations. Here, we study the vibrational and conformational protein dynamics of monomeric and trimeric LHC II from spinach using inelastic neutron scattering (INS) in the temperature range of 20-305 K. INS spectra of trimeric LHC II reveal a distinct vibrational …

Chlorophyll0301 basic medicineMaterials sciencePhononLight-Harvesting Protein Complexes010402 general chemistry01 natural sciencesMolecular physicsInelastic neutron scatteringSpectral line03 medical and health sciencesSpinacia oleraceaMaterials ChemistryPhysics::Chemical PhysicsPhysical and Theoretical ChemistrySofteningQuantitative Biology::BiomoleculesProtein dynamicsAnharmonicityTemperaturefood and beveragesAtmospheric temperature rangeProtein Structure Tertiary0104 chemical sciencesSurfaces Coatings and FilmsNeutron Diffraction030104 developmental biologyEnergy TransferExcitationThe Journal of Physical Chemistry B
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Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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The Folding State of the Lumenal Loop Determines the Thermal Stability of Light-Harvesting Chlorophyll a/b Protein

2004

The major light-harvesting protein of photosystem II (LHCIIb) is the most abundant chlorophyll-binding protein in the thylakoid membrane. It contains three membrane-spanning alpha helices; the first and third one closely interact with each other to form a super helix, and all three helices bind most of the pigment cofactors. The protein loop domains connecting the alpha helices also play an important role in stabilizing the LHCIIb structure. Single amino acid exchanges in either loop were found to be sufficient to significantly destabilize the complex assembled in vitro [Heinemann, B., and Paulsen, H. (1999) Biochemistry 38, 14088-14093. Mick, V., Eggert, K., Heinemann, B., Geister, S., and…

ChlorophyllProtein DenaturationProtein FoldingPhotosystem IILight-Harvesting Protein ComplexesBiochemistryProtein structureTrypsinPlant Proteinschemistry.chemical_classificationChemistryChlorophyll AHydrolysisPeasTemperaturePhotosystem II Protein ComplexSodium Dodecyl SulfateProtein Structure TertiaryAmino acidKineticsCrystallographyAmino Acid SubstitutionMembrane proteinThylakoidHelixBiophysicsElectrophoresis Polyacrylamide GelProtein foldingAlpha helixBiochemistry
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