Search results for "ddc:5"

showing 10 items of 1717 documents

Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

2016

Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A variety of organisms have evolved mechanisms to detect and respond to light, in which the re…

0301 basic medicinePhotoreceptorsTime FactorsPhotoisomerizationLightProtein ConformationPhotochemistryPhotoreceptors MicrobialMYOGLOBINProtein structureMicrobialX-RAY-DIFFRACTIONPHOTOISOMERIZATIONMOTIONSchromophoresta116MultidisciplinarySPECTROSCOPYCrystallographyChemistryPhotochemical ProcessesTime resolved crystallographyTIMEMultidisciplinary SciencesPicosecondFemtosecondphotoactive proteinsScience & Technology - Other Topicsddc:500IsomerizationStereochemistryGeneral Science & TechnologyConjugated systemArticle03 medical and health sciencesBacterial ProteinsIsomerismEXCITATIONx-ray crystallographyPhotonsScience & TechnologyPHOTOCYCLEta114CHROMOPHOREta1182PATHWAYSChromophore030104 developmental biologyfree-electron laserssense organstrans-cis isomerization
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Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

2021

Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to…

0301 basic medicineProgrammed cell deathSettore BIO/06AutophagosomeAutolysosome[SDV]Life Sciences [q-bio]lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4]Autophagy-Related ProteinsReviewComputational biology[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologySettore MED/0403 medical and health sciencesstressChaperone-mediated autophagyddc:570AutophagyLC3AnimalsHumanscancerSettore BIO/10Autophagosome; cancer; flux; LC3; lysosome; macroautophagy; neurodegeneration; phagophore; stress; vacuoleSet (psychology)Molecular Biologyvacuole.phagophore030102 biochemistry & molecular biologyvacuolebusiness.industryInterpretation (philosophy)AutophagyAutophagosomesneurodegenerationCell BiologyfluxMulticellular organismmacroautophagy030104 developmental biologyKnowledge baselysosomeAutophagosome; LC3; cancer; flux; lysosome; macroautophagy; neurodegeneration; phagophore; stress; vacuoleBiological AssayLysosomesbusinessBiomarkers[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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Zero-field nuclear magnetic resonance of chemically exchanging systems.

2019

Zero- to ultralow-field (ZULF) nuclear magnetic resonance (NMR) is an emerging tool for precision chemical analysis. In this work, we study dynamic processes and investigate the influence of chemical exchange on ZULF NMR J-spectra. We develop a computational approach that allows quantitative calculation of J-spectra in the presence of chemical exchange and apply it to study aqueous solutions of [15N]ammonium (15N\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$${\mathrm{H}}_4^ +$$\end{document}H4+) as a model syst…

0301 basic medicineReaction kinetics and dynamicsSciencePhysics::Medical PhysicsGeneral Physics and AstronomyModel system02 engineering and technologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesNuclear magnetic resonanceZero fieldHyperpolarization (physics)lcsh:ScienceDissolutionQuantitative Biology::Biomolecules3403 Macromolecular and Materials ChemistryMultidisciplinaryAqueous solution34 Chemical SciencesChemical exchangeQ500Diagnostic markersGeneral ChemistryNuclear magnetic resonance spectroscopy021001 nanoscience & nanotechnologyequipment and supplies030104 developmental biologylcsh:Qddc:5000210 nano-technologyhuman activitiesSolution-state NMR51 Physical Sciences
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Ancient pigs reveal a near-complete genomic turnover following their introduction to Europe

2019

International audience; Archaeological evidence indicates that pig domestication had begun by ∼10,500 y before the present (BP) in the Near East, and mitochondrial DNA (mtDNA) suggests that pigs arrived in Europe alongside farmers ∼8,500 y BP. A few thousand years after the introduction of Near Eastern pigs into Europe, however, their characteristic mtDNA signature disappeared and was replaced by haplotypes associated with European wild boars. This turnover could be accounted for by substantial gene flow from local Euro-pean wild boars, although it is also possible that European wild boars were domesticated independently without any genetic contribution from the Near East. To test these hyp…

0301 basic medicineSwine[SHS.ANTHRO-BIO]Humanities and Social Sciences/Biological anthropologySkin Pigmentation[SHS]Humanities and Social SciencesGene flowDomesticationddc:590BREEDSDOMESTIC PIGS/dk/atira/pure/subjectarea/asjc/1000HISTORY0601 history and archaeologyNeolithicHistory AncientPhylogenyMultidisciplinary060102 archaeologyINTROGRESSIONEurope ; pigs ; domestication ; genomesWILD06 humanities and the artsArchaeological evidenceGene flowEuropeSPREADCoatMitochondrial DNAEvolutionZoology930Locus (genetics)BiologyAnimal Breeding and GenomicsDNA MitochondrialMiddle East03 medical and health sciencesAnimalsFokkerij en GenomicaDNA AncientGeneralDomesticationddc:930HaplotypeDNA900 Geschichte und Geografie::930 Geschichte des Altertums (bis ca. 499) Archäologie::930 Geschichte des Altertums bis ca. 499 ArchäologieLONGSIZE030104 developmental biologydomestication evolution gene flow NeolithicWIAS
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BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72

2016

The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity. Here, we examined the functional correlation of HSP72, CHIP, and BAG2, employing human primary fibroblasts.…

0301 basic medicineTime FactorsUbiquitin-Protein LigasesImmunoblottingHSP72 Heat-Shock ProteinsUbiquitin-conjugating enzymeProtein degradationArticleCatalysisCell Linelcsh:ChemistryInorganic Chemistry03 medical and health sciencesUbiquitinddc:570Humansaging; BAG2; CHIP; HSP72; proteostasis; ubiquitinationPhysical and Theoretical ChemistryHSP72lcsh:QH301-705.5Molecular BiologyCellular SenescenceSpectroscopySTUB1proteostasisBAG2biologyCHIPagingOrganic ChemistryUbiquitinationGeneral MedicineComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)lcsh:QD1-999Chaperone (protein)biology.proteinRNA InterferenceProtein foldingMolecular ChaperonesInternational Journal of Molecular Sciences
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Statement of the Prolamin Working Group on the Determination of Gluten in Fermented Foods Containing Partially Hydrolyzed Gluten

2021

On August 12, 2020, the U.S. Food and Drug Administration (FDA) has finalized a rule related to gluten-free labeling for foods containing fermented, hydrolyzed ingredients. The FDA believes that there is no scientifically valid analytical method effective for determining gluten in fermented or hydrolyzed foods. In the absence of an analytical method, the FDA has decided to evaluate gluten-free claims on these foods based only on evidence that the food or ingredient used is gluten-free before fermentation or hydrolysis. For example, barley-based beers from which gluten is removed during brewing using special filtration, adsorption and/or enzymatic treatment are therefore excluded from bearin…

0301 basic medicineanalysifermented foodanalysisEndocrinology Diabetes and MetabolismIngredientProlaminFood scienceIngredient0302 clinical medicinehydrolysed beer[SDV.IDA]Life Sciences [q-bio]/Food engineeringFood scienceFermentation in food processingComputingMilieux_MISCELLANEOUS2. Zero hungerchemistry.chemical_classificationNutrition and DieteticsbiologyChemistryHydrolysisdigestive oral and skin physiologyfood and beveragesQuímicaChemistryFermentation in food processingProlamin Working Groupgluten-free foodpartially hydrolyzed glutenlcsh:Nutrition. Foods and food supplyLife sciences; biologyOpinioncompetitive ELISAlcsh:TX341-641030209 endocrinology & metabolismdigestive systemFood and drug administration03 medical and health sciencesHydrolysisddc:570ProlaminLC-MS/MSFood and drug administrationNutrition030109 nutrition & dieteticsbusiness.industrynutritional and metabolic diseasesBrewingGlutendigestive system diseasesPlant BreedingglutenFermentationbiology.proteinBrewingFermentation[SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologiebusiness[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionceliac diseaseFrontiers in Nutrition
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Differentially Expressed tRNA-Derived Small RNAs Co-Sediment Primarily with Non-Polysomal Fractions in Drosophila

2017

Recent studies point to the existence of poorly characterized small regulatory RNAs generated from mRNAs, rRNAs and tRNAs. To explore the subcellular location of tRNA-derived small RNAs, 0–1 and 7–8 h Drosophila embryos were fractionated on sucrose density gradients. Analysis of 12,553,921 deep-sequencing reads from unfractionated and fractionated Drosophila embryos has revealed that tRFs, which are detected mainly from the 5’ends of tRNAs, co-sediment with the non-polysomal fractions. Interestingly, the expression levels of a subset of tRFs change temporally following thematernal-to-zygotic transition in embryos. We detected non-polysomal association of tRFs in S2 cells as well. Differenti…

0301 basic medicineanimal structureslcsh:QH426-470TRNAArticle03 medical and health sciencesExpression patternddc:570PolysomeGeneticstRFDrosophila (subgenus)tRNAGenetics (clinical)biologyTransition (genetics)PolysomeSchneider 2 cellsEmbryobiology.organism_classificationtRF; tRNA; polysome; <i>Drosophila</i>Molecular biologyCell biologylcsh:Genetics030104 developmental biologyTransfer RNADrosophilapolysomeTRFGenes
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Uncoupling of dynamin polymerization and GTPase activity revealed by the conformation-specific nanobody dynab

2017

Dynamin is a large GTPase that forms a helical collar at the neck of endocytic pits, and catalyzes membrane fission (Schmid and Frolov, 2011; Ferguson and De Camilli, 2012). Dynamin fission reaction is strictly dependent on GTP hydrolysis, but how fission is mediated is still debated (Antonny et al., 2016): GTP energy could be spent in membrane constriction required for fission, or in disassembly of the dynamin polymer to trigger fission. To follow dynamin GTP hydrolysis at endocytic pits, we generated a conformation-specific nanobody called dynab, that binds preferentially to the GTP hydrolytic state of dynamin-1. Dynab allowed us to follow the GTPase activity of dynamin-1 in real-time. We…

0301 basic medicineendocrine systemGTP'MouseQH301-705.5FissionScienceEndocytic cycleGTPasemacromolecular substancesEndocytosisGeneral Biochemistry Genetics and Molecular BiologyGTP PhosphohydrolasesPolymerization03 medical and health sciences0302 clinical medicineMembrane fissiondynaminendocytosisHumansBiology (General)Dynamin IDynaminGeneral Immunology and MicrobiologyChemistryGeneral Neuroscienceconformational-specific nanobodyHydrolysisQRGeneral MedicineCell BiologyFibroblastsSingle-Domain Antibodiesenzyme030104 developmental biologyMembraneddc:540BiophysicsMedicineGuanosine Triphosphatebiological phenomena cell phenomena and immunitycell biology conformational-specific nanobody dynamin endocytosis enzyme human mouse030217 neurology & neurosurgeryResearch ArticleHumaneLife
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