Search results for "H30"

showing 10 items of 1587 documents

Special Issue on “Proteostasis and Autophagy”

2019

Autophagy is a highly conserved eukaryotic pathway responsible for the lysosomal degradation (and subsequent recycling) of cellular components such as proteins, protein aggregates, and a growing number of organelles or cellular compartments [...]

Proteasome Endopeptidase ComplexChemistryAutophagyEukaryotaUbiquitin-Protein Ligase ComplexesGeneral MedicineProtein aggregationMitochondriaCell biologyEditorialn/aProteostasislcsh:Biology (General)Cellular componentOrganelleAutophagyProteostasislcsh:QH301-705.5Cellular compartmentCells
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Folding and insertion of transmembrane helices at the ER

2021

In eukaryotic cells, the endoplasmic reticulum (ER) is the entry point for newly synthesized proteins that are subsequently distributed to organelles of the endomembrane system. Some of these proteins are completely translocated into the lumen of the ER while others integrate stretches of amino acids into the greasy 30 Å wide interior of the ER membrane bilayer. It is generally accepted that to exist in this non-aqueous environment the majority of membrane integrated amino acids are primarily non-polar/hydrophobic and adopt an α-helical conformation. These stretches are typically around 20 amino acids long and are known as transmembrane (TM) helices. In this review, we will consider how tra…

Protein Conformation alpha-HelicalfoldingProtein FoldingQH301-705.5ReviewEndoplasmic ReticulumRibosomeCatalysisinsertionInorganic Chemistrytransmembrane segmentAnimalsHumansEndomembrane systemmembrane proteinPhysical and Theoretical ChemistryBiology (General)Molecular BiologyQD1-999Spectroscopytransloconchemistry.chemical_classificationEndoplasmic reticulumOrganic ChemistryProteïnes de membranaMembrane ProteinsGeneral MedicineTransloconTransmembrane proteinComputer Science ApplicationsAmino acidTransmembrane domainChemistrychemistryMembrane proteinribosomeBiophysicsHydrophobic and Hydrophilic InteractionsRibosomes
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Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.

2020

The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial−mesenchymal transition and, alteration of protein homeostasis. In the tumors of the brain, proteotoxic stress represents one of the main triggering agents for cell transformation. Curcumin is a natural compound with anti-inflammatory and anti-cancer properties with promising potential for the development of therapeutic drugs for the treatment of cancer as well as neurodegenerative diseases. Among the mediators of cancer development, HSP60 is a key factor for the maintenance of…

Protein FoldingCurcuminCell SurvivalCellCatalysisMalignant transformationCell Linelcsh:ChemistryInorganic ChemistryMitochondrial Proteinschemistry.chemical_compoundNeuroblastomaDownregulation and upregulationHeat shock proteinmedicinepost-translational modificationsHumansSecretionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCell ProliferationHeat shock proteinDose-Response Relationship DrugCommunicationOrganic Chemistrymolecular chaperonesUbiquitinationGeneral MedicineChaperonin 60Computer Science ApplicationsCell biologyUp-RegulationBrain tumorGene Expression Regulation Neoplasticmedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999chemistryApoptosisheat shock proteinsMolecular chaperoneCurcuminbrain tumorsHSP60Post-translational modificationHSP60extracellular HSP60International journal of molecular sciences
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A Stevedore's protein knot.

2009

Protein knots, mostly regarded as intriguing oddities, are gradually being recognized as significant structural motifs. Seven distinctly knotted folds have already been identified. It is by and large unclear how these exceptional structures actually fold, and only recently, experiments and simulations have begun to shed some light on this issue. In checking the new protein structures submitted to the Protein Data Bank, we encountered the most complex and the smallest knots to date: A recently uncovered α-haloacid dehalogenase structure contains a knot with six crossings, a so-called Stevedore knot, in a projection onto a plane. The smallest protein knot is present in an as yet unclassified …

Protein FoldingHydrolasesProtein ConformationComputational Biology/Macromolecular Structure Analysis02 engineering and technologyBiologyMolecular Dynamics SimulationComputational Biology/Molecular DynamicsCombinatorics03 medical and health sciencesCellular and Molecular NeuroscienceKnot (unit)Protein structureGeneticsStructural motifDatabases ProteinMolecular Biologylcsh:QH301-705.5Ecology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesTopological complexityQuantitative Biology::BiomoleculesEcologycomputer.file_format021001 nanoscience & nanotechnologyProtein Data BankMathematics::Geometric TopologyComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Modeling and SimulationProtein foldingStevedore knot0210 nano-technologySingle loopcomputerResearch ArticlePLoS Computational Biology
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Bioinformatic flowchart and database to investigate the origins and diversity of Clan AA peptidases

2009

Abstract Background Clan AA of aspartic peptidases relates the family of pepsin monomers evolutionarily with all dimeric peptidases encoded by eukaryotic LTR retroelements. Recent findings describing various pools of single-domain nonviral host peptidases, in prokaryotes and eukaryotes, indicate that the diversity of clan AA is larger than previously thought. The ensuing approach to investigate this enzyme group is by studying its phylogeny. However, clan AA is a difficult case to study due to the low similarity and different rates of evolution. This work is an ongoing attempt to investigate the different clan AA families to understand the cause of their diversity. Results In this paper, we…

Protein familySequence analysisImmunologyProtein domainMolecular Sequence DataBiologycomputer.software_genreGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryPhylogeneticsSequence Analysis ProteinSoftware DesignConsensus SequenceConsensus sequenceAspartic Acid EndopeptidasesClanAmino Acid SequenceDatabases ProteinPeptide sequencelcsh:QH301-705.5Ecology Evolution Behavior and SystematicsPhylogenyDatabaseAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Applied MathematicsResearchComputational BiologyGenetic VariationGene AnnotationTemplates GeneticMarkov ChainsProtein Structure Tertiarylcsh:Biology (General)Modeling and SimulationGeneral Agricultural and Biological SciencescomputerBiology Direct
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Fast Photochemistry of Prototypical Phytochromes—A Species vs. Subunit Specific Comparison

2015

Phytochromes are multi-domain red light photosensor proteins, which convert red light photons to biological activity utilizing the multitude of structural and chemical reactions. The steady increase in structural information obtained from various bacteriophytochromes has increased understanding about the functional mechanism of the photochemical processes of the phytochromes. Furthermore, a number of spectroscopic studies have revealed kinetic information about the light-induced reactions. The spectroscopic changes are, however, challenging to connect with the structural changes of the chromophore and the protein environment, as the excited state properties of the chromophores are very sens…

Protein subunitDimertransient absorptionPhotochemistryBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrychemistry.chemical_compoundtransient absorption spectroscopyHypothesis and TheoryUltrafast laser spectroscopyMoleculeexcited state dynamicslcsh:QH301-705.5Molecular BiologyProtein secondary structureta114ChemistryPhysicsta1182ChromophoreFluorescencelcsh:Biology (General)Excited statelaser spectroscopyred photosensorsfluorescenceFrontiers in Molecular Biosciences
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Comparative Quantitative Analysis of Porcine Optic Nerve Head and Retina Subproteomes

2019

Optic nerve head (ONH) and retina (RET) are the main sites of damage in neurodegenerative optic neuropathies including glaucoma. Up to date, little is known about the molecular interplay between these two adjoining ocular components in terms of proteomics. To close this gap, we investigated ONH and RET protein extracts derived from porcine eyes (n = 12) (Sus scrofa domestica Linnaeus 1758) using semi-quantitative mass spectrometry (MS)-based proteomics comprising bottom-up LC&ndash

Proteomics0301 basic medicineretinaProteomegenetic structuresSus scrofaGlaucomaProteomicslcsh:ChemistrySus scrofa domestica0302 clinical medicineTandem Mass SpectrometryProtein Interaction Mapslcsh:QH301-705.5Spectroscopybiologyoptic nerve headGeneral MedicineComputer Science ApplicationsCell biologymedicine.anatomical_structureProteomeOptic nerveProtein Binding<i>Sus scrofa domestica</i>Optic DiskArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineMALDI-TOF MSAnimalsHumansPhysical and Theoretical ChemistryEndoplasminMolecular BiologyRetinaClusterinOrganic Chemistrymedicine.diseaseeye diseasesLC-MSglaucomaGene Ontology030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Spectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinsense organsCeruloplasmin030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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Proteome-wide comparison between the amino acid composition of domains and linkers

2018

Objective Amino acid composition is a sequence feature that has been extensively used to characterize proteomes of many species and protein families. Yet the analysis of amino acid composition of protein domains and the linkers connecting them has received less attention. Here, we perform both a comprehensive full-proteome amino acid composition analysis and a similar analysis focusing on domains and linkers, to uncover domain- or linker-specific differential amino acid usage patterns. Results The amino acid composition in the 38 proteomes studied showcase the greater variability found in archaea and bacteria species compared to eukaryotes. When focusing on domains and linkers, we describe …

Proteomics570BacteriaProteomeAmino acid compositionlcsh:Rlcsh:MedicineEukaryotaArchaea570 Life sciencesResearch Notelcsh:Biology (General)Sequence Analysis ProteinCatalytic DomainDomainsAmino Acid SequenceLinkerslcsh:Science (General)lcsh:QH301-705.5570 Biowissenschaftenlcsh:Q1-390BMC Research Notes
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Integrated multi-omics investigations of metalloproteinases in colon cancer: Focus on MMP2 and MMP9

2021

Colorectal cancer (CRC) develops by genetic and epigenetic alterations. However, the molecular mechanisms underlying metastatic dissemination remain unclear and could benefit from multi-omics investigations of specific protein families. Matrix metalloproteinases (MMPs) are proteolytic enzymes involved in ECM remodeling and the processing of bioactive molecules. Increased MMP expression promotes the hallmarks of tumor progression, including angiogenesis, invasion, and metastasis, and is correlated with a shortened survival. Nevertheless, the collective role and the possible coordination of MMP members in CRC are poorly investigated. Here, we performed a multi-omics analysis of MMP expression…

ProteomicsMMP2Epithelial-Mesenchymal TransitionQH301-705.5Colorectal cancerBioinformaticsKaplan-Meier EstimateBiologyMatrix metalloproteinaseMMP9ArticleCatalysisEpigenesis GeneticMetastasisCohort StudiesInorganic ChemistryLymphocytes Tumor-InfiltratingmedicineHumansEpithelial–mesenchymal transitionBiology (General)Physical and Theoretical ChemistrySettore BIO/06 - Anatomia Comparata E CitologiaQD1-999Molecular BiologySpectroscopyTissue Inhibitor of Metalloproteinase-2Functional analysisMMP9Organic ChemistryProteolytic enzymesGeneral Medicinemedicine.diseasePrognosisComputer Science ApplicationsColon cancerExtracellular MatrixGene Expression Regulation NeoplasticChemistryMatrix metalloproteinasesMatrix Metalloproteinase 9Tumor progressionCase-Control StudiesColonic NeoplasmsCancer researchMatrix Metalloproteinase 2Gene expressionMMP2
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