2024
Neuroinflammation in Alzheimer disease
Heneka M, van der Flier W, Jessen F, Hoozemanns J, Thal D, Boche D, Brosseron F, Teunissen C, Zetterberg H, Jacobs A, Edison P, Ramirez A, Cruchaga C, Lambert J, Laza A, Sanchez-Mut J, Fischer A, Castro-Gomez S, Stein T, Kleineidam L, Wagner M, Neher J, Cunningham C, Singhrao S, Prinz M, Glass C, Schlachetzki J, Butovsky O, Kleemann K, De Jaeger P, Scheiblich H, Brown G, Landreth G, Moutinho M, Grutzendler J, Gomez-Nicola D, McManus R, Andreasson K, Ising C, Karabag D, Baker D, Liddelow S, Verkhratsky A, Tansey M, Monsonego A, Aigner L, Dorothée G, Nave K, Simons M, Constantin G, Rosenzweig N, Pascual A, Petzold G, Kipnis J, Venegas C, Colonna M, Walter J, Tenner A, O’Banion M, Steinert J, Feinstein D, Sastre M, Bhaskar K, Hong S, Schafer D, Golde T, Ransohoff R, Morgan D, Breitner J, Mancuso R, Riechers S. Neuroinflammation in Alzheimer disease. Nature Reviews Immunology 2024, 25: 321-352. PMID: 39653749, DOI: 10.1038/s41577-024-01104-7.Peer-Reviewed Original ResearchAlzheimer's diseasePathogenesis of Alzheimer's diseaseMultiple lines of informationGenetic studiesInfluence of geneticsLines of informationCell typesDisease developmentDementia-causing diseasesStages of Alzheimer's diseasePathological roleMultiple linesTherapeutic strategiesImmune processesPreclinical stage of Alzheimer's diseaseCellsAdaptive immune activationTargeting neuroinflammationPathological mechanismsLifestyle factorsGeneticsThe physiological and pathological roles of RNA modifications in T cells
Deng Y, Zhou J, Li H. The physiological and pathological roles of RNA modifications in T cells. Cell Chemical Biology 2024, 31: 1578-1592. PMID: 38986618, DOI: 10.1016/j.chembiol.2024.06.003.Peer-Reviewed Original ResearchRNA modificationsDynamic chemical modificationsInternal RNA modificationFunctions of mammalian cellsT cell developmentPathological roleRNA transcriptsCellular stimuliMammalian cellsRNA moleculesPost-transcriptionallyT cell biologyT cell survivalT cellsCell developmentCell survivalCell biologyRNAT cell-based immunotherapyCell-based immunotherapyT cell immunityAdaptive immunityCellsDifferentiationCell immunity
2023
Targeted Dephosphorylation of Tau by Phosphorylation Targeting Chimeras (PhosTACs) as a Therapeutic Modality
Hu Z, Chen P, Li W, Douglas T, Hines J, Liu Y, Crews C. Targeted Dephosphorylation of Tau by Phosphorylation Targeting Chimeras (PhosTACs) as a Therapeutic Modality. Journal Of The American Chemical Society 2023, 145: 4045-4055. PMID: 36753634, PMCID: PMC11670127, DOI: 10.1021/jacs.2c11706.Peer-Reviewed Original ResearchProtein tauTau dephosphorylationDisease-modifying therapiesMicrotubule-associated protein tauTau phosphorylation levelsImportant pathological roleTherapeutic modalitiesTau phosphorylationAlzheimer's diseaseTau proteinTherapeutic potentialPathological roleKinase inhibitorsEnhanced downregulationLimited benefitPhosphorylation levelsTauTauopathiesDiseaseCurrent strategiesTau phosphatase
2022
New insights into the role of dipeptidyl peptidase 8 and dipeptidyl peptidase 9 and their inhibitors
Cui C, Tian X, Wei L, Wang Y, Wang K, Fu R. New insights into the role of dipeptidyl peptidase 8 and dipeptidyl peptidase 9 and their inhibitors. Frontiers In Pharmacology 2022, 13: 1002871. PMID: 36172198, PMCID: PMC9510841, DOI: 10.3389/fphar.2022.1002871.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsDipeptidyl peptidase 8Peptidase 8Dipeptidyl peptidase 9Serine proteolytic enzymesBiological processesNew potential targetsPhysiological functionsSpecific substratesCell behaviorNormal developmentEnergy metabolismEssential roleChronic kidney diseaseN-terminal dipeptidePenultimate positionPotential targetOrgan fibrosisPathological rolePathological processesNew insightsTreatment of tumorsProteolytic enzymesRecent research advancesKidney diseaseCell pyroptosis
2020
Freezing and piercing of in vitro asymmetric plasma membrane by α-synuclein
Heo P, Pincet F. Freezing and piercing of in vitro asymmetric plasma membrane by α-synuclein. Communications Biology 2020, 3: 148. PMID: 32235856, PMCID: PMC7109109, DOI: 10.1038/s42003-020-0883-7.Peer-Reviewed Original ResearchMeSH Keywordsalpha-SynucleinCell MembraneElectric CapacitanceFluorescence Recovery After PhotobleachingHydrophobic and Hydrophilic InteractionsLab-On-A-Chip DevicesMembrane FluidityMembrane LipidsMembrane PotentialsMembranes, ArtificialMicrofluidic Analytical TechniquesNeuronsProtein AggregatesProtein Aggregation, PathologicalProtein BindingProtein ConformationStructure-Activity RelationshipSynucleinopathiesConceptsPlasma membraneMembrane-bound proteinsAccumulation of aggregatesΑ-synucleinCytosolic leafletMembrane topologyMembrane hydrophobic coreCytosolic proteinsProteinExtracellular onesHydrophobic corePathological roleDiscrete sizesMembraneLeafletsMembrane capacitanceNeurological diseasesLipidsAccumulationMicrofluidic setup
2017
Silent Allosteric Modulation of mGluR5 Maintains Glutamate Signaling while Rescuing Alzheimer’s Mouse Phenotypes
Haas LT, Salazar SV, Smith LM, Zhao HR, Cox TO, Herber CS, Degnan AP, Balakrishnan A, Macor JE, Albright CF, Strittmatter SM. Silent Allosteric Modulation of mGluR5 Maintains Glutamate Signaling while Rescuing Alzheimer’s Mouse Phenotypes. Cell Reports 2017, 20: 76-88. PMID: 28683325, PMCID: PMC5547898, DOI: 10.1016/j.celrep.2017.06.023.Peer-Reviewed Original ResearchConceptsAD transgenic mouse modelDisease pathologyMetabotropic glutamate receptor 5Allosteric modulationGlutamate receptor 5Alzheimer's disease pathologyTransgenic mouse brainSilent allosteric modulatorsTransgenic mouse modelBroad therapeutic windowMouse phenotypeAD interventionSynaptic depletionBrain slicesGlutamate signalingMouse modelTherapeutic windowAD phenotypeReceptor 5Mouse brainAllosteric modulatorsMemory deficitsCellular prion proteinPathological roleMGluR5Reprimo tissue-specific expression pattern is conserved between zebrafish and human
Figueroa RJ, Carrasco-Avino G, Wichmann IA, Lange M, Owen GI, Siekmann AF, Corvalán AH, Opazo JC, Amigo JD. Reprimo tissue-specific expression pattern is conserved between zebrafish and human. PLOS ONE 2017, 12: e0178274. PMID: 28562620, PMCID: PMC5451059, DOI: 10.1371/journal.pone.0178274.Peer-Reviewed Original ResearchConceptsTissue-specific expression patternsExpression patternsGene familyExpression profilesSpatiotemporal expression profilesSitu hybridizationP53-mediated cell cycle arrestG2/M.Tumor suppressor geneUnique expression profileCell cycle arrestZebrafish developmentPhylogenetic analysisMost speciesMalignant tumor progressionGene transcriptsZebrafishProtein productsSpatiotemporal expressionCycle arrestReprimoCentral nervous systemPathological roleModel systemRT-qPCR
2016
The Wnt Antagonist Dickkopf-1 Promotes Pathological Type 2 Cell-Mediated Inflammation
Chae WJ, Ehrlich AK, Chan PY, Teixeira AM, Henegariu O, Hao L, Shin JH, Park JH, Tang WH, Kim ST, Maher SE, Goldsmith-Pestana K, Shan P, Hwa J, Lee PJ, Krause DS, Rothlin CV, McMahon-Pratt D, Bothwell AL. The Wnt Antagonist Dickkopf-1 Promotes Pathological Type 2 Cell-Mediated Inflammation. Immunity 2016, 44: 246-258. PMID: 26872695, PMCID: PMC4758884, DOI: 10.1016/j.immuni.2016.01.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, DermatophagoidesAntigens, ProtozoanAsthmaBlood PlateletsCell DifferentiationCells, CulturedCytokinesExtracellular Signal-Regulated MAP KinasesGene Expression RegulationHumansInflammationIntercellular Signaling Peptides and ProteinsLeishmania majorLeishmaniasis, CutaneousMiceMice, Inbred BALB CMice, Inbred C57BLMice, TransgenicModels, AnimalPyroglyphidaeSignal TransductionTh2 CellsTOR Serine-Threonine KinasesWnt ProteinsConceptsCell-mediated inflammationTh2 cell cytokine productionCell cytokine productionLeukocyte-platelet aggregatesLeukocyte infiltrationDkk-1Cytokine productionT helper 2 cellsLeishmania major infectionHouse dust miteTranscription factor c-MafAllergen challengeMajor infectionDust miteImmune responseDickkopf-1Parasitic infectionsGATA-3Pathological roleFunctional inhibitionInflammationC-MafP38 MAPKInfiltrationInfection
2015
Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase
Jonas EA, Porter GA, Beutner G, Mnatsakanyan N, Alavian KN. Cell death disguised: The mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase. Pharmacological Research 2015, 99: 382-392. PMID: 25956324, PMCID: PMC4567435, DOI: 10.1016/j.phrs.2015.04.013.BooksConceptsMitochondrial permeability transition poreATP synthaseC subunitCell deathF1Fo-ATP synthaseInner mitochondrial membranePermeability transition poreMitochondrial permeability transitionOuter membraneMitochondrial membraneRegulatory mechanismsOxidative phosphorylationATP productionTransition poreMitochondrial functionPermeability transitionMolecular componentsOsmotic dysregulationLarge conductancePathological roleRecent findingsPersistent openingSynthaseIon transportMembrane
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