2025
CRISPR-Cas13d Functional Transcriptomics Reveals Widespread Isoform-Selective Cancer Dependencies on LncRNAs
Morelli E, Aktas Samur A, Maisano D, Gao C, Favasuli V, Papaioannou D, De Nola G, Henninger J, Liu N, Turi M, Folino P, Vreux L, Cumerlato M, Chen L, Aifantis I, Fulciniti M, Anderson K, Lytton-Jean A, Gulla A, Young R, Samur M, Munshi N. CRISPR-Cas13d Functional Transcriptomics Reveals Widespread Isoform-Selective Cancer Dependencies on LncRNAs. Blood 2025 PMID: 40403231, DOI: 10.1182/blood.2025028746.Peer-Reviewed Original ResearchCRISPR-Cas13dMultiple myelomaTE-lncRNAsIsoform-specific functionsDiverse cancer cell linesMM patientsCancer cell linesCellular proteostasisSubcellular localizationTumor cellsClinical dataCancer transcriptomeCytosolic isoformEndoplasmic reticulumFunctional transcriptomeHeat shock proteinsCancer dependenciesMM-specificClinical relevanceAnimal modelsLong noncoding RNAsLncRNA transcriptomeTherapeutic potentialCharacterize hundredsTranscriptomeDSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress
Alim S, Cheppali S, Pawar S, Swamy M. DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress. Biochimica Et Biophysica Acta (BBA) - Proteins And Proteomics 2025, 1873: 141064. PMID: 39956303, DOI: 10.1016/j.bbapap.2025.141064.Peer-Reviewed Original ResearchConceptsChaperone-like activitySeminal plasmaFibronectin type IITetramer to monomersSperm capacitationSurface hydrophobicityMolecular chaperonesClient proteinsHeat shock proteinsBiophysical studiesAlcohol dehydrogenaseOxidative stressPhysiological ligandsShock proteinsProteinHead group moietySHspsBinding of phosphorylcholineCholine phospholipidsBindingFibronectinDehydrogenaseChaperoneSpermMammals
2024
Carrier-free multifunctional nanomedicine for enhanced hyperthermic intraperitoneal chemotherapy against abdominal pelvic tumors
Fang H, Zhang L, Wu Y, Chen L, Deng Z, Zheng Z, Wang Y, Yang Y, Chen Q. Carrier-free multifunctional nanomedicine for enhanced hyperthermic intraperitoneal chemotherapy against abdominal pelvic tumors. Chemical Engineering Journal 2024, 498: 155781. DOI: 10.1016/j.cej.2024.155781.Peer-Reviewed Original ResearchHyperthermic intraperitoneal chemotherapyImmunogenic cell deathDamage-associated molecular patternsPelvic tumorsIntraperitoneal chemotherapyGambogic acidAnti-tumor immune response in vivoInfiltration of cytotoxic T lymphocytesTriggering immunogenic cell deathRelease of damage-associated molecular patternsCancer cellsImmune responses in vivoCytotoxic T lymphocytesInduce apoptosis of cancer cellsApoptosis of cancer cellsResponses in vivoInhibitor of heat shock proteinCell deathHyperthermia-induced cell deathPenetration of nanoparticlesTumor extracellular matrixHeat shock proteinsOvarian cancerTumor microenvironmentT lymphocytes
2023
Cellular protection from H2O2 toxicity by Fv-Hsp70: protection via catalase and gamma-glutamyl-cysteine synthase
Hino C, Chan G, Jordaan G, Chang S, Saunders J, Bashir M, Hansen J, Gera J, Weisbart R, Nishimura R. Cellular protection from H2O2 toxicity by Fv-Hsp70: protection via catalase and gamma-glutamyl-cysteine synthase. Cell Stress And Chaperones 2023, 28: 429-439. PMID: 37171750, PMCID: PMC10352194, DOI: 10.1007/s12192-023-01349-6.Peer-Reviewed Original ResearchConceptsHeat shock proteinsGamma-glutamylcysteine synthaseCellular protectionAcute oxidative stressLid domainProtein-binding domainsATPase domainCysteine synthaseOxidative stressCellular stressRecombinant proteinsSH-SY5Y cellsEndogenous heat shock proteinsShock proteinsCell deathProteinProtein catalaseHSP70H2O2 toxicityCellsSynthaseΜM concentrationsDomainCatalaseDirect responseHyperosmotic stress response regulates interstitial homeostasis and pathogenic inflammation
Sumida T. Hyperosmotic stress response regulates interstitial homeostasis and pathogenic inflammation. The Journal Of Biochemistry 2023, 173: 159-166. PMID: 36722164, DOI: 10.1093/jb/mvad009.Peer-Reviewed Original ResearchConceptsHyperosmotic stress responseStress responseCell type-specific mannerFundamental cellular responsesType-specific mannerHeat shock proteinsCell cycle arrestImmune cell differentiationOsmolyte synthesisContext of diseaseHyperosmotic stressIon transportersHyperosmotic responseMetabolic remodelingMolecular mechanismsCellular responsesShock proteinsCell differentiationHuman diseasesCellular shrinkageCycle arrestAdaptative responseSpecific mannerTissue microenvironmentTissue immune homeostasis
2020
Gene expression in the epileptic (EL) mouse hippocampus
Lee TS, Li AY, Rapuano A, Mantis J, Eid T, Seyfried TN, de Lanerolle NC. Gene expression in the epileptic (EL) mouse hippocampus. Neurobiology Of Disease 2020, 147: 105152. PMID: 33153970, DOI: 10.1016/j.nbd.2020.105152.Peer-Reviewed Original ResearchConceptsTemporal lobe epilepsyHuman temporal lobe epilepsySeizure focusHippocampal seizure focusRole of neurogliaExtensive neuronal lossMolecular changesEpileptic miceMicroglial activationNeuronal lossNeuron lossEl miceLobe epilepsySeizure modelHippocampal fieldsSeizure generationPathological changesPaucity of studiesMouse hippocampusAnimal modelsHeat shock proteinsNormal populationPathological processesExpression levelsEpilepsy
2018
Molecular regulations and therapeutic targets of Gaucher disease
Chen Y, Sud N, Hettinghouse A, Liu C. Molecular regulations and therapeutic targets of Gaucher disease. Cytokine & Growth Factor Reviews 2018, 41: 65-74. PMID: 29699937, PMCID: PMC8108120, DOI: 10.1016/j.cytogfr.2018.04.003.Peer-Reviewed Original ResearchConceptsGaucher diseaseHeat shock proteinsProper foldingMolecular regulationActivity of GCaseLysosomal localizationShock proteinsCommon lysosomal storage diseaseLysosomal appearanceIon channelsCalcium ion channelsLysosomal accumulationSaposin CLysosomal storage diseaseSubstrate glucosylceramideInflammatory mediatorsProinflammatory moleculesNew targetsPathogenic mechanismsTherapeutic targetGCaseNovel moleculesSmall moleculesDiseaseStorage disease
2017
Direct exposure to mild heat promotes proliferation and neuronal differentiation of neural stem/progenitor cells in vitro
Hossain E, Matsuzaki K, Katakura M, Sugimoto N, Al Mamun AA, Islam R, Hashimoto M, Shido O. Direct exposure to mild heat promotes proliferation and neuronal differentiation of neural stem/progenitor cells in vitro. PLOS ONE 2017, 12: e0190356. PMID: 29287093, PMCID: PMC5747471, DOI: 10.1371/journal.pone.0190356.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrain-Derived Neurotrophic FactorCell DifferentiationCell ProliferationCells, CulturedChromonesCREB-Binding ProteinHeat-Shock ProteinsHot TemperatureMorpholinesNeural Stem CellsNeuronsPhosphorylationProto-Oncogene Proteins c-aktRatsReactive Oxygen SpeciesReal-Time Polymerase Chain ReactionConceptsNSC/NPC proliferationBrain-derived neurotrophic factorNSCs/NPCsNeural stem/progenitor cellsStem/progenitor cellsNeurosphere diameterMild heat exposureNPC proliferationMRNA expressionHeat exposureHeat shock proteinsNeuronal differentiationBDNF mRNA expressionProgenitor cellsEffective therapeutic strategyHeat-acclimated ratsCAMP response element-binding proteinResponse element-binding proteinReactive oxygen species levelsHeat acclimationAkt phosphorylation levelsForebrain cortexProportion of cellsEnhanced neurogenesisNeurotrophic factorComparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein
Yuan P, D’Lima N, Slavoff SA. Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein. Biochemistry 2017, 57: 56-60. PMID: 29039649, PMCID: PMC5761644, DOI: 10.1021/acs.biochem.7b00864.Peer-Reviewed Original ResearchMeSH KeywordsChromatography, High Pressure LiquidEscherichia coliEscherichia coli K12Escherichia coli ProteinsGene Expression Regulation, BacterialGreen Fluorescent ProteinsHeat-Shock ProteinsHeat-Shock Proteins, SmallHeat-Shock ResponseMembrane ProteinsModels, MolecularMolecular Sequence AnnotationOpen Reading FramesPhosphogluconate DehydrogenaseProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein TransportProteogenomicsProteomicsRecombinant Fusion ProteinsTandem Mass SpectrometryConceptsHeat shock proteinsShock proteinsMembrane proteomicsE. coli heat shock proteinsComparative membrane proteomicsSmall open reading framesMembrane protein enrichmentQuantitative membrane proteomicsQuantitative proteomics protocolBacterial stress responseQuantitative mass spectrometryOpen reading frameDiscovery of thousandsEscherichia coli K12Transmembrane helicesProteomics protocolMembrane proteinsEvolutionary spaceReading frameSmall proteinsStress responseProteomicsColi K12Amino acidsProtein enrichment
2016
Protein stabilization improves STAT3 function in autosomal dominant hyper-IgE syndrome
Bocchini C, Nahmod K, Katsonis P, Kim S, Kasembeli M, Freeman A, Lichtarge O, Makedonas G, Tweardy D. Protein stabilization improves STAT3 function in autosomal dominant hyper-IgE syndrome. Blood 2016, 128: 3061-3072. PMID: 27799162, PMCID: PMC5201093, DOI: 10.1182/blood-2016-02-702373.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesCytokinesDiterpenesDNA-Binding ProteinsHalf-LifeHeat Shock Transcription FactorsHerpesvirus 4, HumanHumansInterleukin-17Job SyndromeMiceModels, MolecularMutant ProteinsMutationPhosphotyrosineProtein BindingProtein StabilitySpleenSTAT3 Transcription FactorTranscription FactorsConceptsAutosomal dominant hyper-IgE syndromeSTAT3 mutationsPeripheral blood mononuclear cellsAD-HIESProtein stabilityEpstein-Barr virus-transformed BPY-STAT3Human peripheral blood mononuclear cellsHeat shock proteinsHyper-IgE syndromeSTAT3 target genesProtein half-lifeMouse splenocytesUpregulating heat shock proteinsAD-HIES patientsLevel of STAT3T cellsDominant-negative mutationsTreatment of human peripheral blood mononuclear cellsCD8<sup>+</sup> T cellsSTAT3 functionEpstein-Barr virus-transformed B cellsProtein functionHuman CD4<sup>+</sup>MRNA levels
2014
Overproduction and biophysical characterization of human HSP70 proteins
Boswell-Casteel R, Johnson J, Duggan K, Tsutsui Y, Hays F. Overproduction and biophysical characterization of human HSP70 proteins. Protein Expression And Purification 2014, 106: 57-65. PMID: 25266791, PMCID: PMC4248018, DOI: 10.1016/j.pep.2014.09.013.Peer-Reviewed Original ResearchConceptsHuman HSP70 proteinHeat shock proteinsResponse pathwaysHSP70 proteinBiophysical characterizationFacilitate protein foldingVital cellular functionsInitial biophysical characterizationProtein-protein interactionsFuture biochemical studiesHeterologous overexpressionHSP functionCellular functionsProtein functionProtein foldingHSP70 familyFunctional characterizationConformational rearrangementsShock proteinsChemical stressorsHuman Hsp70HSP proteinsDownstream investigationsBiochemical studiesEscherichia coli
2013
Combating Oxidative/Nitrosative Stress with Electrophilic Counterattack Strategies
Satoh T, Akhtar M, Lipton S. Combating Oxidative/Nitrosative Stress with Electrophilic Counterattack Strategies. 2013, 277-307. DOI: 10.1007/978-94-007-5787-5_10.Peer-Reviewed Original ResearchPro-electrophilic drugsKeap1/Nrf2 pathwayTranscription-dependent pathwayCysteine thiol oxidationNitrosative stressOxidative stressStress-induced oxidationHeat shock proteinsRedox regulationSpecific cysteineProlonged oxidative stressNrf2 pathwayPhase 2 enzymesKeap1/Nrf2Redox stressThiol oxidationElectrophilic compoundsDefense systemHerb rosemaryPathwayNormal cellsCarnosic acidNeurodegenerative disordersCounterattack strategiesDeplete glutathione
2012
3.10 Chaperones and Protein Folding
Horwich A, Buchner J, Smock R, Gierasch L, Saibil H. 3.10 Chaperones and Protein Folding. 2012, 212-237. DOI: 10.1016/b978-0-12-374920-8.00313-1.Peer-Reviewed Original ResearchSubstrate proteinsMolecular chaperonesSolvent-exposed hydrophobic surfaceSmall heat shock proteinsChaperone-bound proteinsProtein binding domainsNon-native conformationsNon-native statesHeat shock proteinsBinding of ATPSpecialized proteinsProtein foldingChaperonesBinding domainsOligomeric assembliesBiophysical methodsShock proteinsConformational changesPolypeptide chainStress conditionsNative stateProteinCurrent understandingFoldingMultimolecular aggregates
2010
Promotion of CHIP-Mediated p53 Degradation Protects the Heart From Ischemic Injury
Naito AT, Okada S, Minamino T, Iwanaga K, Liu ML, Sumida T, Nomura S, Sahara N, Mizoroki T, Takashima A, Akazawa H, Nagai T, Shiojima I, Komuro I. Promotion of CHIP-Mediated p53 Degradation Protects the Heart From Ischemic Injury. Circulation Research 2010, 106: 1692-1702. PMID: 20413784, DOI: 10.1161/circresaha.109.214346.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornApoptosisBase SequenceBenzoquinonesCell HypoxiaChlorocebus aethiopsCOS CellsDisease Models, AnimalGenetic TherapyHSP90 Heat-Shock ProteinsHumansHypoxia-Inducible Factor 1, alpha SubunitLactams, MacrocyclicMaleMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataMutationMyocardial InfarctionMyocytes, CardiacPromoter Regions, GeneticProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalRatsRats, WistarRNA InterferenceTranscriptional ActivationTumor Suppressor Protein p53Ubiquitin-Protein LigasesUbiquitinationVentricular RemodelingConceptsMyocardial infarctionP53 accumulationCardiomyocyte apoptosisCoronary heart diseaseNumber of patientsNovel therapeutic strategiesP53 degradationApoptosis of cardiomyocytesHeat shock proteinsHeart failureIschemic injuryCardioprotective effectsVentricular remodelingCHIP overexpressionHeart diseaseInfarctionTherapeutic strategiesProteasomal degradationMyocardial apoptosisAmount of p53Molecular mechanismsShock proteinsP53 antagonistP53 accumulatesProtein levelsCrystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand
Cortajarena AL, Wang J, Regan L. Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand. The FEBS Journal 2010, 277: 1058-1066. PMID: 20089039, DOI: 10.1111/j.1742-4658.2009.07549.x.Peer-Reviewed Original ResearchConceptsTPR domainC-terminusKey protein-protein interactionsTetratricopeptide repeat modulesChaperone heat shock proteinProtein-protein interactionsHeat shock responseHeat shock proteinsTPR proteinsChaperone functionTPR unitsProtein domainsNew packing arrangementRepeat modulesMolecular basisPeptide ligandsShock proteinsShock responseHsp90Terminal residuesX-ray crystal structureProteinCrystal structureDomainTetratricopeptide
2007
Regionally Specific Regulation of ERK MAP Kinase in a Model of Antidepressant-Sensitive Chronic Depression
Gourley SL, Wu FJ, Kiraly DD, Ploski JE, Kedves AT, Duman RS, Taylor JR. Regionally Specific Regulation of ERK MAP Kinase in a Model of Antidepressant-Sensitive Chronic Depression. Biological Psychiatry 2007, 63: 353-359. PMID: 17889834, PMCID: PMC2277331, DOI: 10.1016/j.biopsych.2007.07.016.Peer-Reviewed Original ResearchMeSH KeywordsAmitriptylineAnimalsAnti-Inflammatory AgentsAntidepressive Agents, TricyclicChronic DiseaseConditioning, OperantCorticosteroneCREB-Binding ProteinDentate GyrusDepressive Disorder, MajorDisease Models, AnimalEndoplasmic Reticulum Chaperone BiPExtracellular Signal-Regulated MAP KinasesFluoxetineHeat-Shock ProteinsHippocampusLocomotionMiceMice, Inbred C57BLMolecular ChaperonesMotivationSelective Serotonin Reuptake InhibitorsConceptsAntidepressant efficacyChronic corticosteroneDentate gyrusChronic depressionCA1/CA3Depression-like behaviorExtracellular signal-regulated kinase 1/2Response element-binding proteinSignal-regulated kinase 1/2Amitriptyline treatmentGlucocorticoid exposureADT treatmentNaive rodentsBehavioral despairLong-term consequencesTail suspensionElement-binding proteinCyclic adenosine monophosphateBiochemical measuresERK MAP kinasePrefrontal cortexHeat shock proteinsOperant conditioning taskCommon mediatorPERK1/2S-Nitrosylation and uncompetitive/fast off-rate (UFO) drug therapy in neurodegenerative disorders of protein misfolding
Nakamura T, Lipton S. S-Nitrosylation and uncompetitive/fast off-rate (UFO) drug therapy in neurodegenerative disorders of protein misfolding. Cell Death & Differentiation 2007, 14: 1305-1314. PMID: 17431424, DOI: 10.1038/sj.cdd.4402138.Peer-Reviewed Original ResearchConceptsS-nitrosylationProtein functionProtein misfoldingCell deathNeuronal cell deathProper protein foldingProtein disulfide isomeraseCysteine thiol groupsHeat shock proteinsExcessive NMDA receptor activityGlucose-regulated protein 78Neurodegenerative disordersProtein foldingExcitotoxic damageFree radical nitric oxideConformational changesMisfoldingForm of neurotoxicityRadical nitric oxideN-methyl-D-aspartate receptorsNitric oxideExcessive activityProteinProtein 78Chronic neurodegenerative disorders
2005
Ha-rasval12 induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Ha-rasval12-transformed cells
Stanhill A, Levin V, Hendel A, Shachar I, Kazanov D, Arber N, Kaminski N, Engelberg D. Ha-rasval12 induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Ha-rasval12-transformed cells. Oncogene 2005, 25: 1485-1495. PMID: 16278678, DOI: 10.1038/sj.onc.1209193.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAnimalsCell Line, TransformedDNA-Binding ProteinsGene Expression RegulationGenes, ReporterHeat Shock Transcription FactorsHeLa CellsHSP70 Heat-Shock ProteinsHumansMiceMice, NudeNIH 3T3 CellsOncogene Protein p21(ras)Oxidation-ReductionPhosphorylationRatsTranscription FactorsTranscription, GeneticConceptsCellular protective responseHeat shock factor 1Shock factor 1Fibroblast expressionProtective responseHeat shock proteinsHSP70 expressionFactor 1Promoter-driven reporter geneSoft agarTumorsHeat shock elementShock proteinsHSF1 activationCellsDirect effectExpressionHsp70 transcriptionPoint mutations
1998
Ischemic Pretreatment Increases Cytoskeletal Association of 25 kD and 70 kD Heat-Shock Proteins and of Na,K-ATPase in Rat Renal Cortex after Repeat Ischemia † 1786
Aufricht C, Bidmon B, Herkner K, Siegel N, Kashgarian M, Van Why S. Ischemic Pretreatment Increases Cytoskeletal Association of 25 kD and 70 kD Heat-Shock Proteins and of Na,K-ATPase in Rat Renal Cortex after Repeat Ischemia † 1786. Pediatric Research 1998, 43: 304-304. DOI: 10.1203/00006450-199804001-01808.Peer-Reviewed Original ResearchHeat-shock protein 25 induction and redistribution during actin reorganization after renal ischemia
Aufricht C, Ardito T, Thulin G, Kashgarian M, Siegel N, Van Why S. Heat-shock protein 25 induction and redistribution during actin reorganization after renal ischemia. American Journal Of Physiology 1998, 274: f215-f222. PMID: 9458842, DOI: 10.1152/ajprenal.1998.274.1.f215.Peer-Reviewed Original ResearchConceptsHSP-25Renal ischemiaHeat shock protein 25Ischemic renal injuryH reflowRat renal cortexControl proximal tubulesRenal injuryPostischemic recoveryRenal cortexIschemiaProximal tubulesIntracytoplasmic accumulationPeak levelsHeat shock proteinsProtein 25Actin stainingInsoluble cytoskeletal fractionPunctate accumulationsCytoskeletal disruptionSmall heat shock proteinsRegulatory roleInductionIntracellular distributionCytoskeletal fraction
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