2025
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
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
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
2018
Pharmacological induction of heat shock proteins ameliorates toxicity of mutant PKCγ in spinocerebellar ataxia type 14
Nakazono A, Adachi N, Takahashi H, Seki T, Hamada D, Ueyama T, Sakai N, Saito N. Pharmacological induction of heat shock proteins ameliorates toxicity of mutant PKCγ in spinocerebellar ataxia type 14. Journal Of Biological Chemistry 2018, 293: 14758-14774. PMID: 30093405, PMCID: PMC6153279, DOI: 10.1074/jbc.ra118.002913.Peer-Reviewed Original ResearchConceptsSpinocerebellar ataxia type 14Pharmacological up-regulationC2 domainHeat shock proteinsDominant-inherited neurodegenerative diseaseRefolding of misfolded proteinsUp-regulation of HSP70Type 14Amyloid-like protein aggregatesAmyloid-like fibril formationHerbimycin AIntracellular formationApoptotic cell deathShock proteinsLevels of apoptotic cell deathEndogenous regulatorProtein chaperonesPrimary cultured Purkinje cellsKinase domainProtein aggregationPurkinje cellsCell deathFibril formationInduction of heat shock proteinsHeat shock protein 70Molecular 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
Comparative 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 enrichmentComparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli
D’Lima N, Khitun A, Rosenbloom AD, Yuan P, Gassaway BM, Barber KW, Rinehart J, Slavoff SA. Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli. Journal Of Proteome Research 2017, 16: 3722-3731. PMID: 28861998, PMCID: PMC5647875, DOI: 10.1021/acs.jproteome.7b00419.Peer-Reviewed Original ResearchConceptsCold shock proteinsComparative proteomicsShock proteinsRelated Gram-negative bacteriaMass spectrometry-based proteomicsSmall open reading framesMolecular genetic approachesWhole genome databaseSpectrometry-based proteomicsOpen reading frameE. coliEukaryotic genomesGram-negative bacteriaCellular functionsDifferent organismsGenetic approachesReading frameBiological roleProteomicsMicroproteinsEnable identificationProteinColiGenomeRecent advances
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
2012
The role of hyperosmotic stress in inflammation and disease
Brocker C, Thompson DC, Vasiliou V. The role of hyperosmotic stress in inflammation and disease. BioMolecular Concepts 2012, 3: 345-364. PMID: 22977648, PMCID: PMC3438915, DOI: 10.1515/bmc-2012-0001.Peer-Reviewed Original ResearchHyperosmotic stressNon-renal tissuesCell cycle arrestHigh extracellular osmolarityOsmolyte synthesisCytoskeletal rearrangementsRegulatory pathwaysMitochondrial depolarizationShock proteinsHyperosmotic conditionsHuman diseasesCell shrinkageDNA damageMammalian kidneyCycle arrestInner medullary regionProtein carbonylationCytoprotective mechanismsExtracellular osmolarityConcentrating mechanismAntioxidant enzymesAdaptive mechanismsPhysiological conditionsPathological consequencesOxidative stress3.10 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
Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases
Nakamura T, Lipton S. Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases. Cellular And Molecular Life Sciences 2007, 64: 1609-1620. PMID: 17453143, PMCID: PMC11136414, DOI: 10.1007/s00018-007-6525-0.Peer-Reviewed Original ResearchConceptsUbiquitin-proteasome systemNormal protein degradationProtein disulfide isomeraseMolecular chaperonesSpecific chaperonesGlucose-regulated protein 78Proper foldingProtein misfoldingAberrant proteinsProtein foldingUPS proteinsProtein degradationMolecular mechanismsShock proteinsConformational changesExcessive reactive oxygenCell deathNeuronal cell deathProteinChaperonesProtein 78Reactive oxygenMisfoldingNitrogen speciesNitrosative stress
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
Heat shock protein 70 of the agent of human granulocytic ehrlichiosis binds to Borrelia burgdorferi antibodies.
Ijdo J, Zhang Y, Anderson M, Goldberg D, Fikrig E. Heat shock protein 70 of the agent of human granulocytic ehrlichiosis binds to Borrelia burgdorferi antibodies. MSphere 1998, 5: 118-20. PMID: 9455892, PMCID: PMC121403, DOI: 10.1128/cdli.5.1.118-120.1998.Peer-Reviewed Original ResearchConceptsHuman granulocytic ehrlichiosisEhrlichial antigenHSP-70Borrelia burgdorferi antibodiesSerologic test resultsHeat shock protein 70Shock protein 70Burgdorferi antibodiesPatient seraGranulocytic ehrlichiosisLyme diseaseFirst weekHeat shock proteinsLyme disease spirochetePrior exposureImmunoglobulin GProtein 70Immunoblot analysisAntigenShock proteinsSerumAntibodiesPatientsIllnessIgG
1994
Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
Craig E, Weissman J, Horwich A. Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell. Cell 1994, 78: 365-372. PMID: 7914834, DOI: 10.1016/0092-8674(94)90416-2.Peer-Reviewed Original Research
1992
Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60
Martin J, Horwich A, Hartl F. Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60. Science 1992, 258: 995-998. PMID: 1359644, DOI: 10.1126/science.1359644.Peer-Reviewed Original ResearchConceptsDihydrofolate reductaseShock proteinsMitochondrial heat shock protein 60Native dihydrofolate reductaseHeat shock proteinsVariety of polypeptidesPreexisting proteinsChaperonin Hsp60Hsp60 familyEnvironmental stressHeat shock protein 60Shock protein 60Stress conditionsHeat stressProteinGeneral mechanismPhysiological responsesProtein 60HSP60Cellular structureThermal denaturationProtein denaturationOrganellesDenaturationRefoldingInduction and intracellular localization of HSP-72 after renal ischemia
Van Why S, Hildebrandt F, Ardito T, Mann A, Siegel N, Kashgarian M. Induction and intracellular localization of HSP-72 after renal ischemia. American Journal Of Physiology 1992, 263: f769-f775. PMID: 1443167, DOI: 10.1152/ajprenal.1992.263.5.f769.Peer-Reviewed Original ResearchConceptsHSP 72Renal ischemiaHeat shock proteinsIschemic renal injuryMin of reperfusionProtein elaborationHSP mRNA expressionHSP-70 mRNARenal injuryIschemic injuryTransient ischemiaProximal tubulesIschemiaRat kidneyMRNA expressionIntracellular localizationMRNA inductionInjuryTubule morphologyImmunofluorescent localizationShock proteinsVesicular patternCellular recoveryHSP proteinsCellular remodelingGamma delta T-cell receptor repertoire in acute multiple sclerosis lesions.
Wucherpfennig KW, Newcombe J, Li H, Keddy C, Cuzner ML, Hafler DA. Gamma delta T-cell receptor repertoire in acute multiple sclerosis lesions. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 4588-4592. PMID: 1374907, PMCID: PMC49128, DOI: 10.1073/pnas.89.10.4588.Peer-Reviewed Original ResearchConceptsGamma delta T cellsDelta T cellsT cellsMultiple sclerosisMS plaquesCentral nervous system inflammatory processesAcute multiple sclerosis lesionsT cell receptor repertoireGamma delta T-cell receptor repertoireHeat shock proteinsAcute MS plaquesMS plaque tissueNormal CNS tissueDistinct lymphocyte populationsT cell populationsMultiple sclerosis lesionsShock proteinsAcute plaquesReactive astrocytesLymphocyte populationsInflammatory processFoamy macrophagesCNS tissueInflammatory sitesQuantitative immunohistochemistry
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