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
Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109
Singh B, Cheppali S, Saha I, Swamy M. Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109. International Journal Of Biological Macromolecules 2023, 254: 127573. PMID: 37923045, DOI: 10.1016/j.ijbiomac.2023.127573.Peer-Reviewed Original ResearchConceptsChaperone-like activityPDC-109Effects of molecular crowdingMembrane destabilizationMolecular crowdingBovine seminal plasma proteinSperm cell surfaceSeminal plasma proteinsBovine seminal plasmaAcrosome reactionClient proteinsProtein stabilityMicroenvironment of proteinsSeminal plasmaMembrane-perturbingProtein oligomersReduced surface hydrophobicityOligomeric proteinsLipid effluxCell surfaceCrowding agentsProteinIsothermal titration calorimetric studiesTitration calorimetric studiesFunctional activity
2017
Phase Ib study of heat shock protein 90 inhibitor, onalespib in combination with paclitaxel in patients with advanced, triple-negative breast cancer (NCT02474173).
Wesolowski R, Lustberg M, Reinbolt R, VanDeusen J, Sardesai S, Williams N, Noonan A, Dewani S, Poi M, Wilson D, Grever M, Stephens J, Puhalla S, Mathew A, Carson W, Ramaswamy B. Phase Ib study of heat shock protein 90 inhibitor, onalespib in combination with paclitaxel in patients with advanced, triple-negative breast cancer (NCT02474173). Journal Of Clinical Oncology 2017, 35: tps1127-tps1127. DOI: 10.1200/jco.2017.35.15_suppl.tps1127.Peer-Reviewed Original ResearchTriple-negative breast cancerBreast cancerDay 1Hormone receptor-positive breast cancerReceptor-positive breast cancerPhase Ib studyPhase II doseProgression-free survivalPositive breast cancerOverall response rateHeat shock protein 90 inhibitorNegative breast cancerCycle 1Shock protein 90 inhibitorsPoor outcomeStandard doseAndrogen receptorHsp90 client proteinsHeat shock protein 90Ib studyResponse durationToxicity profilePaclitaxel resistanceClient proteinsDay 7
2015
Translational Downregulation of HSP90 Expression by Iron Chelators in Neuroblastoma Cells
Sidarovich V, Adami V, Gatto P, Greco V, Tebaldi T, Tonini GP, Quattrone A. Translational Downregulation of HSP90 Expression by Iron Chelators in Neuroblastoma Cells. Molecular Pharmacology 2015, 87: 513-524. PMID: 25564462, DOI: 10.1124/mol.114.095729.Peer-Reviewed Original ResearchConceptsTranslational downregulationHeat shock protein groupIntracellular ironIron chelatorsG0/G1 cell cycle blockCell linesG1 cell cycle blockCombined transcriptomeInduction of apoptosisTranslatome profilingClient proteinsCell cycle blockCell viabilityInvestigational antitumor agentNB cell linesCellular nutrientsHsp90 inhibitionNeuroblastoma cell linesProtein groupsCPX treatmentCell growthNB therapyAchievable concentrationsCycle blockInhibition of growth
2012
Identification of CSPα Clients Reveals a Role in Dynamin 1 Regulation
Zhang YQ, Henderson MX, Colangelo CM, Ginsberg SD, Bruce C, Wu T, Chandra SS. Identification of CSPα Clients Reveals a Role in Dynamin 1 Regulation. Neuron 2012, 74: 136-150. PMID: 22500636, PMCID: PMC3328141, DOI: 10.1016/j.neuron.2012.01.029.Peer-Reviewed Original ResearchConceptsProtein clientsDynamin 1T-SNARE SNAP-25Cysteine string protein αSynaptic vesicle endocytosisSynaptic vesicle fusionChaperone complexClient proteinsVesicle endocytosisSystematic proteomicsSynaptic vesicle numberSuch proteinsCSPαVesicle fusionSNAP-25Synapse maintenanceProtein αVesicle numberProteinNeuronal dysfunctionCochaperonesHsc70ProteomicsEndocytosisHippocampal cultures
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