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
2020
Discernment between candidate mechanisms for KRAS G13D colorectal cancer sensitivity to EGFR inhibitors
McFall T, Schomburg N, Rossman K, Stites E. Discernment between candidate mechanisms for KRAS G13D colorectal cancer sensitivity to EGFR inhibitors. Cell Communication And Signaling 2020, 18: 179. PMID: 33153459, PMCID: PMC7643456, DOI: 10.1186/s12964-020-00645-3.Peer-Reviewed Original ResearchConceptsKRAS mutationsKRAS G13DEGFR inhibitorsColorectal cancerSensitivity to EGFR inhibitorsRas-GTP levelsSensitivity to cetuximabClinical trial evidenceWild-type RasGTPase activityKRAS G13D mutationBind NF1Tumor suppressor NF1EGFR inhibitionG13D mutationKRASCetuximabBiophysical studiesTrial evidenceG13DWild-typeNF1MutationsCellular modelEGFRChaperonin-assisted protein folding: a chronologue
Horwich AL, Fenton WA. Chaperonin-assisted protein folding: a chronologue. Quarterly Reviews Of Biophysics 2020, 53: e4. PMID: 32070442, DOI: 10.1017/s0033583519000143.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsCarbon DioxideChaperoninsCytosolDimerizationHeat-Shock ProteinsHumansHydrophobic and Hydrophilic InteractionsKineticsMiceMitochondriaMutationNeurosporaProtein ConformationProtein DenaturationProtein FoldingRibonuclease, PancreaticRibulose-Bisphosphate CarboxylaseSurface PropertiesTemperatureConceptsProtein foldingProtein assembliesBiophysical studiesChaperoninFoldingATPPhysiologyBiochemicalAssemblyCellsVivoDiscovery
2019
Engineering Lipid Membranes with Programmable DNA Nanostructures
Shen Q, Grome MW, Yang Y, Lin C. Engineering Lipid Membranes with Programmable DNA Nanostructures. Advanced Biology 2019, 4 PMID: 31934608, PMCID: PMC6957268, DOI: 10.1002/adbi.201900215.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsDNA nanostructuresProgrammable DNA nanostructuresGenetic informationLipid membranesCell's genetic informationAmphipathic lipid moleculesLipid/DNA complexesSelf-assembling capabilitiesDNA-based toolsQuantitative biophysical studiesNanoscopic precisionProgrammable nanostructuresControllable structureHybrid materialsChromatin structureGene therapyNanostructuresDistant moleculesSynthetic biologyAbundant biomoleculesLipid moleculesBiophysical studiesDNA complexesExcellent materialCell nucleiStructural Characterization of Arabidopsis thaliana NAP1-Related Protein 2 (AtNRP2) and Comparison with Its Homolog AtNRP1
Kumar A, Singh A, Bobde R, Vasudevan D. Structural Characterization of Arabidopsis thaliana NAP1-Related Protein 2 (AtNRP2) and Comparison with Its Homolog AtNRP1. Molecules 2019, 24: 2258. PMID: 31213016, PMCID: PMC6630525, DOI: 10.3390/molecules24122258.Peer-Reviewed Original ResearchConceptsNucleosome assembly proteinHistone chaperonesFamily proteinsNAP familyIsothermal titration calorimetry experimentsTitration calorimetry experimentsAssembly proteinOligomerization statusPlant tissuesSequence identityDimerization helixSimilar foldSimilar proteinsBiophysical studiesSpecific functionsStructural superpositionProtein 2ProteinPlantsChaperonesElectrophoretic mobilityStructural studiesCrystal structureThermal melting experimentsStructural architecture
2017
Reversible stacking of lipid nanodiscs for structural studies of clotting factors
Grushin K, White M, Stoilova-McPhie S. Reversible stacking of lipid nanodiscs for structural studies of clotting factors. Nanotechnology Reviews 2017, 6: 139-148. DOI: 10.1515/ntrev-2016-0073.Peer-Reviewed Original ResearchMembrane scaffold proteinND populationMembrane-associated proteinsDifferent membrane scaffold proteinsSize of nanodiscsDiscoidal phospholipid bilayerLipid nanodiscsLipid ratioCryo-EMBiophysical studiesMacromolecular compositionFunctional studiesNanodiscsLipid compositionStructural studiesPhospholipid bilayersProteinMillimolar concentrationsCa2Lipid mixturesMSP1D1ND formMicroscopy studiesElectron microscopy studiesPopulation
2014
A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion
Li F, Kümmel D, Coleman J, Reinisch KM, Rothman JE, Pincet F. A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion. Journal Of The American Chemical Society 2014, 136: 3456-3464. PMID: 24533674, PMCID: PMC3985920, DOI: 10.1021/ja410690m.Peer-Reviewed Original ResearchConceptsN-terminal domainMembrane fusionV-SNARET-SNAREsRecent biophysical studiesC-terminal portionSNARE complexTransmembrane domainRegulatory proteinsFunctional intermediatesC-terminusDistinct functionsN-terminusMolecular mechanismsConformational rearrangementsBiophysical studiesVital regulatorZippering mechanismRate-limiting stepBiological membranesSnareFusionComplexinMultiple stagesZippering
2013
How do transporters couple solute movements?
Rudnick G. How do transporters couple solute movements? Molecular Membrane Biology 2013, 30: 355-359. PMID: 24147977, PMCID: PMC4077868, DOI: 10.3109/09687688.2013.842658.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
2002
Water oxidation chemistry of photosystem II
Vrettos J, Brudvig G. Water oxidation chemistry of photosystem II. Philosophical Transactions Of The Royal Society B Biological Sciences 2002, 357: 1395-1405. PMID: 12437878, PMCID: PMC1693042, DOI: 10.1098/rstb.2002.1136.Peer-Reviewed Original ResearchConceptsManganese clusterProton-coupled electron transfer stepsO bond-forming stepPhotosystem IIWater oxidation chemistryBond-forming stepElectron transfer stepFour-electron oxidationTetranuclear manganese clusterOxidation chemistryWater moleculesModel chemistryO bondNucleophilic attackIon selectivityBiophysical studiesChemistryCalcium sitesOxidationSpecific roleModel systemComplexesHis190Recent studiesWater
2001
Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry
Vrettos J, Limburg J, Brudvig G. Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry. Biochimica Et Biophysica Acta 2001, 1503: 229-245. PMID: 11115636, DOI: 10.1016/s0005-2728(00)00214-0.Peer-Reviewed Original ResearchMeSH KeywordsCrystallographyElectron TransportHemerythrinHydrogen-Ion ConcentrationKineticsManganeseModels, ChemicalModels, MolecularOrganometallic CompoundsOxidation-ReductionOxygenPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtonsThylakoidsTyrosineWaterConceptsPhotosynthetic water oxidationWater oxidationOxygen-evolving complexProton-coupled electron transferTetranuclear manganese clusterMu-oxo bridgePhotosystem IIReduction of manganeseOOH speciesWater moleculesElectron transferModel chemistryManganese clusterNucleophilic attackDiferric siteFerric hydroperoxideOxidationD1 polypeptideBiophysical studiesOxyhemerythrinBiophysical resultsStructural modelDioxygenChemistryProtonation
1997
A Biophysical Study of Integral Membrane Protein Folding †
Hunt J, Earnest T, Bousché O, Kalghatgi K, Reilly K, Horváth C, Rothschild K, Engelman D. A Biophysical Study of Integral Membrane Protein Folding †. Biochemistry 1997, 36: 15156-15176. PMID: 9398244, DOI: 10.1021/bi970146j.Peer-Reviewed Original ResearchConceptsAlpha-helical integral membrane proteinsIntegral membrane proteinsMembrane proteinsIntegral membrane protein foldingMembrane protein foldingNon-native conformationsStable secondary structureCellular chaperonesBiophysical dissectionBeta-sheet structureProtein foldingIndividual polypeptidesBiophysical studiesStructure of bacteriorhodopsinTertiary structureSecondary structureReconstitution protocolsG helicesPolypeptideF helixProteinPhospholipid vesiclesHelixFoldingBacteriorhodopsin
1995
High-valent oxomanganese clusters: structural and mechanistic work relevant to the oxygen-evolving center in photosystem II
Manchanda R, Brudvig G, Crabtree R. High-valent oxomanganese clusters: structural and mechanistic work relevant to the oxygen-evolving center in photosystem II. Coordination Chemistry Reviews 1995, 144: 1-38. DOI: 10.1016/0010-8545(95)01147-h.Peer-Reviewed Original ResearchO2-evolving centerActive siteOxygen-evolving centerPhotosystem IIOxomanganese clusterBioinorganic chemistryInorganic chemistsWater oxidationComplex chemistryMechanistic aspectsBiophysical studiesChemistryMagnetic propertiesNative enzymeMechanistic workPS IINuclearityChemistsMetalloproteinsSuch clustersConsiderable interestOxidationRecent effortsChemicalsTetramer
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