2024
Phosphoglycerate kinase is a central leverage point in Parkinson’s disease–driven neuronal metabolic deficits
Kokotos A, Antoniazzi A, Unda S, Ko M, Park D, Eliezer D, Kaplitt M, De Camilli P, Ryan T. Phosphoglycerate kinase is a central leverage point in Parkinson’s disease–driven neuronal metabolic deficits. Science Advances 2024, 10: eadn6016. PMID: 39167658, PMCID: PMC11338267, DOI: 10.1126/sciadv.adn6016.Peer-Reviewed Original ResearchConceptsPhosphoglycerate kinase 1Metabolic deficitsExpressions of Phosphoglycerate Kinase 1Dopamine axonsParkinson's diseasePD-associated pathologyViral expressionLoss of functionNeuronal glycolysisSusceptibility lociIn vivoFamilial Parkinson's diseasePD therapeuticsMetabolic lesionsProduction kineticsKinase 1Mitochondrial integrityPhosphoglycerate kinaseBioenergetic deficitsSynaptic dysfunctionGenetic originDeficitsPARK7/DJ-1Phosphoglycerate
2020
Cytoskeletal Drugs Modulate Off-Target Protein Folding Landscapes Inside Cells
Davis CM, Gruebele M. Cytoskeletal Drugs Modulate Off-Target Protein Folding Landscapes Inside Cells. Biochemistry 2020, 59: 2650-2659. PMID: 32567840, DOI: 10.1021/acs.biochem.0c00299.Peer-Reviewed Original ResearchConceptsCytoskeletal drugsPhosphoglycerate kinaseActin filamentsDynamic cytoskeletal networksEffects of cytoskeletonProtein energy landscapesOff-target proteinsOpposite responseCytoskeletal networkProtein stabilityCellular milieuProtein-like sequencesVariable major protein-like sequenceOverall cell volumeCytoskeletonCell migrationEnergy landscapeMacromolecular crowdingMacromolecular crowdersProteinNonspecific surface interactionsTarget effectsMicrotubulesCytoplasmCellsAn in vitro mimic of in‐cell solvation for protein folding studies
Davis CM, Deutsch J, Gruebele M. An in vitro mimic of in‐cell solvation for protein folding studies. Protein Science 2020, 29: 1046-1054. PMID: 31994240, PMCID: PMC7096716, DOI: 10.1002/pro.3833.Peer-Reviewed Original ResearchConceptsPhosphoglycerate kinaseLysis bufferCytoplasmic protein interactionsSignificant nonadditive effectsVariety of proteinsProtein folding studiesEukaryotic cellsProtein foldingProtein interactionsCellular crowdingProtein-like sequencesEffect of FicollFolding studiesHydrophobic patchVariable major protein-like sequenceNonadditive effectsCellular effectsProteinCell environmentInert macromoleculesBiomolecular interactionsCellsTest tubeSmall crowdersMimics
1979
Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.
Pickover C, McKay D, Engelman D, Steitz T. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. Journal Of Biological Chemistry 1979, 254: 11323-11329. PMID: 387770, DOI: 10.1016/s0021-9258(19)86488-8.Peer-Reviewed Original ResearchConceptsYeast phosphoglycerate kinasePhosphoglycerate kinaseConformational changesTernary complexSubstrate bindingHinge motionKinaseSubstrate MgATPCleft closureSmall-angle X-raySeparate bindingRadius of gyrationAngle X-rayMgATPBindingApparent similarityComplexesCleftEnzymeObserved changesHexokinaseGyration decreasesDomainSimilarity
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