2025
Heme promotes venetoclax resistance in multiple myeloma through MEK-ERK signaling and purine biosynthesis
Nair R, Vu A, Freer A, Bhatia K, Wang D, Savani M, Matulis S, Lonial S, Jaye D, Boise L, Seo S, Corson T, Nooka A, Bhatt S, McBrayer S, Gupta V, Hu X, Barwick B, Reddi A, Shanmugam M. Heme promotes venetoclax resistance in multiple myeloma through MEK-ERK signaling and purine biosynthesis. Blood 2025, 145: 732-747. PMID: 39693611, PMCID: PMC12060166, DOI: 10.1182/blood.2024025690.Peer-Reviewed Original ResearchConceptsElectron transport chainBcl-2Heme biosynthesisBCL-2 antagonismElectron transport chain activityIron-containing prosthetic groupMultiple myelomaB-cell lymphoma 2MEK-ERK signalingGene signatureActivation of prosurvivalApoptotic thresholdPurine biosynthesisPenultimate enzymePyrimidine biosynthesisMetabolic rewiringTransport chainProtein kinaseMultiple Myeloma Research Foundation CoMMpass studyBiosynthesisPurine synthesisGenetic profilePrimary MM cellsProsthetic groupProgression-free survival
2024
Comparative Kidney Uptake of Nanobody-Based PET Tracers Labeled with Various Fluorine-18-Labeled Prosthetic Groups
Olkowski C, Basuli F, Fernandes B, Ghaemi B, Shi J, Zhang H, Farber J, Escorcia F, Choyke P, Jacobson O. Comparative Kidney Uptake of Nanobody-Based PET Tracers Labeled with Various Fluorine-18-Labeled Prosthetic Groups. Molecular Pharmaceutics 2024, 22: 533-543. PMID: 39680709, DOI: 10.1021/acs.molpharmaceut.4c01101.Peer-Reviewed Original Research
2017
Stilbene epoxidation and detoxification in a Photorhabdus luminescens-nematode symbiosis
Park HB, Sampathkumar P, Perez CE, Lee JH, Tran J, Bonanno JB, Hallem EA, Almo SC, Crawford JM. Stilbene epoxidation and detoxification in a Photorhabdus luminescens-nematode symbiosis. Journal Of Biological Chemistry 2017, 292: 6680-6694. PMID: 28246174, PMCID: PMC5399116, DOI: 10.1074/jbc.m116.762542.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Infective AgentsBiological ProductsCatalysisChromatography, High Pressure LiquidCrystallography, X-RayDNA Mutational AnalysisEpoxy CompoundsGene DeletionHydrogen BondingHydrophobic and Hydrophilic InteractionsImmunosuppressive AgentsMagnetic Resonance SpectroscopyMolecular ConformationMutationPhotorhabdusProtein FoldingRhabditoideaStereoisomerismStilbenesSymbiosisConceptsFood signalsInsect infection modelFAD-dependent monooxygenasesFAD prosthetic groupOrphan proteinsInsect larvaeMutualistic relationshipEpoxidase geneNematode developmentCellular detoxificationBiological roleProsthetic groupIntracellular detoxificationAnimal infection modelsInfection modelBiochemical analysisChemical degradation studiesStructural viewNematodesDetoxificationNew insightsCompound 1Major componentNew stilbeneRecovery assays
2014
Radiolabeling of Poly(lactic-co-glycolic acid) (PLGA) Nanoparticles with Biotinylated F‑18 Prosthetic Groups and Imaging of Their Delivery to the Brain with Positron Emission Tomography
Sirianni RW, Zheng MQ, Patel TR, Shafbauer T, Zhou J, Saltzman WM, Carson RE, Huang Y. Radiolabeling of Poly(lactic-co-glycolic acid) (PLGA) Nanoparticles with Biotinylated F‑18 Prosthetic Groups and Imaging of Their Delivery to the Brain with Positron Emission Tomography. Bioconjugate Chemistry 2014, 25: 2157-2165. PMID: 25322194, PMCID: PMC4275164, DOI: 10.1021/bc500315j.Peer-Reviewed Original ResearchConceptsDetection of avidinFate of nanoparticlesAvidin-biotin interactionProsthetic groupNanoparticle deliveryPolymer nanoparticlesNanoparticlesBiotinylated moleculesNoncovalent linkageConvection-enhanced deliveryAvailable biotinHigh purityAvidinBiotinDeliveryFluorobenzylamineSpecific activityFunction of timeMoleculesDerivativesPositron emission tomographySubstratePurityDirect observationKinetics
2000
HELICAL MEMBRANE PROTEIN FOLDING, STABILITY, AND EVOLUTION
Popot J, Engelman D. HELICAL MEMBRANE PROTEIN FOLDING, STABILITY, AND EVOLUTION. Annual Review Of Biochemistry 2000, 69: 881-922. PMID: 10966478, DOI: 10.1146/annurev.biochem.69.1.881.Peer-Reviewed Original Research
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. Quarterly Reviews Of Biophysics 1994, 27: 157-218. PMID: 7984776, DOI: 10.1017/s0033583500004522.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsTransmembrane α-helicesMembrane proteinsΑ-helixMembrane protein foldingMembrane-spanning portionTransmembrane helix associationHelix-helix interactionsParticular helicesProtein foldingHelix associationHelix interactionsProsthetic groupLipid bilayersCharge-charge interactionsStereochemical fitFoldingProteinAccessible statesSpecificityOligomerizationInteractionPromiscuityHelixAssembly
1984
Neutron Diffraction Studies of Bacteriorhodopsin Structure
Trewhella J, Gogol E, Zaccai G, Engelman D. Neutron Diffraction Studies of Bacteriorhodopsin Structure. Basic Life Sciences 1984, 227-246. DOI: 10.1007/978-1-4899-0375-4_14.Peer-Reviewed Original ResearchPlasma membraneSingle protein speciesVertebrate visual pigmentsProtein speciesPurple membraneMembrane bilayerBacteriorhodopsin structureSpecialized membraneProsthetic groupElectrochemical gradientSpecialized regionsStrong pigmentationDiffraction studiesVisual pigmentsHalobacterium halobiumX-ray diffraction studiesVisible light energyLight energyMembraneRetinal prosthetic groupLow ionic strengthSpace group P3Packing arrangementIonic strengthBacteriorhodopsin
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply