2010
Spatial control of EGF receptor activation by reversible dimerization on living cells
Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464: 783-787. PMID: 20208517, DOI: 10.1038/nature08827.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell Line, TumorCell PolarityCell SurvivalCHO CellsCricetinaeCricetulusDiffusionEnzyme ActivationEnzyme StabilityEpidermal Growth FactorErbB ReceptorsGene Expression RegulationGRB2 Adaptor ProteinHumansKineticsLigandsProtein MultimerizationProtein TransportSignal TransductionThermodynamicsConceptsLigand bindingEpidermal growth factor receptor moleculeType I receptor kinaseEGF receptor activationDimer formationReceptor kinaseReceptor dimerizationDimerization dynamicsReceptor dimersLiving cellsReceptor moleculesCell marginsDimer populationSpatial controlHuman carcinomasConformation changeDimerizationCell centerReceptor activationRate of dissociationCellsBindingActivationKinaseReversible dimerization
2000
Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers
De La Cruz E, Ostap E, Brundage R, Reddy K, Sweeney H, Safer D. Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers. Biophysical Journal 2000, 78: 2516-2527. PMID: 10777749, PMCID: PMC1300842, DOI: 10.1016/s0006-3495(00)76797-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBiophysical PhenomenaBiophysicsCircular DichroismCross-Linking ReagentsFluorescent DyesHumansIn Vitro TechniquesKineticsMacromolecular SubstancesModels, MolecularMuscle, SkeletalMutagenesis, Site-DirectedNaphthalenesulfonatesOsmotic PressureProtein BindingProtein ConformationRabbitsRecombinant ProteinsThermodynamicsThymosinTritiumViscosityConceptsActin monomersActin monomer poolMgATP-actinMetazoan cellsNucleotide exchangeC-terminusSubdomain 2Conformational changesMonomer poolN-iodoacetyl-N'Cleavage siteActinThymosin β4Rate of dissociationAmide protonsSulfo-1Unique abilityBindingStructural dynamicsConformationTerminusNucleotidesProteolysisDifferent stabilitiesDegrees C5-Iodo-A-85380, an α4β2 Subtype-Selective Ligand for Nicotinic Acetylcholine Receptors 1
Mukhin A, Gündisch D, Horti A, Koren A, Tamagnan G, Kimes A, Chambers J, Vaupel D, King S, Picciotto M, Innis R, London E. 5-Iodo-A-85380, an α4β2 Subtype-Selective Ligand for Nicotinic Acetylcholine Receptors 1. Molecular Pharmacology 2000, 57: 642-649. DOI: 10.1016/s0026-895x(24)26432-4.Peer-Reviewed Original ResearchAffinity of epibatidineMuscle-type nAChRsBinding to nAChRsSlow rate of dissociationRate of dissociationReceptor-ligand complexesNeuronal nicotinic acetylcholine receptorsSubtype-selective ligandsNAChR subtypesEpibatidineA4B2K d valuesNicotinic acetylcholine receptorsNAChRsSubunits of nAChRsRat adrenal glandAffinityBrain regionsLigandDissociationCompoundsBindingAcetylcholine receptorsIn vivo studiesHuman brain
1997
RecA tests homology at both pairing and strand exchange
Bazemore L, Folta-Stogniew E, Takahashi M, Radding C. RecA tests homology at both pairing and strand exchange. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11863-11868. PMID: 9342328, PMCID: PMC23638, DOI: 10.1073/pnas.94.22.11863.Peer-Reviewed Original Research
1978
Energy-dependence of phlorizin binding to isolated renal microvillus membranes
Aronson P. Energy-dependence of phlorizin binding to isolated renal microvillus membranes. The Journal Of Membrane Biology 1978, 42: 81-98. PMID: 671529, DOI: 10.1007/bf01870395.Peer-Reviewed Original Research
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