2014
MicroRNA silencing for cancer therapy targeted to the tumour microenvironment
Cheng CJ, Bahal R, Babar IA, Pincus Z, Barrera F, Liu C, Svoronos A, Braddock DT, Glazer PM, Engelman DM, Saltzman WM, Slack FJ. MicroRNA silencing for cancer therapy targeted to the tumour microenvironment. Nature 2014, 518: 107-110. PMID: 25409146, PMCID: PMC4367962, DOI: 10.1038/nature13905.Peer-Reviewed Original Research
2000
Biophysical Characterization of gp41 Aggregates Suggests a Model for the Molecular Mechanism of HIV-associated Neurological Damage and Dementia*
Caffrey M, Braddock D, Louis J, Abu-Asab M, Kingma D, Liotta L, Tsokos M, Tresser N, Pannell L, Watts N, Steven A, Simon M, Stahl S, Wingfield P, Clore G. Biophysical Characterization of gp41 Aggregates Suggests a Model for the Molecular Mechanism of HIV-associated Neurological Damage and Dementia*. Journal Of Biological Chemistry 2000, 275: 19877-19882. PMID: 10747981, DOI: 10.1074/jbc.m001036200.Peer-Reviewed Original ResearchMeSH KeywordsAIDS Dementia ComplexBrainBrain DiseasesChromatography, GelEndopeptidasesExtracellular SpaceHIV Envelope Protein gp41HIV SeropositivityHumansHydrogen-Ion ConcentrationImmunohistochemistryMembrane GlycoproteinsMicroscopy, ElectronProtein BindingProtein Structure, TertiaryRetroviridae ProteinsConceptsNeurological damageBrains of HIVHuman immunodeficiency virusImmunodeficiency virusEnvelope protein gp41HIVBrain tissueDementiaHigh molecular weight formExtracellular aggregatesMolecular weight formsSimian immunodeficiency virus gp41Gp41Molecular mechanismsWeight formsHIV gp41HIV envelope protein gp41Extracellular ectodomainBiochemical methodsDamagePatientsImmunohistochemistryHigh molecular weight aggregatesBrain
1994
Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein E: side-chain lactam bridges to constrain the conformation.
Luo P, Braddock D, Subramanian R, Meredith S, Lynn D. Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein E: side-chain lactam bridges to constrain the conformation. Biochemistry 1994, 33: 12367-77. PMID: 7918459, DOI: 10.1021/bi00207a003.Peer-Reviewed Original ResearchConceptsSide-chain lactam bridgePeptide modelsAlpha-helical peptidesLoss of entropyModel peptidesBioactive structuresNMR dataAlpha-helical structureLactam constraintsConformational flexibilityLactam bridgeKcal/Thermodynamic characterizationAlpha-helical domainBiological activityPlasma lipoprotein clearanceUnfolded stateCell surface receptorsBiological functionsPeptidesSurface receptorsStructureResiduesCentral bendCritical role