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2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activitiesQuantitative determination of ion distributions in bacterial lipopolysaccharide membranes by grazing-incidence X-ray fluorescenceBiochemical and structural information transduction at the mesoscopic level in biointerfaces containing sphingolipids.Composition-driven surface domain structuring mediated by sphingolipids and membrane-active proteins. Above the nano- but under the micro-scale: mesoscopic biochemical/structural cross-talk in biomembranes.The self-organization of lipids and proteins of myelin at the membrane interface. Molecular factors underlying the microheterogeneity of domain segregation.The action of sphingomyelinase in lipid monolayers as revealed by microscopic image analysis.The Single Transmembrane Segment of Minimal Sensor DesK Senses Temperature via a Membrane-Thickness CaliperBidirectional control of sphingomyelinase activity and surface topography in lipid monolayers.Cooling induces phase separation in membranes derived from isolated CNS myelin.Equivalent aqueous phase modulation of domain segregation in myelin monolayers and bilayer vesicles.Crucial roles of charged saccharide moieties in survival of gram negative bacteria against protamine revealed by combination of grazing incidence x-ray structural characterizations and Monte Carlo simulations.Compositional domain immiscibility in whole myelin monolayers at the air-water interface and Langmuir-Blodgett films.Surface behavior, microheterogeneity and adsorption equilibrium of myelin at the air-water interface.Ascorbyl palmitate interaction with phospholipid monolayers: electrostatic and rheological preponderancy.Many length scales surface fractality in monomolecular films of whole myelin lipids and proteins.Effect of molecular surface packing on the enzymatic activity modulation of an anchored protein on phospholipid Langmuir monolayers.Mechanical properties of interacting lipopolysaccharide membranes from bacteria mutants studied by specular and off-specular neutron scattering.Hexagonal phase with ordered acyl chains formed by a short chain asymmetric ceramide.CNS myelin structural modification induced in vitro by phospholipases A2.Rheological properties of regular insulin and aspart insulin Langmuir monolayers at the air/water interface: condensing effect of Zn2+ in the subphase.Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers.The Folch–Lees proteolipid induces phase coexistence and transverse reorganization of lateral domains in myelin monolayersInterfacial behavior of glycosphingolipids and chemically related sphingolipidsReflectance and Topography of Glycosphingolipid Monolayers at the Air−Water InterfaceModulation of intermembrane interaction and bending rigidity of biomembrane models via carbohydrates investigated by specular and off-specular neutron scatteringPhysical mechanisms of bacterial survival revealed by combined grazing-incidence X-ray scattering and Monte Carlo simulationRefractive index and thickness determination in Langmuir monolayers of myelin lipidsCharacterization of a Pt mirror to be used to deflect synchrotron radiation beam onto Langmuir monolayersAggregation behaviour and solubilization capability of mixed micellar systems formed by a gemini lipoamino acid and a non-ionic surfactantImproved stability in SBA-15 mesoporous materials as catalysts for photo-degradation processesSurface interactions, thermodynamics and topography of binary monolayers of Insulin with dipalmitoylphosphatidylcholine and 1-palmitoyl-2-oleoylphosphatidylcholine at the air/water interfaceEpifluorescence microscopy of surface domain microheterogeneity in myelin monolayers at the air-water interfaceIncreased velocity and induction of chemotactic response in mouse spermatozoa by follicular and oviductal fluidsSurface behavior of myelin monolayersPhase Diagram of Purified CNS Myelin Reveals Continuous Transformation between Expanded and Compacted Lamellar States
P50
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P50
description
researcher ORCID ID = 0000-0001-5948-5338
@en
wetenschapper
@nl
name
Rafael G Oliveira
@ast
Rafael G Oliveira
@en
Rafael G Oliveira
@es
Rafael G Oliveira
@nl
type
label
Rafael G Oliveira
@ast
Rafael G Oliveira
@en
Rafael G Oliveira
@es
Rafael G Oliveira
@nl
prefLabel
Rafael G Oliveira
@ast
Rafael G Oliveira
@en
Rafael G Oliveira
@es
Rafael G Oliveira
@nl
P106
P1153
7101765930
P21
P31
P496
0000-0001-5948-5338