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Sandra N. Pinto

Researcher at Instituto Superior Técnico

Publications -  51
Citations -  980

Sandra N. Pinto is an academic researcher from Instituto Superior Técnico. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 15, co-authored 35 publications receiving 715 citations. Previous affiliations of Sandra N. Pinto include Technical University of Lisbon & Instituto de Medicina Molecular.

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Journal ArticleDOI

Effect of ceramide structure on membrane biophysical properties: the role of acyl chain length and unsaturation.

TL;DR: The results suggest that generation of different ceramide species in cell membranes has a distinct biophysical impact with acyl chain saturation dictating membrane lateral organization, and chain asymmetry governing interdigitation and membrane morphology.
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Membrane Domain Formation, Interdigitation, and Morphological Alterations Induced by the Very Long Chain Asymmetric C24:1 Ceramide

TL;DR: The application of an established fluorescence multiprobe approach, together with x-ray diffraction, differential scanning calorimetry, and confocal fluorescence microscopy, allowed the characterization of NCer and the determination of the phase diagram of palmitoyloleoylphosphatidylcholine (POPC)/NCer binary mixtures.
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A V-shaped cationic dye for nonlinear optical bioimaging

TL;DR: Fluorescence lifetime imaging microscopy shows that the synthesized symmetric cationic molecule with D-π-A(+)-π-D architecture is also able to penetrate within the nucleus.
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Changes in membrane biophysical properties induced by sphingomyelinase depend on the sphingolipid N-acyl chain.

TL;DR: The results show an increase in the order of cellular membranes in CerS2-transfected cells caused by the enrichment in very long acyl chain SLs, which reinforces the significance of Cer-induced changes on membrane biophysical properties as a likely molecular mechanism by which different acylChain Cers exert their specific biological actions.
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A combined fluorescence spectroscopy, confocal and 2-photon microscopy approach to re-evaluate the properties of sphingolipid domains.

TL;DR: The results suggest that in biological membranes, lipid domains such as rafts and ceramide platforms, might display distinctive biophysical properties depending on the local lipid composition at the site of the membrane where they are formed, further highlighting the potential role of membraneBiophysical properties as an underlying mechanism for mediating specific biological processes.