Search Results - "Mesa‐Galloso, Haydeé"
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Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore‐forming activity
Published in Protein science (01-03-2017)“…Crystallographic data of the dimeric and octameric forms of fragaceatoxin C (FraC) suggested the key role of a small hydrophobic protein–protein interaction…”
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Lipid regulation of hERG1 channel function
Published in Nature communications (03-03-2021)“…The lipid regulation of mammalian ion channel function has emerged as a fundamental mechanism in the control of electrical signalling and transport specificity…”
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Emerging Diversity in Lipid–Protein Interactions
Published in Chemical reviews (08-05-2019)“…Membrane lipids interact with proteins in a variety of ways, ranging from providing a stable membrane environment for proteins to being embedded in to detailed…”
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Pore-forming proteins: From defense factors to endogenous executors of cell death
Published in Chemistry and physics of lipids (01-01-2021)“…•PFPs are fundamental defense and virulence factors in bacteria and as executors of regulated cell death in eukaryotic cells.•Proteins and lipids cooperate to…”
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Cardiomyocyte sarcolemma modelling and lipid-protein interactions
Published in Biophysical journal (10-02-2023)Get full text
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Molecular Mechanism of hERG1 Channel Regulation by Ceramides
Published in Biophysical journal (12-02-2021)Get full text
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Molecular Mechanisms of Human ERG1 Channel Blockade by Ceramides
Published in Biophysical journal (07-02-2020)Get full text
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Understanding the Pore-Forming Mechanism of Peptides Derived From the N-Terminus of Sticholysin
Published in Biophysical journal (02-02-2018)Get full text
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Lipid-Dependent Modulation of Cardiac Ion Channel Activity as an Anti-Arrhythmic Therapy in Long-QT Syndrome
Published in Biophysical journal (07-02-2020)Get full text
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Dimerization, a Key Step for Pore Formation of Fragaceatoxin C, an Actinoporin from the Sea Anemone Actinia Fragacea
Published in Biophysical journal (03-02-2017)Get full text
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Membrane Remodeling by the Lytic Fragment of SticholysinII: Implications for the Toroidal Pore Model
Published in Biophysical journal (05-11-2019)“…Sticholysins are pore-forming toxins of biomedical interest and represent a prototype of proteins acting through the formation of protein-lipid or toroidal…”
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