C. Álvarez

发表

The sticholysin family of pore-forming toxins induces the mixing of lipids in membrane domains.

R. Epand, R. Epand, C. Yip, 2013, Biochimica et biophysica acta.

Effect of pre-exposure of human erythrocytes to oxidants on the haemolytic activity of Sticholysin II. A comparison between peroxynitrite and hypochlorous acid

E. Lissi, M. E. Lanio, C. Álvarez, 2011, Free radical research.

Damage of eukaryotic cells by the pore-forming toxin sticholysin II: Consequences of the potassium efflux.

F. G. van der Goot, U. Ros, M. E. Lanio, 2017, Biochimica et biophysica acta. Biomembranes.

Overview of Marine Toxin Research in Cuba

M. E. Lanio, C. Álvarez, M. Tejuca, 2003 .

Effect of Human Serum Albumin Upon the Permeabilizing Activity of Sticholysin II, a Pore Forming Toxin from Stichodactyla heliantus

E. Lissi, M. E. Lanio, C. Álvarez, 2013, The Protein Journal.

Molecular Cloning, Characterization, and Dynamics of Rat Formiminotransferase Cyclodeaminase, a Golgi-associated 58-kDa Protein*

E. Sztul, C. Álvarez, C. Alvarez, 1998, The Journal of Biological Chemistry.

Effect of sphingomyelin and cholesterol on the interaction of St II with lipidic interfaces.

E. Lissi, J. Arrondo, I. Gutiérrez-Aguirre, 2007, Toxicon : official journal of the International Society on Toxinology.

Cell death mechanisms induced by pore forming toxins with special focus on actinoporins

M. E. Lanio, C. Álvarez, A. M. Hernández, 2021 .

Stycholysin II, a cytolysin from the sea anemone Stichodactyla helianthus promotes higher hemolysis in aged red blood cells.

E. Lissi, M. E. Lanio, C. Álvarez, 2008, Toxicon : official journal of the International Society on Toxinology.

Purification and characterization of two hemolysins from Stichodactyla helianthus.

V. Huerta, V. Besada, G. Padrón, 2001, Toxicon : official journal of the International Society on Toxinology.

Sticholysins, pore-forming proteins from a marine anemone can induce maturation of dendritic cells through a TLR4 dependent-pathway.

M. Starnbach, D. Higgins, L. E. Fernández, 2021, Molecular immunology.

The pore-forming activity of sticholysin I is enhanced by the presence of a phospholipid hydroperoxide in membrane.

R. Itri, M. E. Lanio, C. Álvarez, 2021, Toxicon : official journal of the International Society on Toxinology.

Architecture of the pore forming toxin sticholysin i in membranes.

H. Steinhoff, M. E. Lanio, C. Álvarez, 2019, Journal of Structural Biology.

Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore‐forming activity

A. García-Sáez, H. Mesa-Galloso, P. A. Valiente, 2017, Protein science : a publication of the Protein Society.

Differential binding and activity of the pore-forming toxin sticholysin II in model membranes containing diverse ceramide-derived lipids.

P. A. Valiente, U. Ros, M. E. Lanio, 2017, Biochimie.

Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone

P. A. Valiente, U. Ros, M. E. Lanio, 2017, Biophysical Reviews.

Novel Adjuvant Based on the Pore-Forming Protein Sticholysin II Encapsulated into Liposomes Effectively Enhances the Antigen-Specific CTL-Mediated Immune Response

M. Starnbach, D. Higgins, L. E. Fernández, 2017, The Journal of Immunology.

The pore forming capacity of Sticholysin I in dipalmitoyl phosphatidyl vesicles is tuned by osmotic stress.

E. Lissi, M. E. Lanio, C. Álvarez, 2017, Chemistry and physics of lipids.

The Presence of Sterols Favors Sticholysin I-Membrane Association and Pore Formation Regardless of Their Ability to Form Laterally Segregated Domains.

R. Itri, N. Wilke, U. Ros, 2015, Langmuir : the ACS journal of surfaces and colloids.

Inactivation of the Pore-Forming Toxin Sticholysin I by Peroxynitrite: Protection by Cys Groups Incorporated in the Toxin

E. Lissi, M. E. Lanio, C. Álvarez, 2014, The Protein Journal.

Sticholysin I-membrane interaction: an interplay between the presence of sphingomyelin and membrane fluidity.

B. Maggio, U. Ros, M. E. Lanio, 2014, Biochimica et biophysica acta.

Isolation and partial purification of a hemolytic sphingomyelin-inhibitable fraction from the sea anemone Anthopleura nigrescens

U. Ros, M. E. Lanio, C. Álvarez, 2014 .

Pharmacological effects of two cytolysins isolated from the sea anemone Stichodactyla helianthus

C. Álvarez, F. Pazos, M. Tejuca, 2009, Journal of Biosciences.

Effect of calcium on the hemolytic activity of Stichodactyla helianthus toxin sticholysin II on human erythrocytes.

E. Lissi, M. E. Lanio, C. Álvarez, 2009, Toxicon : official journal of the International Society on Toxinology.

Sticholysins, two pore-forming toxins produced by the Caribbean Sea anemone Stichodactyla helianthus: their interaction with membranes.

J. Mancheño, M. E. Lanio, C. Álvarez, 2009, Toxicon : official journal of the International Society on Toxinology.

Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity.

S. Schreier, E. Lissi, U. Ros, 2007, Toxicon : official journal of the International Society on Toxinology.

Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II.

A. Spisni, S. Schreier, D. Pentón, 2006, Biopolymers.

Role of endogenous channels in red blood cells response to their exposure to the pore forming toxin Sticholysin II.

E. Lissi, M. E. Lanio, C. Álvarez, 2005, Toxicon : official journal of the International Society on Toxinology.

Cross-reactivity and inhibition of haemolysis by polyclonal antibodies raised against St II, a cytolysin from the sea anemone Stichodactyla helianthus.

C. Álvarez, A. Otero, Ariel Basulto, 2004, Toxicon : official journal of the International Society on Toxinology.

Construction of an immunotoxin with the pore forming protein StI and ior C5, a monoclonal antibody against a colon cancer cell line.

L. Roque, R. Figueredo, N. Iznaga-Escobar, 2004, International immunopharmacology.

Effects of sodium dodecyl sulfate on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus.

S. Schreier, E. Lissi, M. E. Lanio, 2003, Toxicon : official journal of the International Society on Toxinology.

Binding of sea anemone pore-forming toxins sticholysins I and II to interfaces--modulation of conformation and activity, and lipid-protein interaction.

S. Schreier, E. Lissi, G. Menestrina, 2003, Chemistry and physics of lipids.

Comparison of pore-forming ability in membranes of a native and a recombinant variant of Sticholysin II from Stichodactyla helianthus.

E. Lissi, M. E. Lanio, C. Álvarez, 2003, Toxicon : official journal of the International Society on Toxinology.

Identity between cytolysins purified from two morphos of the Caribbean sea anemone Stichodactyla helianthus.

M. Raida, G. Padrón, C. Álvarez, 2002, Toxicon : official journal of the International Society on Toxinology.

Effect of a Zwitterionic Surfactant (HPS) on the Conformation and Hemolytic Activity of St I and St II, Two Isotoxins Purified from Stichodactyla helianthus

S. Schreier, E. Lissi, M. E. Lanio, 2002, Journal of protein chemistry.

Sizing the Radius of the Pore Formed in Erythrocytes and Lipid Vesicles by the Toxin Sticholysin I from the Sea Anemone Stichodactyla helianthus

C. Potrich, G. Menestrina, C. Álvarez, 2001, The Journal of Membrane Biology.

Effect of pH on the conformation, interaction with membranes and hemolytic activity of sticholysin II, a pore forming cytolysin from the sea anemone Stichodactyla helianthus.

S. Schreier, E. Lissi, M. E. Lanio, 2001, Toxicon : official journal of the International Society on Toxinology.

Primary structure of two cytolysin isoforms from Stichodactyla helianthus differing in their hemolytic activity.

G. Chinea, V. Huerta, L. González, 2001, Toxicon : official journal of the International Society on Toxinology.

Aggregation induced by concanavalin A of lipid vesicles containing neoglycolipids

E. Disalvo, M. E. Lanio, C. Álvarez, 2002 .

Panusin represents a new family of &bgr;‐defensin‐like peptides in invertebrates

J. Tytgat, S. Peigneur, C. Álvarez, 2017, Developmental and comparative immunology.

Kinetics and Mechanism of St I Modification by Peroxyl Radicals

E. Lissi, M. E. Lanio, C. Álvarez, 1999, Journal of protein chemistry.

Liposomes of phosphatidylcholine and cholesterol induce an M2-like macrophage phenotype reprogrammable to M1 pattern with the involvement of B-1 cells.

M. E. Lanio, C. Álvarez, A. López-Requena, 2014, Immunobiology.

The Sticholysin I mutants St I E 2 C and St I R 52 C show similar binding to liposomal vesicles but differ in their permeabilizing activity

S. Schreier, R. Fando, A. López, 2011 .

Antiparasite activity of sea-anemone cytolysins on Giardia duodenalis and specific targeting with anti-Giardia antibodies.

G. Anderluh, P. Maček, G. Menestrina, 1999, International journal for parasitology.

Phosphocholine-Specific Antibodies Improve T-Dependent Antibody Responses against OVA Encapsulated into Phosphatidylcholine-Containing Liposomes

Y. Machado, M. E. Lanio, C. Álvarez, 2016, Front. Immunol..

Role of B-1 cells in the immune response against an antigen encapsulated into phosphatidylcholine-containing liposomes.

R. Mortara, Y. Machado, M. E. Lanio, 2014, International immunology.

BACILLUS SPECIES IN THE OCEANIC WATERS ADJACENT TO CUBA: ASSOCIATION BETWEEN THEIR DISTRIBUTION AND METABOLIC ACTIVITY

C. Álvarez, O. Coto, G. Espinosa, 2010 .

Cys mutants as tools to study the oligomerization of the pore-forming toxin sticholysin I.

M. E. Lanio, C. Álvarez, Y. P. Hervis, 2022, Toxicon : official journal of the International Society on Toxinology.

A new and simple procedure for the evaluation of the association of surfactants to proteins.

E. Lissi, M. E. Lanio, C. Álvarez, 2002, Journal of biochemical and biophysical methods.

Modification of sticholysin II hemolytic activity by free radicals.

E. Lissi, M. E. Lanio, C. Álvarez, 1998, Toxicon : official journal of the International Society on Toxinology.

T cell-independent B cell response to self-monosialogangliosides: primary response monoclonal antibodies.

J. Zeuthen, L. E. Fernández, M. E. Lanio, 1995, Hybridoma.

Generation of a murine monoclonal antibody specific for N-glycolylneuraminic acid-containing gangliosides that also recognizes sulfated glycolipids.

B. Lanne, K. Karlsson, L. E. Fernández, 1995, Hybridoma.

Cloning, purification and characterization of nigrelysin, a novel actinoporin from the sea anemone Anthopleura nigrescens.

F. Solano-Campos, B. Lomonte, M. E. Lanio, 2019, Biochimie.

The multigene families of actinoporins (part I): Isoforms and genetic structure.

J. Barbosa, M. E. Lanio, C. Álvarez, 2015, Toxicon : official journal of the International Society on Toxinology.

Sticholysin II-mediated cytotoxicity involves the activation of regulated intracellular responses that anticipates cell death.

U. Ros, M. E. Lanio, C. Álvarez, 2018, Biochimie.

Improved purification and enzymatic properties of a mixture of Sticholysin I and II: isotoxins with hemolytic and phospholipase A(2) activities from the sea anemone Stichodactyla helianthus.

M. E. Lanio, C. Álvarez, J. Guisán, 2014, Protein expression and purification.

Pore-forming toxins from sea anemones: from protein-membrane interaction to its implications for developing biomedical applications

M. E. Lanio, C. Álvarez, F. Pazos, 2020 .

The Vacuolar Pathway in Macrophages Plays a Major Role in Antigen Cross-Presentation Induced by the Pore-Forming Protein Sticholysin II Encapsulated Into Liposomes

M. Starnbach, D. Higgins, M. E. Lanio, 2018, Front. Immunol..

Purification and Conformational Characterization of a Novel Interleukin-2 Mutein

Yamile González-González, C. Álvarez, Tammy Boggiano-Ayo, 2021, The Protein Journal.

The role of ionic strength on the enhancement of the hemolytic activity of sticholysin I, a cytolysin from Stichodactyla helianthus.

S. Schreier, E. Lissi, M. E. Lanio, 1998, Toxicon : official journal of the International Society on Toxinology.

Interaction between G protein-operated receptors eliciting secretion in rat adrenals. A possible role of protein kinase C.

C. Álvarez, R. Borges, C. Lorenzo, 1997, Biochemical pharmacology.

Insights on the structure‐activity relationship of peptides derived from Sticholysin II

A. Spisni, S. Schreier, U. Ros, 2018, Biopolymers.

Panorama of the Intracellular Molecular Concert Orchestrated by Actinoporins, Pore-Forming Toxins from Sea Anemones

U. Ros, M. E. Lanio, C. Álvarez, 2021, Toxins.

Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus.

A. García-Sáez, P. A. Valiente, U. Ros, 2015, Biochimie.

Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation.

S. Schreier, E. Lissi, R. Fando, 2011, Toxicon : official journal of the International Society on Toxinology.

Validation of a mutant of the pore-forming toxin sticholysin-I for the construction of proteinase-activated immunotoxins.

T. Pons, R. Fando, D. Pentón, 2011, Protein engineering, design & selection : PEDS.

Properties of St I and St II, two isotoxins isolated from Stichodactyla helianthus: a comparison.

S. Schreier, E. Lissi, C. Vergara, 2001, Toxicon : official journal of the International Society on Toxinology.

Functional and topological studies with Trp-containing analogs of the peptide StII(1-30) derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane.

S. Schreier, U. Ros, M. E. Lanio, 2013, Biopolymers.

The Important Role of Membrane Fluidity on the Lytic Mechanism of the α-Pore-Forming Toxin Sticholysin I

R. Epand, A. García-Sáez, U. Ros, 2023, Toxins.

Membrane remodeling by the lytic fragment of sticholysin II: implications for the toroidal pore model

D. Tieleman, R. Epand, R. Epand, 2019, bioRxiv.

The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels

T. Pons, J. Tytgat, R. García-Fernández, 2016, Toxins.

The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition

S. Schreier, P. A. Valiente, R. Itri, 2011, Journal of Biosciences.

Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins.

S. Schreier, U. Ros, M. E. Lanio, 2007, Toxicon : official journal of the International Society on Toxinology.

Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus.

E Lissi, E. Horjales, S. Schreier, 2006, Toxicon : official journal of the International Society on Toxinology.

N-terminal peptide (1-92) of Sticholysin II generated by the cleavage with cyanogen bromide interacts with lipid bilayer but does not promote pore formation

M. Raida, C. Potrich, S. Schreier, 2006 .

Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins.

S. Schreier, U. Ros, M. E. Lanio, 2019, Biochimie.

CARDIOTOXIC ACTIONS OF STHICHOLYSINS I AND II, TWO CYTOLYSINS ISOLATED FROM THE SEA ANEMONE Stichodactyla helianthus

C. Álvarez, L. Galán, Souto Rd, 2006 .

Primary structure analysis of the haemolytic polypeptide sticholysin isolated from a sea anemone

T. Pons, V. Besada, G. Padrón, 1995 .

Synthesis of a new neoglycolipid (AgH-1) and its effect upon the properties of dipalmitoylphosphatidylcholine: cholesterol liposomes.

E. Lissi, M. E. Lanio, C. Álvarez, 1998, Archives of biochemistry and biophysics.

Damage of eukaryotic cells by the pore-forming toxin sticholysin II: Consequences of the potassium efflux.

M. E. Lanio, C. Álvarez, Sylvia Ho, 2017, Biochimica et biophysica acta. Biomembranes.

Corrigendum to “Stycholysin II, a cytolysin from the sea anemone Stichodactyla helianthus promotes higher hemolysis in aged red blood cells” [Toxicon 51 (2008) 1383–1390]

E. Lissi, M. E. Lanio, C. Álvarez, 2008 .

Response of unilamellar DPPC and DPPC:SM vesicles to hypo and hyper osmotic shocks: A comparison.

E. Lissi, M. E. Lanio, C. Álvarez, 2015, Chemistry and physics of lipids.