Gianfranco Menestrina

Instituto Biofisika — Spain

Biochemistry, Genetics and Molecular Biology · Life Sciences

47h-index5.9kcitations128works0.02yr avg
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Research Topics

Lipid Membrane Structure and Behavior(57), Toxin Mechanisms and Immunotoxins(21), Nanopore and Nanochannel Transport Studies(19), Ion channel regulation and function(16), Bacteriophages and microbial interactions(14)

Publications128 total

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
2006· 1 cited
Homologous versus heterologous interactions in the bicomponent staphylococcal γ-haemolysin pore1
Biochemical Journal·2006· 13 citedOpen Access
Metal binding in amyloid β-peptides shows intra- and inter-peptide coordination modes
European Biophysics Journal·2006· 115 citedOpen Access
Staphylococccus aureus bi-components gamma-hemolysins: looking for the potential inhibitors
Institutional Research Information System (Università degli Studi di Trento)·2006
Alpha-helix and beta-barrel pore-forming toxins (leucocidins, alpha-, gamma-, and delta-cytolysins) of Staphylococcus aureus
Elsevier eBooks·2006· 14 cited
<i>Staphylococcus aureus</i>Bicomponent γ-Hemolysins, HlgA, HlgB, and HlgC, Can Form Mixed Pores Containing All Components
Journal of Chemical Information and Modeling·2005· 28 cited
Molecular organization of the antifungal and anticancer drug 2-(2,4-dihydroxyphenylo)-5,6-dichlorobenzothiazole in solution and in monolayers: An effect of pH
Journal of Photochemistry and Photobiology B Biology·2005· 6 cited
Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins
Biophysical Journal·2005· 99 citedOpen Access
Cytotoxic Activity of a Tumor Protease-Activated Pore-Forming Toxin
Bioconjugate Chemistry·2005· 39 cited
Potential inhibitors of Staphylococccus aureus bi-components gamma-hemolysins
Institutional Research Information System (Università degli Studi di Trento)·2005
Structure, conformation and biological activity of a novel lipodepsipeptide from <i>Pseudomonas corrugata</i>: cormycin A
Biochemical Journal·2004· 75 citedOpen Access
Crystal Structure of Leucotoxin S Component
Journal of Biological Chemistry·2004· 103 citedOpen Access
Reductive activation of ricin and ricin A-chain immunotoxins by protein disulfide isomerase and thioredoxin reductase
Biochemical Pharmacology·2004· 83 cited
Inter- and Intra-octarepeat Cu(II) Site Geometries in the Prion Protein
Journal of Biological Chemistry·2004· 84 citedOpen Access
Reductive activation of ricin and ricin-A chain immunotoxins by Protein Disulfide Isomerase and Thioredoxin Reductase system.
2004
Protein Disulfide Isomerase and Thioredoxin Reductase: a ricin disulfide reducing system in the endoplasmic reticulum.
2004
XAS-analysis reveals two Cu(II) site geometries in prion protein complexes
2004
Fluorescent Assay to Demonstrate the Interaction of Thioredoxin Reductase and Protein Disulfide Isomerase.
2004
Cu(II) site geometry of the octarepeat domain of Prion Protein: a XAS study.
2004
FLUORESCENT ASSAY TO TEST PROTEIN DISULFIDE ISOMERASE ACTIVITY INDUCED BY THIOREDOXIN REDUCTASE.
Institutional Research Information System (Università degli Studi di Trento)·2004
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Frequent Co-authors

Mauro Dalla Serra(20), Peter Maček(13), Mayra Tejuca(6), Gregor Anderluh(6), Giovanna Belmonte(5), Cecilia Pederzolli(5), Gilles Prévost(5), C.L. Bashford(4), C. A. Pasternak(4), María E. Lanio(4), Manuela Coraiola(4), Cristina Potrich(3), Ivonne Bernhart(3), Gabriella Viero(3), Zdravko Podlesek(3), Carlos Álvarez(3), Tom Turk(3), Ariana Barlič(3), Cristina Potrich(3), Monica Ropele(3)