ÁLVARO
MARTÍNEZ DEL POZO
Catedrático de universidad
JOSÉ MIGUEL
MANCHEÑO GÓMEZ
Investigador hasta 2008
Publicaciones en las que colabora con JOSÉ MIGUEL MANCHEÑO GÓMEZ (27)
2004
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Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II
FEBS Letters, Vol. 575, Núm. 1-3, pp. 14-18
2002
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The antifungal protein AFP of Aspergillus giganteus is an oligonucleotide/oligosaccharide binding (OB) fold-containing protein that produces condensation of DNA
Journal of Biological Chemistry, Vol. 277, Núm. 48, pp. 46179-46183
2001
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Arginine 121 is a crucial residue for the specific cytotoxic activity of the ribotoxin α-sarcin
European Journal of Biochemistry, Vol. 268, Núm. 23, pp. 6190-6196
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Involvement of the amino-terminal β-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity
Protein Science, Vol. 10, Núm. 8, pp. 1658-1668
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RNase U2 and α-sarcin: A study of relationships
Methods in Enzymology (Academic Press Inc.), pp. 335-351
2000
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Assignment of the contribution of the tryptophan residues to the spectroscopic and functional properties of the ribotoxin α-Sarcin
Proteins: Structure, Function and Genetics, Vol. 41, Núm. 3, pp. 350-361
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Overproduction in Escherichia coli and purification of the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus
Protein Expression and Purification, Vol. 18, Núm. 1, pp. 71-76
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Ribonuclease U2: Cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant protein
FEMS Microbiology Letters, Vol. 189, Núm. 2, pp. 165-169
1999
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Role of histidine-50, glutamic acid-96, and histidine-137 in the ribonucleolytic mechanism of the ribotoxin α-sarcin
Proteins: Structure, Function and Genetics, Vol. 37, Núm. 3, pp. 474-484
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Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer-tetramer associating protein
FEBS Letters, Vol. 455, Núm. 1-2, pp. 27-30
1998
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A peptide of nine amino acid residues from α-sarcin cytotoxin is a membrane-perturbing structure
Journal of Peptide Research, Vol. 51, Núm. 2, pp. 142-148
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Oligomerization of the cytotoxin α-sarcin associated with phospholipid membranes
Molecular Membrane Biology, Vol. 15, Núm. 3, pp. 141-144
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Secretion of recombinant pro- and mature fungal α-sarcin ribotoxin by the methylotrophic yeast Pichia pastoris: The Lys-Arg motif is required for maturation
Protein Expression and Purification, Vol. 12, Núm. 3, pp. 315-322
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The cytotoxin α-sarcin behaves as a cyclizing ribonuclease
FEBS Letters, Vol. 424, Núm. 1-2, pp. 46-48
1997
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Characterization of a natural larger form of the antifungal protein (AFP) from Aspergillus giganteus
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1340, Núm. 1, pp. 81-87
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Sequence determination and molecular characterization of gigantin, a cytotoxic protein produced by the mould Aspergillus giganteus IFO 5818
Archives of Biochemistry and Biophysics, Vol. 343, Núm. 2, pp. 188-193
1996
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Release of lipid vesicle contents by an antibacterial cecropin A- melittin hybrid peptide
Biochemistry, Vol. 35, Núm. 30, pp. 9892-9899
1995
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Characterization of the antifungal protein secreted by the mould aspergillus giganteus
Archives of Biochemistry and Biophysics, Vol. 324, Núm. 2, pp. 273-281
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Escherichia coli JA221 can suppress the UAG stop signal
Letters in Applied Microbiology, Vol. 21, Núm. 2, pp. 96-98
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Membrane interaction of a beta-structure-forming synthetic peptide comprising the 116–139th sequence region of the cytotoxic protein alpha-sarcin
Biophysical Journal, Vol. 68, Núm. 6, pp. 2387-2395