ÁLVARO
MARTÍNEZ DEL POZO
Catedrático de universidad
Instituto de Química Física Rocasolano
Madrid, EspañaPublicaciones en colaboración con investigadores/as de Instituto de Química Física Rocasolano (27)
2020
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Structure of Fungal α Mating Pheromone in Membrane Mimetics Suggests a Possible Role for Regulation at the Water-Membrane Interface
Frontiers in Microbiology, Vol. 11
2017
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Structure-activity relationship of α mating pheromone from the fungal pathogen fusarium oxysporum
Journal of Biological Chemistry, Vol. 292, Núm. 9, pp. 3591-3602
2014
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The sea anemone actinoporin (Arg-Gly-Asp) conserved motif is involved in maintaining the competent oligomerization state of these pore-forming toxins
FEBS Journal, Vol. 281, Núm. 5, pp. 1465-1478
2013
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Three-dimensional structure of the actinoporin sticholysin i. influence of long-distance effects on protein function
Archives of Biochemistry and Biophysics, Vol. 532, Núm. 1, pp. 39-45
2011
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Intrinsic local disorder and a network of charge-charge interactions are key to actinoporin membrane disruption and cytotoxicity
FEBS Journal, Vol. 278, Núm. 12, pp. 2080-2089
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The behavior of sea anemone actinoporins at the water-membrane interface
Biochimica et Biophysica Acta - Biomembranes, Vol. 1808, Núm. 9, pp. 2275-2288
2010
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1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II
Biomolecular NMR Assignments, Vol. 4, Núm. 1, pp. 69-72
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Specific interactions of sticholysin I with model membranes: An NMR study
Proteins: Structure, Function and Bioinformatics, Vol. 78, Núm. 8, pp. 1959-1970
2009
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1H, 13C, and 15N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II
Biomolecular NMR Assignments, Vol. 3, Núm. 2, pp. 239-241
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1H, 13C, and 15N NMR assignments of the actinoporin Sticholysin i
Biomolecular NMR Assignments, Vol. 3, Núm. 1, pp. 5-7
2006
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Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of α-sarcin
Biological Chemistry, Vol. 387, Núm. 5, pp. 535-541
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pH-dependent conformational stability of the ribotoxin α-sarcin and four active site charge substitution variants
Biochemistry, Vol. 45, Núm. 46, pp. 13705-13718
2005
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Modeling the highly specific ribotoxin recognition of ribosomes
FEBS Letters, Vol. 579, Núm. 30, pp. 6859-6864
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Refined NMR structure of α-sarcin by 15N-1H residual dipolar couplings
European Biophysics Journal, Vol. 34, Núm. 8, pp. 1057-1065
2004
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Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity
Biological Chemistry, Vol. 385, Núm. 12, pp. 1165-1170
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NMR structure of the noncytotoxic α-sarcin mutant Δ(7-22): The importance of the native conformation of peripheral loops for activity
Protein Science, Vol. 13, Núm. 4, pp. 1000-1011
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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
2003
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Dissecting Structural and Electrostatic Interactions of Charged Groups in α-Sarcin. An NMR Study of Some Mutants Involving the Catalytic Residues
Biochemistry, Vol. 42, Núm. 45, pp. 13122-13133
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Leucine 145 of the ribotoxin α-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein
Protein Science, Vol. 12, Núm. 1, pp. 161-169
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Tautomeric state of α-sarcin histidines. Nδ tautomers are a common feature in the active site of extracellular microbial ribonucleases
FEBS Letters, Vol. 534, Núm. 1-3, pp. 197-201