Facultad de Biología
Centro académico
University of Sussex
Brighton, Reino UnidoPublicaciones en colaboración con investigadores/as de University of Sussex (14)
2021
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Autophagy, Vol. 17, Núm. 1, pp. 1-382
2019
2017
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Metabolic and reproductive plasticity of core and marginal populations of the eurythermic saline water bug Sigara selecta (Hemiptera: Corixidae) in a climate change context
Journal of Insect Physiology, Vol. 98, pp. 59-66
2013
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Cxcl8 (IL-8) mediates neutrophil recruitment and behavior in the zebrafish inflammatory response
Journal of Immunology, Vol. 190, Núm. 8, pp. 4349-4359
2002
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Reactions of the class II peroxidases, lignin peroxidase and Arthromyces ramosus peroxidase, with hydrogen peroxide: Catalase-like activity, compound III formation, and enzyme inactivation
Journal of Biological Chemistry, Vol. 277, Núm. 30, pp. 26879-26885
2001
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Catalase-like oxygen production by horseradish peroxidase must predominantly be an enzyme-catalyzed reaction
Archives of Biochemistry and Biophysics, Vol. 392, Núm. 2, pp. 295-302
1998
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Redox- and anion-linked protonation sites in horseradish peroxidase: Analysis of distal haem pocket mutants
Biochemical Journal, Vol. 330, Núm. 1, pp. 303-309
1997
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Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase
Journal of Biological Chemistry, Vol. 272, Núm. 1, pp. 389-395
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Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties
Biochemistry, Vol. 36, Núm. 6, pp. 1532-1543
1996
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Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine
European Journal of Biochemistry, Vol. 236, Núm. 2, pp. 714-722
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Recombinant horseradish peroxidase isoenzyme C: The effect of distal haem cavity mutations (His42→Leu and Arg38→Leu) on compound I formation and substrate binding
Journal of Biological Inorganic Chemistry, Vol. 1, Núm. 2, pp. 136-142
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Role of arginine 38 in horseradish peroxidase: A critical residue for substrate binding and catalysis
Journal of Biological Chemistry, Vol. 271, Núm. 8, pp. 4023-4030
1995
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A COMPARATIVE-STUDY OF THE INACTIVATION OF WILD-TYPE, RECOMBINANT AND 2 MUTANT HORSERADISH-PEROXIDASE ISOENZYMES-C BY HYDROGEN-PEROXIDE AND M-CHLOROPEROXYBENZOIC ACID
EUROPEAN JOURNAL OF BIOCHEMISTRY, Vol. 234, Núm. 2, pp. 506-512
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Laser Photolysis Behavior of Ferrous Florseradish Peroxidase with Carbon Monoxide and Cyanide: Effects of Mutations in the Distal Heme Pocket
Biochemistry, Vol. 34, Núm. 45, pp. 14687-14692