Bioquímica y Biología Molecular
Departamento
JOSÉ MIGUEL
MANCHEÑO GÓMEZ
Investigador hasta 2008
Publicaciones en las que colabora con JOSÉ MIGUEL MANCHEÑO GÓMEZ (46)
2022
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Rational Design of a Thermostable 2′-Deoxyribosyltransferase for Nelarabine Production by Prediction of Disulfide Bond Engineering Sites
International Journal of Molecular Sciences, Vol. 23, Núm. 19
2021
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Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: Insights into cold-adaptation
International Journal of Biological Macromolecules, Vol. 192, pp. 138-150
2018
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2′-deoxyribosyltransferase from bacillus psychrosaccharolyticus: A mesophilic-like biocatalyst for the synthesis of modified nucleosides from a psychrotolerant bacterium
Catalysts, Vol. 8, Núm. 1
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Characterization of an atypical, thermostable, organic solvent- and acid-tolerant 2′-deoxyribosyltransferase from Chroococcidiopsis thermalis
Applied Microbiology and Biotechnology, Vol. 102, Núm. 16, pp. 6947-6957
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Enzymatic Synthesis of Therapeutic Nucleosides using a Highly Versatile Purine Nucleoside 2’-DeoxyribosylTransferase from Trypanosoma brucei
ChemCatChem, Vol. 10, Núm. 19, pp. 4406-4416
2017
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2′-Deoxyribosyltransferase from Leishmania mexicana, an efficient biocatalyst for one-pot, one-step synthesis of nucleosides from poorly soluble purine bases
Applied Microbiology and Biotechnology, Vol. 101, Núm. 19, pp. 7187-7200
2011
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High-resolution structural insights on the sugar-recognition and fusion tag properties of a versatile-trefoil lectin domain from the mushroom Laetiporus sulphureus
Glycobiology, Vol. 21, Núm. 10, pp. 1349-1361
2007
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Insights into the activation of brain serine racemase by the multi-PDZ domain glutamate receptor interacting protein, divalent cations and ATP
FEBS Journal, Vol. 274, Núm. 17, pp. 4561-4571
2006
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A complementary microscopy analysis of Sticholysin II crystals on lipid films: Atomic force and transmission electron characterizations
Biophysical Chemistry, Vol. 119, Núm. 3, pp. 219-223
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The role of electrostatic interactions in the antitumor activity of dimeric RNases
FEBS Journal, Vol. 273, Núm. 16, pp. 3687-3697
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
2003
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Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
Structure, Vol. 11, Núm. 11, pp. 1319-1328
2002
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Crystallization and preliminary X-ray diffraction studies of the water-soluble state of the pore-forming toxin sticholysin II from the sea anemone Stichodactyla helianthus
Acta Crystallographica Section D: Biological Crystallography, Vol. 58, Núm. 7, pp. 1229-1231
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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