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Proteins|December 14, 2007
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-siteNerino Allocati, Luca Federici, Michele Masulli, et al.
The Biochemical Journal|April 2, 2003
Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stressesNerino Allocati, Bartolo Favaloro, Michele Masulli, et al.
The Biochemical Journal|August 24, 2004
Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1Nerino Allocati, Michele Masulli, Marilena Pietracupa, et al.
Folia Microbiologica|August 6, 2013
Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatusNerino Allocati, Michele Masulli, Piero Del Boccio, et al.
The Biochemical Journal|March 21, 2002
Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1Nerino Allocati, Michele Masulli, Enrico Casalone, et al.
The Biochemical Journal|January 17, 2007
Role of Ser11 in the stabilization of the structure of Ochrobactrum anthropi glutathione transferaseLuca Federici, Michele Masulli, Daniele Bonivento, et al.
Frontiers in Microbiology|February 5, 2019
Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic Archaeon Natrialba magadiiAdele Di Matteo, Luca Federici, Michele Masulli, et al.
Biochemistry|April 3, 2002
Properties and utility of the peculiar mixed disulfide in the bacterial glutathione transferase B1-1Anna Maria Caccuri, Giovanni Antonini, Nerino Allocati, et al.
The Journal of Biological Chemistry|March 13, 2002
GSTB1-1 from Proteus mirabilis: a snapshot of an enzyme in the evolutionary pathway from a redox enzyme to a conjugating enzymeAnna Maria Caccuri, Giovanni Antonini, Nerino Allocati, et al.
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