B. Curti

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Glutamate synthase: a complex iron-sulfur flavoprotein

M. Vanoni, B. Curti, 1999, Cellular and Molecular Life Sciences (CMLS).

Isolation, characterization and partial sequence of cyanogen bromide fragments and thiol peptides from pig kidney D-amino-acid oxidase.

M. C. Zapponi, S. Ronchi, B. Curti, 1976, Biochimica et biophysica acta.

Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves.

M. Galliano, G. Zanetti, G. Sacchi, 1977, Biochimica et biophysica acta.

Mechanistic studies on Azospirillum brasilense glutamate synthase.

M. Rescigno, G. Zanetti, D. Edmondson, 1991, Biochemistry.

Immunoelectron microscopic localization ofd-amino acid oxidase in rat kidney and liver

M. Perotti, B. Curti, N. Malgaretti, 1987, The Histochemical Journal.

The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence.

M. Galliano, V. Massey, S. Ronchi, 1982, The Journal of biological chemistry.

Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism, and electron paramagnetic resonance spectroscopies.

G. Zanetti, D. Edmondson, M. Vanoni, 1992, Biochemistry.

Reactivity of D-amino acid oxidase with 1,2-cyclohexanedione: evidence for one arginine in the substrate-binding site.

M. Galliano, M. Simonetta, S. Ronchi, 1981, European journal of biochemistry.

Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl–tRNA synthetase and determination of its oligomeric structure in solution

D. Svergun, M. Petoukhov, P. Konarev, 2009, The FEBS journal.

PROTEINASE ACTIVITY OF PERIPHERAL NERVES DURING WALLERIAN DEGENERATION *

G. Porcellati, B. Curti, Giuseppe Porcellati, 1960, Journal of neurochemistry.

Structure--function studies on the iron-sulfur flavoenzyme glutamate synthase: an unexpectedly complex self-regulated enzyme.

M. Vanoni, B. Curti, 2005, Archives of biochemistry and biophysics.

Structure–function studies on the complex iron–sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation

M. Vanoni, B. Curti, L. Dossena, 2004, Photosynthesis Research.

Structural studies on the interaction between ferredoxin and ferredoxin-NADP+ reductase

G. Zanetti, S. Ronchi, A. Negri, 1988 .

Purification and characterization of glutamate synthase from Azospirillum brasilense

G. Zanetti, B. Curti, E. Galli, 1985, Journal of bacteriology.

Crystallization and preliminary x-ray diffraction studies on met-myoglobin from Aplysia limacina.

T. Blundell, M. Brunori, A. Coda, 1975, Journal of molecular biology.

A temperature-dependent conformational change in D-amino acid oxidase and its effect on catalysis.

H. Ganther, V. Massey, B. Curti, 1966, The Journal of biological chemistry.

Structure of D-amino acid oxidase: new insights from an old enzyme.

A. Mattevi, M. Vanoni, B. Curti, 1997, Current opinion in structural biology.

A study on apoenzyme from Rhodotorula gracilis D-amino acid oxidase.

L. Pollegioni, B. Curti, P. Casalin, 1991, European journal of biochemistry.

Properties of D-amino-acid oxidase from Rhodotorula gracilis.

L. Pollegioni, S. Ronchi, B. Curti, 1989, European journal of biochemistry.

Phenylglyoxal modification of arginines in mammalian D-amino-acid oxidase.

S. Ronchi, A. Negri, M. Vanoni, 1987, European journal of biochemistry.

The unexpected structural role of glutamate synthase [4Fe-4S](+1,+2) clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme beta subunit.

P. Colombi, G. Tedeschi, A. Negri, 2005, Archives of biochemistry and biophysics.

Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein.

M. Vanoni, B. Curti, H. Stabile, 2000, European journal of biochemistry.

Immunochemical properties of D-amino-acid oxidase.

B. Curti, N. Malgaretti, E. Gavazzi, 1987, Biochimica et biophysica acta.

Modification of arginyl residues in ferredoxin-NADP+ reductase from spinach leaves.

G. Zanetti, G. Sacchi, B. Curti, 1979, Biochimica et biophysica acta.

On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase.

V. Massey, B. Curti, 1967, The Journal of biological chemistry.

Involvement of serine 96 in the catalytic mechanism of ferredoxin-NADP+ reductase: structure--function relationship as studied by site-directed mutagenesis and X-ray crystallography.

P. Karplus, G. Zanetti, M. Vanoni, 1995, Biochemistry.

Structure–function studies of glutamate synthases: A class of self‐regulated iron‐sulfur flavoenzymes essential for nitrogen assimilation

M. Vanoni, B. Curti, 2008, IUBMB life.

Interactions between ferredoxin‐nadp+ reductase and ferredoxin at different reduction levels of the two proteins

G. Zanetti, B. Curti, 1981, FEBS letters.

Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate

A. Mattevi, R. V. D. van den Heuvel, M. Vanoni, 2004, Cellular and Molecular Life Sciences CMLS.

Crystallographic studies on D-amino acid oxidase.

M. Bolognesi, S. Ronchi, B. Curti, 1978, Journal of Biological Chemistry.

A new method of preparation of D-amino acid oxidase apoprotein and a conformational change after its combination with flavin adenine dinucleotide.

V. Massey, B. Curti, 1966, The Journal of biological chemistry.

Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins.

M. Vanoni, B. Curti, A. Aliverti, 1999, Methods in molecular biology.

FAD analogues as mechanistic and 'binding-domain' probes of spinach ferredoxin-NADP+ reductase.

G. Zanetti, V. Massey, B. Curti, 1983, European journal of biochemistry.

Active site plasticity in D-amino acid oxidase: a crystallographic analysis.

M. Bolognesi, A. Mozzarelli, A. Mattevi, 1997, Biochemistry.

Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.

A Coda, M Bolognesi, M. Bolognesi, 1996, Proceedings of the National Academy of Sciences of the United States of America.

The kinetic mechanism of the reactions catalyzed by the glutamate synthase from Azospirillum brasilense.

M. Rescigno, G. Zanetti, M. Vanoni, 1991, European journal of biochemistry.

Use of Monospecific Antibodies for the Purification of D-Amino Acid Oxidases from Various Sources

E. Monti, G. Fossati, B. Curti, 1987 .

A cross-linked complex between ferredoxin and ferredoxin-NADP+ reductase.

G. Zanetti, B. Curti, A. Aliverti, 1984, The Journal of biological chemistry.

Immunoelectron microscopic localization of D-amino acid oxidase in rat kidney and liver.

M. Perotti, B. Curti, N. Malgaretti, 1987, The Histochemical journal.

d‐Amino acid oxidase activity in the yeast Rhodotorula gracilis

M. Vanoni, B. Curti, M. Simonetta, 1982 .

The role of cysteine residues of spinach ferredoxin-NADP+ reductase As assessed by site-directed mutagenesis.

R. Herrmann, G. Zanetti, T. Lübberstedt, 1993, Biochemistry.

Probing the role of lysine 116 and lysine 244 in the spinach ferredoxin-NADP+ reductase by site-directed mutagenesis.

R. Herrmann, G. Zanetti, T. Lübberstedt, 1991, The Journal of biological chemistry.

Expression in Escherichia coli of ferredoxin:NADP+ reductase from spinach. Bacterial synthesis of the holoflavoprotein and of an active enzyme form lacking the first 28 amino acid residues of the sequence.

R. Herrmann, G. Zanetti, S. Ronchi, 1990, European journal of biochemistry.

[22] Ferredoxin-NADP+ oxidoreductase

G. Zanetti, B. Curti, 1980 .

Synthesis and biological evaluation of new amino acids structurally related to the antitumor agent acivicin.

G. Roda, P. Conti, M. De Amici, 2003, Farmaco.

On the reaction of borohydride with D- and L-amino acid oxidases.

V. Massey, F. Müller, S. Mayhew, 1968, The Journal of biological chemistry.

Radioimmunoassay and chemical properties of glucose 6-phosphate dehydrogenase and of a specific NADP(H)-binding protein (FX) from human erythrocytes.

M. Galliano, A. De Flora, A. Morelli, 1977, Biochimica et biophysica acta.

The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides.

M. Galliano, V. Massey, S. Ronchi, 1982, Journal of Biological Chemistry.

Cloning and expression in Escherichia coli of the gene encoding Streptomyces PMF PLD, a phospholipase D with high transphosphatidylation activity

D. Monti, S. Servi, G. Carrea, 2003 .

Porcine recombinant dihydropyrimidine dehydrogenase: comparison of the spectroscopic and catalytic properties of the wild-type and C671A mutant enzymes.

W. Hagen, K. Schnackerz, M. Vanoni, 1998, Biochemistry.

Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis.

L. Pollegioni, F. Ceciliani, S. Ronchi, 1995, The Biochemical journal.

Estimation of hepatic arterial and portal venous blood flow by direct catheterization of the vena porta through the umbilical cord in man. Preliminary results.

A. Vaccarino, B. Curti, L Chiandussi, 1968, Acta hepato-splenologica.

Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.

A. Mattevi, S. Wakatsuki, A. Coda, 2000, Structure.

Immunochemical studies of L-amino acid oxidase.

V. Massey, B. Curti, R. Brown, 1971, Biochimica et biophysica acta.

The active conformation of glutamate synthase and its binding to ferredoxin.

D. Svergun, M. Petoukhov, A. Mattevi, 2003, Journal of molecular biology.

Inactivation of snake venom L-amino acid oxidase by freezing.

V. Massey, B. Curti, M. Zmudka, 1968, The Journal of biological chemistry.

Glutamate synthase: a complex iron-sulphur flavoprotein.

M. Vanoni, G. Zanetti, M. Vanoni, 1996, Biochemical Society transactions.

Properties of the recombinant beta subunit of glutamate synthase.

G. Zanetti, M. Vanoni, B. Curti, 1996, European journal of biochemistry.

Improved purification, amino acid analysis and molecular weight of homogenous D-amino acid oxidase from pig kidney.

G. Ferri, S. Ronchi, C. Williams, 1973, Biochimica et biophysica acta.

Renaturation studies of free and immobilized D-amino-acid oxidase.

G. Carrea, B. Curti, P. Pasta, 1983, Biochimica et biophysica acta.

Phospholipid Phosphoric Esters in the Human Placenta

G. Porcellati, B. Curti, S. Luciani, 1959, Nature.

Preparation of apoprotein from spinach ferredoxin-NADP+ reductase. Studies on the resolution process and characterization of the FAD reconstituted holoenzyme.

G. Zanetti, B. Curti, D. Cidaria, 1982, European journal of biochemistry.

Glutamate synthases (GltS) carry out the synthesis of one molecule of L-glutamate from L- glutamine and 2-oxoglutarate (2-OG) by catalysing the reductive transfer of glutamine amide group

M. Vanoni, B. Curti, L. Dossena, 2004 .

Flavins and flavoproteins : proceedings of the Tenth International Symposium on Flavins and Flavoproteins, Como, Italy, July 15-20, 1990

G. Zanetti, S. Ronchi, B. Curti, 1991 .

Molecular dynamics simulation of the interaction between the complex iron–sulfur flavoprotein glutamate synthase and its substrates

A. di Nola, D. Roccatano, M. Aschi, 2004, Protein science : a publication of the Protein Society.

Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.

A. Mattevi, D. Mazzeo, A. Cosma, 1997, Biochemistry.

Structural Studies on the Synchronization of Catalytic Centers in Glutamate Synthase*

A. Mattevi, D. Ferrari, R. V. D. van den Heuvel, 2002, The Journal of Biological Chemistry.

Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.

A. Mattevi, F. Florencio, M. Vanoni, 2002, Biochemistry.

Quaternary Structure of Azospirillum brasilense NADPH-dependent Glutamate Synthase in Solution as Revealed by Synchrotron Radiation X-ray Scattering*

D. Svergun, M. Petoukhov, P. Konarev, 2003, Journal of Biological Chemistry.

Glutamate synthase: self-regulation and oligomeric structure

D. Svergun, S. Jonić, E. Larquet, 2008 .

Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase.

M. Vanoni, B. Curti, S. Ravasio, 2001, Biochemistry.

The recombinant alpha subunit of glutamate synthase: spectroscopic and catalytic properties.

W. Hagen, G. Zanetti, F. Fischer, 1998, Biochemistry.

Interdomain loops and conformational changes of glutamate synthase as detected by limited proteolysis.

G. Zanetti, P. Fumagalli, A. Negri, 1994, European journal of biochemistry.

Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing, and analysis of functional domains.

A. Galizzi, M. Perego, G. Zanetti, 1993, The Journal of biological chemistry.

Glutamate synthase from Azospirillum brasilense

G. Zanetti, B. Curti, S. Ratti, 1984 .