C. Voltattorni

发表

The Chaperoning Activity of Amino-oxyacetic Acid on Folding-Defective Variants of Human Alanine:Glyoxylate Aminotransferase Causing Primary Hyperoxaluria Type I.

V. Porcari, L. Maccari, Elisa Oppici, 2015, ACS chemical biology.

Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation

M. Bertoldi, P. Moore, C. Voltattorni, 1997, Protein science : a publication of the Protein Society.

Human liver peroxisomal alanine:glyoxylate aminotransferase: Different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant.

Elisa Oppici, R. Montioli, Antonio Lorenzetto, 2010, Biochimie.

New variants of AADC deficiency expand the knowledge of enzymatic phenotypes.

M. Bertoldi, R. Montioli, Mirco Dindo, 2020, Archives of biochemistry and biophysics.

Deficit of human ornithine aminotransferase in gyrate atrophy: Molecular, cellular, and clinical aspects.

L. Salviati, M. A. Desbats, I. Bellezza, 2020, Biochimica et biophysica acta. Proteins and proteomics.

The chymotryptic phosphopyridoxyl peptide of DOPA decarboxylase from pig kidney.

F. Bossa, D. Barra, C. Turano, 1977, Biochemical and biophysical research communications.

Interaction of Human Dopa Decarboxylase with L-Dopa: Spectroscopic and Kinetic Studies as a Function of pH

Elisa Oppici, R. Montioli, Mirco Dindo, 2013, BioMed research international.

Parkinson's Disease: Recent Updates in the Identification of Human Dopa Decarboxylase Inhibitors.

M. Bertoldi, R. Montioli, C. Voltattorni, 2016, Current drug metabolism.

Send Orders of Reprints at Bspsaif@emirates.net.ae Biochemical and Computational Approaches to Improve the Clinical Treatment of Dopa Decarboxylase-related Diseases: an Overview

Elisa Oppici, R. Montioli, C. Voltattorni, 2022 .

Molecular and Cellular Studies Reveal Folding Defects of Human Ornithine Aminotransferase Variants Associated With Gyrate Atrophy of the Choroid and Retina

L. Salviati, M. A. Desbats, R. Montioli, 2021, Frontiers in Molecular Biosciences.

Dopaminergic and noradrenergic sympathetic nerves of the dog have different DOPA decarboxylase activities

R. Cotton, R. Cotton, C. Voltattorni, 1986, Neuroscience Letters.

Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis

A. Paiardini, F. Cutruzzolà, G. Giardina, 2017, Scientific Reports.

Limited tryptic proteolysis of pig kidney 3,4-dihydroxyphenylalanine decarboxylase.

D. Barra, M. Simmaco, M. Schininá, 1988, Archives of biochemistry and biophysics.

Dopa decarboxylase exhibits low pH half‐transaminase and high pH oxidative deaminase activities toward serotonin (5‐hydroxytryptamine)

M. Bertoldi, C. Voltattorni, 2001, Protein science : a publication of the Protein Society.

Spectrum of DDC variants causing aromatic l-amino acid decarboxylase (AADC) deficiency and pathogenicity interpretation using ACMG-AMP/ACGS recommendations.

N. Blau, S. Garbade, N. Himmelreich, 2022, Molecular genetics and metabolism.

An essential arginine residue at the binding site of pig kidney 3,4-dihydroxyphenylalanine decarboxylase.

D. Barra, C. Voltattorni, P. Dominici, 1985, Archives of biochemistry and biophysics.

α 5 pyridoxalacetic acid andα 5 pyridoxyl-l-phenylalanine acetic acid: Their action on some B6-dependent enzymes

C. Voltattorni, A. Orlacchio, 1975, Experientia.

An affinity labeling reagent for pyridoxal phosphate dependent enzymes.

C. Turano, C. Voltattorni, A. Orlacchio, 1975, Biochemical and biophysical research communications.

Mapping of human autoantibody epitopes on aromatic L-amino acid decarboxylase.

R. Giordano, M. Bertoldi, M. Mannelli, 2007, The Journal of clinical endocrinology and metabolism.

Multiple roles of the active site lysine of Dopa decarboxylase.

M. Bertoldi, C. Voltattorni, 2009, Archives of biochemistry and biophysics.

Reaction of dopa decarboxylase with alpha-methyldopa leads to an oxidative deamination producing 3,4-dihydroxyphenylacetone, an active site directed affinity label.

B. Maras, M. Bertoldi, P. Moore, 1998, Biochemistry.

A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase

B. Maras, M. Bertoldi, C. Voltattorni, 2005, FEBS letters.

Stereospecificity of sodium borohydride reduction of pig kidney dopa decarboxylase.

C. Voltattorni, P. Dominici, B. Tancini, 1986, Archives of biochemistry and biophysics.

Reaction Specificity of Native and Nicked 3,4-Dihydroxyphenylalanine Decarboxylase*

M. Bertoldi, M. Paci, C. Voltattorni, 1999, The Journal of Biological Chemistry.

Targeting Cystalysin, a Virulence Factor of Treponema denticola‐Supported Periodontitis

Pietro Cozzini, Glen E Kellogg, Francesca Spyrakis, 2014, ChemMedChem.

Purification and Characterization of 3,4-Dihydroxyphenylalanine Decarboxylase from Pig Kidney

C. Turano, C. Voltattorni, A. Minelli, 1979 .

The novel R347g pathogenic mutation of aromatic amino acid decarboxylase provides additional molecular insights into enzyme catalysis and deficiency.

A. Paiardini, M. Bertoldi, S. Heales, 2016, Biochimica et biophysica acta.

Distribution of neurones containing dopa decar☐ylase and dopamine-β-hydroxylase in some sympathetic ganglia of the dog: A quantitative study

C. Voltattorni, T. Harris, C. Bell, 1984, Neuroscience.

Inhibition of pig kidney dopa decarboxylase by coenzyme-5-hydroxytryptophan adducts

M. Curini, C. Voltattorni, P. Dominici, 1984, Experientia.

Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases

Alessandro Paiardini, S. Gianni, A. Paiardini, 2011, Proceedings of the National Academy of Sciences.

Use of polymer conjugates for the intraperoxisomal delivery of engineered human alanine:glyoxylate aminotransferase as a protein therapy for primary hyperoxaluria type I.

M. Vicent, M. Talelli, Elisa Oppici, 2017, Nanomedicine : nanotechnology, biology, and medicine.

The chaperone role of the pyridoxal 5'-phosphate and its implications for rare diseases involving B6-dependent enzymes.

A. Astegno, Elisa Oppici, R. Montioli, 2014, Clinical biochemistry.

Lysine 238 Is an Essential Residue for α,β-Elimination Catalyzed by Treponema denticola Cystalysin*

M. Bertoldi, C. Voltattorni, B. Cellini, 2003, Journal of Biological Chemistry.

Mechanism-based Inactivation of Dopa Decarboxylase by Serotonin*

B. Maras, P. Moore, C. Voltattorni, 1996, The Journal of Biological Chemistry.

Pig kidney 3,4-dihydroxyphenylalanine (dopa) decarboxylase. Primary structure and relationships to other amino acid decarboxylases.

F. Bossa, B. Maras, D. Barra, 1991, European journal of biochemistry.

Identification of Critical Regions on the Primary Structure of Pig Kidney Dopa Decarboxylase

C. Voltattorni, P. Dominici, 1991 .

Pig Kidney DOPA Decarboxylase

D. Barra, C. Voltattorni, P. Dominici, 1990, Annals of the New York Academy of Sciences.

Purification and characterization of rat-liver 3,4-dihydroxyphenylalanine decarboxylase.

D. Barra, C. Voltattorni, P. Dominici, 1987, European journal of biochemistry.

Aromatic-L-amino acid decarboxylase from pig kidney.

C. Turano, C. Voltattorni, A. Giartosio, 1987, Methods in enzymology.

Spectral properties of the coenzyme bound to DOPA decarboxylase from pig kidney.

C. Turano, C. Voltattorni, A. Minelli, 1971, FEBS letters.

The Binding of Coenzymes and Analogues of the Substrate‐Coenzyme Complex to Tyrosine Aminotransferase

C. Turano, C. Voltattorni, F. Conti, 1975 .

Crystal structure of the S187F variant of human liver alanine: Aminotransferase associated with primary hyperoxaluria type I and its functional implications

M. Wilmanns, A. Paiardini, K. Fodor, 2013, Proteins.

Phosphorylation of pyridoxal 5′-phosphate enzymes: an intriguing and neglected topic

M. Bertoldi, R. Phillips, A. Astegno, 2017, Amino Acids.

Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants.

R. Montioli, C. Voltattorni, B. Cellini, 2011, Biochimica et biophysica acta.

Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I

A. Paiardini, Elisa Oppici, R. Montioli, 2010, Proceedings of the National Academy of Sciences.

Molecular Insight into the Synergism between the Minor Allele of Human Liver Peroxisomal Alanine:Glyoxylate Aminotransferase and the F152I Mutation*

A. Paiardini, R. Montioli, Antonio Lorenzetto, 2009, Journal of Biological Chemistry.

Dimerization and folding processes of Treponema denticola cystalysin: the role of pyridoxal 5'-phosphate.

D. Laurents, A. Paiardini, M. Bertoldi, 2006, Biochemistry.

Aromatic amino acid decarboxylase deficiency: Molecular and metabolic basis and therapeutic outlook.

N. Blau, M. Bertoldi, B. Thöny, 2019, Molecular genetics and metabolism.

A comprehensive picture of the mutations associated with aromatic amino acid decarboxylase deficiency: from molecular mechanisms to therapy implications.

A. Giorgetti, Stefano Piccoli, R. Montioli, 2014, Human molecular genetics.

S250F variant associated with aromatic amino acid decarboxylase deficiency: molecular defects and intracellular rescue by pyridoxine.

Elisa Oppici, R. Montioli, Mirco Dindo, 2013, Human molecular genetics.

An engineered folded PLP‐bound monomer of Treponema denticola cystalysin reveals the effect of the dimeric structure on the catalytic properties of the enzyme

A. Paiardini, M. Bertoldi, R. Montioli, 2009, Proteins.

Holo- and apo-cystalysin from Treponema denticola: two different conformations.

D. Laurents, M. Bertoldi, A. Bossi, 2006, Archives of biochemistry and biophysics.

Spectroscopic and kinetic analyses reveal the pyridoxal 5'-phosphate binding mode and the catalytic features of Treponema denticola cystalysin.

M. Bertoldi, T. Clausen, C. Voltattorni, 2002, Biochemistry.

Mutation of Tyrosine 332 to Phenylalanine Converts Dopa Decarboxylase into a Decarboxylation-dependent Oxidative Deaminase*

M. Bertoldi, C. Voltattorni, R. Contestabile, 2002, The Journal of Biological Chemistry.

Interaction of aromatic amino acids in D and L forms with 3,4-dihydroxyphenylalanine decarboxylase from pig kidney.

C. Voltattorni, P. Dominici, A. Minelli, 1983, Biochemistry.

Purification and characterization of 3,4-dihydroxyphenylalanine decarboxyase from pig kidney.

C. Turano, C. Voltattorni, A. Minelli, 1979, European journal of biochemistry.

Dopa decarboxylase exhibits low pH half‐transaminase and high pH oxidative deaminase activities toward serotonin (5‐hydroxytryptamine)

M. Bertoldi, C. Voltattorni, 2001 .

Green tea polyphenols: novel irreversible inhibitors of dopa decarboxylase.

M. Bertoldi, C. Voltattorni, M. Gonsalvi, 2001, Biochemical and biophysical research communications.

Inhibitors binding to L-aromatic amino acid decarboxylase.

C. Voltattorni, M. A. Rosei, M. d'Erme, 1982, Life sciences.

An abnormal reaction occurring in the presence of L-aromatic aminoacid decarboxylase.

C. Turano, C. Voltattorni, M. A. Rosei, 1981, Biochemical and biophysical research communications.

Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis

A. Paiardini, F. Cutruzzolà, G. Giardina, 2017, Scientific Reports.

Reactions of DOPA (3,4-dihydroxyphenylalanine) decarboxylase with DOPA.

C. Voltattorni, R. John, A. Minelli, 1979, The Biochemical journal.

Subunit structure of 3, 4-dihydroxyphenylalanine decarboxylase from pig kidney.

D. Barra, C. Turano, C. Voltattorni, 1982, Archives of Biochemistry and Biophysics.

An engineered folded PLP‐bound monomer of Treponema denticola cystalysin reveals the effect of the dimeric structure on the catalytic properties of the enzyme

A. Paiardini, M. Bertoldi, R. Montioli, 2009, Proteins.

Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases

S. Gianni, A. Paiardini, F. Cutruzzolà, 2011, Proceedings of the National Academy of Sciences of the United States of America.

The novel R347g pathogenic mutation of aromatic amino acid decarboxylase provides additional molecular insights into enzyme catalysis and deficiency.

A. Paiardini, M. Bertoldi, S. Heales, 2016, Biochimica et biophysica acta.

Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes.

P. Moore, C. Voltattorni, P. Dominici, 1996, The Biochemical journal.

Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions.

M. Bertoldi, C. Voltattorni, C. Borri Voltattorni, 2000, The Biochemical journal.