V. de Serrano

发表

Different modes of binding of mono-, di-, and trihalogenated phenols to the hemoglobin dehaloperoxidase from Amphitrite ornata.

Michael F. Davis, Franck A. P. Vendeix, S. Franzen, 2009, Biochemistry.

A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct

Junjie Zhao, S. Franzen, V. de Serrano, 2014, Biochemistry.

Peroxidase versus Peroxygenase Activity: Substrate Substituent Effects as Modulators of Enzyme Function in the Multifunctional Catalytic Globin Dehaloperoxidase.

R. Ghiladi, V. de Serrano, A. McGuire, 2018, Biochemistry.

X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.

Michael F. Davis, S. Franzen, V. de Serrano, 2008, Acta crystallographica. Section D, Biological crystallography.

Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.

Michael F. Davis, S. Franzen, B. Howes, 2010, Biophysical journal.

Bridging the functional gap between reactivity and inhibition in dehaloperoxidase B from Amphitrite ornata: Mechanistic and structural studies with 2,4- and 2,6-dihalophenols.

R. Ghiladi, V. de Serrano, L. Carey, 2022, Journal of inorganic biochemistry.

Involvement of tyrosine-76 of the kringle 2 domain of tissue-type plasminogen activator in its thermal stability and its omega-amino acid ligand binding site.

F. Castellino, V. de Serrano, 1994, Biochemistry.

Specific anionic residues of the recombinant kringle 2 domain of tissue-type plasminogen activator that are responsible for stabilization of its interaction with omega-amino acid ligands.

F. Castellino, V. de Serrano, 1993, Biochemistry.

The cationic locus on the recombinant kringle 2 domain of tissue-type plasminogen activator that stabilizes its interaction with omega-amino acids.

F. Castellino, V. de Serrano, 1992, Biochemistry.

Role of tryptophan-74 of the recombinant kringle 2 domain of tissue-type plasminogen activator in its omega-amino acid binding properties.

F. Castellino, V. de Serrano, 1992, Biochemistry.

Oxidation of bisphenol A (BPA) and related compounds by the multifunctional catalytic globin dehaloperoxidase.

R. Ghiladi, V. de Serrano, Dongju Yun, 2022, Journal of inorganic biochemistry.

X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond.

Michael F. Davis, R. Rose, S. Franzen, 2010, Acta crystallographica. Section D, Biological crystallography.

Purification and properties of a plasminogen activator from cultured rat prostate adenocarcinoma cells.

F. Castellino, D. Strickland, S. Chan, 1983, Biochemistry.

The activation of human [Glu1]plasminogen by human single-chain urokinase.

F. Castellino, P. Gaffney, T. Urano, 1988, Archives of biochemistry and biophysics.

Pirin is an iron-dependent redox regulator of NF-κB

Lirong Chen, I. Rehmani, Fange Liu, 2013, Proceedings of the National Academy of Sciences.

Organic solvents order the dynamic switch II in Ras crystals.

Carla Mattos, C. Mattos, G. Buhrman, 2003, Structure.

The role of the distal histidine in H2O2 activation and heme protection in both peroxidase and globin functions.

Junjie Zhao, S. Franzen, R. Ghiladi, 2012, The journal of physical chemistry. B.

Functional consequences of the creation of an Asp-His-Fe triad in a 3/3 globin.

S. Franzen, R. Ghiladi, H. Gracz, 2011, Biochemistry.

Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata.

L. Betts, S. Franzen, V. de Serrano, 2009, Acta crystallographica. Section D, Biological crystallography.

Examination of the secondary structure of the kringle 4 domain of human plasminogen.

J. M. Beals, F. Castellino, W. Johnson, 1986, Archives of biochemistry and biophysics.

Roles for chloride ion and fibrinogen in the activation of [Glu1]plasminogen in human plasma.

F. Castellino, P. Gaffney, T. Urano, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap.

C. Mattos, N. Nicely, V. de Serrano, 2004, Structure.

Role of the strictly conserved tryptophan-25 residue in the stabilization of the structure and in the ligand binding properties of the kringle 2 domain of tissue-type plasminogen activator.

F. Castellino, V. de Serrano, 1994, Biochemistry.

A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenic Clostridium

E. Pozharski, Franz J. St John, D. Dietrich, 2018, The Biochemical journal.

The multifunctional globin dehaloperoxidase strikes again: Simultaneous peroxidase and peroxygenase mechanisms in the oxidation of EPA pollutants.

R. Ghiladi, V. de Serrano, A. McGuire, 2019, Archives of biochemistry and biophysics.

Structural and kinetic study of an internal substrate binding site in dehaloperoxidase-hemoglobin A from Amphitrite ornata.

Jing Zhao, S. Franzen, V. de Serrano, 2013, Biochemistry.

Structural evidence for stabilization of inhibitor binding by a protein cavity in the dehaloperoxidase-hemoglobin from Amphitrite ornata.

S. Franzen, V. de Serrano, 2011, Biopolymers.

Structure of dehaloperoxidase B at 1.58 A resolution and structural characterization of the AB dimer from Amphitrite ornata.

S. Franzen, R. Ghiladi, V. de Serrano, 2010, Acta crystallographica. Section D, Biological crystallography.

Direct identification of lysine-33 as the principal cationic center of the omega-amino acid binding site of the recombinant kringle 2 domain of tissue-type plasminogen activator.

F. Castellino, V. de Serrano, L. Sehl, 1992, Archives of biochemistry and biophysics.

Pirin is an iron-dependent redox regulator of NF-κB

Lirong Chen, I. Rehmani, Fange Liu, 2013, Proceedings of the National Academy of Sciences.