I. Fita

发表

Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.

F. Gil-Ortiz, V. Rubio, A. Marina, 2002, Structure.

Complete Reversal of Coenzyme Specificity by Concerted Mutation of Three Consecutive Residues in Alcohol Dehydrogenase*

Ignacio Fita, J. Farrés, X. Parés, 2003, Journal of Biological Chemistry.

Structure of the complex of an Fab fragment of a neutralizing antibody with foot‐and‐mouth disease virus: positioning of a highly mobile antigenic loop

D I Stuart, D. Stuart, E. Domingo, 1997, The EMBO journal.

The refined structure of beef liver catalase at 2·5 Å resolution

M. Murthy, M. Rossmann, A. M. Silva, 1986 .

Vibrational entropy of a protein: large differences between distinct conformations.

J. Rubí, I. Fita, M. Goethe, 2015, Journal of chemical theory and computation.

Testing the mutual information expansion of entropy with multivariate Gaussian distributions.

J. Rubí, I. Fita, M. Goethe, 2017, The Journal of chemical physics.

Catalase-peroxidases (KatG) Exhibit NADH Oxidase Activity*

H. Duckworth, L. Donald, Rahul Singh, 2004, Journal of Biological Chemistry.

Apo and Holo structures of an NADPH-dependent cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae.

X. Parés, I. Fita, Eva Valencia, 2004, Journal of molecular biology.

Structural Insights into Subunits Assembly and the Oxyester Splicing Mechanism of Neq pol Split Intein.

A. Benito, I. Usón, M. Vilanova, 2018, Cell chemical biology.

Aldo-keto reductases from the AKR1B subfamily: retinoid specificity and control of cellular retinoic acid levels.

R. Álvarez, C. Rovira, A. D. de Lera, 2009, Chemico-biological interactions.

Review Diversity of structures and properties among catalases

P. Loewen, I. Fita, P. Chelikani, 2004 .

Correction: Selective photoregulation of the activity of glycogen synthase and glycogen phosphorylase, two key enzymes in glycogen metabolism.

J. Guinovart, I. Fita, D. Velasco, 2015, Organic & biomolecular chemistry.

Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi.

J. Farrés, X. Parés, I. Fita, 2003, Acta crystallographica. Section D, Biological crystallography.

Spectroscopic and kinetic investigation of the reactions of peroxyacetic acid with Burkholderia pseudomallei catalase-peroxidase, KatG.

L. Donald, A. Ivancich, B. Wiseman, 2013, Biochemistry.

Thermal motion in proteins: Large effects on the time-averaged interaction energies

J. Rubí, I. Fita, M. Goethe, 2016 .

Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium

A. Frangakis, E. Querol, J. Piñol, 2020, Nature Communications.

Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli

W. Ens, J. Bravo, J. Ferrer, 1997, Protein science : a publication of the Protein Society.

The immunodominant protein P116 extracts cholesterol and other essential lipids

A. Frangakis, J. Piñol, N. Rotllan, 2022, bioRxiv.

The Structure of Human 4F2hc Ectodomain Provides a Model for Homodimerization and Electrostatic Interaction with Plasma Membrane*

M. Orozco, J. Fernández-Recio, J. Turnay, 2007, Journal of Biological Chemistry.

Oxygen Binding to Catalase-Peroxidase

Pietro Vidossich, C. Rovira, P. Loewen, 2011 .

A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules.

E. Domingo, S. Kalko, M. G. Mateu, 2000, The Journal of general virology.

Structure of catalase HPII from Escherichia coli at 1.9 Å resolution

K. Wilson, J. Bravo, K. Wilson, 1999, Proteins.

Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution.

P. Loewen, S. Mongkolsuk, S. Loprasert, 2003, Journal of molecular biology.

Structure of foot-and-mouth disease virus particles.

E. Domingo, F. Sobrino, I. Fita, 2004 .

The structures and electronic configuration of compound I intermediates of Helicobacter pylori and Penicillium vitale catalases determined by X-ray crystallography and QM/MM density functional theory calculations.

G. Murshudov, M. Alfonso-Prieto, C. Rovira, 2007, Journal of the American Chemical Society.

Theoretical study of the mechanisms of substrate recognition by catalase.

M. Orozco, J. Gelpí, S. Kalko, 2001, Journal of the American Chemical Society.

Enzymology and structure of catalases

P. Nicholls, P. Loewen, I. Fita, 2000 .

L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

J. Fernández-Recio, E. Pardon, J. Steyaert, 2019, Nature Communications.

The nucleotide-bound/substrate-bound conformation of the Mycoplasma genitalium DnaK chaperone.

L. Martinelli, I. Fita, B. Calisto, 2018 .

Thirty years of heme catalases structural biology.

P. Loewen, I. Fita, X. Carpena, 2012, Archives of biochemistry and biophysics.

Phosphaturic Mesenchymal Tumor of the Pelvis: A Multidisciplinary Approach

I. Fita, Leonardo M. Cullari, Sebastián Senes, 2022 .

Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 Å resolution.

P. Loewen, I. Fita, X. Carpena, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Efficient neutralization of foot-and-mouth disease virus by monovalent antibody binding

E. Domingo, M. G. Mateu, N. Verdaguer, 1997, Journal of virology.

Synthesis of bis(pentachlorophenyl) silanediol and related compounds. Crystal structure of diethoxybis(pentachlorophenyl) silane

N. Verdaguer, I. Fita, L. Fajarí, 1992 .

Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors

E. Querol, J. Piñol, I. Fita, 2018, Nature Communications.

Crystallization of the lipoxygenase of Pseudomonas aeruginosa 42A2, evolution and phylogenetic study of the subfamilies of the lipoxygenases

A. Garreta, I. Fita, X. Carpena, 2011 .

Crystallization and preliminary X-ray analysis of the hydroperoxidase I C-terminal domain from Escherichia coli.

P. Alzari, J. Ferrer, A. Guarné, 2002, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray analysis of clade I catalases from Pseudomonas syringae and Listeria seeligeri.

M. Klotz, N. Verdaguer, P. Loewen, 2001, Acta crystallographica. Section D, Biological crystallography.

N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms.

V. Rubio, A. Marina, S. Ramón-Maiques, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary structural results of catalase from human erythrocytes.

M. Maté, A. Marina, I. Fita, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae

J. Bravo, P. Alzari, M. Maté, 1997, Protein science : a publication of the Protein Society.

Crystallization, characterization, and preliminary crystallographic studies of mitochondrial carbamoyl phosphate synthetase I of Rana catesbeiana

V. Rubio, J. Bravo, A. Marina, 1995, Proteins.

Crystallization and preliminary x‐ray diffraction studies of a monoclonal antibody fab fragment against foot‐and‐mouth disease virus and of its complex with the main antigenic site peptide

E. Domingo, E. Giralt, J. Bravo, 1994, Proteins.

Crystallization and preliminary X-ray diffraction analysis of catalase HPII from Escherichia coli.

J. Tormo, P. Loewen, I. Fita, 1990, Journal of molecular biology.

The immunodominant protein P116 is a passive transporter of cholesterol and other essential lipids

A. Frangakis, J. Piñol, N. Rotllan, 2022 .

Investigation of shape variations in the antibody binding site by molecular dynamics computer simulation.

A. Mark, W. V. van Gunsteren, J. Tormo, 1994, Journal of molecular biology.

Structure of the Dimeric Exonuclease TREX1 in Complex with DNA Displays a Proline-rich Binding Site for WW Domains*

M. Macias, A. Celada, J. Lloberas, 2007, Journal of Biological Chemistry.

Crystallization and preliminary X-ray analysis of swine vesicular disease virus (SVDV).

N. Verdaguer, V. Ley, M. Jiménez-Clavero, 2003, Acta crystallographica. Section D, Biological crystallography.

Diversity of structures and properties among catalases

P. Loewen, I. Fita, P. Chelikani, 2003, Cellular and Molecular Life Sciences CMLS.

Structure of the major antigenic loop of foot‐and‐mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg‐Gly‐Asp motif in the interaction.

E. Domingo, E. Giralt, M. G. Mateu, 1995, EMBO Journal.

Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation.

Michael M. H. Graf, S. Hofbauer, C. Obinger, 2015, Biochemistry.

Preliminary analysis of two and three dimensional crystals of vault ribonucleoprotein particles.

J. Carrascosa, N. Verdaguer, J. Castón, 2005, Journal of structural biology.

Ca2+ bridges the C2 membrane‐binding domain of protein kinase Cα directly to phosphatidylserine

N. Verdaguer, S. Corbalán-García, J. Gomez-Fernandez, 1999 .

Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae

K. Namba, A. Frangakis, María Lluch-Senar, 2020, Nature Communications.

Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors

E. Querol, J. Piñol, I. Fita, 2018, Nature Communications.

Structural characterization of the NAP; the major adhesion complex of the human pathogen Mycoplasma genitalium

A. Frangakis, E. Querol, J. Piñol, 2017, Molecular microbiology.

Cyclic peptides as conformationally restricted models of viral antigens: application to foot-and-mouth disease virus.

E. Domingo, E. Giralt, M. G. Mateu, 1995, Biomedical peptides, proteins & nucleic acids : structure, synthesis & biological activity.

An Electrical Potential in the Access Channel of Catalases Enhances Catalysis*

P. Loewen, I. Fita, X. Carpena, 2003, Journal of Biological Chemistry.

Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli

J. Bravo, M. Maté, P. Loewen, 2001, Proteins.

Role of the lateral channel in catalase HPII of Escherichia coli

M. Maté, I. Fita, J. Switala, 2008, Protein science : a publication of the Protein Society.

Structure of catalase-A from Saccharomyces cerevisiae.

C. Betzel, P. Alzari, M. Maté, 1999, Journal of molecular biology.

Structure of the Heme d of Penicillium vitale and Escherichia coli Catalases (*)

B. Vainshtein, Z. Dauter, J. Bravo, 1996, The Journal of Biological Chemistry.

Crystal structure of catalase HPII from Escherichia coli.

C. Betzel, J. Bravo, J. Tormo, 1995, Structure.

Comparison of beef liver and Penicillium vitale catalases.

M. Murthy, M. Rossmann, B. Vainshtein, 1986, Journal of molecular biology.

The active center of catalase.

M. Rossmann, I. Fita, Michael G. Rossmann, 1985, Journal of molecular biology.

Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli.

V. Jha, P. Loewen, I. Fita, 2012, Archives of biochemistry and biophysics.

Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli.

L. Donald, V. Jha, P. Loewen, 2011, Biochemistry.

Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 Å resolution

M. Klotz, H. Duckworth, L. Donald, 2003, Proteins.

Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases*

C. Obinger, Pietro Vidossich, C. Rovira, 2009, The Journal of Biological Chemistry.

Crystal Structure of the NADP(H)-Dependent Cinnamyl Alcohol Dehydrogenase from Saccharomyces cerevisiae

X. Parés, I. Fita, Eva Valencia, 2004 .

Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8).

J. Farrés, X. Parés, I. Fita, 2003, Journal of molecular biology.

Molecular structure of the A-tract DNA dodecamer d(CGCAAATTTGCG) complexed with the minor groove binding drug netropsin.

A. Rich, G. A. van der Marel, L. Tabernero, 1993, Biochemistry.

Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains.

N. Verdaguer, S. Corbalán-García, J. Gomez-Fernandez, 2001, Journal of molecular biology.

Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution.

M. Rossmann, B. Vainshtein, V. Borisov, 1983, Journal of molecular biology.

Arginine and nitrogen storage.

V. Rubio, I. Fita, J. Llácer, 2008, Current opinion in structural biology.

Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis

V. Rubio, I. Fita, L. M. Polo, 2015, Scientific Reports.

The dynamic role of distal side residues in heme hydroperoxidase catalysis. Interplay between X-ray crystallography and ab initio MD simulations.

M. Alfonso-Prieto, Pietro Vidossich, C. Rovira, 2010, Archives of biochemistry and biophysics.

Molecular structure of a complete turn of A-DNA.

T. Huynh-Dinh, J. A. Subirana, N. Verdaguer, 1991, Journal of molecular biology.

Lyase activity of glycogen synthase: Is an elimination/addition mechanism a possible reaction pathway for retaining glycosyltransferases?

J. Guinovart, I. Fita, M. Díaz‐Lobo, 2012, IUBMB life.

Entropic Stabilization of Cas4 Protein SSO0001 Predicted with Popcoen

J. Miguel Rubi, Martin Goethe, Ignacio Fita, 2018, Entropy.

Prediction of Protein Configurational Entropy (Popcoen).

Martin Goethe, Ignacio Fita, Jan Gleixner, 2018, Journal of chemical theory and computation.

Membrane Binding C2-Like Domains

N. Verdaguer, S. Corbalán-García, J. Gomez-Fernandez, 2011 .

Structure of human rhinovirus serotype 2 (HRV2).

N. Verdaguer, D. Blaas, I. Fita, 2000, Journal of molecular biology.

Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa

A. Oliver, A. Garreta, A. Ortiz, 2013, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

A Major Determinant for Gliding Motility in Mycoplasma genitalium

E. Querol, J. Piñol, D. Lalli, 2014, The Journal of Biological Chemistry.

Essential protein P116 extracts cholesterol and other indispensable lipids for Mycoplasmas

A. Frangakis, J. Piñol, N. Rotllan, 2023, Nature Structural & Molecular Biology.

Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation.

Giacomo Fiorin, Ignacio Fita, Pietro Vidossich, 2014, The journal of physical chemistry. B.

Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations.

Ignacio Fita, F. Gil-Ortiz, V. Rubio, 2010, Journal of molecular biology.

Characterization of a large subunit catalase truncated by proteolytic cleavage.

H. Duckworth, L. Donald, P. Loewen, 2005, Biochemistry.

Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei.

Rahul Singh, B. Wiseman, P. Loewen, 2005, Journal of molecular biology.

Structure and Function of Picornavirus Proteinases

M. James, A. Guarné, T. Skern, 2002 .

Truncation and heme pocket mutations reduce production of functional catalase HPII in Escherichia coli.

J. Bravo, P. Loewen, I. Fita, 1998, Protein engineering.

The EAGR box structure: a motif involved in mycoplasma motility

E. Querol, J. Piñol, L. Martinelli, 2012, Molecular microbiology.

A first principles study of the binding of formic acid in catalase complementing high resolution X-ray structures

M. Alfonso-Prieto, X. Biarnés, C. Rovira, 2006 .

Mutants That Alter the Covalent Structure of Catalase Hydroperoxidase II from Escherichia coli*

W. Ens, J. Bravo, M. Maté, 1999, The Journal of Biological Chemistry.

Characterization of the Catalase-Peroxidase KatG from Burkholderia pseudomallei by Mass Spectrometry*

Ignacio Fita, Rahul Singh, H. Duckworth, 2003, Journal of Biological Chemistry.

Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli.

P. Loewen, I. Fita, X. Carpena, 2004, Acta crystallographica. Section D, Biological crystallography.

KatG-Mediated Oxidation Leading to Reduced Susceptibility of Bacteria to Kanamycin

L. Donald, P. Loewen, I. Fita, 2018, ACS omega.

Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.

B. Herguedas, Rahul Singh, A. Ivancich, 2006, Biochemistry.

Structure of Swine Vesicular Disease Virus: Mapping of Changes Occurring during Adaptation of Human Coxsackie B5 Virus To Infect Swine

N. Verdaguer, V. Ley, M. Jiménez-Clavero, 2003, Journal of Virology.

Two alternative substrate paths for compound I formation and reduction in catalase–peroxidase KatG from Burkholderia pseudomallei

A. Ivancich, B. Wiseman, I. Fita, 2006, Proteins.

A molecular switch and electronic circuit modulate catalase activity in catalase‐peroxidases

Rahul Singh, A. Ivancich, B. Wiseman, 2005, EMBO reports.

Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine

V. Rubio, J. Bravo, P. Alzari, 2008, Protein science : a publication of the Protein Society.

Three-dimensional Structure and Enzymatic Function of Proapoptotic Human p53-inducible Quinone Oxidoreductase PIG3*

U. Oppermann, A. Pike, J. Farrés, 2009, The Journal of Biological Chemistry.

Processivity and Subcellular Localization of Glycogen Synthase Depend on a Non-catalytic High Affinity Glycogen-binding Site*

J. Ferrer, J. Guinovart, I. Fita, 2011, The Journal of Biological Chemistry.

Molecular basis of substrate-induced permeation by an amino acid antiporter

G. Portella, M. Orozco, M. Palacín, 2011, Proceedings of the National Academy of Sciences.

Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes.

J. Tormo, A. Guarné, B. Hampoelz, 2000, Journal of molecular biology.

The nucleotide‐bound/substrate‐bound conformation of the Mycoplasma genitalium DnaK chaperone

L. Martinelli, I. Fita, B. Calisto, 2018, Protein science : a publication of the Protein Society.

3 Abbreviations NBD , Nucleotide Binding Domain SBD , Substrate Binding Domain PMF , Peptide Mass Fingerprinting

L. Martinelli, I. Fita, B. Calisto, 2018 .

Structural and biochemical studies of TREX1 inhibition by metals. Identification of a new active histidine conserved in DEDDh exonucleases

A. Celada, J. Lloberas, M. Brucet, 2008, Protein science : a publication of the Protein Society.

Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium.

Enrique Querol, Jaume Piñol, Ignacio Fita, 2005, Journal of molecular biology.

The structures of picornaviral proteinases.

M. James, W. Sommergruber, A. Guarné, 1999, Virus research.

A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

A. Guarné, T. Skern, I. Fita, 1998, The Journal of general virology.

Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus.

E. Domingo, J. Bravo, M. G. Mateu, 1996, Journal of molecular biology.

Docking of a human rhinovirus neutralizing antibody onto the viral capsid

J. Tormo, D. Blaas, I. Fita, 1995, Proteins.

Structure-Guided Mutations in the Terminal Organelle Protein MG491 Cause Major Motility and Morphologic Alterations on Mycoplasma genitalium

E. Querol, J. Piñol, L. Martinelli, 2016, PLoS pathogens.

The subunit structure of chromatin fibres

S. Muñoz-Guerra, J. A. Subirana, I. Fita, 2004, Chromosoma.

The structure of a T = 1 icosahedral empty particle from southern bean mosaic virus.

M. Murthy, M. Rossmann, J. Erickson, 1985, Science.

Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution.

A. Ivancich, C. Rovira, P. Nicholls, 2004, Biochemistry.

The NADPH binding site on beef liver catalase.

M G Rossmann, M. Rossmann, I. Fita, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Insight on an Arginine Synthesis Metabolon from the Tetrameric Structure of Yeast Acetylglutamate Kinase

F. Gil-Ortiz, V. Rubio, M. Crabeel, 2012, PloS one.

Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies.

F. Gil-Ortiz, V. Rubio, M. L. Fernández-Murga, 2002, Acta crystallographica. Section D, Biological crystallography.

The Carbamoyl-phosphate Synthetase of Pyrococcus furiosus Is Enzymologically and Structurally a Carbamate Kinase*

V. Rubio, A. Marina, S. Ramón-Maiques, 1999, The Journal of Biological Chemistry.

Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa.

Alexei Vagin, Ignacio Fita, F. Gil-Ortiz, 2006, Journal of molecular biology.

The structure of alfalfa mosaic virus capsid protein assembled as a T=1 icosahedral particle at 4.0-A resolution

John E. Johnson, M. Rossmann, T. Baker, 1997, Journal of virology.

Structural and mechanistic insights into the association of PKCα-C2 domain to PtdIns(4,5)P2

N. Verdaguer, S. Corbalán-García, J. Gomez-Fernandez, 2009, Proceedings of the National Academy of Sciences.

A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase.

Ignacio Fita, Javier Cervera, C. Marco-Marín, 2007, Journal of molecular biology.

Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha.

R. Eritja, N. Verdaguer, S. Corbalán-García, 2002, Journal of molecular biology.

Crystal structure of myeloperoxidase from human leukocytes

C. Obinger, I. Fita, X. Carpena, 2009 .

Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10

Angel R de Lera, Ignacio Fita, C. Rovira, 2007, Proceedings of the National Academy of Sciences.

Structural Asymmetry and Disulfide Bridges among Subunits Modulate the Activity of Human Malonyl-CoA Decarboxylase*

P. Loewen, I. Fita, X. Carpena, 2013, The Journal of Biological Chemistry.

Activity of Human Malonyl-CoA Bridges among Subunits Modulate the Structural Asymmetry and Disulfide Protein Structure and Folding :

I. Fita, Péter, Xavier, 2013 .

High Conformational Stability of Secreted Eukaryotic Catalase-peroxidases

C. Obinger, M. Zámocký, P. Loewen, 2012, The Journal of Biological Chemistry.

L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction

J. Fernández-Recio, E. Pardon, J. Steyaert, 2019, Nature Communications.

Crystal Structure of Brucella abortus Deoxyxylulose-5-phosphate Reductoisomerase-like (DRL) Enzyme Involved in Isoprenoid Biosynthesis*♦

T. Kurz, Christoph T. Behrendt, Jordi Perez-Gil, 2012, The Journal of Biological Chemistry.

Biosynthesis of isoprenoids in plants: Structure of the 2C‐methyl‐d‐erithrytol 2,4‐cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes

M. Bergua, Jordi Perez-Gil, I. Fita, 2007, Protein science : a publication of the Protein Society.

X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein

N. Verdaguer, D. Blaas, I. Fita, 2004, Nature Structural &Molecular Biology.

Structure of d(CACGTG), a Z-DNA hexamer containing AT base pairs.

T. Huynh-Dinh, J. A. Subirana, I. Fita, 1988, Nucleic acids research.

“ Additional binding sites for anionic phospholipids and Ca 2 + ions in the crystal structures of complexes of the C 2 domain of protein kinase

R. Eritja, N. Verdaguer, S. Corbalán-García, 2016 .

Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria.

Alberto Marina, Ignacio Fita, F. Gil-Ortiz, 2010, Journal of molecular biology.

The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic.

Ignacio Fita, F. Gil-Ortiz, V. Rubio, 2003, Journal of molecular biology.

Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O2 Release Mediated by Proton-Coupled Electron Transfer.

C. Rovira, Binju Wang, I. Fita, 2018, Chemistry.

Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine.

N. Verdaguer, S. Corbalán-García, J. Gomez-Fernandez, 1999, The EMBO journal.

Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti‐HRV2 neutralizing antibody

M. Pons, I. Fita, M. A. Molins, 1998, Journal of peptide science : an official publication of the European Peptide Society.

1 Arginine and Nitrogen Storage

V. Rubio, I. Fita, J. Llácer, 2008 .

The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine

Asunción Contreras, Ignacio Fita, C. Marco-Marín, 2007, Proceedings of the National Academy of Sciences.

Electronic state of the molecular oxygen released by catalase.

M. Alfonso-Prieto, Pietro Vidossich, C. Rovira, 2008, The journal of physical chemistry. A.

Versatility of the electronic structure of compound I in catalase-peroxidases.

M. Alfonso-Prieto, Pietro Vidossich, C. Rovira, 2007, Journal of the American Chemical Society.

The need for a shared database infrastructure: combining X-ray crystallography and electron microscopy

Mónica Chagoyen, Natalia Jiménez-Lozano, Susana G. Kalko, 2000, European Biophysics Journal.

Structure of the stacked cyclic oligoamides: 1,6‐diaza‐2,7‐cyclodecadione and 1,5,9‐triaza‐2,6,10‐cyclododecatrione. A ring model of the α‐helix

V. Tereshko, J. A. Subirana, I. Fita, 1994 .

Alternative conformation of the C-domain of the P140 protein from Mycoplasma genitalium.

I. Fita, Jesús Martín, D. Aparicio, 2020, Acta crystallographica. Section F, Structural biology communications.

Crystal Structure of an Archaeal Glycogen Synthase

J. Ferrer, J. Guinovart, I. Fita, 2006, Journal of Biological Chemistry.

Crystal structure of a substrate-bound amino acid antiporter in the outward open conformation: mechanism of substrate recognintion and transport.

Ignacio Fita, L Kowalcyk, Manuel Palacín, 2011 .

Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases*

M. Pons, L. Donald, B. Wiseman, 2010, The Journal of Biological Chemistry.

Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei.

P. Loewen, S. Mongkolsuk, S. Loprasert, 2002, Acta crystallographica. Section D, Biological crystallography.

Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization

M. Mulero, E. Serrano-Candelas, Álvaro Aranguren-Ibáñez, 2015, PloS one.

An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.

Pietro Vidossich, C. Rovira, P. Loewen, 2014, Journal of the American Chemical Society.

The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.

Bruno L. Victor, C. Rovira, M. Machuqueiro, 2017, Biochemistry.

Molecular structure of L-lysyl-L-tyrosyl-L-serine acetate.

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