J. Arolas

发表

A Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane Metallopeptidases*

M. Martí-Renom, C. López-Otín, Francisco Martínez-Jiménez, 2013, The Journal of Biological Chemistry.

Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties.

F. Avilés, A. Rovira, S. Ventura, 2004, Biochemistry.

The pCri System: A Vector Collection for Recombinant Protein Expression and Purification

R. Glockshuber, R. García-Castellanos, T. Goulas, 2014, PloS one.

Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin

K. Djinović-Carugo, T. Marlovits, E. Ribeiro, 2020, Proceedings of the National Academy of Sciences.

Cytotoxicity studies of [PtCl2(H2bim)] (H2bim = 2,2′-biimidazole): Study of its interaction with a small protein PCI (potato carboxypeptidase inhibitor)

F. Avilés, A. Sánchez-González, V. Moreno, 2009 .

The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B.

Francesc X Aviles, David Pantoja-Uceda, F. Avilés, 2008, Biochemistry.

Insights into the two-domain architecture of the metallocarboxypeptidase inhibitor from the Ascaris parasite inferred from the mechanism of its oxidative folding.

F. Avilés, J. Lorenzo, Sílvia Bronsoms, 2009, Biochemistry.

Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite

R. Huber, F. Avilés, F. Gomis-Rüth, 2009, Proceedings of the National Academy of Sciences.

Recombinant expression of disulfide-rich proteins: carboxypeptidase inhibitors as model proteins

F. Avilés, J. Lorenzo, Sílvia Bronsoms, 2006 .

Metallocarboxypeptidases: emerging drug targets in biomedicine.

F. Avilés, L. Fricker, J. Arolas, 2007, Current pharmaceutical design.

The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases

J. Potempa, F. Gomis-Rüth, K. Nguyen, 2011, Molecular microbiology.

Multiple Architectures and Mechanisms of Latency in Metallopeptidase Zymogens.

T. Goulas, F. Gomis-Rüth, J. Arolas, 2018, Chemical reviews.

Structural and functional studies on proteinaceous metallocarboxypeptidase inhibitors

J. Arolas, 2005 .

A Carboxypeptidase Inhibitor from the Tick Rhipicephalus bursa

F. Avilés, A. Rovira, J. Lorenzo, 2005, Journal of Biological Chemistry.

Role of Kinetic Intermediates in the Folding of Leech Carboxypeptidase Inhibitor*

F. Avilés, S. Ventura, J. Lorenzo, 2004, Journal of Biological Chemistry.

Protease inhibitors as models for the study of oxidative folding.

S. Ventura, J. Arolas, 2011, Antioxidants & redox signaling.

Characterizing the Tick Carboxypeptidase Inhibitor

J. Calvete, F. Avilés, S. Ventura, 2006, Journal of Biological Chemistry.

The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode.

Robert Huber, Francesc X Aviles, R. Huber, 2005, Journal of molecular biology.

Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin

R. Konrat, D. Svergun, M. Gautel, 2021, Science Advances.

Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver

F. Avilés, J. Lorenzo, F. Gomis-Rüth, 2010, Journal of Molecular Biology.

Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis.

J. Enghild, F. Avilés, I. Pallarès, 2008, Molecular cell.

Folding of small disulfide-rich proteins: clarifying the puzzle.

F. Avilés, S. Ventura, J. Arolas, 2006, Trends in biochemical sciences.

Mechanism of action of a Janus-faced single-domain protein inhibitor simultaneously targeting two peptidase classes

F. Gomis-Rüth, J. Arolas, S. Martínez-Rodríguez, 2013 .

Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond.

R. Huber, T. Holak, G. Popowicz, 2005, Journal of molecular biology.

Oxidative folding and structural analyses of a Kunitz-related inhibitor and its disulfide intermediates: functional implications.

Francesc X Aviles, David Pantoja-Uceda, F. Avilés, 2011, Journal of molecular biology.

Deciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase Inhibitor*

F. Avilés, D. Pantoja-Uceda, S. Ventura, 2009, The Journal of Biological Chemistry.

Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function.

F. Avilés, S. Ventura, Sílvia Bronsoms, 2009, Journal of molecular biology.

The NMR Structures of the Major Intermediates of the Two-domain Tick Carboxypeptidase Inhibitor Reveal Symmetry in Its Folding and Unfolding Pathways*

F. Avilés, D. Pantoja-Uceda, S. Ventura, 2008, Journal of Biological Chemistry.

Scrambled Isomers as Key Intermediates in the Oxidative Folding of Ligand Binding Module 5 of the Low Density Lipoprotein Receptor*

F. Avilés, J. Sancho, S. Ventura, 2008, Journal of Biological Chemistry.

Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates.

F. Avilés, S. Ventura, Sílvia Bronsoms, 2008, Antioxidants & redox signaling.

NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.

T. Holak, G. Popowicz, F. Avilés, 2005, Structure.

Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog

Theodoros Goulas, T. Goulas, F. Gomis-Rüth, 2011, Proceedings of the National Academy of Sciences.

Structural evidence for standard-mechanism inhibition in metallopeptidases from a complex poised to resynthesize a peptide bond.

A. Vilcinskas, F. Gomis-Rüth, J. Arolas, 2011, Angewandte Chemie.

Insights into the molecular inactivation mechanism of human activated thrombin‐activatable fibrinolysis inhibitor

J. Enghild, F. Avilés, F. Gomis-Rüth, 2010, Journal of thrombosis and haemostasis : JTH.

A Novel Mechanism of Latency in Matrix Metalloproteinases*

J. Potempa, F. Gomis-Rüth, M. Lopez-pelegrin, 2015, The Journal of Biological Chemistry.

Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane

W. Bode, F. Gomis-Rüth, J. Arolas, 2012, Proceedings of the National Academy of Sciences.

Multiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidase.

P. Bernadó, Fátima Herranz-Trillo, F. Gomis-Rüth, 2014, Angewandte Chemie.

Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates*

J. Enghild, D. Otzen, F. Avilés, 2010, The Journal of Biological Chemistry.

Expression and purification of integral membrane metallopeptidase HtpX.

R. García-Castellanos, T. Goulas, F. Gomis-Rüth, 2014, Protein expression and purification.

Ultratight crystal packing of a 10 kDa protein.

W. Minor, M. Domagalski, M. Chruszcz, 2013, Acta crystallographica. Section D, Biological crystallography.

Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.

S. Leppla, T. Goulas, A. Pomerantsev, 2016, Structure.

A Novel Mechanism of Latency in Matrix Metalloproteinases*

J. Potempa, F. Gomis-Rüth, M. Lopez-pelegrin, 2015, The Journal of Biological Chemistry.

Insights into the molecular inactivation mechanism of human activated thrombin‐activatable fibrinolysis inhibitor

J. Enghild, F. Avilés, J. Arolas, 2010, Journal of thrombosis and haemostasis : JTH.

Ultratight crystal packing of a 10 kDa protein.

W. Minor, M. Domagalski, M. Chruszcz, 2013, Acta crystallographica. Section D, Biological crystallography.

The Structure of the Catalytic Domain of Tannerella Forsythia Karilysin Reveals It Is a Bacterial Xenolog of Animal Matrix Metalloproteinases Nih Public Access Author Manuscript

K. Nguyen, J. Arolas, M. Ksiazek, 2022 .