F. X. Avilés

发表

Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking.

M. Sternberg, P. Aloy, E. Querol, 2001, Journal of molecular biology.

The disulfide folding pathway of potato carboxypeptidase inhibitor.

E. Querol, F. X. Avilés, F. Canals, 1994, The Journal of biological chemistry.

Structures of scrambled disulfide forms of the potato carboxypeptidase inhibitor predicted by molecular dynamics simulations with constraints

M. Karplus, M. Martí-Renom, R. Stote, 2000, Proteins.

Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties.

E. Querol, F. X. Avilés, J. Vendrell, 2000, Biochimica et biophysica acta.

Molecular dynamics as a tool to help design mutants

O. Tapia, F. X. Avilés, B. Oliva, 1991 .

A molecular dynamics study of a model built Pro-36-Gly mutant derived from the potato carboxypeptidase A inhibitor protein.

O. Tapia, E. Querol, F. X. Avilés, 1991, Biochemical and biophysical research communications.

The structure of histone H1 and its location in chromatin

P. G. Hartman, James Allan, F. X. Avilés, 1980, Nature.

Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure prediction.

M. Sternberg, P. Bates, E. Querol, 1998, Journal of molecular biology.

Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily

F. X. Avilés, V. Companys, L. Fricker, 1999, The EMBO journal.

An automated classification of the structure of protein loops.

Baldomero Oliva, Francesc X. Avilés, Enrique Querol, 1997, Journal of molecular biology.

Expression of a synthetic gene encoding potato carboxypeptidase inhibitor using a bacterial secretion vector.

E. Querol, F. X. Avilés, M. Molina, 1992, Gene.

Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR

F. X. Avilés, J. Neira, S. Ventura, 2003, Proteins.

The central tryptic fragment of histones H1 and H5 is a fully compacted domain and is the only folded region in the polypeptide chain. A thermodynamic study.

P. Cary, P. Privalov, F. X. Avilés, 1982, European journal of biochemistry.

Characterization of the wound-induced metallocarboxypeptidase inhibitor from potato. cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C-terminal propeptide.

E. Querol, F. X. Avilés, J. Villanueva, 1998, FEBS letters.

Stability and fluctuations of the potato carboxypeptidase A protein inhibitor fold: a molecular dynamics study.

O. Tapia, E. Querol, F. X. Avilés, 1991, Biochemical and biophysical research communications.

Crystallization and preliminary X‐ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas

F. X. Avilés, F. Avilés, S. Ventura, 1995, FEBS letters.

Contribution of C-tail residues of potato carboxypeptidase inhibitor to the binding to carboxypeptidase A A mutagenesis analysis.

E. Querol, F. X. Avilés, B. Oliva, 2000, European journal of biochemistry.

The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.

G. Wider, M. Billeter, K. Wüthrich, 1991, The EMBO journal.

Three‐dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity.

R. Huber, F. X. Avilés, M. Coll, 1991, The EMBO journal.

Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B

R. Huber, G. Wider, M. Billeter, 1992, Journal of biomolecular NMR.

Effect of the reaction field electrostatic term on the molecular dynamics simulation of the activation domain of procarboxypeptidase B.

R. Gargallo, F. X. Avilés, E. Querol, 2000, Protein engineering.

The three‐dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.

R. Huber, F. X. Avilés, W. Bode, 1995, The EMBO journal.

Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulfide bond constraints.

M. Karplus, M. Martí-Renom, R. Stote, 1998, Journal of molecular biology.

C-tail valine is a key residue for stabilization of complex between potato inhibitor and carboxypeptidase A.

E. Querol, F. X. Avilés, B. Oliva, 1994, The Journal of biological chemistry.

Overproduction of a recombinant carboxypeptidase inhibitor by optimization of fermentation conditions

E. Querol, F. X. Avilés, C. Marino-Buslje, 1994, Applied Microbiology and Biotechnology.

M. Martí-Renom, P. Aloy, E. Querol, 1998, Journal of molecular biology.

Urea‐gradient gel electrophoresis studies on the association of procarboxypeptidases A and B, proproteinase E, and their tryptic activation products

F. X. Avilés, M. Vilanova, F. J. Burgos, 1985, FEBS letters.

Conformational flexibility in a highly mobile protein loop of foot-and-mouth disease virus: distinct structural requirements for integrin and antibody binding.

A. Villaverde, F. X. Avilés, A. Benito, 1998, Journal of molecular biology.

Monitoring the expression and purification of recombinant proteins by MALDI-TOF mass spectrometry.

E. Querol, F. X. Avilés, J. Villanueva, 2001, Enzyme and microbial technology.