Search Results - "VILLEGAS, VIRTUDES"

Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain by Villegas, Virtudes, Martı́nez, Jose C, Avilés, Francesc X, Serrano, Luis

“…The transition state for the folding pathway of the activation domain of human procarboxypeptidase A2 (ADA2h) has been analyzed by the protein engineering…”
Get full text

Impaired Binding Affinity of Electronegative Low-Density Lipoprotein (LDL) to the LDL Receptor Is Related to Nonesterified Fatty Acids and Lysophosphatidylcholine Content by Benítez, Sonia, Villegas, Virtudes, Bancells, Cristina, Jorba, Oscar, González-Sastre, Francesc, Ordóñez-Llanos, Jordi, Sánchez-Quesada, José Luis

“…The binding characteristics of electropositive [LDL(+)] and electronegative LDL [LDL(−)] subfractions to the LDL receptor (LDLr) were studied. Saturation…”
Get full text

Protein engineering as a strategy to avoid formation of amyloid fibrils by VILLEGAS, VIRTUDES, ZURDO, JESÚS, FILIMONOV, VLADIMIR V., AVILÉS, FRANCESC X., DOBSON, CHRISTOPHER M., SERRANO, LUIS

“…The activation domain of human procarboxypeptidase A2 (ADA2h) aggregates following thermal or chemical denaturation at acidic pH. The aggregated material…”
Get full text

The Structure of Human Prokallikrein 6 Reveals a Novel Activation Mechanism for the Kallikrein Family by Gomis-Rüth, F. Xavier, Bayés, Álex, Sotiropoulou, Georgia, Pampalakis, Georgios, Tsetsenis, Theodoros, Villegas, Virtudes, Avilés, Francesc X., Coll, Miquel

“…Zyme/protease M/neurosin/human kallikrein 6 (hK6) is a member of the human kallikrein family of trypsin-like serine proteinases and was originally identified…”
Get full text

The Unfolding Pathway of Leech Carboxypeptidase Inhibitor by Salamanca, Silvia, Villegas, Virtudes, Vendrell, Josep, Li, Li, Aviles, Francesc X., Chang, Jui-Yoa

“…The unfolding and denaturation curves of leech carboxypeptidase inhibitor (LCI) were elucidated using the technique of disulfide scrambling. In the presence of…”
Get full text

Monitoring disappearance of monomers and generation of resistance to proteolysis during the formation of the activation domain of human procarboxypeptidase A2 (ADA2h) amyloid fibrils by matrix-assisted laser-desorption ionization-time-of-flight-MS by Villanueva, Josep, Villegas, Virtudes, Querol, Enrique, Avilés, Francesc X, Serrano, Luis

“…The term 'amyloidosis' is used to represent a group of protein misfolding diseases characterized by the polymerization of normally innocuous and soluble…”
Get full text

Overexpression of Human Procarboxypeptidase A2 in Pichia pastoris and Detailed Characterization of Its Activation Pathway by Reverter, D, Ventura, S, Villegas, V, Vendrell, J, Avilés, F X

“…The cDNA of human procarboxypeptidase A2 has been overexpressed in the methylotrophic yeast Pichia pastoris and secreted into the culture medium by means of…”
Get full text

NMR solution structure of the activation domain of human procarboxypeptidase A2 by Jiménez, M. Angeles, Villegas, Virtudes, Santoro, Jorge, Serrano, Luis, Vendrell, Josep, Avilés, Francesc X., Rico, Manuel

“…The activation domain of human procarboxypeptidase A2, ADA2h, is an 81‐residue globular domain released during the proteolytic activation of the proenzyme. The…”
Get full text

Mapping the Pro-region of Carboxypeptidase B by Protein Engineering by Ventura, Salvador, Villegas, Virtudes, Sterner, Jane, Larson, Jeffrey, Vendrell, Josep, Hershberger, Charles L., Avilés, Francesc X.

“…The proteolytic processing of pancreatic procarboxypeptidase B to a mature and functional enzyme is much faster than that of procarboxypeptidase A1. This…”
Get full text

Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme by Ventura, S, Villegas, V, Sterner, J, Larson, J, Vendrell, J, Hershberger, C.L, Aviles, F.X

“…The proteolytic processing of pancreatic procarboxypeptidase B to a mature and functional enzyme is much faster than that of procarboxypeptidase A1. This…”
Get full text

Protein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry by Villanueva, Josep, Villegas, Virtudes, Querol, Enrique, Avilés, Francesc X., Serrano, Luis

“…In the post‐genomic era, several projects focused on the massive experimental resolution of the three‐dimensional structures of all the proteins of different…”
Get full text

Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins by Villanueva, Josep, Canals, Francesc, Villegas, Virtudes, Querol, Enrique, Avilés, Francesc X

“…Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been used to monitor hydrogen exchange on entire proteins. Two…”
Get full text

Favourable native-like helical local interactions can accelerate protein folding by Viguera, Ana Rosa, Villegas, Virtudes, Avilés, F. Xavier, Serrano, Luis

“…Extensive studies of peptide conformation have provided reasonable knowledge of the rules determining helix stability. This knowledge can be used to stabilize…”
Get full text

The activation pathway of procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic processing by Villegas, Virtudes, Vendrell, Josep, Avilés, Francesc X.

“…The activation process of porcine pancreatic procarboxypeptidase B (pro‐CPB) has been studied in detail by a number of complementary methodologies, and a…”
Get full text

Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory by Villegas, Virtudes, Viguera, Ana Rosa, Avilés, F Xavier, Serrano, Luis

“…Increasing protein stability is a major goal of protein engineering because of its potential industrial and pharmacological applications. Several different…”
Get full text

Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B by Aloy, P, Catasús, L, Villegas, V, Reverter, D, Vendrell, J, Avilés, F X

“…A full-length cDNA clone for preprocarboxypeptidase B from human pancreas has been isolated and sequenced. The open reading frame is 1254 bp in length,…”
Get more information

Expression of heat-labile enterotoxin genes is under cyclic AMP control inEscherichia coli by Gibert, Isidre, Villegas, Virtudes, Barbé, Jordi

Get full text

Analysis of the activation process of porcine procarboxypeptidase B and determination of the sequence of its activation segment by Burgos, Francisco J, Salva, Miquel, Villegas, Virtudes, Soriano, Fernando, Mendez, Enrique, Aviles, Francesc X

“…The molecular events which lead to the proteolytic transformation of porcine procarboxypeptidase B (PCPB) in carboxypeptidase B (CPB) have been determined…”
Get full text

Thermodynamic analysis of helix‐engineered forms of the activation domain of human procarboxypeptidase A2 by Fernández, Ana M., Villegas, Virtudes, Martínez, Jose C., van Nuland, Nico A. J., Conejero‐Lara, Francisco, Avilés, Francesc X., Serrano, Luis, Filimonov, Vladimir V., Mateo, Pedro L.

“…Thermodynamic characterization of the activation domain of human procarboxypeptidase A2, ADA2h, and its helix‐engineered mutants was carried out by…”
Get full text

Expression of heat-labile enterotoxin genes is under cyclic AMP control in Escherichia coli by GIBERT, I, VILLEGAS, V, BARBE, J

“…The expression of the linked toxA and toxB genes coding for the A and B subunits of the heat-labile enterotoxin of Escherichia coli , respectively, has been…”
Get full text