J. Vendrell

Publication List Details

Period

1992 - 2009

Number

27

Co-Authors

IL6 gene promoter polymorphisms and type 2 diabetes: joint analysis of individual participants' data from 21 studies (2006)

Huth, C., Heid, I.M., Vollmert, C., Gieger, C., Grallert, H., Wolford, J.K., ...

Several lines of evidence indicate a causal role of the cytokine interleukin (IL)-6 in the development of type 2 diabetes in humans. Two common polymorphisms in the promoter of the IL-6 encoding gene...

Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypepidase B (2006)

Bayes, A, Vendrell, J., Aviles, F.X., Jongsma, M.A., Beekwilder, M.J.

Carboxypeptidase activity participates in the protein digestion process in the gut of lepidopteran insects, supplying free amino-acids to developing larvae. To study the role of different...

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors (2005)

Bayés, A., Comellas-Bigler, M., Maskos, K., Bode, W., Aviles, F.X., ...

Corn earworm (Helicoverpa zea), also called tomato fruitworm, is a common pest of many Solanaceous plants. This insect is known to adapt to the ingestion of plant serine protease inhibitors by using...

A system-level solution to domino synthesis with 2 GHz application (2002)

X. Wang, P. Patra, P. Saxena, J. Vendrell, S. Gupta, S. Varadarajan, ...

System structure and a 2GHz product application result are described for a domino synthesis capability that covers all aspects of domino design, from estimation to silicon-ready layout, with...

Crystal structure of a novel Mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera (2001)

Estebanez-Perpica, E, Bayes, A, Vendrell, J., Jongsma, M.A., Bown, D.P., Gatehouse, J.A., ...

The cotton bollworm Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) is one of the most serious insect pests in Australia, India and China. The larva causes substantial economical losses to...

NON-ASSOCIATION BETWEEN 9.2 KB PvuII RFLP AND SERONEGATIVE SPONDYLOARTHROPATHIES IN SPAIN (1992)

CAÑETE, J. D., SANMARTÍ, R., COLLADO, A., ERCILLA, G., ARMENGOL, P., VENDRELL, J., ...

Several studies of DNA restriction fragment length polymorphism (RFLP) in ankylosing spondylitis (AS) have been carried out. The association between a recently identified class I HLA 9.2kb PvuII RFLP...

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

Vendrell, J, Billeter, M, Wider, G, Avilés, F X, Wüthrich, K

The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR spectroscopy. A group of 20 conformers is used to describe...

1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A.

Vendrell, J, Avilés, F X, Vilanova, M, Turner, C H, Crane-Robinson, C

The isolated activation segment (asA) from pig pancreatic procarboxypeptidase A was studied by 1H-n.m.r. spectroscopy over a wide range of solution conditions. Isolated asA shows many characteristics...

Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A.

Vilanova, M, Vendrell, J, López, M T, Cuchillo, C M, Avilés, F X

A method is reported for the preparative isolation of the two forms of pro-(carboxypeptidase A) from pig pancreas: the monomer and the binary complex with pro-(proteinase E). This method, which is...

Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A.

Vilanova, M, Vendrell, J, Cuchillo, C M, Avilés, F X

The isolated activation segment of pig procarboxypeptidase A binds two Tb3+ ions in a strong and specific way. In contrast, the binding of Ca2+, Cd2+ and Mg2+ is weak. The binding of Tb3+ increases...

The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen.

García-Sáez, I, Reverter, D, Vendrell, J, Avilés, F X, Coll, M

The three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic...

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

Gomis-Rüth, F X, Companys, V, Qian, Y, Fricker, L D, Vendrell, J, Avilés, F X, ...

The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a...

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

Vendrell, J, Billeter, M, Wider, G, Avilés, F X, Wüthrich, K

The three-dimensional structure of the activation domain isolated from porcine pancreatic procarboxypeptidase B was determined using 1H NMR spectroscopy. A group of 20 conformers is used to describe...

1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A.

Vendrell, J, Avilés, F X, Vilanova, M, Turner, C H, Crane-Robinson, C

The isolated activation segment (asA) from pig pancreatic procarboxypeptidase A was studied by 1H-n.m.r. spectroscopy over a wide range of solution conditions. Isolated asA shows many characteristics...

Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A.

Vilanova, M, Vendrell, J, López, M T, Cuchillo, C M, Avilés, F X

A method is reported for the preparative isolation of the two forms of pro-(carboxypeptidase A) from pig pancreas: the monomer and the binary complex with pro-(proteinase E). This method, which is...

Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A.

Vilanova, M, Vendrell, J, Cuchillo, C M, Avilés, F X

The isolated activation segment of pig procarboxypeptidase A binds two Tb3+ ions in a strong and specific way. In contrast, the binding of Ca2+, Cd2+ and Mg2+ is weak. The binding of Tb3+ increases...

The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen.

García-Sáez, I, Reverter, D, Vendrell, J, Avilés, F X, Coll, M

The three-dimensional structure of human procarboxypeptidase A2 has been determined using X-ray crystallography at 1.8 A resolution. This is the first detailed structural report of a human pancreatic...

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

Gomis-Rüth, F X, Companys, V, Qian, Y, Fricker, L D, Vendrell, J, Avilés, F X, ...

The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a...

The activation pathway of procarboxypeptidase B from porcine pancreas: participation of the active enzyme in the proteolytic processing.

Villegas, V., Vendrell, J., Avilés, X.

The activation process of porcine pancreatic procarboxypeptidase B (pro-CPB) has been studied in detail by a number of complementary methodologies, and a description of the molecular events that lead...