D. Convents

Intramolecular Proteolytic Cleavage ofBacillus thuringiensisCry3A δ-Endotoxin May Facilitate Its Coleopteran Toxicity

D. Ellar, J. Carroll, J. Rie, 1997 .

High affinity binding of 3H rauwolscine and 3H RX781094 to alpha 2 adrenergic receptors and non-stereoselective sites in human and rabbit brain cortex membranes.

J. De Keyser, G. Vauquelin, A. Convents, 1989, Biochemical pharmacology.

Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A delta-endotoxin may facilitate its coleopteran toxicity.

J. Van Damme, D. Ellar, J. Van Rie, 1997, Journal of invertebrate pathology.

Tight agonist binding may prevent the correct interpretation of agonist competition binding curves for alpha 2-adrenergic receptors.

G. Vauquelin, A. Convents, D. Convents, 1987, Molecular pharmacology.

Two structural domains as a general fold of the toxic fragment of the Bacillus thuringiensis delta-endotoxins.

I. Lasters, J. Van Damme, M. Lauwereys, 1991, European journal of biochemistry.

The Bacillus thuringiensis delta-endotoxin. Evidence for a two domain structure of the minimal toxic fragment.

I. Lasters, M. Lauwereys, D. Convents, 1990, The Journal of biological chemistry.

The C‐terminal domain of the toxic fragment of a Bacillus thuringiensis crystal protein determines receptor binding

B. Visser, S. Jansens, M. Peferoen, 1991, Molecular microbiology.

Glycoprotein nature of α2‐adrenergic receptors labeled with p‐azido[3H] clonidine in calf retina membranes

G. Vauquelin, A. Convents, D. Convents, 1988, FEBS Letters.