A. Beaumont

发表

Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology.

M. Fournié-Zaluski, B. Roques, F. Noble, 1993, Pharmacological reviews.

Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11).

B. Roques, H. Le Moual, P. Crine, 1991, The Journal of biological chemistry.

Identification of two arginine residues involved in the binding of substrate to neutral endopeptidase 24-11.

B. Roques, H. Le Moual, P. Crine, 1992, Matrix (Stuttgart, Germany). Supplement.

Peptidase inactivation of enkephalins : design of inhibitors and biochemical, pharmacological, and clinical applications

M. Fournié-Zaluski, B. Roques, V. Daugé, 1993 .

Neurotensin high affinity binding sites and endopeptidase 24.11 are present respectively in the meningothelial and in the fibroblastic components of human meningiomas

M. Levivier, B. Roques, J. Vanderhaeghen, 1990, Peptides.

Increase of neutral endopeptidase-24.11 with cellular density and enzyme modulation with an inhibitor on human Reh6 cell line.

B. Roques, P. Milhiet, A. Beaumont, 1992, Biochemical pharmacology.

Neutral endopeptidase 24.11 and angiotensin converting enzyme like activity in CALLA positive and CALLA negative lymphoid cells.

B. Roques, A. Beaumont, J. Brouet, 1989, Biochemical and biophysical research communications.

Opioid peptides: aspects of their origin, release and metabolism.

A. Beaumont, B. Malfroy, J. Hughes, 1980, The Journal of experimental biology.

A 94-kDa protein, identified as neutral endopeptidase-24.11, can inactivate atrial natriuretic peptide in the vascular endothelium.

S. Turcaud, J. Michel, B. Roques, 1992, Molecular pharmacology.

Formation of mercapturic acids from acrylonitrile, crotononitrile, and cinnamonitrile by direct conjugation and via an intermediate oxidation process.

P. van Bladeren, J. J. Hoogeterp, D. Breimer, 1981, Drug metabolism and disposition: the biological fate of chemicals.

STUDIES ON POSSIBLE PRECURSORS FOR THE ENKEPHALINS

A. Dell, H. Morris, A. Beaumont, 1980 .

Biology of opioid peptides.

A. Beaumont, J. Hughes, 1979, Annual review of pharmacology and toxicology.

Cleavage of farnesylated COOH-terminal heptapeptide of mouse N-ras by brain microsomal membranes: evidence for a carboxypeptidase which specifically removes the COOH-terminal methionine.

B. Roques, A. Beaumont, M. Fournié-Zaluski, 1992, Biochemical and biophysical research communications.

The use of a monoclonal antibody for the rapid purification of kidney neutral endopeptidase ("enkephalinase") solubilized in octyl glucoside.

B. Roques, P. Crine, A. Beaumont, 1987, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA.

N. Seidah, J. Mallet, M. Chrétien, 1987, The EMBO journal.

Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin.

B. Roques, M. O’Donohue, A. Beaumont, 1994, The Biochemical journal.

New thiol inhibitors of neutral endopeptidase EC 3.4.24.11: synthesis and enzyme active-site recognition.

B. Roques, I. Gomez-Monterrey, A. Beaumont, 1994, Journal of medicinal chemistry.

Effects of monoclonal antibodies raised against the common acute lymphoblastic leukemia antigen on endopeptidase-24.11 activity.

B. Roques, P. Milhiet, C. Boucheix, 1992, Biochemical pharmacology.

Charge polarity reversal inverses the specificity of neutral endopeptidase-24.11.

B. Barbe, B. Roques, H. Le Moual, 1992, The Journal of biological chemistry.

Neutral endopeptidase-24.11 inhibitors: from analgesics to antihypertensives?

B. Roques, A. Beaumont, 1990, Trends in pharmacological sciences.

Functional residues at the active site of aminopeptidase N.

B. Roques, A. Beaumont, A. Helene, 1991, European journal of biochemistry.

Exploration of the catalytic site of endopeptidase 24.11 by site‐directed mutagenesis Histidine residues 583 and 587 are essential for catalysis

B. Roques, A. Devault, P. Crine, 1988, FEBS letters.

Development of [125I]RB104, a potent inhibitor of neutral endopeptidase 24.11, and its use in detecting nanogram quantities of the enzyme by "inhibitor gel electrophoresis".

S. Turcaud, B. Roques, P. Crine, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Identiflcation of a Proenkephalin Precursor in Striatal Tissue

J. Rossier, K. Metters, A. Beaumont, 1985, Journal of neurochemistry.

Opioid peptide precursors in striatum

K. Metters, A. Beaumont, J. Hughes, 1980, FEBS letters.

A comparison of opioid peptide precursors in guinea pig, rat and bovine striata and guinea pig adrenal

J. Rossier, K. Metters, A. Beaumont, 1985, Neuropeptides.

The Roles of the Prosequence of Thermolysin in Enzyme Inhibition and Folding in Vitro*

M. O’Donohue, A. Beaumont, Michael J. O'Donohue, 1996, The Journal of Biological Chemistry.

Intramolecular Processing of Prothermolysin*

B. Roques, A. Beaumont, Cynthia Marie-Claire, 1998, The Journal of Biological Chemistry.

The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.

B. Roques, A. Beaumont, E. Ruffet, 1999, Journal of molecular biology.

Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action.

B. Roques, N. Luciani, A. Beaumont, 1998, Biochemistry.

The Role of Histidine 231 in Thermolysin-like Enzymes.

N. Rousselet, B. Roques, M. O’Donohue, 1995, The Journal of Biological Chemistry.

Studies on the neurochemical properties of cystathionine.

A. Beaumont, N. Tudball, 1979, Biochimica et biophysica acta.

Presence of a histidine at the active site of the neutral endopeptidase-24.11.

B. Roques, A. Beaumont, B. Roques, 1986, Biochemical and biophysical research communications.