-
1
-
-
0023335033
-
Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA
-
Devault A, Lazure C, Nault C, Le Moual H, Seidah N, Chrétien M, Kahn P, Powell J, Mallet J, Beaumont A, Roques BP, Crine P, Boileau G. Amino acid sequence of rabbit kidney neutral endopeptidase 24.11 (enkephalinase) deduced from a complementary DNA. EMBO J 1987;6:1317-1322.
-
(1987)
EMBO J
, vol.6
, pp. 1317-1322
-
-
Devault, A.1
Lazure, C.2
Nault, C.3
Le Moual, H.4
Seidah, N.5
Chrétien, M.6
Kahn, P.7
Powell, J.8
Mallet, J.9
Beaumont, A.10
Roques, B.P.11
Crine, P.12
Boileau, G.13
-
2
-
-
0027475050
-
Neutral endopeptidase 24.11. Structure, inhibition, and experimental and clinical pharmacology
-
Roques BP, Noble F, Daugé V, Fournié-Zaluski MC, Beaumont A. Neutral endopeptidase 24.11. Structure, inhibition, and experimental and clinical pharmacology. Pharmacol Rev 1993;45:87-146.
-
(1993)
Pharmacol Rev
, vol.45
, pp. 87-146
-
-
Roques, B.P.1
Noble, F.2
Daugé, V.3
Fournié-Zaluski, M.C.4
Beaumont, A.5
-
3
-
-
33845280830
-
Structural basis of the action of thermolysin and related zinc peptidases
-
Matthews BW. Structural basis of the action of thermolysin and related zinc peptidases. Ace Chem Res 1988;21:333-340.
-
(1988)
Ace Chem Res
, vol.21
, pp. 333-340
-
-
Matthews, B.W.1
-
4
-
-
0023200033
-
Relationship between the inhibitory potencies of thiorphan and retrothiorphan enantiomers on thermolysin and neutral endopeptidases 24.11 and their interactions with the thermolysin active site by computer modeling
-
Benchetrit T, Fournié-Zaluski MC, Roques BP. Relationship between the inhibitory potencies of thiorphan and retrothiorphan enantiomers on thermolysin and neutral endopeptidases 24.11 and their interactions with the thermolysin active site by computer modeling. Biochem Biophys Res Commun 1987;147:1034-1040.
-
(1987)
Biochem Biophys Res Commun
, vol.147
, pp. 1034-1040
-
-
Benchetrit, T.1
Fournié-Zaluski, M.C.2
Roques, B.P.3
-
5
-
-
0024297519
-
Primary structure homologies between two Zn-metallopeptidases, the neutral endopeptidase 24.11 "enkephalinase" and the thermolysin through clustering
-
Benchetrit T, Bissery V, Mornon JP, Devault A, Crine P, Roques BP. Primary structure homologies between two Zn-metallopeptidases, the neutral endopeptidase 24.11 "enkephalinase" and the thermolysin through clustering. Biochemistry 1988;27:592-596.
-
(1988)
Biochemistry
, vol.27
, pp. 592-596
-
-
Benchetrit, T.1
Bissery, V.2
Mornon, J.P.3
Devault, A.4
Crine, P.5
Roques, B.P.6
-
6
-
-
0024284245
-
Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis. Histidine residues 583 and 587 are essential for catalysis
-
Devault A, Sales V, Nault C, Beaumont A, Roques BP, Crine P, Boileau G. Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis. Histidine residues 583 and 587 are essential for catalysis. FEBS Lett 1988;231:54-58.
-
(1988)
FEBS Lett
, vol.231
, pp. 54-58
-
-
Devault, A.1
Sales, V.2
Nault, C.3
Beaumont, A.4
Roques, B.P.5
Crine, P.6
Boileau, G.7
-
7
-
-
0025993765
-
Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase 24.11
-
Le Moual H, Devault A, Roques BP, Crine P Boileau G. Identification of glutamic acid 646 as a zinc-coordinating residue in endopeptidase 24.11. J Biol Chem 1991;266:15670-15674.
-
(1991)
J Biol Chem
, vol.266
, pp. 15670-15674
-
-
Le Moual, H.1
Devault, A.2
Roques, B.P.3
Crine, P.4
Boileau, G.5
-
8
-
-
0023855428
-
Expression of neutral endopeptidase (enkephalinase) in heterologous cos-1 cells: Characterization of the recombinant enzyme and evidence for a glutamic acid residue at the active site
-
Devault A, Nault C, Zollinger M, Fournié-Zaluski MC, Roques BP, Crine P, Boileau G. Expression of neutral endopeptidase (enkephalinase) in heterologous cos-1 cells: characterization of the recombinant enzyme and evidence for a glutamic acid residue at the active site. J Biol Chem 1988;263:4033-4040.
-
(1988)
J Biol Chem
, vol.263
, pp. 4033-4040
-
-
Devault, A.1
Nault, C.2
Zollinger, M.3
Fournié-Zaluski, M.C.4
Roques, B.P.5
Crine, P.6
Boileau, G.7
-
10
-
-
0030656495
-
Evidence by site directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neutral endopeptidase play equivalent critical roles in substrate hydrolysis and inhibitor binding
-
Marie-Claire C, Ruffet E, Antonczak S, Beaumont A, O'Donohue M, Roques BP, Fournié-Zaluski MC. Evidence by site directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neutral endopeptidase play equivalent critical roles in substrate hydrolysis and inhibitor binding. Biochemistry 1997;36:13938-13945.
-
(1997)
Biochemistry
, vol.36
, pp. 13938-13945
-
-
Marie-Claire, C.1
Ruffet, E.2
Antonczak, S.3
Beaumont, A.4
O'Donohue, M.5
Roques, B.P.6
Fournié-Zaluski, M.C.7
-
11
-
-
0024500766
-
Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant
-
Bateman RC, Jackson DG, Slaughter CA, Unnithan S, Chai YG, Moomaw C, Hersh LB. Identification of the active-site arginine in rat neutral endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of a glutamine 102 mutant. J Biol Chem 1989;264: 6151-6157.
-
(1989)
J Biol Chem
, vol.264
, pp. 6151-6157
-
-
Bateman, R.C.1
Jackson, D.G.2
Slaughter, C.A.3
Unnithan, S.4
Chai, Y.G.5
Moomaw, C.6
Hersh, L.B.7
-
12
-
-
0027456271
-
711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state
-
711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state. FEBS Lett 1993;318:301-304.
-
(1993)
FEBS Lett
, vol.318
, pp. 301-304
-
-
Dion, N.1
Le Moual, H.2
Crine, P.3
Boileau, G.4
-
14
-
-
0027418428
-
Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin
-
Gomis-Rüth FX, Stöckier W, Huber R, Zwilling R, Bode W. Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin. J Mol Biol 1993;229:945-968.
-
(1993)
J Mol Biol
, vol.229
, pp. 945-968
-
-
Gomis-Rüth, F.X.1
Stöckier, W.2
Huber, R.3
Zwilling, R.4
Bode, W.5
-
15
-
-
0028805811
-
Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
-
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PMD, Cameron PM, Esser CK, Hagmann WK, Hermes JD, Springer JP. Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci 1995;4:1966-1976.
-
(1995)
Protein Sci
, vol.4
, pp. 1966-1976
-
-
Becker, J.W.1
Marcy, A.I.2
Rokosz, L.L.3
Axel, M.G.4
Burbaum, J.J.5
Fitzgerald, P.M.D.6
Cameron, P.M.7
Esser, C.K.8
Hagmann, W.K.9
Hermes, J.D.10
Springer, J.P.11
-
16
-
-
0032912508
-
A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC 3.4.24.11)
-
Tiraboschi G, Jullian N, Antonczak S, Théry V, Fournié-Zaluski MC, Roques BP. A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC 3.4.24.11). Protein Eng 1999;12:141-149.
-
(1999)
Protein Eng
, vol.12
, pp. 141-149
-
-
Tiraboschi, G.1
Jullian, N.2
Antonczak, S.3
Théry, V.4
Fournié-Zaluski, M.C.5
Roques, B.P.6
-
17
-
-
0021395943
-
Differences in the structural requirements for selective interaction with neutral metalloendopeptidase (enkephalinase) or angiotensin converting enzyme: Molecular investigation by use of new thiol inhibitors
-
Fournié-Zaluski MC, Lucas E, Waksman G, Roques BP. Differences in the structural requirements for selective interaction with neutral metalloendopeptidase (enkephalinase) or angiotensin converting enzyme: molecular investigation by use of new thiol inhibitors. Eur J Biochem 1984;139:267-274.
-
(1984)
Eur J Biochem
, vol.139
, pp. 267-274
-
-
Fournié-Zaluski, M.C.1
Lucas, E.2
Waksman, G.3
Roques, B.P.4
-
19
-
-
0003699451
-
-
October 1995. San Diego: Biosym/MSI
-
Insight II user guide, October 1995. San Diego: Biosym/MSI; 1995.
-
(1995)
Insight II User Guide
-
-
-
22
-
-
0020359350
-
Enkephalinase dipeptidyl carboxypeptidase ("enkephalinase") activity: Selective radioassay, properties and regional distribution in human brain
-
Llorens C, Malfroy B, Schwartz JC, Gacel G, Roques BP, Roy J, Morgat JL, Javoy-Agid F, Agid Y. Enkephalinase dipeptidyl carboxypeptidase ("enkephalinase") activity: selective radioassay, properties and regional distribution in human brain. J Neurochem 1982;39:1081-1089.
-
(1982)
J Neurochem
, vol.39
, pp. 1081-1089
-
-
Llorens, C.1
Malfroy, B.2
Schwartz, J.C.3
Gacel, G.4
Roques, B.P.5
Roy, J.6
Morgat, J.L.7
Javoy-Agid, F.8
Agid, Y.9
-
23
-
-
0031767267
-
Differences in transition states stabilization between thermolysin (EC 3.424.27) and neprilysin (EC 3.424.11)
-
Marie-Claire C, Ruffet E, Tiraboschi G, Fournié-Zaluski MC. Differences in transition states stabilization between thermolysin (EC 3.424.27) and neprilysin (EC 3.424.11). FEBS Lett 1998;438: 215-219.
-
(1998)
FEBS Lett
, vol.438
, pp. 215-219
-
-
Marie-Claire, C.1
Ruffet, E.2
Tiraboschi, G.3
Fournié-Zaluski, M.C.4
-
24
-
-
0024580983
-
Thiorphan and retrothiorphan display equivalent interactions when bound to crystalline thermolysin
-
Roderick SL, Fournié-Zaluski MC, Roques BP, Matthews BW. Thiorphan and retrothiorphan display equivalent interactions when bound to crystalline thermolysin. Biochemistry 1989;28: 1493-1497.
-
(1989)
Biochemistry
, vol.28
, pp. 1493-1497
-
-
Roderick, S.L.1
Fournié-Zaluski, M.C.2
Roques, B.P.3
Matthews, B.W.4
|