H Le Moual
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Explore the profile of H Le Moual including associated specialties, affiliations and a list of published articles.
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14
Citations
283
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Recent Articles
1.
Montagne M, Martel A, Le Moual H
J Bacteriol
. 2001 Feb;
183(5):1787-91.
PMID: 11160113
Studies of Escherichia coli membranes that were highly enriched in the Salmonella enterica serovar Typhimurium PhoQ protein showed that the presence of ATP and divalent cations such as Mg2+, Mn2+,...
2.
Le Moual H, Quang T, Koshland Jr D
Biochemistry
. 1998 Oct;
37(42):14852-9.
PMID: 9778360
By using targeted disulfide cross-linking, we have characterized structural changes that the Escherichia coli aspartate receptor undergoes upon modification of the four specific residues that are reversibly methylated during sensory...
3.
Le Moual H, Quang T, Koshland Jr D
Biochemistry
. 1997 Oct;
36(43):13441-8.
PMID: 9341238
The mechanism(s) of methylation of the Escherichia coli chemotaxis receptors was analyzed by experiments involving the construction of a series of aspartate receptor variants. Truncation of five or more residues...
4.
Le Moual H, Koshland Jr D
J Mol Biol
. 1996 Aug;
261(4):568-85.
PMID: 8794877
Twenty-nine proteins from 16 different species of prokaryotes revealed an extensive sequence homology with the cytoplasmic domain of the Escherichia coli aspartate receptor. The high percentage of identity indicated that...
5.
Dion N, Le Moual H, Fournie-Zaluski M, Roques B, Crine P, Boileau G
Biochem J
. 1995 Oct;
311 ( Pt 2):623-7.
PMID: 7487905
Neprilysin (EC 3.4.24.11) is a Zn2+ metallopeptidase involved in the degradation of biologically active peptides, e.g. enkephalins and atrial natriuretic peptide. The substrate specificity and catalytic activity of neprilysin resemble...
6.
Le Moual H, Dion N, Roques B, Crine P, Boileau G
Eur J Biochem
. 1994 Apr;
221(1):475-80.
PMID: 8168535
Neutral endopeptidase (NEP) is a membrane-bound mammalian ectopeptidase that contains a catalytic zinc ion in its active site. Previous studies showed that the active site, and especially the zinc-binding site...
7.
Le Moual H, Roques B, Crine P, Boileau G
FEBS Lett
. 1993 Jun;
324(2):196-200.
PMID: 8099556
Neutral endopeptidase (EC 3.4.24.11; NEP) is a membrane-bound zinc-metallopeptidase. The catalytic zinc ion is coordinated to three amino acid residues (His538, His587 and Glu646) and a water molecule. Here, we...
8.
Dion N, Le Moual H, Crine P, Boileau G
FEBS Lett
. 1993 Mar;
318(3):301-4.
PMID: 8440386
Neutral endopeptidase 24.11 (EC 3.4.24.11; NEP) is a membrane-bound Zn-metalloendopeptidase with a catalytic activity and a specificity very similar to that of thermolysin, a bacterial zinc-endoprotease. NEP can be inactivated...
9.
Beaumont A, Barbe B, Le Moual H, Boileau G, Crine P, Fournie-Zaluski M, et al.
J Biol Chem
. 1992 Feb;
267(4):2138-41.
PMID: 1733922
Attempts to change enzyme specificity by charge polarity reversal have so far met with little success, probably due to a destabilization of the resulting ion pair in an environment naturally...
10.
Le Moual H, Beaumont A, Roques B, Crine P, Boileau G
Matrix Suppl
. 1992 Jan;
1:99.
PMID: 1480105
No abstract available.