Chesneau V - Search Results

1

N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface.

Hospital V, Chesneau V, Balogh A, Joulie C, Seidah NG, Cohen P, Prat A. Hospital V, et al. Among authors: chesneau v. Biochem J. 2000 Jul 15;349(Pt 2):587-97. doi: 10.1042/0264-6021:3490587. Biochem J. 2000. PMID: 10880358 Free PMC article.

2

N-arginine dibasic convertase.

Cohen P, Pierotti AR, Chesneau V, Foulon T, Prat A. Cohen P, et al. Among authors: chesneau v. Methods Enzymol. 1995;248:703-16. doi: 10.1016/0076-6879(95)48047-1. Methods Enzymol. 1995. PMID: 7674957 No abstract available.

3

N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overview.

Chesneau V, Pierotti AR, Prat A, Gaudoux F, Foulon T, Cohen P. Chesneau V, et al. Biochimie. 1994;76(3-4):234-40. doi: 10.1016/0300-9084(94)90151-1. Biochimie. 1994. PMID: 7819328 Review.

4

NRD convertase: a putative processing endoprotease associated with the axoneme and the manchette in late spermatids.

Chesneau V, Prat A, Segretain D, Hospital V, Dupaix A, Foulon T, Jégou B, Cohen P. Chesneau V, et al. J Cell Sci. 1996 Nov;109 ( Pt 11):2737-45. doi: 10.1242/jcs.109.11.2737. J Cell Sci. 1996. PMID: 8937991

5

N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.

Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P. Pierotti AR, et al. Among authors: chesneau v. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):6078-82. doi: 10.1073/pnas.91.13.6078. Proc Natl Acad Sci U S A. 1994. PMID: 8016118 Free PMC article.

6

Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues.

Chesneau V, Pierotti AR, Barré N, Créminon C, Tougard C, Cohen P. Chesneau V, et al. J Biol Chem. 1994 Jan 21;269(3):2056-61. J Biol Chem. 1994. PMID: 8294457 Free article.

7

NRD convertase and aminopeptidase B: two processing metallopeptidases with a selectivity for basic residues.

Foulon T, Cadel S, Prat A, Chesneau V, Hospital V, Segrétain D, Cohen P. Foulon T, et al. Among authors: chesneau v. Ann Endocrinol (Paris). 1997;58(5):357-64. Ann Endocrinol (Paris). 1997. PMID: 9685993

8

Two novel metallopeptidases with a specificity for basic residues: functional properties, structure and cellular distribution.

Foulon T, Cadel S, Chesneau V, Draoui M, Prat A, Cohen P. Foulon T, et al. Among authors: chesneau v. Ann N Y Acad Sci. 1996 Mar 22;780:106-20. doi: 10.1111/j.1749-6632.1996.tb15115.x. Ann N Y Acad Sci. 1996. PMID: 8602724 Review. No abstract available.

9

Purified recombinant insulin-degrading enzyme degrades amyloid beta-protein but does not promote its oligomerization.

Chesneau V, Vekrellis K, Rosner MR, Selkoe DJ. Chesneau V, et al. Biochem J. 2000 Oct 15;351 Pt 2(Pt 2):509-16. Biochem J. 2000. PMID: 11023838 Free PMC article.

10

Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation.

Chesneau V, Perlman RK, Li W, Keller GA, Rosner MR. Chesneau V, et al. Endocrinology. 1997 Aug;138(8):3444-51. doi: 10.1210/endo.138.8.5344. Endocrinology. 1997. PMID: 9231799

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