메뉴 건너뛰기




Volumn 1, Issue , 2004, Pages 426-429

Neprilysin-2

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33845611820     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50117-8     Document Type: Chapter
Times cited : (2)

References (14)
  • 1
    • 0034803572 scopus 로고    scopus 로고
    • Molecular cloning, tissue distribution, and chromosomal localization of MMEL2, a gene coding for a novel human member of the neutral endopeptidase-24.11 family
    • N. Bonvouloir, N. Lemieux, P. Crine, G. Boileau and L. DesGroseillers (2001) Molecular cloning, tissue distribution, and chromosomal localization of MMEL2, a gene coding for a novel human member of the neutral endopeptidase-24.11 family. DNA Cell. Biol. 20 493-498.
    • (2001) DNA Cell. Biol. , vol.20 , pp. 493-498
    • Bonvouloir, N.1    Lemieux, N.2    Crine, P.3    Boileau, G.4    DesGroseillers, L.5
  • 2
    • 0141629602 scopus 로고    scopus 로고
    • The neuropeptide-degrading enzyme NL1 is expressed in specific neurons of mouse brain
    • M. Carpentier, M. Marcinkiewicz, G. Boileau and L. DesGroseillers (2003) The neuropeptide-degrading enzyme NL1 is expressed in specific neurons of mouse brain. Peptides 24 1083-1091.
    • (2003) Peptides , vol.24 , pp. 1083-1091
    • Carpentier, M.1    Marcinkiewicz, M.2    Boileau, G.3    DesGroseillers, L.4
  • 3
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
    • N. Emoto and M. Yanagisawa (1995) Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 270 15262-15268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 4
    • 0037466757 scopus 로고    scopus 로고
    • Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme
    • P. Fachinetti, C. Rose, J.C. Schwartz and T. Ouimet (2003) Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme. Neuroscience 118 627-639.
    • (2003) Neuroscience , vol.118 , pp. 627-639
    • Fachinetti, P.1    Rose, C.2    Schwartz, J.C.3    Ouimet, T.4
  • 6
    • 0033527579 scopus 로고    scopus 로고
    • Molecular identification and characterization of a novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides
    • K. Ikeda, N. Emoto, S.B. Raharjo, Y. Nurhantari, K. Saiki, M. Yokoyama and M. Matsuo (1999) Molecular identification and characterization of a novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides. J. Biol. Chem. 274 32469-32477.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32469-32477
    • Ikeda, K.1    Emoto, N.2    Raharjo, S.B.3    Nurhantari, Y.4    Saiki, K.5    Yokoyama, M.6    Matsuo, M.7
  • 7
    • 0028147134 scopus 로고
    • Role of glycosylation in transport and enzymatic activity of neutral endopeptidase-24.11
    • M.H. Lafrance, C. Vézina, Q. Wang, G. Boileau, P. Crine and G. Lemay (1994) Role of glycosylation in transport and enzymatic activity of neutral endopeptidase-24.11. Biochem. J. 302 683-688.
    • (1994) Biochem. J. , vol.302 , pp. 683-688
    • Lafrance, M.H.1    Vézina, C.2    Wang, Q.3    Boileau, G.4    Crine, P.5    Lemay, G.6
  • 8
    • 0034681296 scopus 로고    scopus 로고
    • Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon
    • C. Oefner, A. D'Arcy, M. Hennig, F.K. Winkler and G.E. Dale (2000) Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon. J. Mol. Biol. 296 341-349.
    • (2000) J. Mol. Biol. , vol.296 , pp. 341-349
    • Oefner, C.1    D'Arcy, A.2    Hennig, M.3    Winkler, F.K.4    Dale, G.E.5
  • 10
    • 0035816592 scopus 로고    scopus 로고
    • Alternative splicing regulates the endoplasmic reticulum localization or secretion of soluble secreted endopeptidase
    • S.B. Raharjo, N. Emoto, K. Ikeda, R. Sato, M. Yokoyama and M. Matsuo (2001) Alternative splicing regulates the endoplasmic reticulum localization or secretion of soluble secreted endopeptidase. J. Biol. Chem. 276 25612-25620.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25612-25620
    • Raharjo, S.B.1    Emoto, N.2    Ikeda, K.3    Sato, R.4    Yokoyama, M.5    Matsuo, M.6
  • 11
    • 0036566092 scopus 로고    scopus 로고
    • Cell-specific activity of neprilysin 2 isoforms and enzymatic specificity compared with neprilysin
    • C. Rose, S. Voisin, C. Gros, J.C. Shwartz and T. Ouimet (2002) Cell-specific activity of neprilysin 2 isoforms and enzymatic specificity compared with neprilysin. Biochem. J. 363 697-705.
    • (2002) Biochem. J. , vol.363 , pp. 697-705
    • Rose, C.1    Voisin, S.2    Gros, C.3    Shwartz, J.C.4    Ouimet, T.5
  • 14
    • 0033857679 scopus 로고    scopus 로고
    • Endothelin-converting enzyme-like 1 (ECEL1; XCE): a putative metallopeptidase crucially involved in the nervous control of respiration
    • O. Valdenaire and A. Schweizer (2000) Endothelin-converting enzyme-like 1 (ECEL1; XCE): a putative metallopeptidase crucially involved in the nervous control of respiration. Biochem. Soc. Trans. 28 426-430.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 426-430
    • Valdenaire, O.1    Schweizer, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.