✦ LIBER ✦

Metalloendopeptidases EC 3.4.24.15 and EC 3.4.24.16: potential roles in vascular physiology

✍ Scribed by M. Ursula Norman; A. Ian Smith; Michael J. Hickey

Publisher: Springer Netherlands
Year: 2001
Tongue: English
Weight: 357 KB
Volume: 8
Category: Article
ISSN: 1573-3149
DOI: 10.1007/bf02446517

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Comparative fine structural distribution

Comparative fine structural distribution of endopeptidase 24.15 (EC3.4.24.15) and 24.16 (EC3.4.24.16) in rat brain

✍ José Domingues Fontenele-Neto; Eduardo Ernst Massarelli; Paula Amaral Gurgel Gar 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 873 KB

## Abstract Endopeptidase 24.15 (EP24.15) and 24.16 (EP24.16) are closely related metalloendopeptidases implicated in the metabolism of several neuropeptides and widely expressed in mammalian brain. To gain insight into the functional role of these two enzymes in the central nervous system, we exam

Role of calcium in the release of EC 3.4

Role of calcium in the release of EC 3.4.24.15 and EC 3.4.24.16 from endothelial cells

✍ M. Ursula Norman; A. Ian Smith; Rebecca A. Lew 📂 Article 📅 1999 🏛 Springer Netherlands 🌐 English ⚖ 327 KB

Selective Neurotensin-Derived Internally

Selective Neurotensin-Derived Internally Quenched Fluorogenic Substrates for Neurolysin (EC 3.4.24.16): Comparison with Thimet Oligopeptidase (EC 3.4.24.15) and Neprilysin (EC 3.4.24.11)

✍ Vitor Oliveira; Marcelo Campos; Jefferson P. Hemerly; Emer S. Ferro; Antonio C.M 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 86 KB

Internally quenched fluorescent peptides derived from neurotensin (pELYENKPRRPYIL) sequence were synthesized and assayed as substrates for neurolysin (EC 3.4.24.16), thimet oligopeptidase (EC 3.4.24.15 or TOP), and neprilysin (EC 3.4.24.11 or NEP). Abz-LYENKPRRPYILQ-EDDnp (where EDDnp is N-(2,4-dini

Liver bradykinin-inactivating-endopeptid

Liver bradykinin-inactivating-endopeptidase is similar to the metalloendopeptidase (EC 3.4.24.15)

✍ Hercilia M. Molina; Adriana K. Carmona; Maria Kouyoumdjian; Durval R. Borges; Lu 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 244 KB

Design and synthesis of inhibitors incor

Design and synthesis of inhibitors incorporating β-amino acids of metalloendopeptidase EC 3.4.24.15

✍ D.L. Steer; R.A. Lew; P. Perlmutter; A.I. Smith; M.-I. Aguilar 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 115 KB 👁 1 views

Novel roles of neuropeptide processing e

Novel roles of neuropeptide processing enzymes: EC3.4.24.15 in the neurome

✍ S.I. Kim; V. Grum-Tokars; T.A. Swanson; E.J. Cotter; P.A. Cahill; J.L. Roberts; 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 409 KB

## Abstract Neuropeptide processing metalloenzymes, such as angiotensin converting enzyme, neprilysin, endothelin converting enzyme, neurolysin, and EC3.4.24.15 (EP24.15), are central to the formation and degradation of bioactive peptides. We present EP24.15 as a paradigm for novel functions ascrib