Neonatal lethality in mice deficient in XCE, a novel member of the endothelin-converting enzyme and neutral endopeptidase family
about
The Kell protein of the common K2 phenotype is a catalytically active metalloprotease, whereas the rare Kell K1 antigen is inactive. Identification of novel substrates for the Kell proteinEndothelin-converting enzyme-like 1 (ECEL1) is present both in the plasma membrane and in the endoplasmic reticulumOrganization and chromosomal localization of the human ECEL1 (XCE) gene encoding a zinc metallopeptidase involved in the nervous control of respirationGain-of-function mutations in the mechanically activated ion channel PIEZO2 cause a subtype of Distal ArthrogryposisGleevec, an Abl family inhibitor, produces a profound change in cell shape and migrationDamage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase expressed in response to neuronal damage and activates superoxide scavengersMutations in ECEL1 cause distal arthrogryposis type 5DAssociation between favorable neuroblastoma and high expression of the novel metalloproteinase gene, nbla3145/XCE, cloned by differential screening of the full-length-enriched oligo-capping neuroblastoma cDNA libraries.Dynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities.The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function.Bioinformatic analysis of the neprilysin (M13) family of peptidases reveals complex evolutionary and functional relationshipsReduced fertility in male mice deficient in the zinc metallopeptidase NL1The wrickkened pathways of FGF23, MEPE and PHEX.Identification and functional analysis of damage-induced neuronal endopeptidase (DINE), a nerve injury associated molecule.Expanding the phenotypic spectrum of ECEL1-related congenital contracture syndromes.The nuclear events guiding successful nerve regeneration.The neuronal endopeptidase ECEL1 is associated with a distinct form of recessive distal arthrogryposis.Role of abnormal neutral endopeptidase-like activities in Hyp mouse bone cells in renal phosphate transport.Damage-induced neuronal endopeptidase (DINE) enhances axonal regeneration potential of retinal ganglion cells after optic nerve injury.Distinct functional consequences of ECEL1/DINE missense mutations in the pathogenesis of congenital contracture disorders.ECEL1 mutation implicates impaired axonal arborization of motor nerves in the pathogenesis of distal arthrogryposis.Identification of three novel ECEL1 mutations in three families with distal arthrogryposis type 5D.ECEL1mutation causes fetal arthrogryposis multiplex congenita
P2860
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P2860
Neonatal lethality in mice deficient in XCE, a novel member of the endothelin-converting enzyme and neutral endopeptidase family
description
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im Juli 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/07/16)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/07/16)
@nl
наукова стаття, опублікована в липні 1999
@uk
name
Neonatal lethality in mice def ...... d neutral endopeptidase family
@ast
Neonatal lethality in mice def ...... d neutral endopeptidase family
@en
Neonatal lethality in mice def ...... d neutral endopeptidase family
@nl
type
label
Neonatal lethality in mice def ...... d neutral endopeptidase family
@ast
Neonatal lethality in mice def ...... d neutral endopeptidase family
@en
Neonatal lethality in mice def ...... d neutral endopeptidase family
@nl
prefLabel
Neonatal lethality in mice def ...... d neutral endopeptidase family
@ast
Neonatal lethality in mice def ...... d neutral endopeptidase family
@en
Neonatal lethality in mice def ...... d neutral endopeptidase family
@nl
P2093
P2860
P356
P1476
Neonatal lethality in mice def ...... d neutral endopeptidase family
@en
P2093
A. Schweizer
G. Schmitt
H. Bluethmann
O. Valdenaire
P2860
P304
20450–20456
P356
10.1074/JBC.274.29.20450
P407
P577
1999-07-16T00:00:00Z