Evidence map›Paper›PMID 10377252›Full record

ArticleThe Biochemical journal1999

The N-terminal segment of endothelin-converting enzyme (ECE)-1b contains a di-leucine motif that can redirect neprilysin to an intracellular compartment in Madin-Darby canine kidney (MDCK) cells.

F Cailler, J P Zappulla, G Boileau, P Crine

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 17 citations in OpenAlex.

  1. Protein Kinase C Regulates the Cell Surface Activity of Endothelin-Converting Enzyme-1.International journal of peptide research and therapeutics · 2006
    Article
  2. beta-Amyloid degradation and Alzheimer's disease.Journal of biomedicine & biotechnology · 2006
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

F CaillerDepartment of Biochemistry, Faculty of Medicine, University of Montreal, CP 6128, Succursale Centre Ville, Montreal, Quebec, H3C 3J7, Canada.
J P Zappulla
G Boileau
P Crine
Université de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelin-converting enzyme (ECE)-1 is a membrane-bound metallopeptidase of the neprilysin (NEP) family. ECE-1 is responsible for the conversion of inactive big-endothelins into active endothelins. Three different isoforms of human ECE-1 (ECE-1a, ECE-1b and ECE-1c) have been identified. They differ in their N-terminal cytosolic regions, have distinct tissue distribution and intracellular localization. ECE-1a and ECE-1c are both located at the cell surface whereas ECE-1b is targeted to an intracellular compartment. To better understand the nature of the signal responsible for the targeting of ECE-1b to the intracellular compartment, we have constructed several ECE/NEP chimaeric proteins and expressed them by transfection into Madin-Darby canine kidney (MDCK) cells. This allowed us to identify a nine amino acid segment in the cytosolic tail of ECE-1b that is sufficient to relocate NEP from the cell surface to an intracellular compartment. Site-directed mutagenesis on these chimaeras led to the identification of two leucine residues as part of the intracellular retention signal.

Indexed as

Cell CompartmentationLeucineAmino Acid SequenceAnimalsAspartic Acid EndopeptidasesCells, CulturedDogsEndothelin-Converting EnzymesHumansIsoenzymesKidneyMembrane ProteinsMetalloendopeptidasesMolecular Sequence DataNeprilysinRecombinant Fusion ProteinsAspartic Acid EndopeptidasesECE1 protein, humanEndothelin-Converting EnzymesIsoenzymesLeucineMembrane ProteinsMetalloendopeptidasesNeprilysinRecombinant Fusion Proteins

Identifiers

PMID10377252
PMCPMC1220337
OpenAlexW1971130526

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.