ArticleThe Biochemical journal2002
The C-terminal domain, but not the interchain disulphide, is required for the activity and intracellular trafficking of aminopeptidase A.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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.
Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- The role of multifunctional M1 metallopeptidases in cell cycle progression.Annals of botany · 2011Review
- The catalytic and protein-protein interaction domains are required for APM1 function.Plant physiology · 2010Article
- Mutation of the membrane-associated M1 protease APM1 results in distinct embryonic and seedling developmental defects in Arabidopsis.The Plant cell · 2009Article
- Biochemical and enzymatic properties of the M1 family of aminopeptidases involved in the regulation of blood pressure.Heart failure reviews · 2008Review
- Article
- Enzymatic pathways of the brain renin-angiotensin system: unsolved problems and continuing challenges.Regulatory peptides · 2007Review
- The deficiency of PIP2 5-phosphatase in Lowe syndrome affects actin polymerization.American journal of human genetics · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian aminopeptidase A (APA; glutamyl aminopeptidase; EC 3.4.11.7) is a type II membrane-spanning protein consisting of a short N-terminal cytosolic domain, a single transmembrane domain and a large extracellular C-terminal domain containing the active site. The extracellular domain consists of a 107 kDa domain, containing the zinc-binding motif and all the residues involved in catalysis, separated by a protease-susceptible hinge region from the 45 kDA C-terminal domain of unknown function. To investigate the role of the 45 kDa domain, a construct of murine APA (G594Delta) lacking this C-terminal domain was expressed in COS-1 cells. This truncated form of APA, although expressed, lacked enzymic activity and failed to reach the cell surface. Confocal immunofluorescence microscopy revealed that G594Delta co-localized with the lectin concanavalin A and had a similar staining pattern as protein disulphide-isomerase, indicating that it was retained in the endoplasmic reticulum. Thus the C-terminal 45 kDa domain appears to be acting like a pro-domain and seems to be required for the correct folding and trafficking of APA. In contrast, mutation of cysteine-43 to serine, which is involved in the disulphide-linkage of the APA homodimer, did not affect the enzymic activity, cellular location or rate of trafficking through the secretory pathway of APA.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.