Evidence map›Paper›PMID 28348001›Full record

ReviewEndocrine connections2017

Dissecting carboxypeptidase E: properties, functions and pathophysiological roles in disease.

Lin Ji, Huan-Tong Wu, Xiao-Yan Qin, Rongfeng Lan

Open access · goldAbstract readReview
In one paragraph

Review in Endocrine connections, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 79 citations in OpenAlex.

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  20. Mapping prohormone processing by proteases in human enteroendocrine cells using genetically engineered organoid models.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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 2 institutions in 1 country.

Lin JiDepartment of Cell Biology & Medical GeneticsSchool of Medicine, Shenzhen University, Shenzhen, China.
Huan-Tong WuBeijing Engineering Research Center of Food Environment and HealthCollege of Life & Environmental Sciences, Minzu University of China, Beijing, China.
Xiao-Yan QinBeijing Engineering Research Center of Food Environment and HealthCollege of Life & Environmental Sciences, Minzu University of China, Beijing, China bjqinxiaoyan@muc.edu.cn lan@szu.edu.cn.
Rongfeng LanDepartment of Cell Biology & Medical GeneticsSchool of Medicine, Shenzhen University, Shenzhen, China bjqinxiaoyan@muc.edu.cn lan@szu.edu.cn.
Minzu University of China · CNShenzhen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since discovery in 1982, carboxypeptidase E (CPE) has been shown to be involved in the biosynthesis of a wide range of neuropeptides and peptide hormones in endocrine tissues, and in the nervous system. This protein is produced from pro-CPE and exists in soluble and membrane forms. Membrane CPE mediates the targeting of prohormones to the regulated secretory pathway, while soluble CPE acts as an exopeptidase and cleaves C-terminal basic residues from peptide intermediates to generate bioactive peptides. CPE also participates in protein internalization, vesicle transport and regulation of signaling pathways. Therefore, in two types of CPE mutant mice,

Indexed as

carboxypeptidase Ediabetesexopeptidaseobesityregulated secretory pathway

Identifiers

PMID28348001
PMCPMC5434747
OpenAlexW2602095364

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.