Evidence map›Paper›PMID 32315567›Full record

ArticleOpen biology2020

Zinc-α2-glycoprotein as an inhibitor of amine oxidase copper-containing 3.

Matthias Romauch

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Matthias RomauchInstitute of Molecular Biosciences, Karl-Franzens-University, Graz, Austria.
University of Graz · AT

Funding

Austrian Science Fund FWF TRP 4
6 · The paper itself

Abstract

Zinc-α2-glycoprotein (ZAG) is a major plasma protein whose levels increase in chronic energy-demanding diseases and thus serves as an important clinical biomarker in the diagnosis and prognosis of the development of cachexia. Current knowledge suggests that ZAG mediates progressive weight loss through β-adrenergic signalling in adipocytes, resulting in the activation of lipolysis and fat mobilization. Here, through cross-linking experiments, amine oxidase copper-containing 3 (AOC3) is identified as a novel ZAG binding partner. AOC3-also known as vascular adhesion protein 1 (VAP-1) and semicarbazide sensitive amine oxidase (SSAO)-deaminates primary amines, thereby generating the corresponding aldehyde, H

Indexed as

3T3-L1 CellsAdipokinesAldehydesAllosteric RegulationAmine Oxidase (Copper-Containing)AmmoniaAnimalsCell Adhesion MoleculesCell LineHEK293 CellsHumansHydrogen PeroxideMiceModels, MolecularOctopamineProtein BindingAdipokinesAldehydesAmine Oxidase (Copper-Containing)AmmoniaAOC3 protein, humanAZGP1 protein, humanAZGP1 protein, mouseCell Adhesion MoleculesHydrogen PeroxideOctopaminesemicarbazide-sensitive amine oxidase-vascular adhesion protein-1, mouseZn-Alpha-2-GlycoproteinAOC3cachexiaglycosylationprotein–protein interactionZAG

Identifiers

PMID32315567
PMCPMC6685929
OpenAlexW2991234713

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.