Evidence map›Paper›PMID 37989209›Full record

ArticleBiochemistry2023

Naiá P Santos, Hans Brandstetter, Elfriede Dall

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.4field-weighted citation impact, top 21% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Naiá P SantosDepartment of Biosciences and Medical Biology, University of Salzburg, 5020 Salzburg, Austria.
Hans BrandstetterDepartment of Biosciences and Medical Biology, University of Salzburg, 5020 Salzburg, Austria.ORCID 0000-0002-6089-3045
Elfriede DallDepartment of Biosciences and Medical Biology, University of Salzburg, 5020 Salzburg, Austria.ORCID 0000-0002-0823-8983
University of Salzburg · AT

Funding

Austrian Science Fund FWF P 31867
6 · The paper itself

Abstract

Cystatins encode a high functional variability not only because of their ability to inhibit different classes of proteases but also because of their propensity to form oligomers and amyloid fibrils. Phytocystatins, essential regulators of protease activity in plants, specifically inhibit papain-like cysteine proteases (PLCPs) and legumains through two distinct cystatin domains. Mammalian cystatins can form amyloid fibrils; however, the potential for amyloid fibril formation of phytocystatins remains unknown. In this study, we demonstrate that

Indexed as

ArabidopsisCystatinsAmyloidAnimalsMammalsPapainPeptide HydrolasesAmyloidCystatinsPapainPeptide Hydrolases

Identifiers

PMID37989209
PMCPMC10702442
OpenAlexW4388850544

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.