Evidence map›Paper›PMID 34140580›Full record

ArticleScientific reports2021

Molecular mechanism of calcium induced trimerization of C1q-like domain of otolin-1 from human and zebrafish.

Rafał Hołubowicz, Andrzej Ożyhar, Piotr Dobryszycki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. 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
0.5field-weighted citation impact, top 38% 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, 7 citations in OpenAlex.

  1. Article
  2. Natural Mutations Affect Structure and Function of gC1q Domain of Otolin-1.International journal of molecular sciences · 2021
    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

3 authors at 1 institution in 1 country.

Rafał HołubowiczDepartment of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland. rafal.holubowicz@pwr.edu.pl.ORCID http://orcid.org/0000-0002-2555-2069
Andrzej OżyharDepartment of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.ORCID http://orcid.org/0000-0002-5874-784X
Piotr DobryszyckiDepartment of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland. piotr.dobryszycki@pwr.edu.pl.ORCID http://orcid.org/0000-0001-5522-2557
Wrocław University of Science and Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C1q superfamily includes proteins involved in innate immunity, insulin sensitivity, biomineralization and more. Among these proteins is otolin-1, which is a collagen-like protein that forms a scaffold for the biomineralization of inner ear stones in vertebrates. The globular C1q-like domain (gC1q), which is the most conserved part of otolin-1, binds Ca

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsCalciumComplement C1qExtracellular Matrix ProteinsHumansModels, MolecularMutationProtein DomainsProtein StabilityProtein Structure, SecondaryTemperatureTerbiumZebrafishCalciumComplement C1qExtracellular Matrix Proteinsotolin-1Terbium

Identifiers

PMID34140580
PMCPMC8211825
OpenAlexW3171944164

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.