Evidence map›Paper›PMID 32085611›Full record

ArticleInternational journal of molecular sciences2020

Localization of Annexin A6 in Matrix Vesicles During Physiological Mineralization.

Ekeveliny Amabile Veschi, Maytê Bolean, Agnieszka Strzelecka-Kiliszek, Joanna Bandorowicz-Pikula, Slawomir Pikula, Thierry Granjon, Saida Mebarek, David Magne, Ana Paula Ramos, Nicola Rosato and 4 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  14. Apigenin Modulates AnxA6- and TNAP-Mediated Osteoblast Mineralization.International journal of molecular sciences · 2022
    Article
  15. Article
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  17. Matrix Vesicles as a Therapeutic Target for Vascular Calcification.Frontiers in cell and developmental biology · 2022
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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

14 authors at 5 institutions in 5 countries.

Ekeveliny Amabile VeschiDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da Universidade de São Paulo (FFCLRP-USP), Ribeirão Preto, São Paulo 14040-900, Brazil.
Maytê BoleanDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da Universidade de São Paulo (FFCLRP-USP), Ribeirão Preto, São Paulo 14040-900, Brazil.
Agnieszka Strzelecka-KiliszekNencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.
Joanna Bandorowicz-PikulaNencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.
Slawomir PikulaNencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.ORCID 0000-0003-4640-3094
Thierry GranjonUniversite Lyon 1, UFR Chimie Biochimie, CEDEX, 69 622 Villeurbanne, France.
Saida MebarekUniversite Lyon 1, UFR Chimie Biochimie, CEDEX, 69 622 Villeurbanne, France.
David MagneUniversite Lyon 1, UFR Chimie Biochimie, CEDEX, 69 622 Villeurbanne, France.
Ana Paula RamosDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da Universidade de São Paulo (FFCLRP-USP), Ribeirão Preto, São Paulo 14040-900, Brazil.ORCID 0000-0001-6200-8989
Nicola RosatoDepartment of Experimental Medicine, University of Rome Tor Vergata, 00133 Rome, Italy.
José Luis MillánSanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037, USA.
Rene BuchetUniversite Lyon 1, UFR Chimie Biochimie, CEDEX, 69 622 Villeurbanne, France.
Massimo BottiniDepartment of Experimental Medicine, University of Rome Tor Vergata, 00133 Rome, Italy.
Pietro CiancagliniDepartamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto da Universidade de São Paulo (FFCLRP-USP), Ribeirão Preto, São Paulo 14040-900, Brazil.ORCID 0000-0002-2785-1345
Universidade de Ribeirão Preto · BRUniversité Claude Bernard Lyon 1 · FRInstytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLUniversity of Rome Tor Vergata · ITSanford Burnham Prebys Medical Discovery Institute · US

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 304021/2017-2Coordenação de Aperfeiçoamento de Pessoal de Nível Superior Finance Code 001, 1738449, 88887.320304/2019-00Fundação de Amparo à Pesquisa do Estado de São Paulo 2014/00371-1, 2015/06814-5, 2016/21236-6, 2017/08892-9
6 · The paper itself

Abstract

Annexin A6 (AnxA6) is the largest member of the annexin family of proteins present in matrix vesicles (MVs). MVs are a special class of extracellular vesicles that serve as a nucleation site during cartilage, bone, and mantle dentin mineralization. In this study, we assessed the localization of AnxA6 in the MV membrane bilayer using native MVs and MV biomimetics. Biochemical analyses revealed that AnxA6 in MVs can be divided into three distinct groups. The first group corresponds to Ca

Indexed as

Calcification, Physiologic1,2-DipalmitoylphosphatidylcholineAnnexin A6Calorimetry, Differential ScanningCholesterolExtracellular MatrixExtracellular VesiclesHumansLipid BilayersMembrane MicrodomainsMicroscopy, Atomic ForceProteolipids1,2-DipalmitoylphosphatidylcholineAnnexin A6CholesterolLipid BilayersProteolipidsproteoliposomesAnnexin A6biomineralizationdifferential scanning calorimetry.Langmuir monolayersmatrix vesiclesproteoliposomes

Identifiers

PMID32085611
PMCPMC7072960
OpenAlexW3007959358

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.