Evidence map›Paper›PMID 34199119›Full record

ArticleInternational journal of molecular sciences2021

Mutagenic Analysis of the Putative ABCC6 Substrate-Binding Cavity Using a New Homology Model.

Flora Szeri, Valentina Corradi, Fatemeh Niaziorimi, Sylvia Donnelly, Gwenaëlle Conseil, Susan P C Cole, D Peter Tieleman, Koen van de Wetering

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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  4. Review
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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

8 authors at 3 institutions in 3 countries.

Flora SzeriDepartment of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0003-2572-6820
Valentina CorradiDepartment of Biological Sciences and Centre for Molecular Simulation, University of Calgary, Calgary, AB T2N 1N4, Canada.ORCID 0000-0001-6546-9780
Fatemeh NiaziorimiDepartment of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Sylvia DonnellyDepartment of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Gwenaëlle ConseilDepartment of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.
Susan P C ColeDepartment of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.
D Peter TielemanDepartment of Biological Sciences and Centre for Molecular Simulation, University of Calgary, Calgary, AB T2N 1N4, Canada.
Koen van de WeteringDepartment of Dermatology and Cutaneous Biology and PXE Center of Excellence in Research and Clinical Care, Thomas Jefferson University, Philadelphia, PA 19107, USA.ORCID 0000-0003-1905-2743
Thomas Jefferson University · USQueen's University · CAUniversity of Calgary · CA

Funding

Novel Treatments for PXER01AR072695 · NIAMS · THOMAS JEFFERSON UNIVERSITY · PI LI, QIAOLI, VAN DE WETERING, KOEN · 2018 to 2022
$1.7M
CIHR MOP 133584NIAMS NIH HHS R01 AR072695NIH HHS R01AR072695
6 · The paper itself

Abstract

Inactivating mutations in ABCC6 underlie the rare hereditary mineralization disorder pseudoxanthoma elasticum. ABCC6 is an ATP-binding cassette (ABC) integral membrane protein that mediates the release of ATP from hepatocytes into the bloodstream. The released ATP is extracellularly converted into pyrophosphate, a key mineralization inhibitor. Although ABCC6 is firmly linked to cellular ATP release, the molecular details of ABCC6-mediated ATP release remain elusive. Most of the currently available data support the hypothesis that ABCC6 is an ATP-dependent ATP efflux pump, an un-precedented function for an ABC transporter. This hypothesis implies the presence of an ATP-binding site in the substrate-binding cavity of ABCC6. We performed an extensive mutagenesis study using a new homology model based on recently published structures of its close homolog, bovine Abcc1, to characterize the substrate-binding cavity of ABCC6. Leukotriene C4 (LTC

Indexed as

Binding SitesModels, MolecularMutationAdenosine TriphosphateAmino AcidsAmino Acid SequenceAnimalsATP-Binding Cassette, Sub-Family C ProteinsLigandsMolecular ConformationMutagenesisProtein BindingProtein TransportRatsStructure-Activity RelationshipSubstrate SpecificityABCC6 protein, humanAdenosine TriphosphateAmino AcidsATP-Binding Cassette, Sub-Family C ProteinsLigandsABC transportercellular ATP effluxhomology modelingmutagenesispseudoxanthoma elasticumsubstrate-binding site

Identifiers

PMID34199119
PMCPMC8267652
OpenAlexW3174664081

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.