Evidence map›Paper›PMID 33995893›Full record

ArticleComputational and structural biotechnology journal2021

Structural modeling of a novel membrane-bound globin-coupled sensor in

Dietmar Hammerschmid, Francesca Germani, Salvador I Drusin, Charline Fagnen, Claudio D Schuster, David Hoogewijs, Marcelo A Marti, Catherine Venien-Bryan, Luc Moens, Sabine Van Doorslaer and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Computational and structural biotechnology journal, 2021. 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
0.2field-weighted citation impact, top 54% 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, 3 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

12 authors at 5 institutions in 5 countries.

Dietmar HammerschmidProteinchemistry, Proteomics and Epigenetic Signalling, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
Francesca GermaniProteinchemistry, Proteomics and Epigenetic Signalling, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
Salvador I DrusinDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires (FCEyN-UBA) e Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN) CONICET, Pabellòn 2 de Ciudad Universitaria, Ciudad de Buenos Aires C1428EHA, Argentina.
Charline FagnenSorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005 Paris, France.
Claudio D SchusterDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires (FCEyN-UBA) e Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN) CONICET, Pabellòn 2 de Ciudad Universitaria, Ciudad de Buenos Aires C1428EHA, Argentina.
David HoogewijsSection of Medicine, Department of Endocrinology, Metabolism and Cardiovascular System, University of Fribourg, Switzerland.
Marcelo A MartiDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires (FCEyN-UBA) e Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN) CONICET, Pabellòn 2 de Ciudad Universitaria, Ciudad de Buenos Aires C1428EHA, Argentina.
Catherine Venien-BryanSorbonne Université, UMR 7590, CNRS, Muséum National d'Histoire Naturelle, Institut de Minéralogie, Physique des Matériaux et Cosmochimie, IMPMC, 75005 Paris, France.
Luc MoensProteinchemistry, Proteomics and Epigenetic Signalling, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
Sabine Van DoorslaerBiophysics and Biomedical Physics, Department of Chemistry, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
Frank SobottBiomolecular & Analytical Mass Spectrometry, Department of Chemistry, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerp, Belgium.
Sylvia DewildeProteinchemistry, Proteomics and Epigenetic Signalling, Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
University of Antwerp · BEConsejo Nacional de Investigaciones Científicas y Técnicas · ARCentre National de la Recherche Scientifique · FRUniversity of Fribourg · CHUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Globin-coupled sensors (GCS) usually consist of three domains: a sensor/globin, a linker, and a transmitter domain. The globin domain (GD), activated by ligand binding and/or redox change, induces an intramolecular signal transduction resulting in a response of the transmitter domain. Depending on the nature of the transmitter domain, GCSs can have different activities and functions, including adenylate and di-guanylate cyclase, histidine kinase activity, aerotaxis and/or oxygen sensing function. The gram-negative delta-proteobacterium

Indexed as

AfGcHK, Anaeromyxobacter sp. Fw109-5 GcHKAsFRMF, Ascaris suum FRMF-amide receptorAvGReg, Azotobacter vinilandii GregBpGReg, Bordetella pertussis GregBsHemAT, Bacillus subtilis HemATCCS, collision cross sectionCeGLB26, Caenorhabditis elegans globin 26CeGLB33, Caenorhabditis elegans globin 33CeGLB6, Caenorhabditis elegans globin 6CIU, collision-induced unfoldingCMC, critical micelle concentrationCV, cyclic voltammetryDDM, n-dodecyl-β-d-maltosideDPV, differential pulse voltammetryEcDosC, Escherichia coli Dos with DGC activityFMRF, H-Phe-Met-Arg-Phe-NH2 neuropeptideGb, globinGCS, globin-coupled sensorGD, globin domainGeobacter sulfurreducensGGDEF, Gly-Gly-Asp-Glu-Phe motiveGintHb, hemoglobin from Gasterophilus intestinalisGlobin-coupled sensorGsGCS162, GD of GsGCSGsGCS, Geobacter sulfurreducens GCSIM-MS, ion mobility-mass spectrometryLmHemAC, Leishmania major HemACMaPgb, Methanosarcina acetivorans protoglobinmNgb, mouse neuroglobinMtTrHbO, Mycobacterium tuberculosis truncated hemoglobin ONH4OAc, ammonium acetateOG, n-octyl-β-d-glucopyranosidePccGCS, Pectobacterium carotivorum GCSPcMb, Physether catodon myoglobinPDE, phosphodiesterasePsiE, phosphate-starvation-inducible ERR, resonance RamanSaktrHb, Streptomyces avermitilis truncated hemoglobin-antibiotic monooxygenaseSCE, saturated calomel electrodeSHE, standard hydrogen electrodeSwMb, myoglobin from sperm whaleTD, Transmitter domainTmD, Transmembrane domainTransmembrane-coupled globinsTransmembrane domain

Identifiers

PMID33995893
PMCPMC8076648
OpenAlexW3143160402

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.