Evidence map›Paper›PMID 25371336›Full record

ReviewLife (Basel, Switzerland)2013

Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story.

Alessio Ausili, Maria Staiano, Jonathan Dattelbaum, Antonio Varriale, Alessandro Capo, Sabato D'Auria

Open access · goldAbstract readReview
In one paragraph

Review in Life (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 14 citations in OpenAlex.

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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

6 authors at 2 institutions in 2 countries.

Alessio AusiliLaboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy. a.ausili@ibp.cnr.it.
Maria StaianoLaboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy. m.staiano@ibp.cnr.it.
Jonathan DattelbaumDepartment of Chemistry, University of Richmond, Richmond, VA 23173, USA. jdattelb@richmond.edu.
Antonio VarrialeLaboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy. a.varriale@ibp.cnr.it.
Alessandro CapoLaboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy. a.capo@ibp.cnr.it.
Sabato D'AuriaLaboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy. s.dauria@ibp.cnr.it.
Institute of Protein Biochemistry · ITUniversity of Richmond · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein possessing the typical two-domain structure of the periplasmic binding proteins family. The protein is characterized by a very high specificity and affinity to bind to arginine, also at high temperatures. Due to its features, this protein could be taken into account as a potential candidate for the design of a biosensor for arginine. It is important to investigate the stability of proteins when they are used for biotechnological applications. In this article, we review the structural and functional features of an arginine-binding protein from the extremophile Thermotoga maritima with a particular eye on its potential biotechnological applications.

Identifiers

PMID25371336
PMCPMC4187188
OpenAlexW2037261450

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.