Evidence map›Paper›PMID 32415427›Full record

ArticleBiomolecular NMR assignments2020

Inês B Trindade, Michele Invernici, Francesca Cantini, Ricardo O Louro, Mario Piccioli

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

Article in Biomolecular NMR assignments, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023
    Article
  2. Protein Interactions inMolecules (Basel, Switzerland) · 2023
    Article
  3. 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

5 authors at 2 institutions in 2 countries.

Inês B TrindadeInstituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal.
Michele InverniciMagnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Francesca CantiniMagnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Ricardo O LouroInstituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal. louro@itqb.unl.pt.
Mario PiccioliMagnetic Resonance Center (CERM), Department of Chemistry and Consorzio Interuniversitario Risonanze Magnetiche Metallo Proteine (C.I.R.M.M.P.), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. piccioli@cerm.unifi.it.ORCID 0000-0001-9882-9754
Interuniversity Consortium for Magnetic Resonance · ITUniversidade Nova de Lisboa · PT

Funding

Ente Cassa di Risparmio di Firenze 2016-0985European Cooperation in Science and Technology CA15133Fundação para a Ciência e a Tecnologia PD/BD/135187/2017Horizon 2020 () TIMB3-Project 810856INSTRUCT-ERIC PID 4509
6 · The paper itself

Abstract

High potential iron-sulfur proteins (HiPIPs) are a class of small proteins (50-100 aa residues), containing a 4Fe-4S iron-sulfur cluster. The 4Fe-4S cluster shuttles between the oxidation states [Fe

Indexed as

Carbon-13 Magnetic Resonance SpectroscopyProton Magnetic Resonance SpectroscopyBacterial ProteinsIron-Sulfur ProteinsNitrogen IsotopesPhotosynthetic Reaction Center Complex ProteinsRhodopseudomonasBacterial Proteinshigh potential iron-sulfur proteinIron-Sulfur ProteinsNitrogen-15Nitrogen IsotopesPhotosynthetic Reaction Center Complex ProteinsFast nuclear relaxationHigh potential iron–sulfur proteinsMetalloproteinsParamagnetic NMR

Identifiers

PMID32415427
PMCPMC7462912
OpenAlexW3024699977

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.