Evidence map›Paper›PMID 35563263›Full record

ArticleInternational journal of molecular sciences2022

The Conformation of the N-Terminal Tails of

João P L Guerra, Clement E Blanchet, Bruno J C Vieira, Ana V Almeida, João C Waerenborgh, Nykola C Jones, Søren V Hoffmann, Pedro Tavares, Alice S Pereira

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
0.4field-weighted citation impact, top 42% 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, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Influence of Cupric (CuInternational journal of molecular sciences · 2023
    Article
  4. Article
  5. Morphological Diversity of Dps Complex with Genomic DNA.International journal of molecular sciences · 2023
    Article
  6. 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

9 authors at 4 institutions in 3 countries.

João P L GuerraAssociate Laboratory i4HB, Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.ORCID 0000-0001-5441-9446
Clement E BlanchetEuropean Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany.
Bruno J C VieiraCentro de Ciências e Tecnologias Nucleares, DECN, Instituto Superior Técnico, Universidade de Lisboa, Estrada Nacional 10, 2695-066 Bobadela, Portugal.ORCID 0000-0002-6536-9875
Ana V AlmeidaAssociate Laboratory i4HB, Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.
João C WaerenborghCentro de Ciências e Tecnologias Nucleares, DECN, Instituto Superior Técnico, Universidade de Lisboa, Estrada Nacional 10, 2695-066 Bobadela, Portugal.ORCID 0000-0001-6171-4099
Nykola C JonesISA, Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark.
Søren V HoffmannISA, Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark.ORCID 0000-0002-8018-5433
Pedro TavaresAssociate Laboratory i4HB, Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.ORCID 0000-0002-7398-2661
Alice S PereiraAssociate Laboratory i4HB, Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal.ORCID 0000-0001-5567-6073
Universidade Nova de Lisboa · PTAarhus University · DKUniversity of Lisbon · PTEuropean Molecular Biology Laboratory · DE

Funding

EU HORIZON 2020 CA15126 MOBIEUEU HORIZON 2020 CALIPSOplusFundação para a Ciência e Tecnologia COVID/BD/152497/2022Fundação para a Ciência e Tecnologia COVID/BD/152498/2022Fundação para a Ciência e Tecnologia LA/P/0140/2020Fundação para a Ciência e Tecnologia PD/00193/2012Fundação para a Ciência e Tecnologia PD/BD/135476/2017Fundação para a Ciência e Tecnologia PD/BD/135477/2017Fundação para a Ciência e Tecnologia PTDC/BIA-PRO/111485/2009Fundação para a Ciência e Tecnologia PTDC/QUI/64248/2006Fundação para a Ciência e Tecnologia UIDB/00068/2020Fundação para a Ciência e Tecnologia UIDB/04378/2020
6 · The paper itself

Abstract

DNA-binding proteins from starved cells (Dps) are homododecameric nanocages, with N- and C-terminal tail extensions of variable length and amino acid composition. They accumulate iron in the form of a ferrihydrite mineral core and are capable of binding to and compacting DNA, forming low- and high-order condensates. This dual activity is designed to protect DNA from oxidative stress, resulting from Fenton chemistry or radiation exposure. In most Dps proteins, the DNA-binding properties stem from the N-terminal tail extensions. We explored the structural characteristics of a Dps from

Indexed as

Bacterial ProteinsDeinococcusAmino Acid SequenceDNAIronModels, MolecularOsmolar ConcentrationBacterial ProteinsDNAIronbiological small-angle X-ray scatteringconformational changesDeinococcus grandisDNA-binding protein from starved cells (Dps)mini-ferritinsMössbauer spectroscopyN-terminal tail extensions

Identifiers

PMID35563263
PMCPMC9103930
OpenAlexW4224983714

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.