Evidence map›Paper›PMID 34985724›Full record

ArticleBiomolecular NMR assignments2022

Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system.

Ameeq Ul Mushtaq, Jörgen Ådén, Athar Alam, Anders Sjöstedt, Gerhard Gröbner

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

Article in Biomolecular NMR assignments, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 100% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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 1 institution in 1 country.

Ameeq Ul MushtaqDepartment of Chemistry, University of Umeå, 901 87, Umeå, Sweden.
Jörgen ÅdénDepartment of Chemistry, University of Umeå, 901 87, Umeå, Sweden.
Athar AlamDepartment of Clinical Microbiology, University of Umeå, 901 87, Umeå, Sweden.
Anders SjöstedtDepartment of Clinical Microbiology, University of Umeå, 901 87, Umeå, Sweden.
Gerhard GröbnerDepartment of Chemistry, University of Umeå, 901 87, Umeå, Sweden. gerhard.grobner@chem.umu.se.ORCID 0000-0001-7380-8797
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and

Indexed as

Escherichia coli ProteinsFrancisella tularensisType VI Secretion SystemsHSP70 Heat-Shock ProteinsNuclear Magnetic Resonance, BiomolecularVirulenceEscherichia coli ProteinsHSP70 Heat-Shock ProteinsType VI Secretion Systems15N relaxationClpB chaperoneFrancisella tularensisNMR resonance assignmentType VI secretion system

Identifiers

PMID34985724
PMCPMC9068650
OpenAlexW4206058078

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.