Evidence map›Paper›PMID 34582998›Full record

ArticleBiochimie2022

Spectroscopic and functional characterization of the [2Fe-2S] scaffold protein Nfu from Synechocystis PCC6803.

Zechariah Thompson, Insiya Fidai, Christine Wachnowsky, Amber L Hendricks, J A Cowan

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

Article in Biochimie, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 60% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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.

Zechariah ThompsonDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA.
Insiya FidaiDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA; The Biophysics Graduate Program, The Ohio State University, USA.
Christine WachnowskyDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA; The Ohio State Biochemistry Program, The Ohio State University, USA.
Amber L HendricksDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA.
J A CowanDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA; The Biophysics Graduate Program, The Ohio State University, USA; The Ohio State Biochemistry Program, The Ohio State University, USA. Electronic address: cowan@chemistry.ohio-state.edu.
The Ohio State University · US

Funding

Novel Therapeutic Approaches to Pathogen InactivationR21AI072443 · NIAID · OHIO STATE UNIVERSITY · PI COWAN, JAMES A · 2009 to 2010
$398k
NIAID NIH HHS R21 AI072443
6 · The paper itself

Abstract

Iron-sulfur clusters are ubiquitous cofactors required for various essential metabolic processes. Conservation of proteins required for their biosynthesis and trafficking allows for simple bacteria to be used as models to aid in exploring these complex pathways in higher organisms. Cyanobacteria are among the most investigated organisms for these processes, as they are unicellular and can survive under photoautotrophic and heterotrophic conditions. Herein, we report the potential role of Synechocystis PCC6803 NifU (now named SyNfu) as the principal scaffold protein required for iron-sulfur cluster biosynthesis in that organism. SyNfu is a well-folded protein with distinct secondary structural elements, as evidenced by circular dichroism and a well-dispersed pattern of

Indexed as

Nuclear Magnetic Resonance, BiomolecularBacterial ProteinsHumansIron-Sulfur ProteinsSynechocystisBacterial ProteinsIron-Sulfur ProteinsIron-sulfur clusterNfuSynechocystisTrafficking

Identifiers

PMID34582998
PMCPMC8724361
OpenAlexW3203392851

What OpenQuestion holds

Textmetadata
LicenceTDM
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.