Evidence map›Paper›PMID 23593335›Full record

ArticlePloS one2013

The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.

Zvonimir Marelja, Mita Mullick Chowdhury, Carsten Dosche, Carsten Hille, Otto Baumann, Hans-Gerd Löhmannsröben, Silke Leimkühler

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  7. Urm1: A Non-Canonical UBL.Biomolecules · 2021
    Review
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  10. The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019
    Review
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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

7 authors at 1 institution in 1 country.

Zvonimir MareljaDepartment of Molecular Enzymology, Institute of Biochemistry, University of Potsdam, Potsdam, Germany.
Mita Mullick Chowdhury
Carsten Dosche
Carsten Hille
Otto Baumann
Hans-Gerd Löhmannsröben
Silke Leimkühler
University of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In humans, the L-cysteine desulfurase NFS1 plays a crucial role in the mitochondrial iron-sulfur cluster biosynthesis and in the thiomodification of mitochondrial and cytosolic tRNAs. We have previously demonstrated that purified NFS1 is able to transfer sulfur to the C-terminal domain of MOCS3, a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation. However, no direct evidence existed so far for the interaction of NFS1 and MOCS3 in the cytosol of human cells. Here, we present direct data to show the interaction of NFS1 and MOCS3 in the cytosol of human cells using Förster resonance energy transfer and a split-EGFP system. The colocalization of NFS1 and MOCS3 in the cytosol was confirmed by immunodetection of fractionated cells and localization studies using confocal fluorescence microscopy. Purified NFS1 was used to reconstitute the lacking molybdoenzyme activity of the Neurospora crassa nit-1 mutant, giving additional evidence that NFS1 is the sulfur donor for Moco biosynthesis in eukaryotes in general.

Indexed as

Carbon-Sulfur LyasesCoenzymesCysteineCytosolFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHeLa CellsHumansMetalloproteinsMicroscopy, FluorescenceMolybdenum CofactorsMutant ProteinsNeurosporaNitrate ReductaseNucleotidyltransferasesProtein Interaction MappingCarbon-Sulfur LyasesCoenzymesCysteineenhanced green fluorescent proteinGreen Fluorescent ProteinsMetalloproteinsMOCS3 protein, humanMolybdenum CofactorsmolybdopterinMutant ProteinsNFS1 protein, humanNitrate ReductaseNucleotidyltransferasesPteridinesRecombinant Fusion ProteinsSulfurSulfurtransferases

Identifiers

PMID23593335
PMCPMC3625234
OpenAlexW1999383598

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.