Evidence map›Paper›PMID 23946482›Full record

ArticleThe Journal of biological chemistry2013

FAD synthesis and degradation in the nucleus create a local flavin cofactor pool.

Teresa Anna Giancaspero, Giovanni Busco, Concetta Panebianco, Claudia Carmone, Angelica Miccolis, Grazia Maria Liuzzi, Matilde Colella, Maria Barile

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 84 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Teresa Anna GiancasperoFrom the Istituto di Biomembrane e Bioenergetica, Consiglio Nazionale delle Ricerche, and.
Giovanni Busco
Concetta Panebianco
Claudia Carmone
Angelica Miccolis
Grazia Maria Liuzzi
Matilde Colella
Maria Barile
University of Bari Aldo Moro · ITInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FAD is a redox cofactor ensuring the activity of many flavoenzymes mainly located in mitochondria but also relevant for nuclear redox activities. The last enzyme in the metabolic pathway producing FAD is FAD synthase (EC 2.7.7.2), a protein known to be localized both in cytosol and in mitochondria. FAD degradation to riboflavin occurs via still poorly characterized enzymes, possibly belonging to the NUDIX hydrolase family. By confocal microscopy and immunoblotting experiments, we demonstrate here the existence of FAD synthase in the nucleus of different experimental rat models. HPLC experiments demonstrated that isolated rat liver nuclei contain ∼300 pmol of FAD·mg(-1) protein, which was mainly protein-bound FAD. A mean FAD synthesis rate of 18.1 pmol·min(-1)·mg(-1) protein was estimated by both HPLC and continuous coupled enzymatic spectrophotometric assays. Rat liver nuclei were also shown to be endowed with a FAD pyrophosphatase that hydrolyzes FAD with an optimum at alkaline pH and is significantly inhibited by adenylate-containing nucleotides. The coordinate activity of these FAD forming and degrading enzymes provides a potential mechanism by which a dynamic pool of flavin cofactor is created in the nucleus. These data, which significantly add to the biochemical comprehension of flavin metabolism and its subcellular compartmentation, may also provide the basis for a more detailed comprehension of the role of flavin homeostasis in biologically and clinically relevant epigenetic events.

Indexed as

AnimalsCell LineCell NucleusChromatography, High Pressure LiquidFlavin-Adenine DinucleotideHomeostasisHumansHydrolysisImmunoblottingLiverMicroscopy, FluorescenceModels, BiologicalMyocytes, CardiacNucleotidyltransferasesRatsRats, WistarFlavin-Adenine DinucleotideFMN adenylyltransferaseNucleotidyltransferasesConfocal MicroscopyFADFAD HydrolysisFAD SynthaseFMNNucleusNUDIX HydrolaseRatRiboflavin

Identifiers

PMID23946482
PMCPMC3790006
OpenAlexW2005467138

What OpenQuestion holds

Textmetadata
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.