Evidence map›Paper›PMID 31614972›Full record

ArticleInternational journal of molecular sciences2019

Specific Features for the Competent Binding of Substrates at the FMN Adenylyltransferase Site of FAD Synthase from

Sonia Arilla-Luna, Ana Serrano, Milagros Medina

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. 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
0.3field-weighted citation impact, top 43% 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, 5 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 1 institution in 1 country.

Sonia Arilla-LunaDepartment of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, 50009 Zaragoza, Spain. arilun2@gmail.com.
Ana SerranoDepartment of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, 50009 Zaragoza, Spain. anaserra1979@gmail.com.
Milagros MedinaDepartment of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, 50009 Zaragoza, Spain. mmedina@unizar.es.ORCID 0000-0001-8743-0182
Universidad de Zaragoza · ES

Funding

Gobierno de Aragón E35_17R-FEDERMinisterio de Economía, Industria y Competitividad, Gobierno de España BIO2016-75183-P AEI/FEDER
6 · The paper itself

Abstract

Bifunctional FAD synthases (FADSs) catalyze FMN (flavin mononucleotide) and FAD (flavinadenine dinucleotide) biosynthesis at their C-riboflavin kinase (RFK) and N-FMN:adenylyltransferase (FMNAT) modules, respectively. Biophysical properties and requirements for their FMNAT activity differ among species. Here, we evaluate the relevance of the integrity of the binding site of the isoalloxazine of flavinic substrates for FMNAT catalysis in

Indexed as

ThermodynamicsAdenosine TriphosphateBinding SitesCatalytic DomainCorynebacteriumFlavin-Adenine DinucleotideKineticsLigandsModels, MolecularNitric Oxide SynthaseNucleotidyltransferasesSubstrate SpecificityAdenosine TriphosphateFlavin-Adenine DinucleotideFMN adenylyltransferaseLigandsNitric Oxide SynthaseNucleotidyltransferasesadenylyltransferase activitybiosynthesishead-to-tail organizationisothermal titration calorimetryprokaryotic FAD synthasesite-directed mutagenesisspecies-specific traitssteady-state kinetics

Identifiers

PMID31614972
PMCPMC6829536
OpenAlexW2980225738

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.