Evidence map›Paper›PMID 34019876›Full record

ArticleThe Journal of biological chemistry

Identification and characterization of the pyridoxal 5'-phosphate allosteric site in Escherichia coli pyridoxine 5'-phosphate oxidase.

Anna Barile, Theo Battista, Annarita Fiorillo, Martino Luigi di Salvo, Francesco Malatesta, Angela Tramonti, Andrea Ilari, Roberto Contestabile

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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

8 authors at 2 institutions in 1 country.

Anna BarileIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Theo BattistaIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Annarita FiorilloIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Martino Luigi di SalvoDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Francesco MalatestaDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Angela TramontiIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy.
Andrea IlariIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy.
Roberto ContestabileDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Sapienza Università di Roma, Roma, Italy. Electronic address: roberto.contestabile@uniroma1.it.
Institute of Molecular Biology and Pathology · ITIstituto Pasteur · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyridoxal 5'-phosphate (PLP), the catalytically active form of vitamin B

Indexed as

Allosteric SiteCrystallography, X-RayEscherichia coliEscherichia coli InfectionsEscherichia coli ProteinsHumansModels, MolecularProtein ConformationPyridoxal PhosphatePyridoxaminephosphate OxidaseEscherichia coli ProteinsPyridoxal PhosphatePyridoxaminephosphate Oxidaseallosteric regulationasymmetrybacterial metabolismcrystal structureenzyme inhibitorpyridoxal phosphatepyridoxine 5’-phosphate oxidasevitamin B(6) metabolism

Identifiers

PMID34019876
PMCPMC8215295
OpenAlexW3163894148

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.