Evidence map›Paper›PMID 39604152›Full record

ArticleProtein science : a publication of the Protein Society2024

The ubiquitous pyridoxal 5'-phosphate-binding protein is also an RNA-binding protein.

Claudio Graziani, Anna Barile, Alessia Parroni, Martino Luigi di Salvo, Irene De Cecio, Teresa Colombo, Jill Babor, Valérie de Crécy-Lagard, Roberto Contestabile, Angela Tramonti

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. From Fly to Human: Translational Relevance ofInternational journal of molecular sciences · 2026
    Review
  2. Article
  3. The ubiquitous pyridoxal 5'-phosphate-binding protein is also an RNA-binding protein.Protein science : a publication of the Protein Society · 2024
    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

10 authors.

Claudio GrazianiDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Rome, Italy.
Anna BarileIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Rome, Italy.
Alessia ParroniIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Rome, Italy.
Martino Luigi di SalvoDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Rome, Italy.
Irene De CecioDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Rome, Italy.
Teresa ColomboIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Rome, Italy.
Jill BaborDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.ORCID 0000-0002-9900-2414
Valérie de Crécy-LagardDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA.
Roberto ContestabileDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Rome, Italy.ORCID 0000-0002-5235-9993
Angela TramontiIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Rome, Italy.ORCID 0000-0002-5625-1170

Funding

Pyridoxal 5'-phosphate homeostasis in Escherichia coliR01GM129793 · NIGMS · UNIVERSITY OF FLORIDA · PI DE CRECY-LAGARD, VALERIE A · 2019 to 2022
$1.2M
Consiglio Nazionale delle Ricerche - CNR SAC.AD002.020.032Istituto Pasteur Italia - Fondazione Cenci BolognettiMIUR PRIN 2022 20228395KWNIH HHS GM129793Sapienza Università di Roma RM12117A610B653ESapienza Università di Roma RM122181618E2878
6 · The paper itself

Abstract

The pyridoxal 5'-phosphate binding protein (PLP-BP) is believed to play a crucial role in PLP homeostasis, which may explain why it is found in living organisms from all kingdoms. Escherichia coli YggS is the most studied homolog, but human PLP-BP has also attracted much attention because variants of this protein are responsible for a severe form of B

Indexed as

Pyridoxal PhosphateRNA-Binding ProteinsBinding SitesCarrier ProteinsEscherichia coliEscherichia coli ProteinsHumansModels, MolecularProtein BindingRNACarrier ProteinsEscherichia coli ProteinsPyridoxal PhosphateRNARNA-Binding Proteinspyridoxal 5′‐phosphatepyridoxal 5′‐phosphate‐binding proteinpyridoxal 5′‐phosphate homeostasisRNA‐binding proteinvitamin B6 metabolism

Identifiers

PMID39604152
PMCPMC11602438

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.