Evidence map›Paper›PMID 39148770›Full record

ArticleChemical science2024

Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement.

Guilherme Vilela-Alves, Rita R Manuel, Aldino Viegas, Philippe Carpentier, Frédéric Biaso, Bruno Guigliarelli, Inês A C Pereira, Maria João Romão, Cristiano Mota

Abstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Recent Progress in Understanding the Mechanism of Formate Dehydrogenases.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Semiartificial COChemical reviews · 2026
    Review
  4. Toward Solar-Powered Growth of AutotrophicJournal of the American Chemical Society · 2026
    Article
  5. Article
  6. Structural Insights Into COAngewandte Chemie (International ed. in English) · 2026
    Article
  7. Review
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

9 authors.

Guilherme Vilela-AlvesAssociate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa 2829-516 Caparica Portugal cd.mota@fct.unl.pt mjr@fct.unl.pt.ORCID https://orcid.org/0000-0003-0003-9637
Rita R ManuelInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa Av. da República 2780-157 Oeiras Portugal ipereira@itqb.unl.pt.ORCID https://orcid.org/0000-0001-8068-2053
Aldino ViegasAssociate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa 2829-516 Caparica Portugal cd.mota@fct.unl.pt mjr@fct.unl.pt.ORCID https://orcid.org/0000-0003-1733-136X
Philippe CarpentierEuropean Synchrotron Radiation Facility Grenoble France.
Frédéric BiasoAix Marseille Univ, CNRS, BIP, Laboratoire de Bioénergétique et Ingénierie des Protéines Marseille 13402 France.
Bruno GuigliarelliAix Marseille Univ, CNRS, BIP, Laboratoire de Bioénergétique et Ingénierie des Protéines Marseille 13402 France.ORCID https://orcid.org/0000-0003-3807-1421
Inês A C PereiraInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa Av. da República 2780-157 Oeiras Portugal ipereira@itqb.unl.pt.ORCID https://orcid.org/0000-0003-3283-4520
Maria João RomãoAssociate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa 2829-516 Caparica Portugal cd.mota@fct.unl.pt mjr@fct.unl.pt.ORCID https://orcid.org/0000-0002-3004-0543
Cristiano MotaAssociate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa 2829-516 Caparica Portugal cd.mota@fct.unl.pt mjr@fct.unl.pt.ORCID https://orcid.org/0000-0002-8999-0420

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal-dependent formate dehydrogenases are very promising targets for enzyme optimization and design of bio-inspired catalysts for CO

Identifiers

PMID39148770
PMCPMC11323313

What OpenQuestion holds

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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.