ReviewIUCrJ2023
Structure and function relationship of formate dehydrogenases: an overview of recent progress.
Review in IUCrJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
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.
Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Recent Progress in Understanding the Mechanism of Formate Dehydrogenases.Chembiochem : a European journal of chemical biology · 2026Review
- An unexpected alternative viologen electron mediator site in tungsten-containing formate dehydrogenase.FEBS letters · 2026Article
- To Biotic or Abiotic: Biohybrid Systems for Artificial Photosynthesis.Chemical reviews · 2026Review
- Recent advances in exploring the composition and evolution of the prokaryotic selenoproteome.Applied and environmental microbiology · 2026Review
- Structural Insights Into COAngewandte Chemie (International ed. in English) · 2026Article
- Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Closing the Loop in the Carbon Cycle: Enzymatic Reactions Housed in Metal-Organic Frameworks for COApplied biochemistry and biotechnology · 2025Review
- Synthetic Challenges toward Modeling Formate Dehydrogenases Using [WInorganic chemistry · 2024Article
- Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.Nature communications · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.