ReviewEcoSal Plus2015
Biosynthesis and Insertion of the Molybdenum Cofactor.
Review in EcoSal Plus, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 31 citations in OpenAlex.
- A tungsten-specific maturation pathway governs cofactor assembly of a COThe Journal of biological chemistry · 2026Article
- TheISME communications · 2026Article
- The Mechanisms of Molybdate Distribution and Homeostasis with Special Focus on the Model PlantMolecules (Basel, Switzerland) · 2023Review
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- A step into the rare biosphere: genomic features of the new genusFrontiers in microbiology · 2023Article
- Methionine oxidation under anaerobic conditions in Escherichia coli.Molecular microbiology · 2022Article
- The History of the Molybdenum Cofactor-A Personal View.Molecules (Basel, Switzerland) · 2022Review
- Physiological Importance of Molybdate Transporter Family 1 in Feeding the Molybdenum Cofactor Biosynthesis Pathway inMolecules (Basel, Switzerland) · 2022Article
- Identification and characterization of a noncanonical menaquinone-linked formate dehydrogenase.The Journal of biological chemistry · 2022Article
- Biogeographic and Evolutionary Patterns of Trace Element Utilization in Marine Microbial World.Genomics, proteomics & bioinformatics · 2021Article
- Tungsten enzymes play a role in detoxifying food and antimicrobial aldehydes in the human gut microbiome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bioinformatics of Metalloproteins and Metalloproteomes.Molecules (Basel, Switzerland) · 2020Review
- Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Transition metals and host-microbe interactions in the inflamed intestine.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019Review
- Horizontal acquisition of a hypoxia-responsive molybdenum cofactor biosynthesis pathway contributed to Mycobacterium tuberculosis pathoadaptation.PLoS pathogens · 2017Article
- Protein complex formation during denitrification by Pseudomonas aeruginosa.Microbial biotechnology · 2017Review
- Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transition element molybdenum (Mo) is of primordial importance for biological systems, because it is required by enzymes catalyzing key reactions in the global carbon, sulfur, and nitrogen metabolism. To gain biological activity, Mo has to be complexed by a special cofactor. With the exception of bacterial nitrogenase, all Mo-dependent enzymes contain a unique pyranopterin-based cofactor coordinating a Mo atom at their catalytic site. Various types of reactions are catalyzed by Mo-enzymes in prokaryotes including oxygen atom transfer, sulfur or proton transfer, hydroxylation, or even nonredox reactions. Mo-enzymes are widespread in prokaryotes and many of them were likely present in the Last Universal Common Ancestor. To date, more than 50--mostly bacterial--Mo-enzymes are described in nature. In a few eubacteria and in many archaea, Mo is replaced by tungsten bound to the same unique pyranopterin. How Mo-cofactor is synthesized in bacteria is reviewed as well as the way until its insertion into apo-Mo-enzymes.
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.