ReviewBiochemistry2018
Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.
Review in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
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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.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Catalase-peroxidase (KatG): a potential frontier in tuberculosis drug development.Critical reviews in biochemistry and molecular biology · 2024Review
- Formation of the pyruvoyl-dependent proline reductase Prd fromPNAS nexus · 2024Article
- Gentiopicroside improves high-fat diet-induced NAFLD in association with modulation of host serum metabolome and gut microbiome in mice.Frontiers in microbiology · 2023Article
- Characterizing metabolic drivers ofFrontiers in pharmacology · 2023Article
- Widespread occurrence of covalent lysine-cysteine redox switches in proteins.Nature chemical biology · 2022Article
- Discovery of Potent and Selective Inhibitors against Protein-Derived Electrophilic Cofactors.Journal of the American Chemical Society · 2022Article
- Review
- The Autotrophic Core: An Ancient Network of 404 Reactions Converts HMicroorganisms · 2021Article
- Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor.Nature communications · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.International journal of molecular sciences · 2020Review
- Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.The Journal of biological chemistry · 2020Article
- Optimizing Group Transfer Catalysis by Copper Complex with Redox-Active Ligand in an Entatic State.iScience · 2020Article
- Heme-Cu Binucleating Ligand Supports Heme/OInorganic chemistry · 2019Article
- Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea.Archives of biochemistry and biophysics · 2019Article
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- The Redox Properties of a Cysteine Tryptophylquinone-Dependent Glycine Oxidase Are Distinct from Those of Tryptophylquinone-Dependent Dehydrogenases.Biochemistry · 2019Article
- Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
A protein-derived cofactor is a catalytic or redox-active site in a protein that is formed by post-translational modification of one or more amino acid residues. These post-translational modifications are irreversible and endow the modified amino acid residues with new functional properties. This Perspective focuses on the following advances in this area that have occurred during recent years. The biosynthesis of the tryptophan tryptophylquinone cofactor is catalyzed by a diheme enzyme, MauG. A bis-Fe
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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.