ReviewCurrent opinion in chemical biology2014
Metalloenzyme design and engineering through strategic modifications of native protein scaffolds.
Review in Current opinion in chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed.
- Synzymes: The Future of Modern Enzyme Engineering.Applied biochemistry and biotechnology · 2025Review
- Exploiting SpyTag/SpyCatcher Technology to Design New Artificial Catalytic Copper Proteins.Chembiochem : a European journal of chemical biology · 2025Article
- Application of artificial backbone connectivity in the development of metalloenzyme mimics.Current opinion in chemical biology · 2024Review
- Choose Your Own Adventure: A Comprehensive Database of Reactions Catalyzed by Cytochrome P450 BM3 Variants.ACS catalysis · 2024Review
- Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase.International journal of molecular sciences · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Functional Conversion of Acetyl-Coenzyme a Synthase to a Nickel Superoxide Dismutase via Rational Design of Coordination Microenvironment for the NiInternational journal of molecular sciences · 2022Article
- Machine Learning Approaches for Metalloproteins.Molecules (Basel, Switzerland) · 2022Review
- From Data Mining ofMicroorganisms · 2021Article
- Redesign of a Copper Storage Protein into an Artificial Hydrogenase.ACS catalysis · 2019Article
- Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin.RSC advances · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Article
- Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials.International journal of molecular sciences · 2018Article
- A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme.Science (New York, N.Y.) · 2018Article
- Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.Chemical science · 2018Article
- Coordination chemistry within a protein host: regulation of the secondary coordination sphere.Chemical communications (Cambridge, England) · 2018Article
- Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.Journal of the American Chemical Society · 2017Article
- Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering.Scientific reports · 2017Article
- Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.Angewandte Chemie (International ed. in English) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Metalloenzymes are among the major targets of protein design and engineering efforts aimed at attaining novel and efficient catalysis for biochemical transformation and biomedical applications, due to the diversity of functions imparted by the metallo-cofactors along with the versatility of the protein environment. Naturally evolved protein scaffolds can often serve as robust foundations for sustaining artificial active sites constructed by rational design, directed evolution, or a combination of the two strategies. Accumulated knowledge of structure-function relationship and advancement of tools such as computational algorithms and unnatural amino acids incorporation all contribute to the design of better metalloenzymes with catalytic properties approaching the needs of practical applications.
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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.