ArticleInorganic chemistry2018
Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.
Article in Inorganic chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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.
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Who cites it
12 citing papers in PubMed.
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Design of complicated all-α protein structures.Nature structural & molecular biology · 2024Article
- Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Nitrite reductase activity within an antiparallel de novo scaffold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.Journal of the American Chemical Society · 2020Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Review
- Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Selective coordination of three transition metal ions within a coiled-coil peptide scaffold.Chemical science · 2019Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Cupredoxins are copper-dependent electron-transfer proteins that can be categorized as blue, purple, green, and red depending on the spectroscopic properties of the Cu(II) bound forms. Interestingly, despite significantly different first coordination spheres and nuclearity, all cupredoxins share a common Greek Key β-sheet fold. We have previously reported the design of a red copper protein within a completely distinct three-helical bundle protein, α
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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.