The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Designing artificial enzymes by intuition and computation
Open accessAbstract
The rational design of artificial enzymes either by applying physio-chemical intuition of protein structure and function or with the aid of computation methods is a promising area of research with the potential to tremendously impact medicine, industrial chemistry and energy production. Designed proteins also provide a powerful platform for dissecting enzyme mechanisms of natural systems. Artificial enzymes have come a long way, from simple α-helical peptide catalysts to proteins that facilitate multi-step chemical reactions designed by state-of-the-art computational methods. Looking forward, we examine strategies employed by natural enzymes which could be used to improve the speed and selectivity of artificial catalysts.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
The antiquity of RNA-based evolution.
Joyce, G. F. (2002) · Nature · doi:10.1038/418214a · Cited by 1,070
Computational design of antibody-affinity improvement beyond in vivo maturation
Lippow, S. M., Wittrup, K. D., & Tidor, B. (2007) · Nature Biotechnology · doi:10.1038/nbt1336 · Cited by 342
A chiroselective peptide replicator
Saghatelian, A., Yokobayashi, Y., Soltani, K., & Ghadiri, M. R. (2001) · Nature · doi:10.1038/35057238 · Cited by 310
Cited by
Hydrolytic catalysis and structural stabilization in a designed metalloprotein
Zastrow, M. L., Peacock, A. F. A., Stuckey, J. A., & Pecoraro, V. L. (2012) · Nature Chemistry · doi:10.1038/nchem.1201 · Cited by 355
Metadata
- Authors
- Nanda, V., & Koder, R. L.
- Venue
- Nature Chemistry
- Published
- 2009-12-17
- Volume
- 2
- Issue
- 1
- Pages
- 15-24
- ISSN
- 1755-4330 (ISSN-L)
- 1755-4349
- OpenAlex
- W2024296243
- Cited by
- 263
- References
- 4
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Designing artificial enzymes by intuition and computation. https://app.cochat.ai/papers/10.1038/nchem.473
- The paper
- Nanda, V., & Koder, R. L. (2010). Designing artificial enzymes by intuition and computation. Nature Chemistry. https://doi.org/10.1038/nchem.473
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
