The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.
Halogenase engineering and its utility in medicinal chemistry
Abstract
Halogenation is commonly used in medicinal chemistry to improve the potency of pharmaceutical leads. While synthetic methods for halogenation present selectivity and reactivity challenges, halogenases have evolved over time to perform selective reactions under benign conditions. The optimization of halogenation biocatalysts has utilized enzyme evolution and structure-based engineering alongside biotransformation in a variety of systems to generate stable site-selective variants. The recent improvements in halogenase-catalyzed reactions has demonstrated the utility of these biocatalysts for industrial purposes, and their ability to achieve a broad substrate scope implies a synthetic tractability with increasing relevance in medicinal chemistry.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Nonetheless, fluorinase has been successfully leveraged in biosynthetic pathways to produce a variety of simple organofluorines used as PET tracers and medical imaging agents58–60.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [58]
Experimental — accuracy not yet measured
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
Applications of Fluorine in Medicinal Chemistry
Gillis, E. P., Eastman, K. J., Hill, M. D., Donnelly, D. J., & Meanwell, N. A. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00258 · Cited by 3,692
A Medicinal Chemist’s Guide to Molecular Interactions
Bissantz, C., Kuhn, B., & Ståhl, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100112j · Cited by 1,810
Halogen bonding: an electrostatically-driven highly directional noncovalent interaction.
Politzer, P., Murray, J., & Clark, T. (2010) · Physical Chemistry, Chemical Physics - PCCP · doi:10.1039/c004189k · Cited by 1,430
Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. J. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,087
Renata, H., Wang, Z. J., & Arnold, F. H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201409470 · Cited by 529
Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse
Agarwal, V., Miles, Z. D., Winter, J. M., Eustáquio, A. S., Gamal, A. E., & Moore, B. S. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00571 · Cited by 439
Halogen Bond: Its Role beyond Drug–Target Binding Affinity for Drug Discovery and Development
Xu, Z., Yang, Z., Liu, Y., Lu, Y., Chen, K., & Zhu, W. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci400539q · Cited by 431
Tryptophan 7-Halogenase (PrnA) Structure Suggests a Mechanism for Regioselective Chlorination
Dong, C., Flecks, S., Unversucht, S., Haupt, C., PÉE, K.-H. V., & Naismith, J. H. (2005) · Science · doi:10.1126/science.1116510 · Cited by 397
Development of Halogenase Enzymes for Use in Synthesis
Latham, J., Brandenburger, E., Shepherd, S. A., Menon, B. R. K., & Micklefield, J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00032 · Cited by 358
Crystal structure and mechanism of a bacterial fluorinating enzyme
Dong, C., Huang, F., Deng, H., Schaffrath, C., Spencer, J. B., O'Hagan, D., & Naismith, J. H. (2004) · Nature · doi:10.1038/nature02280 · Cited by 335
Research works printed but not linked: 1
- Zhu, 2007, Mechanism and enzymatic fluorination in Streptomyces cattleya, J Am Chem Soc, 129, 14597, 10.1021/ja0731569 · DOI
Cited by
Stockbridge, R. B., & Wackett, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-49018-1 · Cited by 80
Metadata
- Authors
- Fraley, A. E., & Sherman, D. H.
- Venue
- Bioorganic & Medicinal Chemistry Letters
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 28
- Issue
- 11
- Pages
- 1992-1999
- ISSN
- 0960-894X
- PMC
- PMC5964047
- Cited by
- 45
- References
- 71
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
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
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.
