The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Flexizymes for genetic code reprogramming
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Citations
Cites
A General Method for Site-specific Incorporation of Unnatural Amino Acids into Proteins
Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., & Schultz, P. G. (1989) · Science · doi:10.1126/science.2649980 · Cited by 1,019 · cited 1×
“Importantly, the nonproteinogenic amino acids in past studies using sense or nonsense suppression strategie”
BackgroundAn in vitro evolved precursor tRNA with aminoacylation activity
Saito, H., Kourouklis, D., & Suga, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1797 · Cited by 145 · cited 1×
“It is also possible to monitor the formation of Xaa-tRNAs by treating with an appropriate biotinylation reagent, followed by streptavidin gel-shift assay using PAGE, although this method is limited to the use of substrates with a free α-amino grou”
MethodSelf-citation
Cited by
Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges
Vinogradov, A. A., Yin, Y., & Suga, H. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13178 · Cited by 848
Self-citationNew developments in RiPP discovery, enzymology and engineering
Montalbán-López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2021) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 787
Self-citationModulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497
Rapid and efficient protein synthesis through expansion of the native chemical ligation concept
Kulkarni, S. S., Sayers, J., Premdjee, B., & Payne, R. J. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0122 · Cited by 323
RNA Display Methods for the Discovery of Bioactive Macrocycles
Huang, Y., Wiedmann, M. M., & Suga, H. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00430 · Cited by 298
Self-citationModulating protein–protein interactions: the potential of peptides
Nevola, L., & Giralt, E. (2015) · Chemical Communications · doi:10.1039/c4cc08565e · Cited by 289
Structure of the bacterial ribosome at 2 Å resolution
Watson, Z. L., Ward, F. R., Méheust, R., Ad, O., Schepartz, A., Banfield, J. F., & Cate, J. H. (2020) · eLife · doi:10.7554/elife.60482 · Cited by 263
Synthesis and applications of mirror-image proteins
Harrison, K., Mackay, A. S., Kambanis, L., Maxwell, J. W. C., & Payne, R. J. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00493-y · Cited by 104
Reciprocally-coupled Gating: Strange Loops in Bioenergetics, Genetics, and Catalysis
Carter, Jr., & Wills, P. R. (2021) · doi:10.20944/preprints202101.0057.v1 · Cited by 18
Metadata
- Authors
- Goto, Y., Katoh, T., & Suga, H.
- Venue
- Nature Protocols
- Published
- 2011-05-12
- Volume
- 6
- Issue
- 6
- Pages
- 779-790
- ISSN
- 1750-2799 (ISSN-L)
- 1754-2189
- OpenAlex
- W2087181770
- Cited by
- 472
- References
- 2
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- closed
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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.