Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality
Open accessAbstract
The study of biomolecules in their native environments is a challenging task because of the vast complexity of cellular systems. Technologies developed in the last few years for the selective modification of biological species in living systems have yielded new insights into cellular processes. Key to these new techniques are bioorthogonal chemical reactions, whose components must react rapidly and selectively with each other under physiological conditions in the presence of the plethora of functionality necessary to sustain life. Herein we describe the bioorthogonal chemical reactions developed to date and how they can be used to study biomolecules.
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Currently there are limited methods to selectively covalently bind to a protein.
“Currently there are limited methods to selectively covalently bind to a protein56–58”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [56]
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Self-citationMadl, C. M., Katz, L. M., & Heilshorn, S. C. (2016) · Advanced Functional Materials · doi:10.1002/adfm.201505329 · Cited by 156 · see citing works
Investigating Protein–Ligand Interactions by Solution Nuclear Magnetic Resonance Spectroscopy
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Deconstructing behavioral neuropharmacology with cellular specificity
Shields, B. C., Kahuno, E., Kim, C., Apostolides, P. F., Brown, J., Lindo, S., Mensh, B. D., Dudman, J. T., Lavis, L. D., & Tadross, M. R. (2017) · Science · doi:10.1126/science.aaj2161 · Cited by 135 · see citing works
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
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van Buggenum, J. A. G. L., Gerlach, J. P., Eising, S., Schoonen, L., van Eijl, R. A. P. M., Tanis, S. E. J., Hogeweg, M., Hubner, N. C., van Hest, J. C., Bonger, K. M., et al. (2016) · Scientific Reports · doi:10.1038/srep22675 · Cited by 93 · see citing works
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Global profiling of arginine reactivity and ligandability in the human proteome
Wang, Y., Hu, T., Zhu, L., Xie, S., Yang, X., Xu, C., Zhai, Y., Li, Y., Huang, X., Yang, B., et al. (2026) · Nature Chemistry · doi:10.1038/s41557-025-02012-6 · Cited by 12 · see citing works
Improved ClickTags enable live-cell barcoding for highly multiplexed single cell sequencing
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- Authors
- Sletten, E. M., & Bertozzi, C. R.
- Affiliations
- University of California, Berkeley (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Bertozzi, Carolyn R.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2009-09
- Volume
- 48
- Issue
- 38
- Pages
- 6974-6998
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- PMC
- PMC2864149
- OpenAlex
- W2151709132
- Cited by
- 3,165
- References
- 362
- Citations by year
- 2026: 160 · 2025: 174 · 2024: 189 · 2023: 223 · 2022: 173 · 2021: 192 · 2020: 185 · 2019: 200 · 2018: 230 · 2017: 196 · 2016: 193 · 2015: 200 · 2014: 233 · 2013: 194 · 2012: 143
- FWCI
- 68.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Angewandte Chemie International Edition (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R37GM058867)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Physical Sciences › Chemistry › Organic Chemistry › Advanced Polymer Synthesis and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- bioorthogonal chemistry, bioorthogonal reactions, biological systems, cellular processes
- MeSH terms
- Alkynes, Animals, Azides, Biochemical Phenomena, Biochemistry, Fluorescent Dyes, Humans, Indicators and Reagents, Molecular Sequence Data, Staining and Labeling, Molecular Structure, Cellular Structures, Green Fluorescent Proteins
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