The DOI matches its Crossref record; 362 of the 362 references it cites were found in a registry or an index.
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.
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?
In the citing paper
“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]
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
1 retracted
A New Strategy for the Synthesis of Glycoproteins
Zhang, Z., Gildersleeve, J. C., Yang, Y., Xu, R., Loo, J. A., Uryu, S. A., Wong, C., & Schultz, P. G. (2004) · Science · doi:10.1126/science.1089509 · Cited by 152
RetractedTornøe, C. W., Christensen, C., & Meldal, M. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo011148j · Cited by 8,696
Tsien, R. Y. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.509 · Cited by 6,178
Metals, Toxicity and Oxidative Stress
Valko, M., Morris, H., & Cronin, M. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867053764635 · Cited by 5,018
(1978) · Cited by 4,918
Synthesis of Proteins by Native Chemical Ligation
Dawson, P. E., Muir, T. W., Clark‐Lewis, I., & Kent, S. B. H. (1994) · Science · doi:10.1126/science.7973629 · Cited by 4,190
Agard, N. J., Prescher, J. A., & Bertozzi, C. R. (2004) · Journal of the American Chemical Society · doi:10.1021/ja044996f · Cited by 3,160
Self-citationThe growing impact of click chemistry on drug discovery
Kolb, H. C., & Sharpless, K. B. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02933-7 · Cited by 3,155
1,3‐Dipolar Cycloadditions. Past and Future
Huisgen, R. (1963) · Angewandte Chemie International Edition in English · doi:10.1002/anie.196305651 · Cited by 2,929
A guide to choosing fluorescent proteins
Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005) · Nature Methods · doi:10.1038/nmeth819 · Cited by 2,823
Gratzner, H. G. (1982) · Science · doi:10.1126/science.7123245 · Cited by 2,653
Cell Surface Engineering by a Modified Staudinger Reaction
Saxon, E., & Bertozzi, C. R. (2000) · Science · doi:10.1126/science.287.5460.2007 · Cited by 2,463
Self-citationPEGylation, successful approach to drug delivery
Veronese, F. M., & Pasut, G. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03575-0 · Cited by 2,344
A general method for the covalent labeling of fusion proteins with small molecules in vivo
Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H. M., Vogel, H., & Johnsson, K. (2002) · Nature Biotechnology · doi:10.1038/nbt765 · Cited by 1,964
A chemical method for fast and sensitive detection of DNA synthesis in vivo
Salic, A. N., & Mitchison, T. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712168105 · Cited by 1,859
Copper-free click chemistry for dynamic in vivo imaging
Baskin, J. M., Prescher, J. A., Laughlin, S. T., Agard, N. J., Chang, P. V., Miller, I. A., Lo, A., Codelli, J. A., & Bertozzi, C. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707090104 · Cited by 1,834
Self-citationHimo, F., Lovell, T., Hilgraf, R., Rostovtsev, V. V., Noodleman, L., Sharpless, K. B., & Fokin, V. V. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0471525 · Cited by 1,829
Tetrazine Ligation: Fast Bioconjugation Based on Inverse-Electron-Demand Diels−Alder Reactivity
Blackman, M. L., Royzen, M., & Fox, J. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8053805 · Cited by 1,691
Bioconjugation by Copper(I)-Catalyzed Azide-Alkyne [3 + 2] Cycloaddition
Wang, Q., Chan, T. R., Hilgraf, R., Fokin, V. V., Sharpless, K. B., & Finn, M. G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja021381e · Cited by 1,638
Specific Covalent Labeling of Recombinant Protein Molecules Inside Live Cells
Griffin, B. A., Adams, S., & Tsien, R. Y. (1998) · Science · doi:10.1126/science.281.5374.269 · Cited by 1,580
Über neue organische Phosphorverbindungen III. Phosphinmethylenderivate und Phosphinimine
Staudinger, H., & Meyer, J. (1919) · Helvetica Chimica Acta · doi:10.1002/hlca.19190020164 · Cited by 1,551
Lutz, J. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604050 · Cited by 1,542
Polytriazoles as Copper(I)-Stabilizing Ligands in Catalysis
Chan, T. R., Hilgraf, R., Sharpless, K. B., & Fokin, V. V. (2004) · Organic Letters · doi:10.1021/ol0493094 · Cited by 1,532
Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,473
Self-citationOverview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
Terpe, K. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-1158-6 · Cited by 1,344
1.3‐Dipolare Cycloadditionen Rückschau und Ausblick
Huisgen, R. (1963) · Angewandte Chemie · doi:10.1002/ange.19630751304 · Cited by 1,311
Expressed protein ligation: A general method for protein engineering
Muir, T. W., Sondhi, D., & Cole, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.6705 · Cited by 1,192
Ruthenium-Catalyzed Cycloaddition of Alkynes and Organic Azides
Zhang, L., Chen, X., Xue, P., Sun, H. H. Y., Williams, I. D., Sharpless, K. B., Fokin, V. V., & Jia, G. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054114s · Cited by 1,124
An Engineered Protein Tag for Multiprotein Labeling in Living Cells
Gautier, A., Juillerat, A., Heinis, C., Junior, I. R. C., Kindermann, M., Beaufils, F., & Johnsson, K. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.01.007 · Cited by 1,119
Synthesis of Native Proteins by Chemical Ligation
Dawson, P. E., & Kent, S. B. H. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.923 · Cited by 1,093
Staphylococcus aureus Sortase, an Enzyme that Anchors Surface Proteins to the Cell Wall
Mazmanian, S. K., Liu, G., Ton-That, H., & Schneewind, O. (1999) · Science · doi:10.1126/science.285.5428.760 · Cited by 1,053
Arming antibodies: prospects and challenges for immunoconjugates
Wu, A. M., & Senter, P. D. (2005) · Nature Biotechnology · doi:10.1038/nbt1141 · Cited by 1,053
In Vivo Imaging of Membrane-Associated Glycans in Developing Zebrafish
Laughlin, S. T., Baskin, J. M., Amacher, S. L., & Bertozzi, C. R. (2008) · Science · doi:10.1126/science.1155106 · Cited by 1,050
Self-citationA 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
(1996) · Elsevier eBooks · doi:10.1016/b978-0-12-342335-1.x5000-3 · Cited by 1,019
Tron, G. C., Pirali, T., Billington, R. A., Canonico, P. L., Sorba, G., & Genazzani, A. A. (2007) · Medicinal Research Reviews · doi:10.1002/med.20107 · Cited by 999
Development and Use of Fluorescent Protein Markers in Living Cells
Lippincott‐Schwartz, J., & Patterson, G. H. (2003) · Science · doi:10.1126/science.1082520 · Cited by 993
Speers, A. E., Adam, G. C., & Cravatt, B. F. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034490h · Cited by 955
Adams, S., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., & Tsien, R. Y. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017687n · Cited by 947
Ning, X., Guo, J., Wolfert, M. A., & Boons, G. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705456 · Cited by 925
Kiick, K. L., Saxon, E., Tirrell, D. A., & Bertozzi, C. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012583299 · Cited by 911
Self-citationMulticolor and Electron Microscopic Imaging of Connexin Trafficking
Gaietta, G. M., Deerinck, T. J., Adams, S., Bouwer, J. C., Tour, O., Laird, D. W., Sosinsky, G. E., Tsien, R. Y., & Ellisman, M. H. (2002) · Science · doi:10.1126/science.1068793 · Cited by 909
Dieterich, D. C., Link, A. J., Graumann, J., Tirrell, D. A., & Schuman, E. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601637103 · Cited by 874
Tetrazine-Based Cycloadditions: Application to Pretargeted Live Cell Imaging
Devaraj, N. K., Weissleder, R., & Hilderbrand, S. A. (2008) · Bioconjugate Chemistry · doi:10.1021/bc8004446 · Cited by 859
Chemical remodelling of cell surfaces in living animals
Prescher, J. A., Dube, D. H., & Bertozzi, C. R. (2004) · Nature · doi:10.1038/nature02791 · Cited by 844
Self-citationAn Expanded Eukaryotic Genetic Code
Chin, J. W., Cropp, T. A., Anderson, J. C., Mukherji, M., Zhang, Z., & Schultz, P. G. (2003) · Science · doi:10.1126/science.1084772 · Cited by 820
Engineering Chemical Reactivity on Cell Surfaces Through Oligosaccharide Biosynthesis
Mahal, L. K., Yarema, K. J., & Bertozzi, C. R. (1997) · Science · doi:10.1126/science.276.5315.1125 · Cited by 796
Self-citationAdvances in fluorescent protein technology
Shaner, N. C., Patterson, G. H., & Davidson, M. W. (2007) · Journal of Cell Science · doi:10.1242/jcs.005801 · Cited by 789
Clicking polymers: a straightforward approach to novel macromolecular architectures
Fournier, D., Hoogenboom, R., & Schubert, U. S. (2007) · Chemical Society Reviews · doi:10.1039/b700809k · Cited by 785
Profiling Enzyme Activities In Vivo Using Click Chemistry Methods
Speers, A. E., & Cravatt, B. F. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.03.012 · Cited by 774
Chemoselective Ligation and Modification Strategies for Peptides and Proteins
Hackenberger, C. P. R., & Schwarzer, D. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200801313 · Cited by 760
A Comparative Study of Bioorthogonal Reactions with Azides
Agard, N. J., Baskin, J. M., Prescher, J. A., Lo, A., & Bertozzi, C. R. (2006) · ACS Chemical Biology · doi:10.1021/cb6003228 · Cited by 744
Self-citationAddition of p -Azido- l -phenylalanine to the Genetic Code of Escherichia c oli
Chin, J. W., Santoro, S. W., Martin, A., King, D., Wang, L., & Schultz, P. G. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027007w · Cited by 725
Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
Chin, J. W., Martin, A., King, D., Wang, L., & Schultz, P. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172226299 · Cited by 708
Selective reduction of disulfides by tris(2-carboxyethyl)phosphine
Burns, J. A., Butler, J. C., Moran, J. T., & Whitesides, G. M. (1991) · The Journal of Organic Chemistry · doi:10.1021/jo00008a014 · Cited by 696
Semisynthesis of Proteins by Expressed Protein Ligation
Muir, T. W. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161900 · Cited by 695
Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria
Marraffini, L. A., DeDent, A. C., & Schneewind, O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.70.1.192-221.2006 · Cited by 688
A “Traceless” Staudinger Ligation for the Chemoselective Synthesis of Amide Bonds
Saxon, E., Armstrong, J. I., & Bertozzi, C. R. (2000) · Organic Letters · doi:10.1021/ol006054v · Cited by 681
Self-citationExploring RNA transcription and turnover in vivo by using click chemistry
Jao, C. Y., & Salic, A. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808480105 · Cited by 674
Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
Chen, I., Howarth, M. R., Lin, W., & Ting, A. Y. (2005) · Nature Methods · doi:10.1038/nmeth735 · Cited by 668
Wang, L., & Schultz, P. G. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200460627 · Cited by 661
The Emergence of Thiol–Ene Coupling as a Click Process for Materials and Bioorganic Chemistry
Dondoni, A. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802516 · Cited by 621
A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
Hang, H. C., Yu, C., Kato, D. L., & Bertozzi, C. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2335201100 · Cited by 580
Self-citationCell Surface Labeling of Escherichia coli via Copper(I)-Catalyzed [3+2] Cycloaddition
Link, A. J., & Tirrell, D. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036765z · Cited by 578
Repair of O6-alkylguanine by alkyltransferases
Pegg, A. E. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00017-x · Cited by 576
Mechanism-Based Profiling of Enzyme Families
Evans, M. J., & Cravatt, B. F. (2006) · Chemical Reviews · doi:10.1021/cr050288g · Cited by 574
Second-Generation Difluorinated Cyclooctynes for Copper-Free Click Chemistry
Codelli, J. A., Baskin, J. M., Agard, N. J., & Bertozzi, C. R. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803086r · Cited by 553
Self-citationTargeting quantum dots to surface proteins in living cells with biotin ligase
Howarth, M. R., Takao, K., Hayashi, Y., & Ting, A. Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503125102 · Cited by 544
Sortagging: a versatile method for protein labeling
Popp, M. W., Antos, J. M., Grotenbreg, G. M., Spooner, E., & Ploegh, H. L. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.31 · Cited by 542
A chemical approach for identifying O -GlcNAc-modified proteins in cells
Vocadlo, D. J., Hang, H. C., Kim, E.-J., Hanover, J. A., & Bertozzi, C. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632821100 · Cited by 539
Self-citationStaudinger Ligation: A Peptide from a Thioester and Azide
Nilsson, B. L., Kiessling, L. L., & Raines, R. T. (2000) · Organic Letters · doi:10.1021/ol0060174 · Cited by 533
Sortase-Mediated Protein Ligation: A New Method for Protein Engineering
Mao, H., Hart, S. A., Schink, A., & Pollok, B. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039915e · Cited by 533
Trafficking and signaling by fatty-acylated and prenylated proteins
Resh, M. D. (2006) · Nature Chemical Biology · doi:10.1038/nchembio834 · Cited by 521
Kawahara, T., Konishi, Y., Tada, H., Tohge, N., Nishii, J., & Ito, S. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020802)41:15 · Cited by 513
Nucleophilic Catalysis of Oxime Ligation
Dirksen, A., Hackeng, T. M., & Dawson, P. E. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200602877 · Cited by 488
A FlAsH-based FRET approach to determine G protein–coupled receptor activation in living cells
Hoffmann, C., Gaietta, G. M., Bünemann, M., Adams, S., Oberdorf‐Maass, S. U., Behr, B., Vilardaga, J., Tsien, R. Y., Ellisman, M. H., & Lohse, M. J. (2005) · Nature Methods · doi:10.1038/nmeth742 · Cited by 481
Development of Thermal and Photochemical Strategies for Thiol−Ene Click Polymer Functionalization
Campos, L. M., Killops, K. L., Sakai, R., Paulusse, J. M. J., Damiron, D., Drockenmuller, É., Messmore, B. W., & Hawker, C. J. (2008) · Macromolecules · doi:10.1021/ma801630n · Cited by 472
Cis–trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
Lummis, S. C. R., Beene, D. L., Lee, L. W., Lester, H. A., Broadhurst, R. W., & Dougherty, D. A. (2005) · Nature · doi:10.1038/nature04130 · Cited by 455
The therapeutic application of lanthanides
Fricker, S. P. (2006) · Chemical Society Reviews · doi:10.1039/b509608c · Cited by 446
Labeling of fusion proteins with synthetic fluorophores in live cells
Keppler, A., Pick, H. M., Arrivoli, C., Vogel, H., & Johnsson, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401923101 · Cited by 443
Introducing genetically encoded aldehydes into proteins
Carrico, I. S., Carlson, B. L., & Bertozzi, C. R. (2007) · Nature Chemical Biology · doi:10.1038/nchembio878 · Cited by 438
Self-citationHigh-efficiency labeling of sialylated glycoproteins on living cells
Zeng, Y., Ramya, T. N. C., Dirksen, A., Dawson, P. E., & Paulson, J. C. (2009) · Nature Methods · doi:10.1038/nmeth.1305 · Cited by 431
Catalytic azide-alkyne cycloaddition: Reactivity and applications
Wu, P., & Fokin, V. V. (2007) · Aldrichimica acta · Cited by 425
Martin, B. R., Giepmans, B. N. G., Adams, S., & Tsien, R. Y. (2005) · Nature Biotechnology · doi:10.1038/nbt1136 · Cited by 424
Ligand-Accelerated Cu-Catalyzed Azide−Alkyne Cycloaddition: A Mechanistic Report
Rodionov, V. O., Presolski, S. I., Díaz, D. D., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072679d · Cited by 420
Postsynthetic DNA Modification through the Copper‐Catalyzed Azide–Alkyne Cycloaddition Reaction
Gramlich, P. M. E., Wirges, C. T., Manetto, A., & Carell, T. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802077 · Cited by 419
Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo
Sawa, M., Hsu, T.-L., Itoh, T., Sugiyama, M., Hanson, S. R., Vogt, P. K., & Wong, C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605418103 · Cited by 417
Yin, J., Straight, P. D., McLoughlin, S. M., Zhou, Z., Lin, A. J., Golan, D. E., Kelleher, N. L., Kolter, R., & Walsh, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507705102 · Cited by 408
Production of cyclic peptides and proteins in vivo
Scott, C. P., Abel-Santos, E., Wall, M., Wahnon, D. C., & Benkovic, S. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13638 · Cited by 402
Song, W., Wang, Y., Qu, J., et al. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705805 · Cited by 394
Non-canonical amino acids in protein engineering
Link, A. J., Mock, M. L., & Tirrell, D. A. (2003) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2003.10.011 · Cited by 393
Zur Existenz niedergliedriger Cycloalkine, I
Wittig, G., & Krebs, A. W. (1961) · Chemische Berichte · doi:10.1002/cber.19610941213 · Cited by 388
High-Affinity Adaptors for Switchable Recognition of Histidine-Tagged Proteins
Lata, S., Reichel, A., Brock, R. E., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050690c · Cited by 384
Dierks, T., Schmidt, B., Borissenko, L. V., Peng, J., Preusser-Kunze, A., Mariappan, M., & FIGURA, K. V. (2003) · Cell · doi:10.1016/s0092-8674(03)00347-7 · Cited by 384
Mechanistic Investigation of the Staudinger Ligation
Lin, F. L., Hoyt, H. M., van HALBEEK, H., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044461m · Cited by 383
N‐Terminal Protein Modification through a Biomimetic Transamination Reaction
Gilmore, J. M., Scheck, R. A., Esser-Kahn, A. P., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600368 · Cited by 381
Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
Fernández-Suárez, M., Baruah, H., Martínez-Hernández, L., Xie, K. T., Baskin, J. M., Bertozzi, C. R., & Ting, A. Y. (2007) · Nature Biotechnology · doi:10.1038/nbt1355 · Cited by 376
Self-citationGenetic incorporation of unnatural amino acids into proteins in mammalian cells
Liu, W. R., Brock, A., Chen, S., Chen, S., & Schultz, P. G. (2007) · Nature Methods · doi:10.1038/nmeth1016 · Cited by 374
Nicotine binding to brain receptors requires a strong cation–π interaction
Xiu, X., Puskar, N. L., Shanata, J. A. P., Lester, H. A., & Dougherty, D. A. (2009) · Nature · doi:10.1038/nature07768 · Cited by 363
Protein ligation: an enabling technology for the biophysical analysis of proteins
Muralidharan, V., & Muir, T. W. (2006) · Nature Methods · doi:10.1038/nmeth886 · Cited by 363
Addition of the keto functional group to the genetic code of Escherichia coli
Wang, L., Zhang, Z., Brock, A., & Schultz, P. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0234824100 · Cited by 356
Geoghegan, K. F., & Stroh, J. G. (1992) · Bioconjugate Chemistry · doi:10.1021/bc00014a008 · Cited by 356
Song, W., Wang, Y., Qu, J., & Lin, Q. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803598e · Cited by 354
Bernardes, G. J. L., Chalker, J. M., Errey, J. C., & Davis, B. G. (2008) · Journal of the American Chemical Society · doi:10.1021/ja800800p · Cited by 354
A Three-Component Mannich-Type Reaction for Selective Tyrosine Bioconjugation
Joshi, N. S., Whitaker, L. R., & Francis, M. B. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0439017 · Cited by 348
Studies on the Mechanism of Oxime and Semicarbazone Formation1
Jencks, W. P. (1959) · Journal of the American Chemical Society · doi:10.1021/ja01511a053 · Cited by 348
Lin, Y. A., Chalker, J. M., Floyd, N., Bernardes, G. J. L., & Davis, B. G. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8026168 · Cited by 330
A tagging-via-substrate technology for detection and proteomics of farnesylated proteins
Kho, Y., Kim, S. C., Chen, J., Barma, D. K., Kwon, S. W., Cheng, J., Jaunbergs, J., Weinbaum, C., Tamanoi, F., Falck, J. R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403413101 · Cited by 328
Kingsley, D. M., Kozarsky, K., Hobble, L., & Krieger, M. (1986) · Cell · doi:10.1016/0092-8674(86)90841-x · Cited by 327
Kayser, H., Zeitler, R., Kannicht, C., Grunow, D., Nuck, R., & Reutter, W. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41874-1 · Cited by 323
Advances in PEGylation of important biotech molecules: delivery aspects
Ryan, S. M., Mantovani, G., Wang, X., Haddleton, D. M., & Brayden, D. J. (2008) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.5.4.371 · Cited by 323
Highly Active Water-Soluble Olefin Metathesis Catalyst
Hong, S. H., & Grubbs, R. H. (2006) · Journal of the American Chemical Society · doi:10.1021/ja058451c · Cited by 322
Specific Labeling of Cell Surface Proteins with Chemically Diverse Compounds
George, N., Pick, H. M., Vogel, H., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja048396s · Cited by 321
A Genetically Encoded Fluorescent Amino Acid
Wang, J., Xie, J., & Schultz, P. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062666k · Cited by 319
Alkynyl sugar analogs for the labeling and visualization of glycoconjugates in cells
Hsu, T.-L., Hanson, S. R., Kishikawa, K., Wang, S., Sawa, M., & Wong, C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611307104 · Cited by 319
Site-specific labeling of proteins with small molecules in live cells
Chen, I., & Ting, A. Y. (2004) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2004.12.003 · Cited by 314
Quantitative four-dimensional tracking of cytoplasmic and nuclear HIV-1 complexes
Arhel, N. J., Genovesio, A., Kim, K.-A., Miko, S. C., Perret, E., Olivo‐Marín, J., Shorte, S. L., & Charneau, P. (2006) · Nature Methods · doi:10.1038/nmeth928 · Cited by 312
Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase.
Reiss, Y., Stradley, S. J., Gierasch, L. M., Brown, M. S., & Goldstein, J. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.3.732 · Cited by 312
A Genetically Encoded Photocaged Amino Acid
Wu, N., Deiters, A., Cropp, T. A., King, D., & Schultz, P. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja040175z · Cited by 311
Investigating Cellular Metabolism of Synthetic Azidosugars with the Staudinger Ligation
Saxon, E., Luchansky, S. J., Hang, H. C., Yu, C., Lee, S. C., & Bertozzi, C. R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027748x · Cited by 309
Self-citationFluorescence Visualization of Newly Synthesized Proteins in Mammalian Cells
Beatty, K. E., Liu, J. C., Xie, F., Dieterich, D. C., Schuman, E. M., Wang, Q., & Tirrell, D. A. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200602114 · Cited by 306
Studies on the Mechanism of Oxime and Semicarbazone Formation
Jencks, W. P. (1968) · Elsevier eBooks · doi:10.1016/b978-0-08-203484-1.50017-x · Cited by 306
Presentation and Detection of Azide Functionality in Bacterial Cell Surface Proteins
Link, A. J., Vink, M. K. S., & Tirrell, D. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047629c · Cited by 297
Selective Tryptophan Modification with Rhodium Carbenoids in Aqueous Solution
Antos, J. M., & Francis, M. B. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047272c · Cited by 296
A Hydrophilic Azacyclooctyne for Cu-Free Click Chemistry
Sletten, E. M., & Bertozzi, C. R. (2008) · Organic Letters · doi:10.1021/ol801141k · Cited by 296
Self-citationHomomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking
Han, S., Collins, B. E., Bengtson, P., & Paulson, J. C. (2005) · Nature Chemical Biology · doi:10.1038/nchembio713 · Cited by 291
Reversible site-selective labeling of membrane proteins in live cells
Guignet, E. G., Hovius, R., & Vogel, H. (2004) · Nature Biotechnology · doi:10.1038/nbt954 · Cited by 291
Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur
Cowie, D. B., & Cohen, G. N. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90003-3 · Cited by 290
Biochemical engineering of the N-acyl side chain of sialic acid: biological implications
Keppler, O. T., Horstkorte, R., Pawlita, M., Schmidt, C., & Reutter, W. G. (2001) · Glycobiology · doi:10.1093/glycob/11.2.11r · Cited by 288
Generation of a Bacterium with a 21 Amino Acid Genetic Code
Mehl, R. A., Anderson, J. C., Santoro, S. W., Wang, L., Martin, A., King, D., Horn, D. M., & Schultz, P. G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0284153 · Cited by 287
Tyrosine-Selective Protein Alkylation Using π-Allylpalladium Complexes
Tilley, S. D., & Francis, M. B. (2006) · Journal of the American Chemical Society · doi:10.1021/ja057106k · Cited by 287
Wieland, T., Bokelmann, E., Bauer, L., et al. (1953) · Justus Liebig s Annalen der Chemie · doi:10.1002/jlac.19535830110 · Cited by 284
A genetically encoded fluorescent amino acid
Summerer, D., Chen, S., Wu, N., Deiters, A., Chin, J. W., & Schultz, P. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603965103 · Cited by 274
Efficient Incorporation of Unsaturated Methionine Analogues into Proteins in Vivo
van Hest, J. C. M., Kiick, K. L., & Tirrell, D. A. (2000) · Journal of the American Chemical Society · doi:10.1021/ja992749j · Cited by 268
Budiša, N. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200300646 · Cited by 263
Chemical Strategies for Activity‐Based Proteomics
Speers, A. E., & Cravatt, B. F. (2003) · ChemBioChem · doi:10.1002/cbic.200300721 · Cited by 259
Selective Fluorescence Labeling of Lipids in Living Cells
Neef, A. B., & Schultz, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805507 · Cited by 259
Control of protein phosphorylation with a genetically encoded photocaged amino acid
Lemke, E. A., Summerer, D., Geierstanger, B. H., Brittain, S. M., & Schultz, P. G. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.44 · Cited by 256
Selective Dye-Labeling of Newly Synthesized Proteins in Bacterial Cells
Beatty, K. E., Xie, F., Wang, Q., & Tirrell, D. A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054643w · Cited by 252
Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide
Bain, J. D., Diala, E. S., Glabe, C. G., Dix, T. A., & Chamberlin, A. R. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00202a052 · Cited by 250
Incorporation of Nonnatural Amino Acids Into Proteins
Hendrickson, T. L., de Crécy‐Lagard, V., & SCHIMMEL, P. R. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.012803.092429 · Cited by 245
Triazole: the Keystone in Glycosylated Molecular Architectures Constructed by a Click Reaction
Dondoni, A. (2007) · Chemistry - An Asian Journal · doi:10.1002/asia.200700015 · Cited by 245
High-Yielding Staudinger Ligation of a Phosphinothioester and Azide To Form a Peptide
Nilsson, B. L., Kiessling, L. L., & Raines, R. T. (2000) · Organic Letters · doi:10.1021/ol006739v · Cited by 243
Unnatural amino acids as probes of protein structure and function
Dougherty, D. D. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00148-4 · Cited by 243
Wu, P., Shui, W., Carlson, B. L., Hu, N., Rabuka, D., Lee, J., & Bertozzi, C. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807820106 · Cited by 237
Self-citationFluorescent labeling of recombinant proteins in living cells with FlAsH
Griffin, B. A., Adams, S., Jones, J. M., et al. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)27302-3 · Cited by 234
Ueber die Einwirkung von Diazobenzolimid auf Acetylendicarbonsäuremethylester
Michael, A. (1893) · Journal für praktische Chemie · doi:10.1002/prac.18930480114 · Cited by 234
Segmental Isotope Labeling for Protein NMR Using Peptide Splicing
Yamazaki, T., Otomo, T., Oda, N., Kyogoku, Y., Uegaki, K., Ito, N., Ishino, Y., & Nakamura, H. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980776o · Cited by 234
Lin, C., & Ting, A. Y. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0604111 · Cited by 230
Zhou, Z., Cironi, P., Lin, A. J., Xu, Y., Hrvatin, S., Golan, D. E., Silver, P. A., Walsh, C. T., & Yin, J. (2007) · ACS Chemical Biology · doi:10.1021/cb700054k · Cited by 230
Metabolic Labeling of Sialic Acids in Living Animals with Alkynyl Sugars
Chang, P. V., Chen, X., Smyrniotis, C. J., Xenakis, A., Hu, T., Bertozzi, C. R., & Wu, P. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200806319 · Cited by 228
Self-citationTransition metal catalyzed methods for site-selective protein modification
Antos, J. M., & Francis, M. B. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.04.009 · Cited by 226
A Genetically Encoded Photocaged Tyrosine
Deiters, A., Groff, D., Ryu, Y., Xie, J., & Schultz, P. G. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600264 · Cited by 223
Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine
Hackenberger, C. P. R., & Schwarzer, D. (2008) · Angewandte Chemie · doi:10.1002/ange.200801313 · Cited by 220
Schoenebeck, F., Ess, D. H., Jones, G. O., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9003624 · Cited by 219
A Fluorogenic Dye Activated by the Staudinger Ligation
Lemieux, G. A., de Graffenried, C. L., & Bertozzi, C. R. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029013y · Cited by 218
Self-citationProbing mucin-type O-linked glycosylation in living animals
Dube, D. H., Prescher, J. A., Quang, C. N., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506855103 · Cited by 215
Azide–Alkyne Coupling: A Powerful Reaction for Bioconjugate Chemistry
Breinbauer, R., & Köhn, M. (2003) · ChemBioChem · doi:10.1002/cbic.200300705 · Cited by 213
Ess, D. H., Jones, G. O., & Houk, K. N. (2008) · Organic Letters · doi:10.1021/ol8003657 · Cited by 212
Reduction of aryl azides by thiols: Implications for the use of photoaffinity reagents
Staros, J. V., Bayley, H., Standring, D. N., et al. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91606-6 · Cited by 211
An efficient system for the evolution of aminoacyl-tRNA synthetase specificity
Santoro, S. W., Wang, L., Herberich, B., King, D., & Schultz, P. G. (2002) · Nature Biotechnology · doi:10.1038/nbt742 · Cited by 211
Ning, X., Guo, J., Wolfert, M. A., & Boons, G. (2008) · Angewandte Chemie · doi:10.1002/ange.200705456 · Cited by 211
Lutz, J. (2007) · Angewandte Chemie · doi:10.1002/ange.200604050 · Cited by 209
Imaging Cell Surface Glycans with Bioorthogonal Chemical Reporters
Chang, P. V., Prescher, J. A., Hangauer, M. J., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja070238o · Cited by 208
Photochemical Surface Patterning by the Thiol‐Ene Reaction
Jonkheijm, P., Weinrich, D., Köhn, M., Engelkamp, H., Christianen, P. C. M., Kuhlmann, J., Maan, J. C., Nüsse, D., Schroeder, H., Wacker, R., et al. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200800101 · Cited by 207
Chemical Probes for the Rapid Detection of Fatty-Acylated Proteins in Mammalian Cells
Hang, H. C., Geutjes, E.-J., Grotenbreg, G. M., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0685001 · Cited by 205
Metal‐Free Triazole Formation as a Tool for Bioconjugation
van Berkel, S. S., Dirks, A. J., Debets, M. F., van Delft, F. L., Cornelissen, J. J. L. M., Nolte, R. J. M., & Rutjes, F. P. J. T. (2007) · ChemBioChem · doi:10.1002/cbic.200700278 · Cited by 202
Labeling Proteins with Small Molecules by Site-Specific Posttranslational Modification
Yin, J., Liu, F., Li, X., & Walsh, C. T. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047749k · Cited by 200
Lanthanide‐Binding Tags as Versatile Protein Coexpression Probes
Franz, K. J., Nitz, M., & Imperiali, B. (2003) · ChemBioChem · doi:10.1002/cbic.200390046 · Cited by 197
Metabolic Delivery of Ketone Groups to Sialic Acid Residues
Yarema, K. J., Mahal, L. K., Bruehl, R. E., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31168 · Cited by 194
Kapanidis, A. N., Ebright, Y. W., & Ebright, R. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja017074a · Cited by 193
A FRET‐Based Fluorogenic Phosphine for Live‐Cell Imaging with the Staudinger Ligation
Hangauer, M. J., & Bertozzi, C. R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200704847 · Cited by 192
Self-citationA New Strategy for the Site-Specific Modification of Proteins in Vivo
Zhang, Z., Smith, B. A. C., Wang, L., Brock, A., Cho, C., & Schultz, P. G. (2003) · Biochemistry · doi:10.1021/bi0300231 · Cited by 191
Site-Specific Incorporation of Novel Backbone Structures into Proteins
Ellman, J. A., Mendel, D., & Schultz, P. G. (1992) · Science · doi:10.1126/science.1553546 · Cited by 189
Synthesis of Conformationally Restricted Amino Acids and Peptides Employing Olefin Metathesis
Miller, S. J., & Grubbs, R. H. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00126a027 · Cited by 189
Small‐Molecule N‐Heterocyclic‐Carbene‐Containing Olefin‐Metathesis Catalysts for Use in Water
Jordan, J. P., & Grubbs, R. H. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701258 · Cited by 189
Link, A. J., Vink, M. K. S., Agard, N. J., Prescher, J. A., Bertozzi, C. R., & Tirrell, D. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601167103 · Cited by 189
Self-citationEvans, T. C., Martin, D. D., Kolly, R., Panne, D., Sun, L., Ghosh, I., Chen, L., Benner, J., Liu, X., & Xu, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9091 · Cited by 188
The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli
Bose, M., Groff, D., Xie, J., Brustad, E. M., & Schultz, P. G. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055467u · Cited by 188
Reaction Mechanism and Kinetics of the Traceless Staudinger Ligation
Soellner, M. B., Nilsson, B. L., & Raines, R. T. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060484k · Cited by 188
Clark, T. D., & Ghadiri, M. R. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00154a051 · Cited by 185
Halo, T. L., Appelbaum, J., Hobert, E. M., Balkin, D. M., & Schepartz, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja807872s · Cited by 185
Site-Specific Protein Modification Using a Ketone Handle
Cornish, V. W., Hahn, K. M., & Schultz, P. G. (1996) · Journal of the American Chemical Society · doi:10.1021/ja961216x · Cited by 182
Specific Chemical Modification of Proteins
Glazer, A. N. (1970) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.39.070170.000533 · Cited by 182
A Powerful Combinatorial Screen to Identify High‐Affinity Terbium( III )‐Binding Peptides
Nitz, M., Franz, K. J., Maglathlin, R. L., et al. (2003) · ChemBioChem · doi:10.1002/cbic.200390047 · Cited by 181
In vivo incorporation of an alkyne into proteins in Escherichia coli
Deiters, A., & Schultz, P. G. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.12.065 · Cited by 180
Unnatural Amino Acid Incorporation into Virus-Like Particles
Strable, E., Prasuhn, D. E., Udit, A. K., Brown, S. D., Link, A. J., Ngo, J. T., Lander, G. C., Quispe, J. D., Potter, C. S., Carragher, B. O., et al. (2008) · Bioconjugate Chemistry · doi:10.1021/bc700390r · Cited by 179
Inhibition of Cell Adhesion to Fibronectin by Oligopeptide-Substituted Polynorbornenes
Maynard, H. D., Okada, S. Y., & Grubbs, R. H. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003305m · Cited by 175
[15] Biosynthetic method for introducing unnatural amino acids site-specifically into proteins
Ellman, J. A., Mendel, D., Anthony‐Cahill, S. J., Noren, C. J., & Schultz, P. G. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)02017-4 · Cited by 174
Chemistry in Living Cells: Detection of Active Proteasomes by a Two‐Step Labeling Strategy
Ovaa, H., van Swieten, P. F., Kessler, B. M., Leeuwenburgh, M. A., Fiebiger, E., van den Nieuwendijk, A. M. C. H., Galardy, P. J., van der Marel, G. A., Ploegh, H. L., & Overkleeft, H. S. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200351314 · Cited by 173
A Chemical Reporter Strategy to Probe Glycoprotein Fucosylation
Rabuka, D., Hubbard, S. C., Laughlin, S. T., Argade, S. P., & Bertozzi, C. R. (2006) · Journal of the American Chemical Society · doi:10.1021/ja064619y · Cited by 173
Self-citationA Genetically Encoded Boronate‐Containing Amino Acid
Brustad, E. M., Bushey, M. L., Lee, J. W., Groff, D., Liu, W. R., & Schultz, P. G. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200803240 · Cited by 172
Evolution of Nitrate Reductase: Molecular and Structural Variations on a Common Function
Stolz, J. F., & Basu, P. (2002) · ChemBioChem · doi:10.1002/1439-7633(20020301)3:2/3 · Cited by 171
Oligo-Asp Tag/Zn(II) Complex Probe as a New Pair for Labeling and Fluorescence Imaging of Proteins
Ojida, A., Honda, K., Shinmi, D., Kiyonaka, S., Mori, Y., & Hamachi, I. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0618604 · Cited by 170
Keppler, O. T., Stehling, P., Herrmann, M., Kayser, H., Grunow, D., Reutter, W. G., & Pawlita, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1308 · Cited by 169
Reductive Alkylation of Proteins Using Iridium Catalyzed Transfer Hydrogenation
McFarland, J. M., & Francis, M. B. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054686c · Cited by 169
Protein Semi-Synthesis in Living Cells
Giriat, I., & Muir, T. W. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034736i · Cited by 168
Global Identification of O-GlcNAc-Modified Proteins
Nandi, A., Sprung, R. W., Barma, D. K., Zhao, Y., Kim, S. C., Falck, J. R., & Zhao, Y. (2005) · Analytical Chemistry · doi:10.1021/ac051207j · Cited by 168
Ye, S., Köhrer, C., Huber, T., Kazmi, M. A., Sachdev, P., Yan, E. C. Y., Bhagat, A., RajBhandary, U. L., & Sakmar, T. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707355200 · Cited by 163
Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases
Dierks, T., Lecca, M. R., Schlotterhose, P., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.8.2084 · Cited by 160
Research works printed but not linked: 8
- Los G. V., 2005, J. Neurochem., 94, 15
- Padwa A., 1984, 1,3‐Dipolar Cycloaddition Chemistry, Vol. 1
- 10.1002/1521-3757(20020715)114:14<2708::AID-ANGE2708>3.0.CO;2-0 · DOI
- Wu P., 2007, Aldrichimica Acta, 40, 7
- Bock V. D., 2005, Eur. J. Org. Chem., 51
- Wang Y., 2008, Org. Lett., 10, 3752
- 10.1021/ja970826 · DOI
- Gurcel C., 2008, Anal. Biochem., 390, 2089
Cited by
Sorted by citations
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395
Cu-free click cycloaddition reactions in chemical biology
Jewett, J. C., & Bertozzi, C. R. (2010) · Chemical Society Reviews · doi:10.1039/b901970g · Cited by 1,684
Self-citationPhotosensitizers with Aggregation‐Induced Emission: Materials and Biomedical Applications
Hu, F., Xu, S., & Liu, B. (2018) · Advanced Materials · doi:10.1002/adma.201801350 · Cited by 859
Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones
Jewett, J. C., Sletten, E. M., & Bertozzi, C. R. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100014q · Cited by 697
Self-citationImaging of EdU, an Alkyne-Tagged Cell Proliferation Probe, by Raman Microscopy
Yamakoshi, H., Dodo, K., Okada, M., Ando, J., Palonpon, A., Fujita, K., Kawata, S., & Sodeoka, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja108404p · Cited by 356
Metadata
- 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
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