Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins

Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology

Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry - An Asian Journal · doi:10.1002/asia.200800427 · Cited by 653

Protein Modification, Bioconjugation, and Disulfide Bridging Using Bromomaleimides

Smith, M. E. B., Schumacher, F. F., Ryan, C. P., Tedaldi, L. M., Papaioannou, D., Waksman, G., Caddick, S., & Baker, J. R. (2010) · Journal of the American Chemical Society · doi:10.1021/ja908610s · Cited by 378

On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases

Ekkebus, R., van Kasteren, S. I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P. P., de Jong, A., Goerdayal, S. S., Neefjes, J., Heck, A. J. R., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja309802n · Cited by 346

Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification

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

Occurrence, conformational features and amino acid propensities for the π-helix

Fodje, M. N., & Al‐Karadaghi, S. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.5.353 · Cited by 272

Site-Specific PEGylation of Protein Disulfide Bonds Using a Three-Carbon Bridge

Balan, S., Choi, J.-W., Godwin, A., Teo, I. A., Laborde, C. M., Heidelberger, S., Zloh, M., Shaunak, S., & Brocchini, S. (2006) · Bioconjugate Chemistry · doi:10.1021/bc0601471 · Cited by 172

Conjugation-Induced Fluorescent Labeling of Proteins and Polymers Using Dithiomaleimides

Robin, M. P., Wilson, P., Mabire, A. B., Kiviaho, J. K., Raymond, J. E., Haddleton, D. M., & O’Reilly, R. K. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3105494 · Cited by 123

Electron‐Deficient Alkynes as Cleavable Reagents for the Modification of Cysteine‐Containing Peptides in Aqueous Medium

Shiu, H., Chan, T. H., Ho, C., Liu, Y., Wong, M., & Che, C. (2009) · Chemistry - A European Journal · doi:10.1002/chem.200800669 · Cited by 121

Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol–alkyne addition

Sommer, S., Weikart, N. D., Linne, U., & Mootz, H. D. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.02.039 · Cited by 115

Bromomaleimides: new reagents for the selective and reversible modification of cysteine

Tedaldi, L. M., Smith, M. E. B., Nathani, R. I., & Baker, J. R. (2009) · Chemical Communications · doi:10.1039/b915136b · Cited by 108

Advances in Chemical Protein Modification

Boutureira, O., & Bernardes, G. J. L. (2015) · Chemical Reviews · doi:10.1021/cr500399p · Cited by 1,137

Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation

McKay, C. S., & Finn, M. G. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.002 · Cited by 804

Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology

Gehringer, M., & Laufer, S. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01153 · Cited by 772

Residue-Specific Peptide Modification: A Chemist’s Guide

deGruyter, J. N., Malins, L. R., & Baran, P. S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00536 · Cited by 571

Contemporary approaches to site-selective protein modification

Hoyt, E. A., Cal, P. M. S. D., Oliveira, B. L., & Bernardes, G. J. L. (2019) · Nature Reviews Chemistry · doi:10.1038/s41570-019-0079-1 · Cited by 542

Chemical Protein Modification through Cysteine

Gunnoo, S. B., & Madder, A. (2016) · ChemBioChem · doi:10.1002/cbic.201500667 · Cited by 412

Site-Selective C(sp3)–H Functionalization of Di-, Tri-, and Tetrapeptides at the N-Terminus

Gong, W., Zhang, G., Liu, T., Giri, R., & Yu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510233h · Cited by 290

Covalent Modification of Biomolecules through Maleimide-Based Labeling Strategies

Renault, K., Fredy, J. W., Renard, P., & Sabot, C. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00252 · Cited by 264

Proteome‐Wide Profiling of Targets of Cysteine reactive Small Molecules by Using Ethynyl Benziodoxolone Reagents

Abegg, D., Frei, R., Cerato, L., Hari, D. P., Wang, C., Waser, J., & Adibekian, A. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201505641 · Cited by 158

Recent developments in chemical conjugation strategies targeting native amino acids in proteins and their applications in antibody–drug conjugates

Kang, M. S., Kong, T. W. S., Khoo, Y. X. J., & Loh, T. (2021) · Chemical Science · doi:10.1039/d1sc02973h · Cited by 153

Cysteine‐Selective Reactions for Antibody Conjugation

Cal, P. M. S. D., Bernardes, G. J. L., & Góis, P. M. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201405702 · Cited by 127

Water-promoted C-S bond formation reactions

Xie, P., Wang, J., Liu, Y., Fan, J., Wo, X., Fu, W., Sun, Z., & Loh, T. (2018) · Nature Communications · doi:10.1038/s41467-018-03698-8 · Cited by 123

“Doubly Orthogonal” Labeling of Peptides and Proteins

Tessier, R., Ceballos, J., Guidotti, N., Simonet‐Davin, R., Fierz, B., & Waser, J. (2019) · Chem · doi:10.1016/j.chempr.2019.06.022 · Cited by 118

Field Guide to Challenges and Opportunities in Antibody–Drug Conjugates for Chemists

Gordon, M. R., Canakci, M., Li, L., Zhuang, J., Osborne, B. A., & Thayumanavan, S. (2015) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00399 · Cited by 119

Traceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification

Tung, C. L., Wong, C. T. T., Fung, Y. M. E., & Li, X. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b00983 · Cited by 105

Rapid biocompatible macrocyclization of peptides with decafluoro-diphenylsulfone

Kalhor‐Monfared, S., Jafari, M. R., Patterson, J. T., Kitov, P. I., Dwyer, J. J., Nuss, J. M., & Derda, R. (2016) · Chemical Science · doi:10.1039/c5sc03856a · Cited by 105

Recent Progress in Chemical Modification of Proteins

Sakamoto, S., & Hamachi, I. (2018) · Analytical Sciences · doi:10.2116/analsci.18r003 · Cited by 102

Water-soluble allyl sulfones for dual site-specific labelling of proteins and cyclic peptides

Wang, T., Riegger, A., Lamla, M., Wiese, S., Oeckl, P., Otto, M., Wu, Y., Fischer, S., Barth, H., Kuan, S. L., et al. (2016) · Chemical Science · doi:10.1039/c6sc00005c · Cited by 96

Exocyclic Olefinic Maleimides: Synthesis and Application for Stable and Thiol‐Selective Bioconjugation

Kalia, D., Malekar, P. V., & Parthasarathy, M. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508118 · Cited by 93

Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum

Tiambeng, T. N., Roberts, D. S., Brown, K. A., Zhu, Y., Chen, B., Wu, Z., Mitchell, S. D., Guardado-Alvarez, T. M., Jin, S., & Ge, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-17643-1 · Cited by 76

CBTF: New Amine-to-Thiol Coupling Reagent for Preparation of Antibody Conjugates with Increased Plasma Stability

Kolodych, S., Koniev, O., Baatarkhuu, Z., Bonnefoy, J., Debaene, F., Cianférani, S., DORSSELAER, A. V., & Wagner, A. (2015) · Bioconjugate Chemistry · doi:10.1021/bc500610g · Cited by 73

Chemical technology principles for selective bioconjugation of proteins and antibodies

Chauhan, P. S., Ragendu, V., Kumar, M., Molla, R., Mishra, S. D., Basa, S., & Rai, V. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00715d · Cited by 70

Site-Specific Dual Functionalization of Cysteine Residue in Peptides and Proteins with 2-Azidoacrylates

Ariyasu, S., Hayashi, H., Xing, B., & Chiba, S. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00024 · Cited by 67

Gold-catalyzed direct alkynylation of tryptophan in peptides using TIPS-EBX

Tolnai, G. L., Brand, J. P., & Waser, J. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.74 · Cited by 66

Thia-Michael addition: the route to promising opportunities for fast and cysteine-specific modification

Ahangarpour, M., Kavianinia, I., & Brimble, M. A. (2023) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob02262a · Cited by 61

Stable and Rapid Thiol Bioconjugation by Light‐Triggered Thiomaleimide Ring Hydrolysis

Kalia, D., Pawar, S. P., & Thopate, J. S. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201609733 · Cited by 55

A programmable chemical switch based on triggerable Michael acceptors

Zhuang, J., Zhao, B., Meng, X., Schiffman, J. D., Perry, S. L., Vachet, R. W., & Thayumanavan, S. (2020) · Chemical Science · doi:10.1039/c9sc05841a · Cited by 53

Chemical modifications of proteins and their applications in metalloenzyme studies

Naowarojna, N., Cheng, R., Lopez, J., Wong, C., Qiao, L., & Liu, P. (2021) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2021.01.001 · Cited by 52

Selective lysine modification of native peptides via aza-Michael addition

Chen, H., Huang, R., Li, Z., Zhu, W., Chen, J., Zhan, Y., & Jiang, B. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob01866e · Cited by 46

Irreversible Cysteine‐Selective Protein Labeling Employing Modular Electrophilic Tetrafluoroethylation Reagents

Václavík, J., Zschoche, R., Klimánková, I., Matoušek, V., Beier, P., Hilvert, D., & Togni, A. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201700607 · Cited by 44

Highly Reactive and Tracelessly Cleavable Cysteine‐Specific Modification of Proteins via 4‐Substituted Cyclopentenone

Yu, J., Yang, X., Sun, Y., & Yin, Z. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201804801 · Cited by 44

Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation

Griffiths, R. C., Smith, F. R., Long, J., Williams, H. E. L., Layfield, R., & Mitchell, N. J. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202006260 · Cited by 44

Synthesis of Vinylic Sulfones in Aqueous Media

Goh, J., Maraswami, M., & Loh, T. (2021) · Organic Letters · doi:10.1021/acs.orglett.0c04257 · Cited by 43

Proteome‐Wide Profiling of Targets of Cysteine reactive Small Molecules by Using Ethynyl Benziodoxolone Reagents

Abegg, D., Frei, R., Cerato, L., Hari, D. P., Wang, C., Waser, J., & Adibekian, A. (2015) · Angewandte Chemie · doi:10.1002/ange.201505641 · Cited by 40

Chemoselective and photocleavable cysteine modification of peptides and proteins using isoxazoliniums

Deng, J., Chung, S., Leung, A. S., Yip, W.-M., Yang, B., Choi, M.-C., Cui, J., Kung, K. K., Zhang, Z., Lo, K.-W., et al. (2019) · Communications Chemistry · doi:10.1038/s42004-019-0193-5 · Cited by 38

Silicon-Containing Thiol-Specific Bioconjugating Reagent

Zhang, Z., Li, L., Xu, H., Lee, C.-L. K., Jia, Z., & Loh, T. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12050 · Cited by 37

Pd-Catalyzed Site-Selective C(sp 2 )–H Olefination and Alkynylation of Phenylalanine Residues in Peptides

Zheng, Y. T., & Song, W. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b00987 · Cited by 36

2 H -Azirines as Potential Bifunctional Chemical Linkers of Cysteine Residues in Bioconjugate Technology

Chen, Y., Yang, W., Wu, J., Sun, W., Loh, T., & Jiang, Y. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c00415 · Cited by 36

Cleavable and tunable cysteine-specific arylation modification with aryl thioethers

Li, J., Deng, J., Yin, Z., Hu, Q.-L., Yang, G., Song, Z., Zhang, Y., Chan, A. S. C., Li, H., & Xiong, X. (2021) · Chemical Science · doi:10.1039/d0sc06576e · Cited by 35

A Sulfonium Triggered Thiol-yne Reaction for Cysteine Modification

Hou, Z., Wang, D., Li, Y., Zhao, R., Wan, C., Ma, Y., Lian, C., Yin, F., & Li, Z. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b02505 · Cited by 34

Recent advances in protein modifications techniques for the targeting N‐terminal cysteine

Asiimwe, N., Mazid, M. F. A., Murale, D. P., Kim, Y. K., & Lee, J. (2021) · Peptide Science · doi:10.1002/pep2.24235 · Cited by 34

Chemical and Enzymatic Strategies for Bacterial and Mammalian Cell Surface Engineering

Bi, X., Yin, J., Guanbang, A. C., & Liu, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201705049 · Cited by 34

Cysteinselektive Reaktionen zur Konjugation von Antikörpern

Cal, P. M. S. D., Bernardes, G. J. L., & Góis, P. M. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201405702 · Cited by 33

Assessment of reagents for selenocysteine conjugation and the stability of selenocysteine adducts

Pedzisa, L., Li, X., Rader, C. M., & Roush, W. R. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00775a · Cited by 33

Allene Functionalized Azobenzene Linker Enables Rapid and Light-Responsive Peptide Macrocyclization

Jafari, M. R., Lakusta, J., Lundgren, R. J., & Derda, R. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00026 · Cited by 32

Allenamide as a bioisostere of acrylamide in the design and synthesis of targeted covalent inhibitors

Chen, D., Guo, D., Yan, Z., & Zhao, Y. (2017) · MedChemComm · doi:10.1039/c7md00571g · Cited by 32

Thiol-derivatized minihepcidins retain biological activity

Fung, E., Chua, K. J., Ganz, T., Nemeth, E., & Ruchala, P. P. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.12.094 · Cited by 31

Tunable heteroaromatic azoline thioethers (HATs) for cysteine profiling

Tang, K. C., Maddox, S. M., Backus, K. M., & Raj, M. (2021) · Chemical Science · doi:10.1039/d1sc04139h · Cited by 31

On‐Resin Preparation of Allenamidyl Peptides: A Versatile Chemoselective Conjugation and Intramolecular Cyclisation Tool

Cameron, A. J., Harris, P. W. R., & Brimble, M. A. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004656 · Cited by 30

Long-Acting Human Growth Hormone Analogue by Noncovalent Albumin Binding

Ramírez-Andersen, H. S., Behrens, C., Buchardt, J., Fels, J. J., Folkesson, C. G., Chen, J., Nørskov‐Lauritsen, L., Nielsen, P. F., Reslow, M., Rischel, C., et al. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00463 · Cited by 29

Genetically encoded fragment-based discovery

Derda, R., & Ng, S. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.03.014 · Cited by 28

Development and Applications of Water-Compatible Reactions: A Journey to Be Continued

Lu, M., & Loh, T. (2023) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00555 · Cited by 28

Development of catalyst-free carbon-sulfur bond formation reactions under aqueous media and their applications

Kang, M. S., Khoo, Y. X. J., Jia, Z., & Loh, T. (2022) · Green Synthesis and Catalysis · doi:10.1016/j.gresc.2022.09.002 · Cited by 28

Peptide and Protein Cysteine Modification Enabled by Hydrosulfuration of Ynamide

Wang, C., Zhao, Z., Ghadir, R., Yang, D., Zhang, Z., Ding, Z., Cao, Y., Li, Y., Fassler, R., Reichmann, D., et al. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c01148 · Cited by 27

Diversification of Peptidomimetics and Oligopeptides through Microwave‐Assisted Rhodium(III)‐Catalyzed Intramolecular Annulation

Song, L., Tian, G., Blanpain, A., Meervelt, L. V., & der Eycken, E. V. V. (2019) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201900550 · Cited by 25

Recent Advances in the Synthesis of 5‐Membered N ‐Heterocycles via Rhodium Catalysed Cascade Reactions

Mishra, D. R., Panda, B. S., Nayak, S., Panda, J., & Mohapatra, S. (2022) · ChemistrySelect · doi:10.1002/slct.202200531 · Cited by 24

N -Methyl- N -phenylvinylsulfonamides for Cysteine-Selective Conjugation

Huang, R., Li, Z., Sheng, Y., Yu, J., Wu, Y., Zhan, Y., Chen, H., & Jiang, B. (2018) · Organic Letters · doi:10.1021/acs.orglett.8b02849 · Cited by 24

Pd-catalyzed intramolecular C(sp 2 )–H amination of phenylalanine moieties in dipeptides: synthesis of indoline-2-carboxylate-containing dipeptides

Zheng, Y. T., Song, W., Zhu, Y., Wei, B., & Xuan, L. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00207j · Cited by 23

Alkynone β-trifluoroborates: A new class of amine-specific biocompatible click reagents

Teng, S., Ng, E. W. H., Zhang, Z., Soon, C. N., Xu, H., Li, R., Hirao, H., & Loh, T. (2023) · Science Advances · doi:10.1126/sciadv.adg4924 · Cited by 22

Thiol‐Specific Silicon‐Containing Conjugating Reagent: β‐Silyl Alkynyl Carbonyl Compounds

Teng, S., Zhang, Z., Li, B., Li, L., Tan, M. C. L., Jia, Z., & Loh, T. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202311906 · Cited by 22

Computational Study of the Addition of Methanethiol to 40+ Michael Acceptors as a Model for the Bioconjugation of Cysteines

Costa, A. M., Bosch, L., Petit, E., & Vilarrasa, J. (2021) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.1c00349 · Cited by 21

A Plug-and-Play Platform for the Formation of Trifunctional Cysteine Bioconjugates that also Offers Control over Thiol Cleavability

Bahou, C., Szijj, P. A., Spears, R. J., Wall, A., Javaid, F., Sattikar, A., Love, E. A., Baker, J. R., & Chudasama, V. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00057 · Cited by 21

Chemical Modification of Lipase for Rational Enhancement of Enantioselectivity

Ema, T., & Inoue, H. (2015) · Chemistry Letters · doi:10.1246/cl.150667 · Cited by 18

Site-Selective Modification of Peptides via Late-Stage Pd-Catalyzed Tandem Reaction of Phenylalanine with Benzoquinone

Tang, J. S., Lu, F., Geng, Y., Liu, Y., & Zhang, E. (2023) · Organic Letters · doi:10.1021/acs.orglett.3c01952 · Cited by 18

Catalyst-free C–N bond formation under biocompatible reaction conditions

Goh, J., Ong, S. K., Tan, Y. S., & Loh, T. (2022) · Green Chemistry · doi:10.1039/d2gc00027j · Cited by 16

Modified synthetic peptides: from therapeutics to chemosensors

Wynne, C., & Elmes, R. B. P. (2024) · Sensors & Diagnostics · doi:10.1039/d4sd00022f · Cited by 16

Photo‐and Electrochemical Modification of Amino Acids, Peptides and Proteins through Cysteine: Recent Advances and Future Perspectives

Xiang, F., Hu, F., Weng, Y., & Gao, M. (2024) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202400772 · Cited by 16

Dichloroacetophenone Derivatives: A Class of Bioconjugation Reagents for Disulfide Bridging

Wu, L., Zhou, S., Luo, Q., Tian, J., & Loh, T. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c02477 · Cited by 15

Rapid C–S Coupling in Water via Ion-Pair-Catalyzed Dehydration

Zhu, Y., Yang, C., Lin, Q., Li, J., Loh, T., Peng, C., & Jia, Z. (2025) · Organic Letters · doi:10.1021/acs.orglett.5c00126 · Cited by 14

Exocyclic Olefinic Maleimides: Synthesis and Application for Stable and Thiol‐Selective Bioconjugation

Kalia, D., Malekar, P. V., & Parthasarathy, M. (2015) · Angewandte Chemie · doi:10.1002/ange.201508118 · Cited by 14

Modulation of protein activity and assembled structure by polymer conjugation: PEGylation vs glycosylation

Bao, C., & Zhang, Q. (2019) · European Polymer Journal · doi:10.1016/j.eurpolymj.2019.01.020 · Cited by 13

Interactive Bioconjugation at N‐Terminal Cysteines by Using O‐Salicylaldehyde Esters towards Dual Site‐Selective Functionalization

Silva, M. J., Cavadas, R. A. N., Faustino, H., Veiros, L. F., & Góis, P. M. P. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202202377 · Cited by 13

Recent Advances in Chemical Protein Modification via Cysteine

Wang, C., Zhao, Y., & Zhao, J. (2022) · Chinese Journal of Organic Chemistry · doi:10.6023/cjoc202203008 · Cited by 13

Allenamides as a Powerful Tool to Incorporate Diversity: Thia‐Michael Lipidation of Semisynthetic Peptides and Access to β‐Keto Amides

Na, T., Sander, V., Davidson, A. J., Lin, R., Hermant, Y. O., Boys, M. T. H., Pletzer, D., Campbell, G., Ferguson, S. A., Cook, G. M., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202407764 · Cited by 12

Aptamer-Guided, Hydrolysis-Resistant Deoxyoxanosine Enables Epitope- and Moiety-Selective Conjugation to Nonengineered Proteins Even in Complex Environments

Jo, H., Ju, S., Kim, M., Beon, J., Jang, S.-Y., Pack, S. P., Son, C. Y., Kim, J., & Oh, S. S. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c15674 · Cited by 12

Synthesis of 1,3-oxazine-2,4-diones by DBU-catalyzed incorporation of carbon dioxide into 3-ynamides

Veltri, L., Amuso, R., Vitale, P., Chiacchio, M. A., Benincasa, C., & Gabriele, B. (2021) · Journal of CO2 Utilization · doi:10.1016/j.jcou.2021.101695 · Cited by 11

Alkenylation and Arylation of Peptides via Ni-Catalyzed Reductive Coupling of α-C-Tosyl Peptides with Csp2 Triflates/Halides

Tao, X., Ma, G., Song, Y., Chen, Y., Qian, Q., Sun, D., & Gong, H. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c02601 · Cited by 11

Highly Reactive and Tracelessly Cleavable Cysteine‐Specific Modification of Proteins via 4‐Substituted Cyclopentenone

Yu, J., Yang, X., Sun, Y., & Yin, Z. (2018) · Angewandte Chemie · doi:10.1002/ange.201804801 · Cited by 11

Selective Derivatization of N-Terminal Cysteines Using Cyclopentenediones

Brun, O., Agramunt, J., Raich, L., Rovira, C., Pedroso, E., & Grandas, A. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b02301 · Cited by 10

Catalyst-Free Regio- and Stereoselective C(sp2)–H Chlorination of Enamides at Room Temperature

Deng, M.-L., Sheng, M.-W., Wen, X.-K., Cao, R.-N., Li, M., Loh, T., & Lu, M. (2025) · Organic Letters · doi:10.1021/acs.orglett.5c01110 · Cited by 9

Deep-NIR to NIR-II hemicyanine fluorophore scaffolds with dual optically tunable sites for in vivo multiplexed imaging

Liu, Q., Li, Z., Huang, Y., Lin, Z., Shen, X., & Chen, H. (2025) · Chemical Science · doi:10.1039/d5sc06690e · Cited by 9

Stable and Rapid Thiol Bioconjugation by Light‐Triggered Thiomaleimide Ring Hydrolysis

Kalia, D., Pawar, S. P., & Thopate, J. S. (2017) · Angewandte Chemie · doi:10.1002/ange.201609733 · Cited by 8

Identification of an Allene Warhead That Selectively Targets a Histidine Residue in the Escherichia coli Oxidoreductase Enzyme DsbA

Tasdan, Y., Balaji, G. R., Akhtar, N., Ilyichova, O. V., Cunliffe, T., Heras, B., Strat, L. L., Murray, J. B., Capuano, B., Scanlon, M. J., et al. (2025) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00016 · Cited by 7

Metal-Free Access to N , S -Acetals via N -Acyliminium Borate Intermediate under Biocompatible Conditions

Wang, L., Mondal, B., Li, B., Zhang, Z., Loh, T., Chen, P., & Jia, Z. (2025) · ACS Catalysis · doi:10.1021/acscatal.5c06339 · Cited by 7

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Gavriel, K., & Neumann, K. (2026) · Precision Chemistry · doi:10.1021/prechem.5c00323 · Cited by 7

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Brulet, J. W., Ciancone, A. M., Yuan, K., & Hsu, K. (2023) · Israel Journal of Chemistry · doi:10.1002/ijch.202300001 · Cited by 6

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Shepperson, O. A., Harris, P. W. R., Brimble, M. A., & Cameron, A. J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1487338 · Cited by 6

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Sreejith, S., Kishor, R., Abbas, A., Thomas, R., Yeo, T., Ranjan, V., Vaidyanathan, R., Seah, Y. P., Xing, B., Wang, Z., et al. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b20315 · Cited by 6

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Shepperson, O. A., Harris, P. W. R., Brimble, M. A., & Cameron, A. J. (2024) · Antibiotics · doi:10.3390/antibiotics13070615 · Cited by 5

Kinetic studies of conjugate addition of amines to allenic and acrylic esters and their correlation with antibacterial activities against Staphylococcus aureus

Kiattisewee, C., Kaidad, A., Jiarpinitnun, C., & Luanphaisarnnont, T. (2018) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-018-2175-1 · Cited by 5

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Catalyst-Free Reactions under Biocompatible Conditions

Loh, T., Ren, M., & Lu, M. (2022) · Synlett · doi:10.1055/a-1994-3327 · Cited by 5

Tracking down protein–protein interactions via a FRET-system using site-specific thiol-labeling

Söveges, B., Imre, T., Póti, Á., Sok, P., Kele, Z., Alexa, A., Kele, P., & Németh, K. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00742j · Cited by 5

Site‐Selective Modification of Peptides and Proteins via Interception of Free‐Radical‐Mediated Dechalcogenation

Griffiths, R. C., Smith, F. R., Long, J., Williams, H. E. L., Layfield, R., & Mitchell, N. J. (2020) · Angewandte Chemie · doi:10.1002/ange.202006260 · Cited by 6

Biocompatible ultrafast thiol-acetalization enabled by triaryl carbenium ion-pair

Chen, P., Zou, M., Zhang, Y., Li, N., Ruiding, L. I., Liang, L., Zhang, Z., Loh, T., & Jia, Z. (2025) · Green Chemistry · doi:10.1039/d5gc03823e · Cited by 5

Computational study on the mechanism of CBT-Cys click reaction

Xu, Y., Qi, C., & Wang, C. (2020) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2020.112874 · Cited by 4

Covalent Epidermal Growth Factor Receptor (EGFR) Inhibitors in Targeted Therapy of Drug-Resistant Non-Small Cell Lung Cancer (A Review)

Shvetsov, A. B., & Semenov, A. (2024) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162024060347 · Cited by 3

Synthesis of Multisubstituted 2,3-Allenamides via Palladium-Catalyzed Carbonylation of Propargylic Esters

Zhang, Z., Ji, M.-M., Wu, X., He, Y.-Y., & Peng, J. (2024) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.4c00977 · Cited by 3

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Wu, L., Liu, K., Shi, Y., Peng, Y., Wang, J., Zhang, C., Strongin, R. M., & Yang, X. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.4c05887 · Cited by 3

Allenamides : synthesis and applications as orthogonal handle for protein modification and bioconjugation

Abbas, A. (2016) · DR-NTU (Nanyang Technological University)

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Schuler, B., & Pannell, L. K. (2002) · Bioconjugate Chemistry · doi:10.1021/bc025509t · Cited by 50

On‐Resin Preparation of Allenamidyl Peptides: A Versatile Chemoselective Conjugation and Intramolecular Cyclisation Tool

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ChemInform Abstract: Gold‐Mediated Selective Cysteine Modification of Peptides Using Allenes.

Chan, A. O., Tsai, J. L., Lo, V. K., Li, G., Wong, M., & Che, C. (2013) · ChemInform · doi:10.1002/chin.201317192

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Tessier, R., Nandi, R. K., Dwyer, B. G., Abegg, D., Sornay, C., Ceballos, J., Erb, S., Cianférani, S., Wagner, A., Chaubet, G., et al. (2020) · Angewandte Chemie · doi:10.1002/ange.202002626 · Cited by 11