Mirror-image T7 transcription of chirally inverted ribosomal and functional RNAs
Abstract
To synthesize a chirally inverted ribosome with the goal of building mirror-image biology systems requires the preparation of kilobase-long mirror-image ribosomal RNAs that make up the structural and catalytic core and about two-thirds of the molecular mass of the mirror-image ribosome. Here, we chemically synthesized a 100-kilodalton mirror-image T7 RNA polymerase, which enabled efficient and faithful transcription of the full-length mirror-image 5 S , 16 S , and 23 S ribosomal RNAs from enzymatically assembled long mirror-image genes. We further exploited the versatile mirror-image T7 transcription system for practical applications such as biostable mirror-image riboswitch sensor, long-term storage of unprotected kilobase-long l -RNA in water, and l -ribozyme–catalyzed l -RNA polymerization to serve as a model system for basic RNA research.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Recent advances have enabled chemical synthesis of mirror-image kilobase-length nucleic acids and large functional proteins.
“recent advances have enabled chemical synthesis of mirror-image kilobase-length nucleic acids and large functional proteins ( 6 ).”
From Confronting risks of mirror life (2024) · cites this paper as [6]
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,694 · see citing works
Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide
Merrifield, R. B. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00897a025 · Cited by 7,645 · see citing works
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 4,142 · see citing works
Engineering and characterization of a superfolder green fluorescent protein
Pédelacq, J. D., Cabantous, S., Tran, T. H., Terwilliger, T. C., & Waldo, G. S. (2005) · Nature Biotechnology · doi:10.1038/nbt1172 · Cited by 2,295 · see citing works
RNA Mimics of Green Fluorescent Protein
Paige, J. S., Wu, K., & Jaffrey, S. R. (2011) · Science · doi:10.1126/science.1207339 · Cited by 1,353 · see citing works
RNA-peptide fusions for the in vitro selection of peptides and proteins
Roberts, R. W., & Szostak, J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12297 · Cited by 1,108 · see citing works
Wan, Q., & Danishefsky, S. J. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200704195 · Cited by 880 · see citing works
Protein Chemical Synthesis by Ligation of Peptide Hydrazides
Fang, G., Li, Y., Shen, F., Huang, Y., Li, J., Lin, Y., Cui, H., & Liu, L. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201100996 · Cited by 812 · see citing works
Yan, L. Z., & Dawson, P. E. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003265m · Cited by 663 · see citing works
Li, Y., & Breaker, R. R. (1999) · Journal of the American Chemical Society · doi:10.1021/ja990592p · Cited by 587 · see citing works
Fluorescence Imaging of Cellular Metabolites with RNA
Paige, J. S., Nguyen-Duc, T., Song, W., & Jaffrey, S. R. (2012) · Science · doi:10.1126/science.1218298 · Cited by 523 · see citing works
An in vitro polysome display system for identifying ligands from very large peptide libraries.
Mattheakis, L. C., Bhatt, R. R., & Dower, W. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9022 · Cited by 515 · see citing works
A highly flexible tRNA acylation method for non-natural polypeptide synthesis
Murakami, H., Ohta, A., Ashigai, H., & Suga, H. (2006) · Nature Methods · doi:10.1038/nmeth877 · Cited by 470 · see citing works
Milton, R. C. D., Milton, S. C. F., & Kent, S. B. H. (1992) · Science · doi:10.1126/science.1604320 · Cited by 427 · see citing works
Convergent Chemical Synthesis of Proteins by Ligation of Peptide Hydrazides
Fang, G., Wang, J., & Liu, L. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203843 · Cited by 381 · see citing works
Protocells and RNA Self-Replication
Joyce, G. F., & Szostak, J. W. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034801 · Cited by 308 · see citing works
In-ice evolution of RNA polymerase ribozyme activity
Attwater, J., Wochner, A., & Holliger, P. (2013) · Nature Chemistry · doi:10.1038/nchem.1781 · Cited by 279 · see citing works
Amplification of RNA by an RNA polymerase ribozyme
Horning, D. P., & Joyce, G. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610103113 · Cited by 261 · see citing works
A synthetic molecular system capable of mirror-image genetic replication and transcription
Wang, Z., Xu, W., Liu, L., & Zhu, T. F. (2016) · Nature Chemistry · doi:10.1038/nchem.2517 · Cited by 209 · see citing works
Self-citationA cross-chiral RNA polymerase ribozyme
Sczepanski, J. T., & Joyce, G. F. (2014) · Nature · doi:10.1038/nature13900 · Cited by 186 · see citing works
A ‘resource allocator’ for transcription based on a highly fragmented T7 RNA polymerase
Segall-Shapiro, T. H., Meyer, A. J., Ellington, A. D., Sontag, E. D., & Voigt, C. A. (2014) · Molecular Systems Biology · doi:10.15252/msb.20145299 · Cited by 181 · see citing works
Maity, S. K., Jbara, M., Laps, S., & Brik, A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201603169 · Cited by 169 · see citing works
Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
Weinstock, M. T., Jacobsen, M. T., & Kay, M. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410900111 · Cited by 142 · see citing works
Synthesis and applications of RNAs with position-selective labelling and mosaic composition
Liu, Y., Holmstrom, E. D., Zhang, J., Yu, P., Wang, J., Dyba, M., Chen, D., Ying, J., Lockett, S., Nesbitt, D. J., et al. (2015) · Nature · doi:10.1038/nature14352 · Cited by 126 · see citing works
An RNA polymerase ribozyme that synthesizes its own ancestor
Tjhung, K. F., Shokhirev, M. N., Horning, D. P., & Joyce, G. F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914282117 · Cited by 121 · see citing works
Huang, J., Brieba, L. G., & Sousa, R. (2000) · Biochemistry · doi:10.1021/bi000579d · Cited by 113 · see citing works
Bioorthogonal information storage in l-DNA with a high-fidelity mirror-image Pfu DNA polymerase
Fan, C., Deng, Q., & Zhu, T. F. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00969-6 · Cited by 108 · see citing works
Self-citationOberthüer, D., Achenbach, J., Gabdulkhakov, A. G., Buchner, K., Maasch, C., Falke, S., Rehders, D., Klußmann, S., & Betzel, C. (2015) · Nature Communications · doi:10.1038/ncomms7923 · Cited by 102 · see citing works
Zawadzke, L. E., & Berg, J. M. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00036a073 · Cited by 96 · see citing works
Synthesis of l ‐ and d ‐Ubiquitin by One‐Pot Ligation and Metal‐Free Desulfurization
Huang, Y., Chen, C., Gao, S., Wang, Y., Xiao, H., Wang, F., Tian, C., & Li, Y. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201600101 · Cited by 91 · see citing works
An ultraprocessive, accurate reverse transcriptase encoded by a metazoan group II intron
Zhao, C., Liu, F., & Pyle, A. M. (2017) · RNA · doi:10.1261/rna.063479.117 · Cited by 89 · see citing works
Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer
Yatime, L., Maasch, C., Hoehlig, K., Klußmann, S., Andersen, G. R., & Vater, A. (2015) · Nature Communications · doi:10.1038/ncomms7481 · Cited by 88 · see citing works
Enzymatic properties of a proteolytically nicked RNA polymerase of bacteriophage T7.
Ikeda, R. A., & Richardson, C. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61425-5 · Cited by 86 · see citing works
Binding of a Structured d -RNA Molecule by an l -RNA Aptamer
Sczepanski, J. T., & Joyce, G. F. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406634g · Cited by 84 · see citing works
A thermostable d-polymerase for mirror-image PCR
Pech, A., Achenbach, J., Jahnz, M., Schülzchen, S., Jarosch, F., Bordusa, F., & Klußmann, S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx079 · Cited by 83 · see citing works
Sousa, R., & Mukherjee, S. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01001-8 · Cited by 81 · see citing works
Guymon, R., Pomerantz, S. C., Crain, P. F., & McCloskey, J. A. (2006) · Biochemistry · doi:10.1021/bi052579p · Cited by 75 · see citing works
Directed evolution and selection of biostable l-DNA aptamers with a mirror-image DNA polymerase
Chen, J., Chen, M., & Zhu, T. F. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01337-8 · Cited by 71 · see citing works
Self-citationMirror-image polymerase chain reaction
Jiang, W., Zhang, B., Fan, C., Wang, M., Wang, J., Deng, Q., Liu, X., Ji, C., Zheng, J., Liu, L., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.37 · Cited by 67 · see citing works
Self-citationTotal chemical synthesis of a thermostable enzyme capable of polymerase chain reaction
Xu, W., Jiang, W., Wang, J., Yu, L., Ji, C., Liu, X., Liu, L., & Zhu, T. F. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.8 · Cited by 55 · see citing works
Self-citationCopying Life: Synthesis of an Enzymatically Active Mirror-Image DNA-Ligase Made of D-Amino Acids
Weidmann, J., Schnölzer, M., Dawson, P. E., & Hoheisel, J. D. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.02.008 · Cited by 55 · see citing works
Modifications in Thermus thermophilus 23 S Ribosomal RNA Are Centered in Regions of RNA-RNA Contact
Mengel‐From, J., Jensen, S. S., Rasmussen, A., Poehlsgaard, J., Iversen, J. J. L., & Kirpekar, F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600377200 · Cited by 53 · see citing works
Circular L-RNA aptamer promotes target recognition and controls gene activity
Ji, D., Lyu, K., Zhao, H., & Kwok, C. K. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab593 · Cited by 53 · see citing works
Huang, Y., Chen, C., Li, S.-J., Gao, S., Shi, J. M., & Li, Y. (2014) · Tetrahedron · doi:10.1016/j.tet.2014.03.022 · Cited by 51 · see citing works
Specific Inhibition of MicroRNA Processing Using l -RNA Aptamers
Sczepanski, J. T., & Joyce, G. F. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06696 · Cited by 49 · see citing works
How to Win the Battle with RNasePreprint
Green, M. R., & Sambrook, J. (2019) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top101857 · Cited by 49 · see citing works
Non‐Enzymatic Assembly of a Minimized RNA Polymerase Ribozyme
Wachowius, F., & Holliger, P. (2019) · ChemSystemsChem · doi:10.1002/syst.201900004 · Cited by 46 · see citing works
Mirror-Image Gene Transcription and Reverse Transcription
Wang, M., Jiang, W., Liu, X., Wang, J., Zhang, B., Fan, C., Liu, L., Pena-Alcantara, G., Ling, J., Ji, C., et al. (2019) · Chem · doi:10.1016/j.chempr.2019.01.001 · Cited by 41 · see citing works
Self-citationTotal synthesis and biochemical characterization of mirror image barnase
Vinogradov, A. A., Evans, E. D., & Pentelute, B. L. (2015) · Chemical Science · doi:10.1039/c4sc03877k · Cited by 35 · see citing works
Mirror‐Image 5S Ribonucleoprotein Complexes
Ling, J., Fan, C., Qin, H., Wang, M., Ji, C., Wittung-Stafshede, P. E., & Zhu, T. F. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201914799 · Cited by 34 · see citing works
Self-citationWitnessing the structural evolution of an RNA enzyme
Portillo, X., Huang, Y.-T., Breaker, R. R., Horning, D. P., & Joyce, G. F. (2021) · eLife · doi:10.7554/elife.71557 · Cited by 28 · see citing works
Translating protein enzymes without aminoacyl-tRNA synthetases
Ji, C., Chen, M., & Zhu, T. F. (2021) · Chem · doi:10.1016/j.chempr.2021.01.017 · Cited by 19 · see citing works
Self-citationCross-Chiral, RNA-Catalyzed Exponential Amplification of RNA
Bare, G. A. L., & Joyce, G. F. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c09233 · Cited by 19 · see citing works
Caton‐Williams, J., Hoxhaj, R., Fiaz, B., & Huang, Z. (2013) · Current Protocols in Nucleic Acid Chemistry · doi:10.1002/0471142700.nc0130s52 · Cited by 15 · see citing works
Characteristics of Amino Acids
Ellington, A. D., & Cherry, J. M. (1996) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mba01cs33 · Cited by 14 · see citing works
Peplow, M. (2018) · ACS Central Science · doi:10.1021/acscentsci.8b00432 · Cited by 12 · see citing works
Characteristics of Amino Acids
(1996) · Current Protocols in Protein Science · doi:10.1002/0471140864.psa01as04 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
CRISPR-Based Diagnostics: Challenges and Potential Solutions toward Point-of-Care Applications
Ghouneimy, A., Mahas, A., Maršić, T., Aman, R. A., & Mahfouz, M. M. (2022) · ACS Synthetic Biology · doi:10.1021/acssynbio.2c00496 · Cited by 169 · see citing works
Recent advances in chemical protein synthesis: method developments and biological applications
Dong, S., Zheng, J., Li, Y., Wang, H., Chen, G., Chen, Y., Fang, G., Guo, J., He, C., Hu, H., et al. (2024) · Science China Chemistry · doi:10.1007/s11426-024-1950-1 · Cited by 167 · see citing works
Design and regulation of engineered bacteria for environmental release
Chemla, Y., Sweeney, C. J., Wozniak, C. A., & Voigt, C. A. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01918-0 · Cited by 142 · see citing works
Regulation of biological processes by intrinsically chiral engineered materials
Ma, B., & Bianco, A. (2023) · Nature Reviews Materials · doi:10.1038/s41578-023-00561-1 · Cited by 126 · see citing works
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 · see citing works
Confronting risks of mirror life
Adamala, K. P., Agashe, D., Belkaid, Y., Bittencourt, D. M. D. C., Cai, Y., Chang, M. W., Chen, I. A., Church, G. M., Cooper, V. S., Davis, M. M., et al. (2024) · Science · doi:10.1126/science.ads9158 · Cited by 91 · see citing works
Modified nucleic acid aptamers: development, characterization, and biological applications
Ji, D., Feng, H., Liew, S. W., & Kwok, C. K. (2023) · Trends in biotechnology · doi:10.1016/j.tibtech.2023.05.005 · Cited by 74 · see citing works
Differentiating enantiomers by directional rotation of ions in a mass spectrometer
Zhou, X., Wang, Z., Li, S., Rong, X., Bu, J., Liu, Q., & Ouyang, Z. (2024) · Science · doi:10.1126/science.adj8342 · Cited by 68 · see citing works
Controlled enzymatic synthesis of oligonucleotides
Pichon, M. M., & Hollenstein, M. (2024) · Communications Chemistry · doi:10.1038/s42004-024-01216-0 · Cited by 50 · see citing works
Mirror-image ligand discovery enabled by single-shot fast-flow synthesis of D-proteins
Callahan, A. J., Gandhesiri, S., Travaline, T. L., Reja, R. M., Salazar, L. L., Hanna, S., Lee, Y., Li, K., Tokareva, O. S., Swiecicki, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45634-z · Cited by 50 · see citing works
Natural, modified and conjugated carbohydrates in nucleic acids
Dhara, D., Mulard, L. A., & Hollenstein, M. (2025) · Chemical Society Reviews · doi:10.1039/d4cs00799a · Cited by 44 · see citing works
Precision in protein chemical modification and total synthesis
Sun, Z., Liu, H., & Li, X. (2023) · Chem · doi:10.1016/j.chempr.2023.10.020 · Cited by 41 · see citing works
Chirality conferral enables the observation of hyper-Raman optical activity
Jones, R. R., Kerr, J. F., Kwon, H., Clowes, S. R., Ji, R., Petronijevic, E., Zhang, L., Pantoş, G. D., Smith, B., Batten, T., et al. (2024) · Nature Photonics · doi:10.1038/s41566-024-01486-z · Cited by 37 · see citing works
Accurate de novo design of heterochiral protein–protein interactions
Sun, K., Li, S., Zheng, B., Zhu, Y., Wang, T., Liang, M., Yao, Y., Zhang, K., Zhang, J., Li, H., et al. (2024) · Cell Research · doi:10.1038/s41422-024-01014-2 · Cited by 33 · see citing works
Chaput, J. C., Egli, M., & Herdewijn, P. A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf635 · Cited by 28 · see citing works
Single-step discovery of high-affinity RNA ligands by UltraSelex
Zhang, Y., Jiang, Y. Y., Kuster, D., Ye, Q., Huang, W., Fürbacher, S., Zhang, J., Doll, P., Lin, W., Dong, S., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01868-6 · Cited by 24 · see citing works
Mirror-image trypsin digestion and sequencing of D-proteins
Zhang, G., & Zhu, T. F. (2024) · Nature Chemistry · doi:10.1038/s41557-023-01411-x · Cited by 22 · see citing works
Self-citationGenerating a mirror-image monobody targeting MCP-1 via TRAP display and chemical protein synthesis
Hayashi, G., Naito, T., Miura, S., Iwamoto, N., Usui, Y., Bando-Shimizu, M., Suzuki, S., Higashi, K., Nonaka, M., Oishi, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54902-x · Cited by 20 · see citing works
Development of mirror-image monobodies targeting the oncogenic BCR::ABL1 kinase
Schmidt, N., Kumar, A., Korf, L., Dinh-Fricke, A. V., Abendroth, F., Koide, A., Linne, U., Rakwalska‐Bange, M., Koide, S., Essen, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54901-y · Cited by 16 · see citing works
Aptamers for mycotoxin recognition in food: Recent advances and future considerations
Fang, P., Qu, H., Mao, Y., & Zheng, L. (2023) · Advanced Agrochem · doi:10.1016/j.aac.2023.06.002 · Cited by 14 · see citing works
Single-Shot Flow Synthesis of D-Proteins for Mirror-Image Phage DisplayPreprint
Callahan, A. J., Gandhesiri, S., Travaline, T. L., Salazar, L. L., Hanna, S., Lee, Y., Li, K., Tokareva, O. S., Swiecicki, J., Loas, A., et al. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-x86xp · Cited by 16 · see citing works
Automated Flow Synthesis of Artificial Heme Enzymes for Enantiodivergent Biocatalysis
Fittolani, G., Kutateladze, D. A., Loas, A., Buchwald, S. L., & Pentelute, B. L. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c13832 · Cited by 13 · see citing works
Harnessing CRISPR-Cas systems for point-of-care diagnostic applications
Ghouneimy, A., Aman, R. A., Jiang, W., Ali, Z., & Mahfouz, M. M. (2025) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2025.118417 · Cited by 13 · see citing works
Fluorogenic RNA-Based Biosensors of Small Molecules: Current Developments, Uses, and Perspectives
Kehrli, J., Husser, C., & Ryckelynck, M. (2024) · Biosensors · doi:10.3390/bios14080376 · Cited by 13 · see citing works
Sethi, S., Xu, T., Sarkar, A., Drees, C., Jacob, C., & Walther, A. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202413983 · Cited by 13 · see citing works
Vinogradov, A. A., Bashiri, G., & Suga, H. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c11013 · Cited by 13 · see citing works
Engineering a Low-Immunogenic Mirror-Image VHH against Vascular Endothelial Growth Factor
Aoki, K., Higashi, K., Oda, S., Manabe, A., Maeda, K., Morise, J., Oka, S., Inuki, S., Ohno, H., Oishi, S., et al. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00197 · Cited by 12 · see citing works
The clinical potential of l -oligonucleotides: challenges and opportunities
Shearer, V., Yu, C., Han, X., & Sczepanski, J. T. (2024) · Chemical Science · doi:10.1039/d4sc05157b · Cited by 14 · see citing works
Chemically Synthetic d -Sortase Enables Enzymatic Ligation of d -Peptides
Ding, R., Shi, W., & Zheng, J. (2023) · Organic Letters · doi:10.1021/acs.orglett.3c01657 · Cited by 12 · see citing works
Selective Activation of Peptide‐Thioester Precursors for Templated Native Chemical Ligations
Spaltenstein, P., Giesler, R. J., Scherer, S. R., Erickson, P. W., & Kay, M. S. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202413644 · Cited by 11 · see citing works
How scientists are hacking the genetic code to give proteins new powers
Kwon, D. (2023) · Nature · doi:10.1038/d41586-023-01980-4 · Cited by 10 · see citing works
Gong, X., Yang, Y., Zhang, K., Li, T., Wang, Q., Li, J., Liu, W., Tu, P., & Song, Y. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.4c05733 · Cited by 9 · see citing works
Serine Octamer Clusters Direct the Chirality of Peptides Formed in Water Microdroplets
Shira, B. A., & Cooks, R. G. (2025) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.5c00473 · Cited by 8 · see citing works
The Use of CRISPR-Cas Systems for Viral Detection: A Bibliometric Analysis and Systematic Review
Jeddoub, O., Touil, N., Nyabi, O., Fahime, E. E., Ennibi, K., Gala, J., Benjouad, A., & Belayachi, L. (2025) · Biosensors · doi:10.3390/bios15060379 · Cited by 8 · see citing works
Mirror Life: Bridging Chirality, Ethics, and the Foundations of Life Creation
Li, Y., Moradialvand, M., Asbridge, L., FRAZIER, K. B., Tay, F. R., & Makvandi, P. (2025) · Advanced Materials · doi:10.1002/adma.202510791 · Cited by 11 · see citing works
Functional Ambidexterity of an Ancient Nucleic Acid‐Binding Domain
Weil‐Ktorza, O., Naveh‐Tassa, S., Fridmann‐Sirkis, Y., Despotović, D., Cherukuri, K. P., Corlett, T., Levy, Y., Metanis, N., & Longo, L. M. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202505188 · Cited by 12 · see citing works
Carpenter, E. J., Peng, C., Haregu, S., Twells, N., Woudstra, L., Sood, A., Cartmell, J., Woods, R. J., Mahal, L. K., Wang, S.-K., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx6373 · Cited by 10 · see citing works
Prior disulfide bond-mediated Ser/Thr ligation
Liu, H., Chow, H. Y., Liu, J., Shi, P., & Li, X. (2024) · Chemical Science · doi:10.1039/d4sc04825c · Cited by 7 · see citing works
Xie, X.-L., Qi, J.-Z., Wan, X.-C., Zhang, S.-D., Zhang, Y., & Fang, G. (2023) · Organic Letters · doi:10.1021/acs.orglett.3c00998 · Cited by 7 · see citing works
Engineering Bacteria for Environmental Release: Regulatory Challenges and Design StrategiesPreprint
Chemla, Y., Sweeney, C. J., Wozniak, C. A., & Voigt, C. A. (2024) · doi:10.22541/au.171933709.97462270/v1 · Cited by 7 · see citing works
The path to biotechnological singularity: Current breakthroughs and outlook
Wen, Z., Yang, D., Yang, Y., Hu, J., Parviainen, A., Chen, X., Li, Q., VanDeusen, E. A., Ma, J., & Tay, F. R. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2025.108667 · Cited by 7 · see citing works
Stereoselective RNA reaction with chiral 2′-OH acylating agents
Shioi, R., Xiao, L., Chatterjee, S., & Kool, E. T. (2023) · Chemical Science · doi:10.1039/d3sc03067a · Cited by 6 · see citing works
Mirror of the unknown: should research on mirror-image molecular biology be stopped?
Zhu, T. F. (2025) · Nature · doi:10.1038/d41586-025-02912-0 · Cited by 5 · see citing works
Self-citationChemical Synthesis, Refolding, and Characterization of Mirror-Image Cyclophilin A
Yeşilçimen, A., Gandhesiri, S., Travaline, T. L., Callahan, A. J., Tokareva, O. S., Loas, A., McGee, J. H., & Pentelute, B. L. (2025) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.4c03049 · Cited by 4 · see citing works
Cross-chiral exponential amplification of an RNA enzyme
Cochrane, W. G., Bare, G. A. L., Joyce, G. F., & Horning, D. P. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2413668121 · Cited by 4 · see citing works
Homochiral ligations of amino acids by N-phosphorylation in water
Zhang, Y., Zhou, L., Chen, C., Wang, X., Liu, Y., Tang, G., Zhao, Y., & Gao, X. (2025) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2025.102495 · Cited by 3 · see citing works
An expanded substrate scope for cross-chiral ligation enables efficient synthesis of long l -RNAs
Han, X., & Sczepanski, J. T. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00253a · Cited by 3 · see citing works
Haroon, M. Y., Huang, L., Hayat, A., Chen, H., & You, X. (2025) · Advanced Optical Materials · doi:10.1002/adom.202501589 · Cited by 2 · see citing works
Duan, Y., Chen, S., Wang, Y., Liu, Z., Wei, L., Luo, B., Liu, W., & Gao, H. (2025) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2025.115328 · Cited by 2 · see citing works
Sanger Sequencing of Xeno‐Nucleic Acid
Wang, Y., Zhang, Z., Chen, L., Zhu, J., Qin, S., Wei, D., Zhang, J., Han, F., Wang, F., Lin, Q., et al. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.202516617 · Cited by 2 · see citing works
Protein engineering: status report
Ai, H., Arnold, F. H., Barrick, D., Bayley, H., Brownless, A.-L. R., Campbell, R. E., Castells‐Graells, R., Chaiyen, P., Chica, R. A., Chisholm, L. O., et al. (2026) · Protein Engineering Design and Selection · doi:10.1093/protein/gzag020 · Cited by 2 · see citing works
Selective Activation of Peptide‐Thioester Precursors for Templated Native Chemical Ligations
Spaltenstein, P., Giesler, R. J., Scherer, S. R., Erickson, P. W., & Kay, M. S. (2024) · Angewandte Chemie · doi:10.1002/ange.202413644 · Cited by 2 · see citing works
Wang, M., Cui, T., Huang, S., Han, D., Deng, X., Liu, Y., & Shi, C. (2025) · Organic & Biomolecular Chemistry · doi:10.1039/d5ob00243e · Cited by 2 · see citing works
Reconstituting alternative life using the test-bed of cell-free systems
Hofmann, M., Abdo, F., Borkowski, O., & Kushwaha, M. (2025) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2024.0293 · Cited by 2 · see citing works
Automated Flow Synthesis of Artificial Heme Enzymes for Enantioselective BiocatalysisPreprint
Fittolani, G., Kutateladze, D. A., Loas, A., Buchwald, S. L., & Pentelute, B. L. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2024-k0wkb · Cited by 2 · see citing works
Making Sense of Helices: Right and Wrong Models in Science and Art
Egli, M., & Zhang, S. (2023) · Molecular Frontiers Journal · doi:10.1142/s2529732523500086 · Cited by 1 · see citing works
Silicon Is the Next Frontier in Plant Synthetic Biology
Acharya, A., Hopkins, K. A., & Simms, T. (2025) · SynBio · doi:10.3390/synbio3030012 · Cited by 1 · see citing works
Oa AEP1-Mediated Ligation of Mirror-Image Peptides via Acyl Donor Substrate Engineering
Shu, Q., Wang, Y., Shi, C., Sun, Y., Zhao, R., & Shi, J. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c00057 · Cited by 1 · see citing works
Spiegelmer Aptamers: Innovative Approach in Breast Cancer
Hezave, Y. A., Najafi, R., Amini, R., & Shojaeian, A. (2026) · Breast Cancer Basic and Clinical Research · doi:10.1177/11782234261456036 · Cited by 1 · see citing works
Automated Flow Synthesis of Nature-Derived, Engineered, and De Novo -Designed Functional Luciferases
Sarabia-Castillo, D., Cowfer, A. E., Pal, S., Farquhar, C. E., Loas, A., & Pentelute, B. L. (2026) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.6c01513 · Cited by 1 · see citing works
Nucleoside modification-based flexizymes with versatile activity for tRNA aminoacylation
Zhang, X.-D., Wang, Y.-S., Xiang, H., Bai, L., Cheng, P., Li, K., Huang, R. T., Wang, X., & Lei, X. (2024) · Chemical Communications · doi:10.1039/d3cc05673b · Cited by 1 · see citing works
BracketMaker : Visualization and optimization of chemical protein synthesis
Evangelista, J. L., & Kay, M. S. (2024) · Protein Science · doi:10.1002/pro.5174 · Cited by 1 · see citing works
Chen, G., Chen, Z., Huang, S., Liu, Y., Lu, Z. J., Ou, G., Qi, Y., Wang, X., Wang, Y., Xie, W., et al. (2024) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2024-0541 · Cited by 1 · see citing works
Functional Ambidexterity of an Ancient Nucleic Acid‐Binding Domain
Weil‐Ktorza, O., Naveh‐Tassa, S., Fridmann‐Sirkis, Y., Despotović, D., Cherukuri, K. P., Corlett, T., Levy, Y., Metanis, N., & Longo, L. M. (2025) · Angewandte Chemie · doi:10.1002/ange.202505188 · Cited by 1 · see citing works
Chiral Single Molecule Localization Microscopy (chiralSMLM)Preprint
Aravinth, S., Pant, N., & Mondal, P. P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.10.637296 · Cited by 1 · see citing works
How should ‘mirror life’ research be restricted? Debate heats up
Peplow, M. (2025) · Nature · doi:10.1038/d41586-025-02902-2 · Cited by 1 · see citing works
Kim, D. H., Huang, B.-S., Yik, E. J., Baker, J. R., Rajasekaran, G., Jangili, P., Zhou, G., Sismour, A. M., Medina, E. L., & Lee, J. S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.03.692211 · Cited by 1 · see citing works
Woźniak, K., & Brzeziński, K. (2023) · Biomolecules · doi:10.3390/biom13050782
Sethi, S., Xu, T., Sarkar, A., Drees, C., Jacob, C., & Walther, A. (2024) · Angewandte Chemie · doi:10.1002/ange.202413983
Theoretical Framework for Novel Catalytic Biomolecules Composed of Multiple Peptides
Ambo, A., Ohno, S., Yamaguchi, Y., & Seki, M. (2024) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c24-00155
POLETicians in the Mud: Preprokaryotic Organismal Lifeforms Existing Today (POLET) Hypothesis
Ruden, D. M., & Hood, G. R. (2025) · Bacteria · doi:10.3390/bacteria4030042
Leveraging protein representations to explore uncharted fold spaces with generative modelsPreprint
Miao, Y., Pačesa, M., Georgeon, S., Schmidt, J. H., Lu, T., Huang, P., & Correia, B. E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.10.681606
Leveraging protein representations to explore uncharted fold spaces with generative modelsPreprint
Correia, B. E., Miao, Y., Pačesa, M., Georgeon, S., Schmidt, J. H., Lu, T., & Huang, P. (2025) · Research Square · doi:10.21203/rs.3.rs-7827245/v1
Theory of conferred hyper-Raman optical activity
Andrews, D. L., & Valev, V. K. (2025) · Journal of Optics · doi:10.1088/2040-8986/ae248d
Fourier Helicity Spectra as Quantifiers of Multiscale ChiralityPreprint
Im, S. W., Ma, J., Moudgal, N., & Kotov, N. A. (2025) · bioRxiv · doi:10.64898/2025.12.15.694500
Metabolic diversity of microorganisms toward atypical sugar enantiomersPreprint
Nishijima, H., Igarashi, K., Kitagawa, W., Tabata, H., Nakanishi, S., & Kato, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.17.700050
Sanger Sequencing of Xeno‐Nucleic Acid
Wang, Y., Zhang, Z., Chen, L., Zhu, J., Qin, S., Wei, D., Zhang, J., Han, F., Wang, F., Lin, Q., et al. (2026) · Angewandte Chemie · doi:10.1002/ange.202516617
Recent instrumental developments in chiral mass spectrometry
Chu, F., & Pan, Y. (2026) · Advanced Scientific Instruments · doi:10.1016/j.asi.2026.100002
Second-harmonic chiroptical scattering spectroscopy from plasmonic nanohelices
Olohan, B. J., Choi, H., Kwon, H., Ji, R., Kerrigan, B., Nedderman, O. R. J., Pantoş, G. D., Fischer, P., & Valev, V. K. (2026) · Optics Express · doi:10.1364/oe.582687
Face au spectre de la vie miroir
Cooper, V. S. (2026) · Pour la Science · doi:10.3917/pls.581.0028
Total chemical synthesis of pentameric cholera toxin subunit B
Spaltenstein, P., Scherer, S. R., Jones, T. E., Giesler, R. J., & Kay, M. S. (2026) · Chemical Communications · doi:10.1039/d5cc06935a
Mirror-image biology: perspectives and challenges
Chen, Y., Han, Y., Mu, Z., Dong, S., Chu, H., Lu, J., & Qian, Z. (2026) · Journal of Biosafety and Biosecurity · doi:10.1016/j.jobb.2026.04.003
Xenonucleic Acids and Their Applications
Abdi, G., Dave, K., Gautam, S., & Panchal, U. (2026) · Springer eBooks · doi:10.1007/978-981-95-3957-4_12
Engineered Template-Dependent DNA Polymerases with an Expanded Substrate Scope
Egerström, A., Eadsforth, M. A., Choo, J. P. S., & Lovelock, S. L. (2026) · ACS Catalysis · doi:10.1021/acscatal.6c00722
Ding, X., Li, C., Wang, X., & Liang, L.-J. (2026) · Organic & Biomolecular Chemistry · doi:10.1039/d6ob00780e
Ji, R., Reuven, B., Kerrigan, B., Markovich, G., & Valev, V. K. (2026) · Nano Letters · doi:10.1021/acs.nanolett.6c01271
Wang, J., Wang, G., Li, J., & Zhu, B. (2026) · Applied Sciences · doi:10.3390/app16147008
Lean, C. H., Vincent, R. M., Lynch, K. E., Jamrozik, E., & Jaschke, P. R. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2026.1833212
In Vitro Selection of Functional Neoproteins Containing Highly Fluorinated Cores
Beattie, A. T., Vinogradov, A. A., Okada, C., Sengoku, T., Katoh, T., & Suga, H. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.5293145
In Vitro Selection of Functional Neoproteins Containing Highly Fluorinated Cores
Beattie, A. T., Vinogradov, A. A., Okada, C., Sengoku, T., Katoh, T., & Suga, H. (2026) · Angewandte Chemie · doi:10.1002/ange.5293145
Bag, S. S., Banerjee, A., & Barman, S. (2026) · ACS Omega · doi:10.1021/acsomega.6c07950
- Authors
- Xu, Y., & Zhu, T. F.
- Affiliations
- Westlake University (CN)
- Corresponding author
- Zhu, Ting F.
- ORCID
- Venue
- Science
- Published
- 2022-10-28
- Volume
- 378
- Issue
- 6618
- Pages
- 405-412
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W4307412638
- Semantic Scholar
- 890d326d545e2f65c02484f497e8b6a4f6152720
- Cited by
- 94
- References
- 57
- Citations by year
- 2026: 21 · 2025: 32 · 2024: 28 · 2023: 12 · 2022: 1
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- rDNA transcription, 5S rRNA, 16S rRNA, 23S rRNA
- MeSH terms
- DNA-Directed DNA Polymerase, Nucleic Acid Conformation, Ribosomes, DNA-Directed RNA Polymerases, RNA, Ribosomal, 16S, RNA, Ribosomal, 23S, RNA, Ribosomal, 5S, Transcription, Genetic, Viral Proteins, RNA, Catalytic
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