Cited by 404Biochemical and Structural CharacterizationChemical Synthesis and AnalysisBacterial Genetics and Biotechnology

The DOI matches its Crossref record; 38 of the 40 references it cites were found in a registry or an index.

Production of cyclic peptides and proteins in vivo

Open access

Scott, Charles P., Abel-Santos, Ernesto, Wall, Mark, Wahnon, Daphne C., Benkovic, Stephen J.·1999·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.96.24.13638PMC PMC24117

Open this paper in CoChat — free account Open PDF

Abstract

Combinatorial libraries of synthetic and natural products are an important source of molecular information for the interrogation of biological targets. Methods for the intracellular production of libraries of small, stable molecules would be a valuable addition to existing library technologies by combining the discovery potential inherent in small molecules with the large library sizes that can be realized by intracellular methods. We have explored the use of split inteins ( in ternal pro teins ) for the intracellular catalysis of peptide backbone cyclization as a method for generating proteins and small peptides that are stabilized against cellular catabolism. The DnaE split intein from Synechocystis sp. PCC6803 was used to cyclize the Escherichia coli enzyme dihydrofolate reductase and to produce the cyclic, eight-amino acid tyrosinase inhibitor pseudostellarin F in bacteria. Cyclic dihydrofolate reductase displayed improved in vitro thermostability, and pseudostellarin F production was readily apparent in vivo through its inhibition of melanin production catalyzed by recombinant Streptomyces antibioticus tyrosinase. The ability to generate and screen for backbone cyclic products in vivo is an important milestone toward the goal of generating intracellular cyclic peptide and protein libraries.

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

Crossref · 10.1073/pnas.96.24.13638

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

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.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
The Chemist's Companion: A Handbook of Practical Data, Techniques, and References
Gordon, A. J., & Ford, R. A. (1972) · Medical Entomology and Zoology · Cited by 1,857
A bacterial two-hybrid system based on a reconstituted signal transduction pathway
Karimova, G., Pidoux, J., Ullmann, A., & Ladant, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5752 · Cited by 1,707
Method for Determination of the Amino Acid Sequence in Peptides.
Edman, P., Högfeldt, E., Sillén, L. G., & Kinell, P. (1950) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.04-0283 · Cited by 1,398
Applications of Combinatorial Technologies to Drug Discovery. 2. Combinatorial Organic Synthesis, Library Screening Strategies, and Future Directions
Gordon, E. M., Barrett, R. W., Dower, W. J., Fodor, S. P. A., & Gallop, M. A. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00036a001 · Cited by 1,142
Applications of Combinatorial Technologies to Drug Discovery. 1. Background and Peptide Combinatorial Libraries
Gallop, M. A., Barrett, R. W., Dower, W. J., Fodor, S. P. A., & Gordon, E. M. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00035a001 · Cited by 1,135
A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
Xu, Y. Q., Piston, D. W., & Johnson, C. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.151 · Cited by 613
Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel “unnatural” natural products
McDaniel, R. N., Thamchaipenet, A., Gustafsson, C., Fu, H., Betlach, M. C., Betlach, M. C., & Ashley, G. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1846 · Cited by 463
Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
Colas, P., Cohen, B. A., Jessen, T., Grishina, I. A., McCoy, J. M., & Brent, R. (1996) · Nature · doi:10.1038/380548a0 · Cited by 459
Protein trans -splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803
Wu, H., Hu, Z., & Liu, X. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9226 · Cited by 379

Show all 40 references

Research works printed but not linked: 1

G Della-Cioppa, S J Garger, G G Sverlow, T H Turpen, L K Grill Biotechnology 8, 634–638 (1990).

Sorted by citations

Items 101–200 of 404

Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains
Wang, X., & Zhang, W. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201705194 · Cited by 65
Kinetic Control of One‐Pot Trans‐Splicing Reactions by Using a Wild‐Type and Designed Split Intein
Shah, N. H., Vila‐Perelló, M., & Muir, T. W. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201102909 · Cited by 64
In vivo biosynthesis of an Ala-scan library based on the cyclic peptide SFTI-1
Austin, J., Kimura, R. H., Woo, Y., & Camarero, J. A. (2009) · Amino Acids · doi:10.1007/s00726-009-0338-4 · Cited by 64
Synthetic Genomics and Synthetic Biology Applications Between Hopes and Concerns
König, H., Frank, D. O., Heil, R., & Coenen, C. (2013) · Current Genomics · doi:10.2174/1389202911314010003 · Cited by 63
A simple strategy for the construction of combinatorial cyclic peptoid libraries
Lee, J. H., Meyer, A. M., & Lim, H. (2010) · Chemical Communications · doi:10.1039/c0cc03272g · Cited by 63
Mechanistic and Kinetic Considerations of Protein Splicing
Evans, T. C., & Xu, M. (2002) · Chemical Reviews · doi:10.1021/cr9601369 · Cited by 63
Small and Simple, yet Sturdy: Conformationally Constrained Peptides with Remarkable Properties
Bozovičar, K., & Bratkovič, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041611 · Cited by 63
Expression of Fluorescent Cyclotides using Protein Trans‐Splicing for Easy Monitoring of Cyclotide–Protein Interactions
Jagadish, K., Borra, R., Lacey, V. K., Majumder, S., Shekhtman, A. G., Wang, L., & Camarero, J. A. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201209219 · Cited by 61
Zinc Inhibition of Protein trans-Splicing and Identification of Regions Essential for Splicing and Association of a Split Intein*
Ghosh, I., Sun, L., & Xu, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011049200 · Cited by 61
Protein trans-splicing in transgenic plant chloroplast: Reconstruction of herbicide resistance from split genes
Chin, H. G., Kim, G., Marin, I., Mersha, F. B., Evans, T. C., Chen, L., Xu, M., & Pradhan, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0736538100 · Cited by 59
Discovery of antibacterial cyclic peptides that inhibit the ClpXP protease
Cheng, L. Z., Naumann, T. A., Horswill, A. R., Hong, S., Venters, B. J., Tomsho, J. W., Benkovic, S. J., & Keiler, K. C. (2007) · Protein Science · doi:10.1110/ps.072933007 · Cited by 58
Self-citation
Live-cell protein engineering with an ultra-short split intein
Burton, A. J., Haugbro, M., Parisi, E., & Muir, T. W. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003613117 · Cited by 57
From nature to creation: Going around in circles, the art of peptide cyclization
Zhang, R., Thapa, P., Espiritu, M. J., Menon, V., & Bingham, J. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.11.017 · Cited by 56
Cell-free synthetic biology for natural product biosynthesis and discovery
Rice, A. J., Sword, T. T., Chengan, K., Mitchell, D. A., Mouncey, N. J., Moore, S. J., & Bailey, C. B. (2025) · Chemical Society Reviews · doi:10.1039/d4cs01198h · Cited by 58
DNA‐Encoded Libraries: Towards Harnessing their Full Power with Darwinian Evolution
Dockerill, M., & Winssinger, N. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202215542 · Cited by 57
Split-inteins and their bioapplications
Li, Y. (2015) · Biotechnology Letters · doi:10.1007/s10529-015-1905-2 · Cited by 55
A molecular engineering toolbox for the structural biologist
Debelouchina, G. T., & Muir, T. W. (2017) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583517000051 · Cited by 55
Detection of protein–protein interactions in vivo based on protein splicing
Ozawa, T., & Umezawa, Y. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00244-1 · Cited by 54
Genetically programmed cell-based synthesis of non-natural peptide and depsipeptide macrocycles
Spinck, M., Piedrafita, C., Robertson, W. E., Elliott, T. S., Cervettini, D., de la Torre, D., & Chin, J. W. (2022) · Nature Chemistry · doi:10.1038/s41557-022-01082-0 · Cited by 53
Cyclic peptides: A powerful instrument for advancing biomedical nanotechnologies and drug development
Martian, P. C., Tertiş, M., Leonte, D., Hădade, N. D., Cristea, C., & Crisan, O. (2024) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2024.116488 · Cited by 52
Extracellular Self-Assembly of Functional and Tunable Protein Conjugates from Bacillus subtilis
Gilbert, C., Howarth, M. R., Harwood, C. R., & Ellis, T. (2017) · ACS Synthetic Biology · doi:10.1021/acssynbio.6b00292 · Cited by 50
Recent advances in protein splicing: manipulating proteins in vitro and in vivo
Xu, M., & Evans, T. C. (2005) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2005.06.012 · Cited by 50
Stabilization of Native Protein Fold by Intein-Mediated Covalent Cyclization
Williams, N. K., Liepinsh, E., WATT, S. J., Prosselkov, P. V., Matthews, J. M., Attard, P., Beck, J. L., Dixon, N. E., & Otting, G. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.037 · Cited by 50
Synthetic biology approaches in drug discovery and pharmaceutical biotechnology
Neumann, H., & Neumann‐Staubitz, P. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2578-3 · Cited by 50
Generation of a Genetically Encoded, Photoactivatable Intein for the Controlled Production of Cyclic Peptides
Böcker, J. K., Friedel, K., Matern, J. C. J., Bachmann, A., & Mootz, H. D. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201409848 · Cited by 49
Protein Splicing in the Absence of an Intein Penultimate Histidine
Chen, L., Benner, J. S., & Perler, F. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000178200 · Cited by 49
Biosynthesis of Staphylococcus aureus Autoinducing Peptides by Using the Synechocystis DnaB Mini-Intein
Malone, C. L., Boles, B. R., & Horswill, A. R. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.00912-07 · Cited by 49
Intein-mediated assembly of a functional β-glucuronidase in transgenic plants
Yang, J., Fox, G. C., & Henry-Smith, T. V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0635899100 · Cited by 49
A Split‐Intein‐Based Method for the Efficient Production of Circularized Nanodiscs for Structural Studies of Membrane Proteins
Miehling, J., Goričanec, D., & Hagn, F. (2018) · ChemBioChem · doi:10.1002/cbic.201800345 · Cited by 48
A cleavable scaffold strategy for the synthesis of one-bead one-compound cyclic peptoid libraries that can be sequenced by tandem mass spectrometry
Simpson, L. S., & Kodadek, T. J. (2012) · Tetrahedron Letters · doi:10.1016/j.tetlet.2012.02.112 · Cited by 47
Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool
Ciragan, A., Aranko, A. S., Tascón, I., & Iwaï, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.10.006 · Cited by 47
Cyclic peptides as potential therapeutic agents for skin disorders
Namjoshi, S., & Benson, H. A. (2010) · Biopolymers · doi:10.1002/bip.21476 · Cited by 47
Bioinspired Strategy for the Ribosomal Synthesis of Thioether-Bridged Macrocyclic Peptides in Bacteria
Bionda, N., Cryan, A. L., & Fasan, R. (2014) · ACS Chemical Biology · doi:10.1021/cb500311k · Cited by 46
Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics
Swenson, C., Mandava, G., Thomas, D. M., & Moellering, R. E. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00423 · Cited by 55
“Splicing up” drug discovery.☆Cell-based expression and screening of genetically-encoded libraries of backbone-cyclized polypeptides
Sancheti, H., & Camarero, J. A. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.07.003 · Cited by 45
Synthesis and Screening of One-Bead-One-Compound Cyclic Peptide Libraries
Qian, Z., Upadhyaya, P., & Pei, D. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2020-4_3 · Cited by 45
Split Inteins: Nature’s Protein Ligases
Shah, N. H., & Muir, T. W. (2011) · Israel Journal of Chemistry · doi:10.1002/ijch.201100094 · Cited by 44
Encoded combinatorial libraries for the construction of cyclic peptoid microarrays
Kwon, Y.-U., & Kodadek, T. J. (2008) · Chemical Communications · doi:10.1039/b812735b · Cited by 44
Access to Large Cyclic Peptides by a One-Pot Two-Peptide Segment Ligation/Cyclization Process
Boll, E., Ebran, J., Drobecq, H., Mahdi, O. E., Raibaut, L., Ollivier, N., & Melnyk, O. (2014) · Organic Letters · doi:10.1021/ol503359w · Cited by 44
Using protein engineering to understand and modulate aggregation
Ebo, J. S., Guthertz, N., Radford, S. E., & Brockwell, D. J. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.01.005 · Cited by 44
Methodologies for Backbone Macrocyclic Peptide Synthesis Compatible With Screening Technologies
Shinbara, K., Liu, W., van Neer, R. H. P., Katoh, T., & Suga, H. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00447 · Cited by 44
Dynamically Tunable, Macroscopic Molecular Networks Enabled by Cellular Synthesis of 4-Arm Star-like Proteins
Yang, Z., Yang, Y., Wang, M., Wang, T., Fok, H. K. F., Jiang, B., Xiao, W., Kou, S., Guo, Y., Yan, Y., et al. (2019) · Matter · doi:10.1016/j.matt.2019.09.013 · Cited by 42
Herbicide resistance from a divided EPSPS protein: the split Synechocystis DnaE intein as an in vivo affinity domain
Chen, L., Pradhan, S., & Evans, T. C. (2001) · Gene · doi:10.1016/s0378-1119(00)00568-0 · Cited by 43
Ribosomal Synthesis of Macrocyclic Peptides in Vitro and in Vivo Mediated by Genetically Encoded Aminothiol Unnatural Amino Acids
Frost, J. R., Jacob, N. T., Papa, L. J., Owens, A. E., & Fasan, R. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00119 · Cited by 42
Methods for the Creation of Cyclic Peptide Libraries for Use in Lead Discovery
Foster, A. D., Ingram, J. D., Leitch, E. K., Lennard, K. R., Osher, E. L., & Tavassoli, A. (2015) · SLAS DISCOVERY · doi:10.1177/1087057114566803 · Cited by 42
Protein splicing: A versatile tool for drug discovery☆
Cheriyan, M., & Perler, F. B. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.04.021 · Cited by 41
Design, synthesis, and diversification of ribosomally derived peptide macrocycles
Frost, J. R., Smith, J. M., & Fasan, R. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.06.015 · Cited by 40
Ribosomal synthesis of backbone macrocyclic peptides
Katoh, T., Goto, Y., Reza, M. S., & Suga, H. (2011) · Chemical Communications · doi:10.1039/c1cc12647d · Cited by 39
Site‐Selective Peptide Macrocyclization
Wills, R. D., Adebomi, V., & Raj, M. (2020) · ChemBioChem · doi:10.1002/cbic.202000398 · Cited by 39
A systematic approach to inserting split inteins for Boolean logic gate engineering and basal activity reduction
Ho, T. Y. H., Shao, A., Lu, Z. M., Savilahti, H., Menolascina, F., Wang, L., Dalchau, N., & Wang, B. (2021) · Nature Communications · doi:10.1038/s41467-021-22404-9 · Cited by 39
Ribosomal Synthesis of Natural‐Product‐Like Bicyclic Peptides in Escherichia coli
Bionda, N., & Fasan, R. (2015) · ChemBioChem · doi:10.1002/cbic.201500179 · Cited by 38
Traceless Production of Cyclic Peptide Libraries in E. coli
Townend, J., & Tavassoli, A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00095 · Cited by 38
PROTEIN SPLICING ELEMENTS AND PLANTS: From Transgene Containment to Protein Purification
Evans, T. C., Xu, M., & Pradhan, S. (2005) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.56.032604.144242 · Cited by 38
Biosynthesis of the Cyclotide Kalata B1 by Using Protein Splicing
Kimura, R. H., Tran, A., & Camarero, J. A. (2006) · Angewandte Chemie · doi:10.1002/ange.200503882 · Cited by 38
Head‐to‐Tail Cyclized Cystine‐Knot Peptides by a Combined Recombinant and Chemical Route of Synthesis
Avrutina, O., Schmoldt, H., Gabrijelcic‐Geiger, D., Wentzel, A., Frauendorf, H., Sommerhoff, C. P., Diederichsen, U., & Kolmar, H. (2007) · ChemBioChem · doi:10.1002/cbic.200700452 · Cited by 37
Chemical and Biological Production of Cyclotides
Li, Y., Bi, T., & Camarero, J. A. (2015) · Advances in botanical research · doi:10.1016/bs.abr.2015.08.006 · Cited by 36
Probing protein function by chemical modification
Wu, Y., & Goody, R. S. (2010) · Journal of Peptide Science · doi:10.1002/psc.1287 · Cited by 35
Expanding the Chemical Diversity of Genetically Encoded Libraries
Iskandar, S. E., Haberman, V. A., & Bowers, A. A. (2020) · ACS Combinatorial Science · doi:10.1021/acscombsci.0c00179 · Cited by 35
Inteins in Science: Evolution to Application
Nanda, A., Nasker, S. S., Mehra, A., Panda, S., & Nayak, S. (2020) · Microorganisms · doi:10.3390/microorganisms8122004 · Cited by 35
Cyclisation strategies for stabilising peptides with irregular conformations
Vu, Q. N., Young, R., Sudhakar, H. K., Gao, T., Huang, T., Tan, Y. S., & Lau, Y. H. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00098e · Cited by 35
Macrocyclization of Organo‐Peptide Hybrids through a Dual Bio‐orthogonal Ligation: Insights from Structure–Reactivity Studies
Frost, J. R., Vitali, F., Jacob, N. T., Brown, M. D., & Fasan, R. (2012) · ChemBioChem · doi:10.1002/cbic.201200579 · Cited by 33
Intein-Mediated Cyclization of Randomized Peptides in the Periplasm of Escherichia coli and Their Extracellular Secretion
Deschuyteneer, G., Garcia, S., Michiels, B., Baudoux, B., Degand, H., Morsomme, P., & Soumillion, P. (2010) · ACS Chemical Biology · doi:10.1021/cb100072u · Cited by 33
An efficient route to VEGF-like peptide porphyrin conjugates via microwave-assisted ‘click-chemistry’
Bakleh, M.-E., Sol, V., Estieu‐Gionnet, K., Granet, R., Déléris, G., & Krausz, P. (2009) · Tetrahedron · doi:10.1016/j.tet.2009.07.028 · Cited by 33
Emerging Strategies to Access Peptide Macrocycles from Genetically Encoded Polypeptides
Smith, J. M., Frost, J. R., & Fasan, R. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo400119s · Cited by 32
Cell-Based Assay To Identify Inhibitors of the Hfq-sRNA Regulatory Pathway
El-Mowafi, S. A., Alumasa, J. N., Ades, S. E., & Keiler, K. C. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03311-14 · Cited by 32
Synthesis of Multi-Domain Proteins Using Expressed Protein Ligation: Strategies for Segmental Isotopic Labeling of Internal Regions
Blaschke, U. K., Cotton, G., & Muir, T. W. (2000) · Tetrahedron · doi:10.1016/s0040-4020(00)00830-9 · Cited by 32
Diverse organo-peptide macrocyclesvia a fast and catalyst-free oxime/intein-mediated dual ligation
Maragani, S., Vitali, F., Frost, J. R., & Fasan, R. (2011) · Chemical Communications · doi:10.1039/c1cc13533c · Cited by 31
SpyRings Declassified
Schoene, C., Bennett, S., & Howarth, M. R. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.05.004 · Cited by 31
An integrated bacterial system for the discovery of chemical rescuers of disease-associated protein misfolding
Matis, I., Delivoria, D. C., Mavroidi, B., Papaevgeniou, N., Panoutsou, S., Bellou, S., Papavasileiou, K. D., Linardaki, Z. I., Stavropoulou, A. V., Vekrellis, K., et al. (2017) · Nature Biomedical Engineering · doi:10.1038/s41551-017-0144-3 · Cited by 32
A novel artificial loop scaffold for the noncovalent constraint of peptides
Gururaja, T. L., Shanaiah, N., Payan, D. G., & Anderson, D. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00137-x · Cited by 31
‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair
Braner, M., Kollmannsperger, A., Wieneke, R., & Tampé, R. (2015) · Chemical Science · doi:10.1039/c5sc02936h · Cited by 30
Cyclization of Single-Chain Fv Antibodies Markedly Suppressed Their Characteristic Aggregation Mediated by Inter-Chain VH-VL Interactions
Yamauchi, S., Kobashigawa, Y., Fukuda, N., Teramoto, M., Toyota, Y., Liu, C., Ikeguchi, Y., Sato, T., Sato, Y., Kimurâ, H., et al. (2019) · Molecules · doi:10.3390/molecules24142620 · Cited by 31
Protein Macrocyclization for Tertiary Structure Stabilization
Haim, A., Neubacher, S., & Grossmann, T. N. (2021) · ChemBioChem · doi:10.1002/cbic.202100111 · Cited by 30
Stabilization of a binary protein complex by intein‐mediated cyclization
Jeffries, C. M., Graham, S. C., Stokes, P. H., Collyer, C. A., Guss, J. M., & Matthews, J. M. (2006) · Protein Science · doi:10.1110/ps.062377006 · Cited by 30
Intein-mediated site-specific conjugation of Quantum Dots to proteins in vivo
Charalambous, A., Andreou, M., & Skourides, P. A. (2009) · Journal of Nanobiotechnology · doi:10.1186/1477-3155-7-9 · Cited by 30
Design and applications of cyclic peptides
Claro, B., Bastos, M., & García‐Fandiño, R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-100736-5.00004-1 · Cited by 30
Semisynthesis of Biologically Active Glycoforms of the Human Cytokine Interleukin 6
Reif, A., Siebenhaar, S., Tröster, A., Schmälzlein, M., Lechner, C. C., Velisetty, P., Gottwald, K., Pöhner, C., Boos, I., Schubert, V., et al. (2014) · Angewandte Chemie · doi:10.1002/ange.201407160 · Cited by 29
Protein trans -Splicing To Produce Herbicide-Resistant Acetolactate Synthase
Sun, L., Ghosh, I., Paulus, H., & Xu, M. (2001) · Applied and Environmental Microbiology · doi:10.1128/aem.67.3.1025-1029.2001 · Cited by 29
Use of Inteins for the In Vivo Production of Stable Cyclic Peptide Libraries in E. coli
Abel‐Santos, E., Scott, C. P., & Benkovic, S. J. (2003) · Humana Press eBooks · doi:10.1385/1-59259-301-1:281 · Cited by 29
Self-citation
The denaturation of circular enterocin AS-48 by urea and guanidinium hydrochloride
Cobos, E. S., Filimonov, V. V., Gálvez, A., Valdivia, E., Maqueda, M., Martínez, J. C., & Mateo, P. L. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s0167-4838(02)00341-2 · Cited by 29
Covalent and Noncovalent Bioconjugation Strategies
Sunasee, R., & Narain, R. (2014) · Wiley eBooks · doi:10.1002/9781118775882.ch1 · Cited by 33
Mechanism of C-terminal intein cleavage in protein splicing from QM/MM molecular dynamics simulations
Mujika, J. I., López, X., & Mulholland, A. J. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c1ob06444d · Cited by 28
Genetically Encoded Libraries of Nonstandard Peptides
Kawakami, T., & Murakami, H. (2012) · Journal of Nucleic Acids · doi:10.1155/2012/713510 · Cited by 28
Convergent protein synthesis
Casi, G. (2003) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.09.008 · Cited by 28
Cyclic Peptide Inhibitors of the β-Sliding Clamp in Staphylococcus aureus
Kjelstrup, S., Hansen, P. M. P., Thomsen, L. E., Hansen, P. B., & Løbner‐Olesen, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072273 · Cited by 28
Immobilization and Intracellular Delivery of Circular Proteins by Modifying a Genetically Incorporated Unnatural Amino Acid
Bi, X., Yin, J., Hemu, X., Rao, C., Tam, J. P., & Liu, C. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00244 · Cited by 28
Design, synthesis, and biological activity of a cyclic peptide: An inhibitor of HIV-1 tat–TAR interactions in human cells
Tamilarasu, N., Huq, I., & Rana, T. M. (2000) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(00)00140-2 · Cited by 28
Effect of Backbone Cyclization on Protein Folding Stability: Chain Entropies of both the Unfolded and the Folded States are Restricted
Zhou, H. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00886-6 · Cited by 28
Effects of the Difference in the Unfolded-state Ensemble on the Folding of Escherichia coli Dihydrofolate Reductase
Arai, M., Kataoka, M., Kuwajima, K., Matthews, C. R., & Iwakura, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00511-4 · Cited by 28
Recombinant expression of backbone‐cyclized polypeptides
Borra, R., & Camarero, J. A. (2013) · Biopolymers · doi:10.1002/bip.22306 · Cited by 27
Reprogramming the Transcriptional Response to Hypoxia with a Chromosomally Encoded Cyclic Peptide HIF-1 Inhibitor
Mistry, I. N., & Tavassoli, A. (2016) · ACS Synthetic Biology · doi:10.1021/acssynbio.6b00219 · Cited by 27
Targeting the INCENP IN-box–Aurora B interaction to inhibit CPC activity in vivo
Gohard, F. H., St‐Cyr, D. J., Tyers, M., & Earnshaw, W. C. (2014) · Open Biology · doi:10.1098/rsob.140163 · Cited by 26
Inhibition of low-density lipoprotein receptor degradation with a cyclic peptide that disrupts the homodimerization of IDOL E3 ubiquitin ligase
Leitch, E. K., Elumalai, N., Fridén-Saxin, M., Dahl, G., Wan, P., Clarkson, P., Valeur, E., Pairaudeau, G., Boyd, H., & Tavassoli, A. (2018) · Chemical Science · doi:10.1039/c8sc01186a · Cited by 25
Development of a cell-based fluorescence resonance energy transfer reporter for Bacillus anthracis lethal factor protease
Kimura, R. H., Steenblock, E. R., & Camarero, J. A. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.05.014 · Cited by 25
Phenotypic screens for compounds that target the cellular pathologies underlying Parkinson's disease
Tardiff, D. F., & Lindquist, S. L. (2012) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2012.02.003 · Cited by 25
Backbone circularization of Bacillus subtilis family 11 xylanase increases its thermostability and its resistance against aggregation
Waldhauer, M. C., Schmitz, S. N., Ahlmann-Eltze, C., Gleixner, J., Schmelas, C., Huhn, A. G., Bunne, C., Büscher, M., Horn, M., Klughammer, N., et al. (2015) · Molecular BioSystems · doi:10.1039/c5mb00341e · Cited by 25
Intein-mediated Cyclization of Bacterial Acyl Carrier Protein Stabilizes Its Folded Conformation but Does Not Abolish Function
Volkmann, G., Murphy, P. W., Rowland, E. E., Cronan, J. E., Liu, X. Q., Blouin, C., & Byers, D. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.060863 · Cited by 24
Enhancing cyclotide bioproduction: harnessing biological synthesis methods and various expression systems for large-scale manufacturing
Taghizadeh, M. S., Niazi‎, A., Mirzapour‐Kouhdasht, A., Pereira, E. C., & García‐Vaquero, M. (2024) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2024.2412780 · Cited by 23
Targeting Bacillus anthracis toxicity with a genetically selected inhibitor of the PA/CMG2 protein-protein interaction
Male, A. L., Forafonov, F., Cuda, F., Zhang, G., Zheng, S., Oyston, P. C. F., Chen, P. R., Williamson, E. D., & Tavassoli, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-03253-3 · Cited by 23
Intein-mediated cyclization of a soluble and a membrane protein in vivo: function and stability
Siebold, C., & Erni, B. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00012-1 · Cited by 23

Authors: Scott, C. P., Abel-Santos, E., Wall, M., Wahnon, D. C., & Benkovic, S. J.
Affiliations: Pennsylvania State University (US)
Department of Chemistry, Pennsylvania State University, University Park, PA 16802-6300
ORCID: Scott, Charles P.
Benkovic, Stephen J.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1999-11-23
Volume: 96
Issue: 24
Pages: 13638-13643
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.96.24.13638
PMC: PMC24117
OpenAlex: W2152458717
Cited by: 402
References: 40
Citations by year: 2026: 9 · 2025: 13 · 2024: 13 · 2023: 15 · 2022: 13 · 2021: 15 · 2020: 13 · 2019: 9 · 2018: 15 · 2017: 24 · 2016: 14 · 2015: 12 · 2014: 30 · 2013: 19 · 2012: 13
FWCI: 4.14
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: University of Pennsylvania
Pennsylvania State University
National Institutes of Health
National Institute of General Medical Sciences (GM19891-01, F32GM019891)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: split intein, cyclic peptides, dihydrofolate reductase, tyrosinase inhibitors, melanogenesis inhibition, Streptomyces antibioticus, Synechocystis sp. PCC 6803, thermal stability
MeSH terms: Bacterial Proteins, Genetic Engineering, Peptides, Cyclic, Tetrahydrofolate Dehydrogenase, Monophenol Monooxygenase

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

Production of cyclic peptides and proteins in vivo

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks