Production of cyclic peptides and proteins in vivo

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

Monitoring protein–protein interactions in intact eukaryotic cells by β-galactosidase complementation

Rossi, F. M. V., Charlton, C. A., & Blau, H. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8405 · Cited by 323

Aptamers as therapeutic and diagnostic reagents: problems and prospects

Osborne, S. E. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80102-0 · Cited by 289

Compilation and analysis of intein sequences

Perler, F. B. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1087 · Cited by 202

Genetic Selection of Peptide Inhibitors of Biological Pathways

Norman, T., Smith, D. L., Sorger, P. K., Drees, B., O’Rourke, S. M., Hughes, T. R., Roberts, C. J., Friend, S. H., Fields, S., & Murray, A. W. (1999) · Science · doi:10.1126/science.285.5427.591 · Cited by 190

Folded proteins occur frequently in libraries of random amino acid sequences.

Davidson, A. R., & Sauer, R. T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2146 · Cited by 185

The nucleotide sequence of the tyrosinase gene from Streptomyces antibioticus and characterization of the gene product

Bernan, V. S., Filpula, D. R., Herber, W. K., Bibb, M. J., & Katz, E. (1985) · Gene · doi:10.1016/0378-1119(85)90262-8 · Cited by 168

An in vivo library-versus-library selection of optimized protein–protein interactions

Pelletier, J. N., Arndt, K. M., Plückthun, A., & Michnick, S. W. (1999) · Nature Biotechnology · doi:10.1038/10897 · Cited by 168

Biosynthesis of a Head-to-Tail Cyclized Protein with Improved Biological Activity

Camarero, J. A., & Muir, T. W. (1999) · Journal of the American Chemical Society · doi:10.1021/ja990929n · Cited by 143

A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli

Dimitrova, M., Younès-Cauet, G., Oertel‐Buchheit, P., Porte, D., Granger‐Schnarr, M., & Schnarr, M. (1998) · Molecular and General Genetics MGG · doi:10.1007/s004380050640 · Cited by 139

The Cyclization and Polymerization of Bacterially Expressed Proteins Using Modified Self-splicing Inteins

Evans, T. C., Benner, J., & Xu, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18359 · Cited by 134

Combinatorial protein engineering by incremental truncation

Ostermeier, M., Nixon, A. E., Shim, J. H., & Benkovic, S. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3562 · Cited by 131

“Mutagenesis” by peptide aptamers identifies genetic network members and pathway connections

Geyer, C. R., Colman‐Lerner, A., & Brent, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8567 · Cited by 103

Encoding methods for combinatorial chemistry

Czarnik, A. W. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80109-3 · Cited by 101

Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands

Uversky, V. N., Protasova, N. Y., Rogov, V. V., Vassilenko, K. S., Gudkov, A. T., & Kutyshenko, V. P. (1996) · Protein Science · doi:10.1002/pro.5560050910 · Cited by 77

Pseudostellarins D - F, new tyrosinase inhibitory cyclic peptides from Pseudostellaria heterophylla

Morita, H., Kayashita, T., Kobata, H., Gonda, A., Takeya, K., & Itokawa, H. (1994) · Tetrahedron · doi:10.1016/s0040-4020(01)89612-5 · Cited by 76

A fully active variant of dihydrofolate reductase with a circularly permuted sequence

Buchwalder, A., Szadkowski, H., & Kirschner, K. (1992) · Biochemistry · doi:10.1021/bi00121a006 · Cited by 75

Transdominant genetic analysis of a growth control pathway

Caponigro, G., Abedi, M. R., Hurlburt, A. P., Maxfield, A. B., Judd, W., & Kamb, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7508 · Cited by 74

Melanin Production in Escherichia coli from a Cloned Tyrosinase Gene

della-Cioppa, G., Garger, S. J., Sverlow, G. G., Turpen, T. H., & Grill, L. K. (1990) · Nature Biotechnology · doi:10.1038/nbt0790-634 · Cited by 64

An arabinose-inducible expression vector, pAR3, compatible with ColE1-derived plasmids

Pérez‐Pérez, J., & Gutiérrez, J. (1995) · Gene · doi:10.1016/0378-1119(95)00127-r · Cited by 63

Deletion of a Highly Motional Residue Affects Formation of the Michaelis Complex for Escherichia coli Dihydrofolate Reductase

Miller, G. P., & Benkovic, S. J. (1998) · Biochemistry · doi:10.1021/bi972922t · Cited by 57

Synthetic Peptides Derived from the Fourth Domain of CD4 Antagonize CD4 Function and Inhibit T Cell Activation

Satoh, T. K., Li, S., Friedman, T. M., Wiaderkiewicz, R., Korngold, R., & Huang, Z. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1045 · Cited by 53

Effects of the length of a glycine linker connecting the N-and C- termini of a circularly permuted dihydrofolate reductase

Iwakura, M., & Nakamura, T. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.8.707 · Cited by 49

Inhibition of Translation and Cell Growth by Minigene Expression

Tenson, T., Herrera, J. V., Kloss, P., Guarneros, G., & Mankin, A. S. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.5.1617-1622.1999 · Cited by 46

Synthesis of Peptides as Cloned Ubiquitin Extensions

Yoo, Y., Rote, K. V., & RECHSTEINER, M. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71461-0 · Cited by 39

[23] Laser desorption mass spectrometry

Moore, W. T. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)89062-3 · Cited by 34

Genetic selection of short peptides that support protein oligomerization in vivo

Zhang, Z., Murphy, A., Hu, J. C., & Kodadek, T. J. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80188-2 · Cited by 25

Stability and Reversibility of Thermal Denaturation Are Greatly Improved by Limiting Terminal Flexibility of Escherichia coli Dihydrofolate Reductase

Iwakura, M., & Honda, S. (1996) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021257 · Cited by 24

[25] Using the lac repressor system to identify interacting proteins

Stricker, N. L., Schatz, P. J., & Li, M. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)03027-x · Cited by 5

Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality

Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165

Semisynthesis of Proteins by Expressed Protein Ligation

Muir, T. W. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161900 · Cited by 695

Gelatinase-mediated migration and invasion of cancer cells

Björklund, M., & Koivunen, E. (2005) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2005.03.001 · Cited by 668

Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome

Neumann, H., Wang, K., Davis, L., Garcia-Alai, M., & Chin, J. W. (2010) · Nature · doi:10.1038/nature08817 · Cited by 622

Understanding Cell Penetration of Cyclic Peptides

Dougherty, P. G., Sahni, A., & Pei, D. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00008 · Cited by 598

Structural requirements for the biosynthesis of backbone cyclic peptide libraries

Scott, C. P., Abel‐Santos, E., Jones, A. D., & Benkovic, S. J. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00052-7 · Cited by 101

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

Cover Feature: Mechanistic Insights into Cyclic Peptide Generation by DnaE Split‐Inteins through Quantitative and Structural Investigation (ChemBioChem 22/2017)

Kick, L. M., Harteis, S., Koch, M. F., & Schneider, S. (2017) · ChemBioChem · doi:10.1002/cbic.201700568

Split-intein mediated circular ligation used in the synthesis of cyclic peptide libraries in E. coli

Tavassoli, A., & Benkovic, S. J. (2007) · Nature Protocols · doi:10.1038/nprot.2007.152 · Cited by 174

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