General approach to the synthesis of short .alpha.-helical peptides

Self-Assembly and Mineralization of Peptide-Amphiphile Nanofibers

Hartgerink, J. D., Beniash, E., & Stupp, S. I. (2001) · Science · doi:10.1126/science.1063187 · Cited by 3,607 · see citing works

β-Peptides: From Structure to Function

Cheng, R. P., Gellman, S. H., & DeGrado, W. F. (2001) · Chemical Reviews · doi:10.1021/cr000045i · Cited by 1,866 · see citing works

Hydrocarbon-Stapled Peptides: Principles, Practice, and Progress

Walensky, L. D., & Bird, G. H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4011675 · Cited by 803 · see citing works

Structure‐Based Design of Inhibitors of Protein–Protein Interactions: Mimicking Peptide Binding Epitopes

Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201412070 · Cited by 718 · see citing works

Design of Folded Peptides

Venkatraman, J., Shankaramma, S. C., & Balaram, P. (2001) · Chemical Reviews · doi:10.1021/cr000053z · Cited by 689 · see citing works

Peptide stapling techniques based on different macrocyclisation chemistries

Lau, Y. H., de Andrade, P., Wu, Y., & Spring, D. R. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00246f · Cited by 593 · see citing works

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works

Macrocycles: lessons from the distant past, recent developments, and future directions

Yudin, A. K. (2014) · Chemical Science · doi:10.1039/c4sc03089c · Cited by 497 · see citing works

New Modalities for Challenging Targets in Drug Discovery

Valeur, E., Guéret, S. M., Adihou, H., Gopalakrishnan, R., Lemurell, M., Waldmann, H., Grossmann, T. N., & Plowright, A. T. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201611914 · Cited by 382 · see citing works

Stability of alpha-helices

Creighton, T. E. (1987) · Nature · doi:10.1038/326547a0 · Cited by 354 · see citing works

Multicomponent Reaction Toolbox for Peptide Macrocyclization and Stapling

Reguera, L., & Rivera, D. G. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00744 · Cited by 341 · see citing works

Photo-control of helix content in a short peptide

Kumita, J. R., Smart, O. S., & Woolley, G. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3803 · Cited by 291 · see citing works

Hydrocarbon Stapled Peptides as Modulators of Biological Function

Cromm, P. M., Spiegel, J., & Grossmann, T. N. (2015) · ACS Chemical Biology · doi:10.1021/cb501020r · Cited by 289 · see citing works

Contemporary strategies for the stabilization of peptides in the α-helical conformation

Henchey, L. K., Jochim, A. L., & Arora, P. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.08.019 · Cited by 289 · see citing works

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

Jo, H., Meinhardt, N., Wu, Y., Kulkarni, S., Hu, X., Low, K. E., Davies, P. L., DeGrado, W. F., & Greenbaum, D. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307599z · Cited by 261 · see citing works

Strategies for Improving Peptide Stability and Delivery

Musaimi, O. A., Lombardi, L., Williams, D. R., & Alberício, F. (2022) · Pharmaceuticals · doi:10.3390/ph15101283 · Cited by 263 · see citing works

BCL-2 in the crosshairs: tipping the balance of life and death

Walensky, L. D. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401992 · Cited by 245 · see citing works

Theory of Circular Dichroism of Proteins

Woody, R. W. (1996) · Springer eBooks · doi:10.1007/978-1-4757-2508-7_2 · Cited by 242 · see citing works

Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor–coactivator interactions

Leduc, A.-M., Trent, J. O., Wittliff, J. L., Bramlett, K. S., Briggs, S. L., Chirgadze, N. Y., Wang, Y., Burris, T. P., & Spatola, A. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934759100 · Cited by 222 · see citing works

Non-standard amino acids in peptide design and protein engineering

Balaram, P. (1992) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(92)90110-s · Cited by 200 · see citing works

The synthesis and study of side‐chain lactam‐bridged peptides

Taylor, J. W. (2002) · Biopolymers · doi:10.1002/bip.10203 · Cited by 191 · see citing works

Conformationally restricted amino acids and dipeptides, (non)peptidomimetics and secondary structure mimetics

Liskamp, R. M. J. (1994) · Recueil des Travaux Chimiques des Pays-Bas · doi:10.1002/recl.19941130102 · Cited by 189 · see citing works

Acetone‐Linked Peptides: A Convergent Approach for Peptide Macrocyclization and Labeling

Assem, N., Ferreira, D. J., Wolan, D. W., & Dawson, P. E. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502607 · Cited by 181 · see citing works

Stapled Peptides Inhibitors: A New Window for Target Drug Discovery

Ali, A. M., Atmaj, J., Oosterwijk, N. V., Groves, M. R., & Dömling, A. S. S. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.01.012 · Cited by 177 · see citing works

Forming stable helical peptides using natural and artificial amino acids

Andrews, M. J. I., & Tabor, A. B. (1999) · Tetrahedron · doi:10.1016/s0040-4020(99)00678-x · Cited by 169 · see citing works

Using an Azobenzene Cross-Linker to Either Increase or Decrease Peptide Helix Content upon Trans-to-Cis Photoisomerization

Flint, D. G., Kumita, J. R., Smart, O. S., et al. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00109-6 · Cited by 167 · see citing works

Stitched α-Helical Peptides via Bis Ring-Closing Metathesis

Hilinski, G. J., Kim, Y., Hong, J., Kutchukian, P. S., Nartey, C. M., Berkovitch, S. S., Chang, A. T., Ham, S., & Verdine, G. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505141j · Cited by 163 · see citing works

A gold mine for drug discovery: Strategies to develop cyclic peptides into therapies

Jing, X., & Jin, K. (2019) · Medicinal Research Reviews · doi:10.1002/med.21639 · Cited by 162 · see citing works

Synthetic Peptides as Protein Mimics

Groß, A., Hashimoto, C., Sticht, H., & Eichler, J. (2016) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2015.00211 · Cited by 154 · see citing works

Universal Peptidomimetics

Ko, E., Liu, J., Pérez, L. M., Lu, G., Schaefer, A., & Burgess, K. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1071916 · Cited by 151 · see citing works

An In‐tether Chiral Center Modulates the Helicity, Cell Permeability, and Target Binding Affinity of a Peptide

Hu, K., Geng, H. R., Zhang, Q., Liu, Q., Xie, M., Sun, C., Li, W., Lin, H., Jiang, F., Wang, T., et al. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201602806 · Cited by 141 · see citing works

Urethane-protected α-amino acid N-carboxyanhydrides and peptide synthesis

Fuller, W. D., Goodman, M., Naider, F. R., & Zhu, Y. (1996) · Biopolymers · doi:10.1002/(sici)1097-0282(1996)40:2 · Cited by 40 · see citing works

Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity

Okamoto, T., Zobel, K., Fedorova, A., Quan, C., Yang, H., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2013) · ACS Chemical Biology · doi:10.1021/cb3005403 · Cited by 136 · see citing works

Antibacterial activity of 15‐residue lactoferricin derivatives

Strøm, M. B., Svendsen, J. S. M., & Rekdal, Ø. (2000) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2000.00770.x · Cited by 135 · see citing works

Nitrogen Arylation for Macrocyclization of Unprotected Peptides

Lautrette, G., Touti, F., Lee, H. G., Dai, P., & Pentelute, B. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03757 · Cited by 131 · see citing works

Design and synthesis of α-helical peptides and mimetics

Garner, J., & Harding, M. M. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b710425a · Cited by 126 · see citing works

Stability of alpha-helices.

Chakrabartty, A., & Baldwin, R. L. (1995) · PubMed · Cited by 122 · see citing works

All-Atom Model for Stabilization of α-Helical Structure in Peptides by Hydrocarbon Staples

Kutchukian, P. S., Yang, J. S., Verdine, G. L., & Shakhnovich, E. I. (2009) · Journal of the American Chemical Society · doi:10.1021/ja805037p · Cited by 120 · see citing works

α-Helix mimetics: Outwards and upwards

Jayatunga, M. K. P., Thompson, S., & Hamilton, A. D. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.12.003 · Cited by 117 · see citing works

Stapled peptide design: principles and roles of computation

Tan, Y. S., Lane, D. P., & Verma, C. S. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.06.012 · Cited by 111 · see citing works

Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition

Madden, M. M., Muppidi, A., Li, Z., Li, X., Chen, J., & Lin, Q. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.004 · Cited by 104 · see citing works

Minimalist and universal peptidomimetics

Ko, E., Liu, J., & Burgess, K. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00218f · Cited by 99 · see citing works

Molecular determinants of the aggregation behavior of α‐ and β‐synuclein

Rivers, R. C., Kumita, J. R., Tartaglia, G. G., Dedmon, M. M., Pawar, A. P., Vendruscolo, M., Dobson, C. M., & Christodoulou, J. C. (2008) · Protein Science · doi:10.1110/ps.073181508 · Cited by 93 · see citing works

Chapter 22 Synthesis and Biophysical Characterization of Stabilized α‐Helices of BCL‐2 Domains

Bird, G. H., Bernal, F., Pitter, K. L., & Walensky, L. D. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01622-4 · Cited by 95 · see citing works

Peptide Scanning for Studying Structure‐Activity Relationships in Drug Discovery

Jamieson, A. G., Boutard, N., Sabatino, D. A., & Lubell, W. D. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12042 · Cited by 95 · see citing works

Strukturbasierte Entwicklung von Protein‐Protein‐Interaktionsinhibitoren: Stabilisierung und Nachahmung von Peptidliganden

Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie · doi:10.1002/ange.201412070 · Cited by 90 · see citing works

Stabilization of Helical Domains in Short Peptides Using Hydrophobic Interactions

Albert, J. S., & Hamilton, A. D. (1995) · Biochemistry · doi:10.1021/bi00003a033 · Cited by 90 · see citing works

Covalent Capture: Merging Covalent and Noncovalent Synthesis

Prins, L. J., & Scrimin, P. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200803583 · Cited by 89 · see citing works

α-Helix nucleation by a calcium-binding peptide loop

Siedlecka, M., Goch, G., Ejchart, A., Sticht, H., & Bierzyński, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.903 · Cited by 89 · see citing works

Fit To Be Tied: Conformation-Directed Macrocyclization of Peptoid Foldamers

Holub, J. M., Jang, H., & Kirshenbaum, K. (2007) · Organic Letters · doi:10.1021/ol071169l · Cited by 88 · see citing works

Nanostrukturen und Topologien von Nucleinsäuren

Seeman, N. C. (1998) · Angewandte Chemie · doi:10.1002/(sici)1521-3757(19981204)110:23 · Cited by 98 · see citing works

Achieving cell penetration with distance-matching cysteine cross-linkers: a facile route to cell-permeable peptide dual inhibitors of Mdm2/Mdmx

Muppidi, A., Wang, Z., Li, X., Chen, J., & Lin, Q. (2011) · Chemical Communications · doi:10.1039/c1cc13320a · Cited by 87 · see citing works

Phage Selection of Chemically Stabilized α-Helical Peptide Ligands

Diderich, P., Bertoldo, D., Dessen, P., Maola, K. M. G., Pizzitola, I., Held, W., Huelsken, J., & Heinis, C. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00963 · Cited by 87 · see citing works

Novel Amphiphilic α-Helix Mimetics Based on a Bis-benzamide Scaffold

Marimganti, S., Cheemala, M. N., & Ahn, J. (2009) · Organic Letters · doi:10.1021/ol901785v · Cited by 86 · see citing works

α-Turn Mimetics: Short Peptide α-Helices Composed of Cyclic Metallopentapeptide Modules

Kelso, M. J., Beyer, R. L., Hoang, H. N., Lakdawala, A. S., Snyder, J. P., Oliver, W., Robertson, T. A., Appleton, T. G., & Fairlie, D. P. (2004) · Journal of the American Chemical Society · doi:10.1021/ja037980i · Cited by 85 · see citing works

Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links

Haney, C. M., Loch, M. T., & Horne, W. S. (2011) · Chemical Communications · doi:10.1039/c1cc12010g · Cited by 84 · see citing works

A two-component 'double-click' approach to peptide stapling

Lau, Y. H., Wu, Y., de Andrade, P., Galloway, W. R. J. D., & Spring, D. R. (2015) · Nature Protocols · doi:10.1038/nprot.2015.033 · Cited by 84 · see citing works

Macrocyclic Control in Helix Mimetics

Guarracino, D. A., Riordan, J. A., Barreto, G. M., Oldfield, A. L., Kouba, C. M., & Agrinsoni, D. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00623 · Cited by 86 · see citing works

Photo-induced radical thiol–ene chemistry: a versatile toolbox for peptide-based drug design

Ahangarpour, M., Kavianinia, I., Harris, P. W. R., & Brimble, M. A. (2021) · Chemical Society Reviews · doi:10.1039/d0cs00354a · Cited by 84 · see citing works

Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides

Zou, Y., Spokoyny, A. M., Zhang, C., Simon, M. D., Yu, H., Lin, Y., & Pentelute, B. L. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob42168f · Cited by 85 · see citing works

Bioconjugation – using selective chemistry to enhance the properties of proteins and peptides as therapeutics and carriers

Gunnoo, S. B., & Madder, A. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00808a · Cited by 77 · see citing works

Facile synthesis of stapled, structurally reinforced peptide helices via a photoinduced intramolecular 1,3-dipolar cycloaddition reaction

Madden, M. M., Vera, C. I. R., Song, W., & Lin, Q. (2009) · Chemical Communications · doi:10.1039/b912094g · Cited by 77 · see citing works

The development of peptide nanostructures

Voyer, N. (1996) · Topics in current chemistry · doi:10.1007/3-540-61388-9_61 · Cited by 75 · see citing works

Facile and E-Selective Intramolecular Ring-Closing Metathesis Reactions in 310-Helical Peptides: A 3D Structural Study

Boal, A. K., Guryanov, I., Moretto, A., Crisma, M., Lanni, E. L., Toniolo, C., Grubbs, R. H., & O’Leary, D. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja071148m · Cited by 74 · see citing works

Folding a De Novo Designed Peptide into an α‐Helix through Hydrophobic Binding by a Bowl‐Shaped Host

Tashiro, S., Tominaga, M., Yamaguchi, Y., et al. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200502802 · Cited by 73 · see citing works

Stabilized helical peptides: overview of the technologies and therapeutic promises

Estieu‐Gionnet, K., & Guichard, G. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.603723 · Cited by 71 · see citing works

Consecutive Cyclic Pentapeptide Modules Form Short α‐Helices that are Very Stable to Water and Denaturants

Shepherd, N. E., Abbenante, G., & Fairlie, D. P. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200352659 · Cited by 71 · see citing works

Engineering a long-acting, potent GLP-1 analog for microstructure-based transdermal delivery

Yang, P., Zou, H., Chao, E., Sherwood, L., Núñez, V., Keeney, M., Ghartey-Tagoe, E. B., Ding, Z., Quirino, H., Luo, X., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601653113 · Cited by 69 · see citing works

Stapled, Long-Acting Glucagon-like Peptide 2 Analog with Efficacy in Dextran Sodium Sulfate Induced Mouse Colitis Models

Yang, P., Zou, H., Lee, C., Muppidi, A., Chao, E., Fu, Q., Luo, X., Wang, D., Schultz, P. G., & Shen, W. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00768 · Cited by 68 · see citing works

Solid-phase synthesis of short α-helices stabilized by the hydrogen bond surrogate approach

Patgiri, A., Menzenski, M. Z., Mahon, A. B., & Arora, P. S. (2010) · Nature Protocols · doi:10.1038/nprot.2010.146 · Cited by 68 · see citing works

Parallel β-Sheet Secondary Structure Is Stabilized and Terminated by Interstrand Disulfide Cross-Linking

Almeida, A. M., Li, R., & Gellman, S. H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja208856c · Cited by 66 · see citing works

Development of small molecules designed to modulate protein–protein interactions

Che, Y., Brooks, B. R., & Marshall, G. R. (2006) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-006-9040-8 · Cited by 66 · see citing works

Selective Dynamic Assembly of Disulfide Macrocyclic Helical Foldamers with Remote Communication of Handedness

Tsiamantas, C., de Hatten, X., Douat, C., et al. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601156 · Cited by 66 · see citing works

Facile synthesis of benzamides to mimic an α-helix

Ahn, J., & Han, S.-Y. (2007) · Tetrahedron Letters · doi:10.1016/j.tetlet.2007.03.108 · Cited by 65 · see citing works

Bent into shape: Folded peptides to mimic protein structure and modulate protein function

Merritt, H. I., Sawyer, N., & Arora, P. S. (2020) · Peptide Science · doi:10.1002/pep2.24145 · Cited by 65 · see citing works

Curvature Engineering: Positive Membrane Curvature Induced by Epsin N-Terminal Peptide Boosts Internalization of Octaarginine

Pujals, S., Miyamae, H., Afonin, S., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb4002987 · Cited by 63 · see citing works

Stapling of a 310-Helix with Click Chemistry

Jacobsen, Ø., Maekawa, H., Ge, N., Görbitz, C. H., Rongved, P., Ottersen, O. P., Amiry-Moghaddam, M. R., & Klaveness, J. (2011) · The Journal of Organic Chemistry · doi:10.1021/jo101670a · Cited by 62 · see citing works

Understanding base‐assisted desulfurization using a variety of disulfide‐bridged peptides

Galande, A. K., Trent, J. O., & Spatola, A. F. (2003) · Biopolymers · doi:10.1002/bip.10532 · Cited by 62 · see citing works

Non-standard amino acids in peptide design and protein engineering

Balaram, P. (1992) · Current Biology · doi:10.1016/0960-9822(92)90104-i · Cited by 62 · see citing works

Conformational Restriction via Cyclization in β-Amyloid Peptide Aβ(1-28) Leads to an Inhibitor of Aβ(1-28) Amyloidogenesis and Cytotoxicity

Kapurniotu, A., Buck, A. K., Weber, M., Schmauder, A., Hirsch, T., Bernhagen, J., & Tatarek‐Nossol, M. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00022-x · Cited by 59 · see citing works

Template-constrained macrocyclic peptides prepared from native, unprotected precursors

Lawson, K. V., Rose, T. E., & Harran, P. G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311706110 · Cited by 60 · see citing works

Helix Stabilization of Poly(ethylene glycol)–Peptide Conjugates

Jain, A. K., & Ashbaugh, H. S. (2011) · Biomacromolecules · doi:10.1021/bm2005017 · Cited by 60 · see citing works

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 62 · see citing works

The improvement effect of L ‐Lys as a chemical chaperone on STZ‐induced diabetic rats, protein structure and function

Jafarnejad, A., Bathaie, S. Z., Nakhjavani, M., Hassan, M., & Banasadegh, S. (2007) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.769 · Cited by 58 · see citing works

Reversible stapling of unprotected peptides via chemoselective methionine bis-alkylation/dealkylation

Shi, X., Zhao, R., Jiang, Y., Zhao, H., Tian, Y., Jiang, Y., Li, J., Qin, W., Yin, F., & Li, Z. (2018) · Chemical Science · doi:10.1039/c7sc05109c · Cited by 60 · see citing works

The effect of cold atmospheric plasma on diabetes-induced enzyme glycation, oxidative stress, and inflammation; in vitro and in vivo

Rezaeinezhad, A., Eslami, P., Mirmiranpour, H., & Ghomi, H. (2019) · Scientific Reports · doi:10.1038/s41598-019-56459-y · Cited by 58 · see citing works

Unfolding of an α‐helix in peptide crystals by solvation: Conformational fragility in a heptapeptide

Karle, I. L., Flippen-Anderson, J. L., Uma, K., et al. (1993) · Biopolymers · doi:10.1002/bip.360330511 · Cited by 58 · see citing works

Does Adsorption at Hydroxyapatite Surfaces Induce Peptide Folding? Insights from Large-Scale B3LYP Calculations

Rimola, A., Aschi, M., Orlando, R., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302262y · Cited by 57 · see citing works

Biphenyls as potential mimetics of protein α-helix

Jacoby, E. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00031-8 · Cited by 56 · see citing works

Enantioselective epoxidation of α,β-unsaturated ketones catalyzed by stapled helical l-Leu-based peptides

Demizu, Y., Yamagata, N., Nagoya, S., et al. (2011) · Tetrahedron · doi:10.1016/j.tet.2011.06.075 · Cited by 55 · see citing works

Helix induction by dirhodium: access to biocompatible metallopeptides with defined secondary structure.

深谷, 妙., Popp, B. V., & Ball, Z. T. (2010) · PubMed · doi:10.1002/chem.200903092

Covalent capture: a natural complement to self-assembly

Hartgerink, J. D. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.10.001 · Cited by 52 · see citing works

Application of the All-Hydrocarbon Stapling Technique in the Design of Membrane-Active Peptides

Xuan, H. L., Phuong, H. B. T., & Tùng, T. T. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01744 · Cited by 52 · see citing works

Increased antibacterial activity of 15‐residue murine lactoferricin derivatives

Strøm, M. B., Stensen, W., Svendsen, J. S. M., & Rekdal, Ø. (2001) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2001.00806.x · Cited by 50 · see citing works

Design of potent and proteolytically stable oxyntomodulin analogs

Muppidi, A., Zou, H., Yang, P. Y., Chao, E., Sherwood, L., Nunez, V., Woods, A. K., Schultz, P. G., Lin, Q., & Shen, W. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00787 · Cited by 44 · see citing works

Parallel β-sheet conformation in macrocycles

Wagner, G., & Feigel, M. (1993) · Tetrahedron · doi:10.1016/s0040-4020(01)80237-4 · Cited by 47 · see citing works

Bis‐Azobenzene Crosslinkers for Photocontrol of Peptide Structure

Samanta, S., & Woolley, G. A. (2011) · ChemBioChem · doi:10.1002/cbic.201100204 · Cited by 46 · see citing works

Inducing α-Helices in Short Oligopeptides through Binding by an Artificial Hydrophobic Cavity

Dolain, C., Hatakeyama, Y., Sawada, T., Tashiro, S., & Fujita, M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100585w · Cited by 45 · see citing works

Reversible α-helix formation controlled by a hydrogen bond surrogate

Miller, S. E., Kallenbach, N. R., & Arora, P. S. (2011) · Tetrahedron · doi:10.1016/j.tet.2011.12.068 · Cited by 45 · see citing works

Precisely Regulated and Efficient Locking of Linear Peptides into Stable Multicyclic Topologies through a One‐Pot Reaction

Liu, W., Zheng, Y., Kong, X., Heinis, C., Zhao, Y., & Wu, C. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201610942 · Cited by 46 · see citing works

Susquehanna Chorale Spring Concert "Roots and Wings"

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