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Hydrocarbon Stapled Peptides as Modulators of Biological Function
Abstract
Peptide-based drug discovery has experienced a significant upturn within the past decade since the introduction of chemical modifications and unnatural amino acids has allowed for overcoming some of the drawbacks associated with peptide therapeutics. Strengthened by such features, modified peptides become capable of occupying a niche that emerges between the two major classes of today's therapeutics-small molecules (<500 Da) and biologics (>5000 Da). Stabilized α-helices have proven particularly successful at impairing disease-relevant PPIs previously considered "undruggable." Among those, hydrocarbon stapled α-helical peptides have emerged as a novel class of potential peptide therapeutics. This review provides a comprehensive overview of the development and applications of hydrocarbon stapled peptides discussing the benefits and limitations of this technique.
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Citations
Cites
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
The phosphoinositide 3-kinase pathway
Cantley, L. C. (2002) · Science · doi:10.1126/science.296.5573.1655 · Cited by 5,621
Wnt/β-catenin signaling and disease
Clevers, H., & Nusse, R. (2012) · Cell · doi:10.1016/j.cell.2012.05.012 · Cited by 5,554
Natural products as sources of new drugs over the 30 years from 1981 to 2010
Newman, D. J., & Cragg, G. M. (2012) · Journal of Natural Products · doi:10.1021/np200906s · Cited by 4,687
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Activating Mutations of NOTCH1 in Human T Cell Acute Lymphoblastic Leukemia
Weng, A. P., Ferrando, A. A., Lee, W., Morris, J. P., Silverman, L. B., Sanchez-Irizarry, C., Blacklow, S. C., Look, A. T., & Aster, J. C. (2004) · Science · doi:10.1126/science.1102160 · Cited by 2,715
Notch signalling: a simple pathway becomes complex
Bray, S. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2009 · Cited by 2,620
Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,272
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
Cohen, S. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83739-0 · Cited by 2,193
The Future of Peptide‐based Drugs
Craik, D. J., Fairlie, D. P., Liras, S., & Price, D. (2013) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12055 · Cited by 1,979
Estrogen receptors: how do they signal and what are their targets
Heldring, N., Pike, A., Andersson, S., Matthews, J., Cheng, G., Hartman, J., Tujague, M., Ström, A., Treuter, E., Warner, M., et al. (2007) · Physiological Reviews · doi:10.1152/physrev.00026.2006 · Cited by 1,857
Wei, X., Decker, J. M., Liu, H., Zhang, Z., Arani, R. B., Kilby, J. M., Saag, M. S., Wu, X., Shaw, G. M., & Kappes, J. C. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.6.1896-1905.2002 · Cited by 1,569
Björnström, L., & Sjöberg, M. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0486 · Cited by 1,362
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065
Schafmeister, C. E., Po, J., & Verdine, G. L. (2000) · Journal of the American Chemical Society · doi:10.1021/ja000563a · Cited by 1,037
The ERBB network: at last, cancer therapy meets systems biology
Yarden, Y., & Pines, G. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3309 · Cited by 988
Kilby, J. M., Hopkins, S., Venetta, T. M., DiMassimo, B., Cloud, G. A., Lee, J. Y., Alldredge, L., Hunter, E., Lambert, D., Bolognesi, D., et al. (1998) · Nature Medicine · doi:10.1038/3293 · Cited by 987
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
Cohen, S., Carpenter, G., & King, L. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85573-4 · Cited by 858
Cell‐penetrating peptides: 20 years later, where do we stand?
Bechara, C., & Sagan, S. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.031 · Cited by 857
Hydrocarbon-Stapled Peptides: Principles, Practice, and Progress: Miniperspective
Walensky, L. D., & Bird, G. H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4011675 · Cited by 795
Direct inhibition of the NOTCH transcription factor complex
Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E. (2009) · Nature · doi:10.1038/nature08543 · Cited by 752
Future directions for peptide therapeutics development
Kaspar, A. A., & Reichert, J. M. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.05.011 · Cited by 750
eIF-4E expression and its role in malignancies and metastases
De Benedetti, A., & Graff, J. R. (2004) · Oncogene · doi:10.1038/sj.onc.1207545 · Cited by 728
Inhibition of α-helix-mediated protein–protein interactions using designed molecules
Azzarito, V., Long, K., Murphy, N. S., & Wilson, A. J. (2013) · Nature Chemistry · doi:10.1038/nchem.1568 · Cited by 727
Drugging the p53 pathway: understanding the route to clinical efficacy
Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 719
BAX activation is initiated at a novel interaction site
Gavathiotis, E., Suzuki, M., Davis, M. L., Pitter, K., Bird, G. H., Katz, S. G., Tu, H.-C., Kim, H., Cheng, E. H.-Y., Tjandra, N., et al. (2008) · Nature · doi:10.1038/nature07396 · Cited by 700
Chang, Y. S., Graves, B., Guerlavais, V., Tovar, C., Packman, K., To, K.-H., Olson, K. A., Kesavan, K., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 660
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
Jura, N., Endres, N. F., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J. (2009) · Cell · doi:10.1016/j.cell.2009.04.025 · Cited by 606
A dynamic model for replication protein A (RPA) function in DNA processing pathways
Fanning, E. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl550 · Cited by 571
Highly Efficient Synthesis of Covalently Cross-Linked Peptide Helices by Ring-Closing Metathesis
Blackwell, H. E., & Grubbs, R. H. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19981217)37:23<3281::aid-anie3281>3.0.co;2-v · Cited by 558
Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide
Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 556
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
Self-citationBCL-2 Family Proteins: Critical Checkpoints of Apoptotic Cell Death
Danial, N. N. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1598 · Cited by 433
The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
Stewart, M. L., Fire, E., Keating, A. E., & Walensky, L. D. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.391 · Cited by 418
Constraining Cyclic Peptides To Mimic Protein Structure Motifs
Hill, T. A., Shepherd, N. E., Diness, F., & Fairlie, D. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201401058 · Cited by 418
Discovery of RG7112: a small-molecule MDM2 inhibitor in clinical development
Vu, B., Wovkulich, P., Pizzolato, G., Lovey, A., Ding, Q., Jiang, N., Liu, J.-J., Zhao, C., Glenn, K., Wen, Y., et al. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml4000657 · Cited by 395
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391
Guo, Z., Mohanty, U., Noehre, J., Sawyer, T. K., Sherman, W., & Krilov, G. (2010) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2010.00951.x · Cited by 384
A Stapled BID BH3 Helix Directly Binds and Activates BAX
Walensky, L. D., Pitter, K., Morash, J., Oh, K. J., Barbuto, S., Fisher, J., Smith, E., Verdine, G. L., & Korsmeyer, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.020 · Cited by 383
Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis
Kim, Y.-W., Grossmann, T. N., & Verdine, G. L. (2011) · Nature Protocols · doi:10.1038/nprot.2011.324 · Cited by 376
Self-citationVerdine, G. L., & Walensky, L. D. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-2184 · Cited by 361
Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
Bird, G. H., Madani, N., Perry, A. F., Princiotto, A. M., Supko, J. G., He, X., Gavathiotis, E., Sodroski, J. G., & Walensky, L. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002713107 · Cited by 347
Nakase, I., Takeuchi, T., Tanaka, G., & Futaki, S. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.10.006 · Cited by 342
Targeted disruption of the EZH2–EED complex inhibits EZH2-dependent cancer
Kim, W., Bird, G. H., Neff, T., Guo, G., Kerenyi, M. A., Walensky, L. D., & Orkin, S. H. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1331 · Cited by 338
Lambert, D. M., Barney, S., Lambert, A. L., Guthrie, K., Medinas, R., Davis, D. E., Bucy, T., Erickson, J., Merutka, G., & Petteway, S. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.2186 · Cited by 336
MDM4 is a key therapeutic target in cutaneous melanoma
Gembarska, A., Luciani, F., Fedele, C., Russell, E. A., Dewaele, M., Villar, S., Zwolinska, A., Haupt, S., de Lange, J., Yip, D., et al. (2012) · Nature Medicine · doi:10.1038/nm.2863 · Cited by 327
N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptides
Doig, A. J., & Baldwin, R. L. (1995) · Protein Science · doi:10.1002/pro.5560040708 · Cited by 319
General approach to the synthesis of short .alpha.-helical peptides
Jackson, D. Y., King, D. S., Chmielewski, J., Singh, S., & Schultz, P. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00024a067 · Cited by 313
Dual role of proapoptotic BAD in insulin secretion and beta cell survival
Danial, N. N., Walensky, L. D., Zhang, C.-Y., Choi, C. S., Fisher, J. K., Molina, A. J. A., Datta, S. R., Pitter, K. L., Bird, G. H., Wikstrom, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm1717 · Cited by 307
An orthosteric inhibitor of the Ras-Sos interaction
Patgiri, A., Yadav, K. K., Arora, P. S., & Bar-Sagi, D. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.612 · Cited by 295
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 288
A Stapled p53 Helix Overcomes HDMX-Mediated Suppression of p53
Bernal, F., Wade, M., Godes, M., Davis, T. N., Whitehead, D. G., Kung, A. L., Wahl, G. M., & Walensky, L. D. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.024 · Cited by 285
Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin
Grossmann, T. N., Yeh, J. T.-H., Bowman, B. R., Chu, Q., Moellering, R. E., & Verdine, G. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208396109 · Cited by 268
Self-citationStructure of the Stapled p53 Peptide Bound to Mdm2
Baek, S., Kutchukian, P. S., Verdine, G. L., Huber, R., Holak, T. A., Lee, K. W., & Popowicz, G. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2090367 · Cited by 259
Design and Structure of Stapled Peptides Binding to Estrogen Receptors
Phillips, C., Roberts, L. R., Schade, M., Bazin, R., Bent, A., Davies, N. L., Moore, R., Pannifer, A. D., Pickford, A. R., Prior, S. H., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202946k · Cited by 247
Targeted Disruption of the BCL9/β-Catenin Complex Inhibits Oncogenic Wnt Signaling
Takada, K., Zhu, D., Bird, G. H., Sukhdeo, K., Zhao, J.-J., Mani, M., Lemieux, M., Carrasco, D. E., Ryan, J., Horst, D., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003808 · Cited by 245
Structures of peptides from α‐amino acids methylated at the α‐carbon,
Toniolo, C., Crisma, M., Formaggio, F., Valle, C., Cavicchioni, G., Precigoux, G., Aubry, A., & Kamphuis, J. (1993) · Biopolymers · doi:10.1002/bip.360330708 · Cited by 238
The Uptake of Arginine-Rich Cell-Penetrating Peptides: Putting the Puzzle Together
Brock, R. (2014) · Bioconjugate Chemistry · doi:10.1021/bc500017t · Cited by 238
EZH2: biology, disease, and structure-based drug discovery
Tan, J.-Z., Yan, Y., Wang, X.-X., Jiang, Y., & Xu, H. E. (2014) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.161 · Cited by 234
A peptide inhibitor of HIV-1 assembly in vitro
Sticht, J., Humbert, M., Findlow, S., Bodem, J., Müller, B., Dietrich, U., Werner, J., & Kräusslich, H.-G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb964 · Cited by 224
Bock, J. E., Gavenonis, J., & Kritzer, J. A. (2013) · ACS Chemical Biology · doi:10.1021/cb300515u · Cited by 221
Towards understanding cell penetration by stapled peptides
Chu, Q., Moellering, R. E., Hilinski, G. J., Kim, Y.-W., Grossmann, T. N., Yeh, J. T.-H., & Verdine, G. L. (2015) · MedChemComm · doi:10.1039/c4md00131a · Cited by 219
Self-citationA Cell-penetrating Helical Peptide as a Potential HIV-1 Inhibitor
Zhang, H., Zhao, Q., Bhattacharya, S., Waheed, A. A., Tong, X., Hong, A., Heck, S., Curreli, F., Goger, M., Cowburn, D., et al. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.066 · Cited by 215
Small-molecule modulation of Ras signaling
Spiegel, J., Cromm, P. M., Zimmermann, G., Grossmann, T. N., & Waldmann, H. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1560 · Cited by 214
Self-citationEfficient p53 Activation and Apoptosis by Simultaneous Disruption of Binding to MDM2 and MDMX
Hu, B., Gilkes, D. M., & Chen, J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1140 · Cited by 213
Stapled Peptides with Improved Potency and Specificity That Activate p53
Brown, C. J., Quah, S. T., Jong, J., Goh, A. M., Chiam, P. C., Khoo, K. H., Choong, M. L., Lee, M. A., Yurlova, L., Zolghadr, K., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb3005148 · Cited by 209
Gamma-carboxyglutamate in a neuroactive toxin.
McIntosh, J. M., Olivera, B. M., Cruz, L. J., & Gray, W. R. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42601-9 · Cited by 201
Kilby, J. M., Lalezari, J. P., Eron, J. J., Carlson, M., Cohen, C., Arduino, R. C., Goodgame, J. C., Gallant, J. E., Volberding, P., Murphy, R. L., et al. (2002) · AIDS Research and Human Retroviruses · doi:10.1089/088922202760072294 · Cited by 198
Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors as Anticancer Agents
Ciardiello, F. (2000) · Drugs · doi:10.2165/00003495-200060001-00003 · Cited by 194
The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
Huang, L., Yan, Z., Liao, X., Li, Y., Yang, J., Wang, Z.-G., Zuo, Y., Kawai, H., Shadfan, M., Ganapathy, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102309108 · Cited by 193
Bergman, L. W., Kaiser, K., Fujioka, H., Coppens, I., Daly, T. M., Fox, S., Matuschewski, K., Nussenzweig, V., & Kappe, S. H. I. (2003) · Journal of Cell Science · doi:10.1242/jcs.00194 · Cited by 189
Regulation of apicomplexan actin-based motility
Baum, J., Papenfuss, A. T., Baum, B., Speed, T. P., & Cowman, A. F. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1465 · Cited by 186
The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
Ternois, F., Sticht, J., Duquerroy, S., Kräusslich, H.-G., & Rey, F. A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb967 · Cited by 176
Comparative α‐Helicity of Cyclic Pentapeptides in Water
de Araujo, A. D., Hoang, H. N., Kok, W. M., Diness, F., Gupta, P., Hill, T. A., Driver, R. W., Price, D. A., Liras, S., & Fairlie, D. P. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310245 · Cited by 174
Stitched α-Helical Peptides via Bis Ring-Closing Metathesis
Hilinski, G. J., Kim, Y.-W., Hong, J., Kutchukian, P. S., Crenshaw, C. M., Berkovitch, S. S., Chang, A., Ham, S., & Verdine, G. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505141j · Cited by 164
NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses
Nettles, K. W., Bruning, J. B., Gil, G., Nowak, J., Sharma, S. K., Hahm, J. B., Kulp, K., Hochberg, R. B., Zhou, H., Katzenellenbogen, J. A., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.76 · Cited by 159
Kourtesi, C., Ball, A. R., Huang, Y.-Y., Jachak, S. M., Vera, D. M. A., Khondkar, P., Gibbons, S., Hamblin, M. R., & Tegos, G. P. (2013) · The Open Microbiology Journal · doi:10.2174/1874285801307010034 · Cited by 159
Thiel, K. W., & Carpenter, G. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703854104 · Cited by 158
Boersma, M., Haase, H. S., Peterson‐Kaufman, K. J., Lee, E. F., Clarke, O. B., Colman, P. M., Smith, B. J., Horne, W. S., Fairlie, W. D., & Gellman, S. H. (2011) · Journal of the American Chemical Society · doi:10.1021/ja207148m · Cited by 156
Wang, D., Chen, K., Kulp, J. L., & Arora, P. S. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062710w · Cited by 156
Systematic Mutational Analysis of Peptide Inhibition of the p53–MDM2/MDMX Interactions
Li, C. V., Pazgier, M., Li, C., Yuan, W., Liu, M., Wei, G., Lu, W., & Lu, W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.005 · Cited by 151
Cohen, N. A., Stewart, M. L., Gavathiotis, E., Tepper, J. L., Bruekner, S. R., Koss, B. S., Opferman, J. T., & Walensky, L. D. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.07.018 · Cited by 148
Čuljković, B., Topisirović, I., & Borden, K. L. B. (2007) · Cell Cycle · doi:10.4161/cc.6.1.3688 · Cited by 147
Yang, Y., Schmitz, R., Mitala, J., Whiting, A., Xiao, W., Ceribelli, M., Wright, G. W., Zhao, H., Yang, Y., Xu, W., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0915 · Cited by 146
Glas, A., Bier, D., Hahne, G., Rademacher, C., Ottmann, C., & Grossmann, T. N. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310082 · Cited by 145
Self-citationOkamoto, 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
Göttlinger, H. G. (2001) · AIDS · doi:10.1097/00002030-200100005-00003 · Cited by 136
Assessment of helical interfaces in protein–protein interactions
Jochim, A. L., & Arora, P. S. (2009) · Molecular BioSystems · doi:10.1039/b903202a · Cited by 134
Panagotopulos, S. E., Witting, S. R., Horace, E. M., Hui, D. Y., Maiorano, J. N., & Davidson, W. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207005200 · Cited by 127
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
Introduction of All-Hydrocarbon i,i+3 Staples into α-Helices via Ring-Closing Olefin Metathesis
Kim, Y., Kutchukian, P. S., & Verdine, G. L. (2010) · Organic Letters · doi:10.1021/ol1010449 · Cited by 116
Hao, Y., Wang, C., Cao, B., Hirsch, B. M., Song, J. K., Markowitz, S. D., Ewing, R. M., Sedwick, D., Liu, L., Zheng, W., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.03.021 · Cited by 110
Recent advances in helix–coil theory
Doig, A. J. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00170-9 · Cited by 106
Bracken, C., Gulyás, J., Taylor, J. W., & Baum, J. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00093a052 · Cited by 97
Distinct BimBH3 (BimSAHB) Stapled Peptides for Structural and Cellular Studies
Bird, G. H., Gavathiotis, E., LaBelle, J. L., Katz, S. G., & Walensky, L. D. (2013) · ACS Chemical Biology · doi:10.1021/cb4003305 · Cited by 97
Direct Targeting of Rab‐GTPase–Effector Interactions
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Metadata
- Authors
- Cromm, P. M., Spiegel, J., & Grossmann, T. N.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-03-31
- Volume
- 10
- Issue
- 6
- Pages
- 1362-1375
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2076083257
- Cited by
- 290
- References
- 154
- FWCI
- 14.67
- Type
- journal article
- Language
- en
- Open access
- closed
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