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

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407 · see citing works

Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function

Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816 · see citing works

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 · see citing works

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 · see citing works

Life in the balance: how BH3-only proteins induce apoptosis

Willis, S. N., & Adams, J. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.10.001 · Cited by 743 · see citing works

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 · see citing works

Structural insights into the degradation of Mcl-1 induced by BH3 domains

Czabotar, P. E., Lee, E. F., van Delft, M. F., Day, C. L., Smith, B. J., Huang, D. C. S., Fairlie, W. D., Hinds, M. G., & Colman, P. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701297104 · Cited by 449 · see citing works

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 · see citing works

Proteases Universally Recognize Beta Strands In Their Active Sites

Tyndall, J. D. A., Nall, T. A., & Fairlie, D. P. (2005) · Chemical Reviews · doi:10.1021/cr040669e · Cited by 413 · see citing works

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 · see citing works

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 · 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

New-Generation Amber United-Atom Force Field

Yang, L., Tan, C.-H., Hsieh, M., Wang, J., Duan, Y., Cieplak, P., Caldwell, J. W., Kollman, P. A., & Luo, R. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp060163v · Cited by 202 · see citing works

A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers

LaBelle, J. L., Katz, S. G., Bird, G. H., Gavathiotis, E., Stewart, M. L., Lawrence, C. E., Fisher, J. K., Godes, M., Pitter, K. L., Kung, A. L., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci46231 · Cited by 176 · see citing works

A novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradation

Lee, E. F., Czabotar, P. E., van Delft, M. F., Michalak, E. M., Boyle, M. J., Willis, S. N., Puthalakath, H., Bouillet, P., Colman, P. M., Huang, D. C. S., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708096 · Cited by 172 · see citing works

High‐Resolution Structural Characterization of a Helical α/β‐Peptide Foldamer Bound to the Anti‐Apoptotic Protein Bcl‐x L

Lee, E. F., Sadowsky, J., Smith, B. J., Czabotar, P. E., Peterson‐Kaufman, K. J., Colman, P. M., Gellman, S. H., & Fairlie, W. D. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805761 · Cited by 159 · see citing works

Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization

Dai, H., Smith, A., Meng, X. W., Schneider, P. A., Pang, Y.-P., & Kaufmann, S. H. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102027 · Cited by 159 · see citing works

Structural Plasticity Underpins Promiscuous Binding of the Prosurvival Protein A1

Smits, C., Czabotar, P. E., Hinds, M. G., & Day, C. L. (2008) · Structure · doi:10.1016/j.str.2008.02.009 · Cited by 111 · 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

Stapled peptides in the p53 pathway: Computer simulations reveal novel interactions of the staples with the target protein

Joseph, T. L., Lane, D. P., & Verma, C. S. (2010) · Cell Cycle · doi:10.4161/cc.9.22.13816 · Cited by 51 · see citing works

Synthesis and helical structure of lactam bridged BH3 peptides derived from pro-apoptotic Bcl-2 family proteins

Yang, B. S., Liu, D., & Huang, Z. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.09.101 · Cited by 43 · see citing works

Structure−Function Analysis of a Phage Display-Derived Peptide That Binds to Insulin-like Growth Factor Binding Protein 1

Skelton, N. J., Chen, Y. M., Dubree, N., Quan, C. L., Jackson, D. Y., Cochran, A. G., Zobel, K., Deshayes, K., Baca, M., Pisabarro, M. T., et al. (2001) · Biochemistry · doi:10.1021/bi0103866 · Cited by 40 · see citing works

Preorganization in biological systems: Are conformational constraints worth the energy?

Martin, S. F. (2007) · Pure and Applied Chemistry · doi:10.1351/pac200779020193 · Cited by 36 · see citing works

Chemogenomics with Protein Secondary-Structure Mimetics

Marshall, G. R., Kuster, D. J., & Che, Y. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-274-2_5 · Cited by 10 · see citing works

EGL-1 BH3 mutants reveal the importance of protein levels and target affinity for cell-killing potency

Lee, E. F., Chen, L., Yang, H. J., Colman, P. M., Huang, D. C. S., & Fairlie, W. D. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.86 · Cited by 9 · see citing works

Untitled work

(1998) · doi:10.1002/(sici)1096-987x(19981115)19:14

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219 · see citing works

Getting Across the Cell Membrane: An Overview for Small Molecules, Peptides, and Proteins

Yang, N. J., & Hinner, M. J. (2015) · Methods in Molecular Biology · doi:10.1007/978-1-4939-2272-7_3 · Cited by 826 · 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

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 723 · see citing works

Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design

Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641 · see citing works

BCL-2 proteins and apoptosis: Recent insights and unknowns

Edlich, F. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.190 · Cited by 631 · 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

Understanding Cell Penetration of Cyclic Peptides

Dougherty, P. G., Sahni, A., & Pei, D. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00008 · Cited by 581 · 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

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 · 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

Oncogenic protein interfaces: small molecules, big challenges

Nero, T. L., Morton, C. J., Holien, J. K., Wielens, J., & Parker, M. W. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3690 · Cited by 312 · see citing works

Stapled Helical Peptides Bearing Different Anchoring Residues

Li, X., Chen, S., Zhang, W., & Hu, H. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00532 · Cited by 296 · see citing works

Modulating protein–protein interactions: the potential of peptides

Nevola, L., & Giralt, E. (2014) · Chemical Communications · doi:10.1039/c4cc08565e · 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

Biophysical determinants for cellular uptake of hydrocarbon-stapled peptide helices

Bird, G. H., Mazzola, E., Opoku-Nsiah, K., Lammert, M., Godes, M., Neuberg, D. S., & Walensky, L. D. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2153 · Cited by 217 · see citing works

Functionalised staple linkages for modulating the cellular activity of stapled peptides

Lau, Y. H., de Andrade, P., Quah, S. T., Rossmann, M., Laraia, L., Sköld, N., Sum, T. J., Rowling, P. J. E., Joseph, T. L., Verma, C. S., et al. (2014) · Chemical Science · doi:10.1039/c4sc00045e · Cited by 215 · see citing works

Pore-forming proteins as drivers of membrane permeabilization in cell death pathways

Vandenabeele, P., Bultynck, G., & Savvides, S. N. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00564-w · Cited by 207 · see citing works

Pro-apoptotic complexes of BAX and BAK on the outer mitochondrial membrane

Wolf, P., Schoeniger, A., & Edlich, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119317 · Cited by 205 · see citing works

BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector ProteinsPreprint

Moldoveanu, T., & Czabotar, P. E. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036319 · Cited by 182 · 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

Phase 1 Trial of ALRN-6924, a Dual Inhibitor of MDMX and MDM2, in Patients with Solid Tumors and Lymphomas Bearing Wild-type <i>TP53</i>

Saleh, M. N., Patel, M. R., Bauer, T. M., Goel, S., Falchook, G. S., Shapiro, G. I., Chung, K. Y., Infante, J. R., Conry, R. M., Rabinowits, G., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-0715 · Cited by 159 · see citing works

The deadly landscape of pro‐apoptotic BCL ‐2 proteins in the outer mitochondrial membrane

Luna‐Vargas, M. P. A., & Chipuk, J. E. (2015) · FEBS Journal · doi:10.1111/febs.13624 · Cited by 142 · see citing works

Discovery of Sulanemadlin (ALRN-6924), the First Cell-Permeating, Stabilized α-Helical Peptide in Clinical Development

Guerlavais, V., Sawyer, T. K., Carvajal, L. A., Chang, Y. S., Graves, B. J., Ren, J.-G., Sutton, D., Olson, K. A., Packman, K. E., Darłak, K., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00623 · Cited by 145 · see citing works

Peptide-based inhibitors of protein–protein interactions: biophysical, structural and cellular consequences of introducing a constraint

Wang, H., Dawber, R. S., Zhang, P., Walko, M., Wilson, A. J., & Wang, X. (2021) · Chemical Science · doi:10.1039/d1sc00165e · Cited by 138 · see citing works

α/β-Peptide Foldamers Targeting Intracellular Protein–Protein Interactions with Activity in Living Cells

Checco, J. W., Lee, E. F., Evangelista, M., Sleebs, N., Rogers, K. L., Pettikiriarachchi, A., Kershaw, N. J., Eddinger, G. A., Belair, D. G., Wilson, J. L., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05896 · Cited by 133 · see citing works

Protein–protein interactions as druggable targets: recent technological advances

Higueruelo, A. P., Jubb, H. C., & Blundell, T. L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.05.009 · Cited by 126 · see citing works

Cell death and the mitochondria: therapeutic targeting of the BCL ‐2 family‐driven pathway

Roy, M. J., Vom, A., Czabotar, P. E., & Lessène, G. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12431 · Cited by 118 · 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

Double quick, double click reversible peptide “stapling”

Grison, C. M., Burslem, G. M., Miles, J. A., Pilsl, L. K. A., Yeo, D. J., Imani, Z., Warriner, S. L., Webb, M. E., & Wilson, A. J. (2017) · Chemical Science · doi:10.1039/c7sc01342f · Cited by 102 · see citing works

New dimension in therapeutic targeting of BCL-2 family proteins

Besbes, S., Mirshahi, M., Pocard, M. D., & Billard, C. (2015) · Oncotarget · doi:10.18632/oncotarget.3868 · Cited by 101 · see citing works

A Potent α/β-Peptide Analogue of GLP-1 with Prolonged Action in Vivo

Johnson, L. M., Barrick, S., Hager, M. V., McFedries, A., Homan, E. A., Rabaglia, M. E., Keller, M. P., Attie, A., Saghatelian, A., Bisello, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja507168t · Cited by 96 · see citing works

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 96 · see citing works

New Horizons in Therapeutic Antibody Discovery: Opportunities and Challenges versus Small-Molecule Therapeutics

Smith, A. J. (2014) · SLAS DISCOVERY · doi:10.1177/1087057114562544 · Cited by 89 · see citing works

Targeting recognition surfaces on natural proteins with peptidic foldamers

Checco, J. W., & Gellman, S. H. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.06.014 · Cited by 88 · 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

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

A Versatile Platform to Analyze Low-Affinity and Transient Protein-Protein Interactions in Living Cells in Real Time

Li, Y., Rodewald, L. W., Hoppmann, C., Wong, E. T., Lebreton, S., Šafář, P., Pátek, M., Wang, L., Wertman, K. F., & Wahl, G. M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.058 · Cited by 83 · see citing works

Discovery and optimization of peptide macrocycles

White, A. M., & Craik, D. J. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2016.1245720 · Cited by 83 · see citing works

Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase

Cromm, P. M., Spiegel, J., Küchler, P., Dietrich, L., Kriegesmann, J., Wendt, M., Goody, R. S., Waldmann, H., & Grossmann, T. N. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00386 · Cited by 82 · see citing works

Lead discovery and optimization strategies for peptide macrocycles

Bhat, A., Roberts, L. R., & Dwyer, J. J. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.07.083 · Cited by 78 · see citing works

The Structural Biology of Bcl-xL

Lee, E. F., & Fairlie, W. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092234 · Cited by 78 · see citing works

Hydrocarbon constrained peptides – understanding preorganisation and binding affinity

Miles, J. A., Yeo, D. J., Rowell, P. R., Rodriguez‐Marin, S., Pask, C. M., Warriner, S. L., Edwards, T. A., & Wilson, A. J. (2016) · Chemical Science · doi:10.1039/c5sc04048e · Cited by 75 · see citing works

Effect of Stapling Architecture on Physiochemical Properties and Cell Permeability of Stapled α‐Helical Peptides: A Comparative Study

Tian, Y., Jiang, Y., Li, J., Wang, D., Zhao, H., & Li, Z. (2017) · ChemBioChem · doi:10.1002/cbic.201700352 · Cited by 76 · see citing works

Fixierung cyclischer Peptide: Mimetika von Proteinstrukturmotiven

Hill, T. A., Shepherd, N. E., Diness, F., & Fairlie, D. P. (2014) · Angewandte Chemie · doi:10.1002/ange.201401058 · Cited by 72 · see citing works

BCL-2: Long and winding path from discovery to therapeutic target

Schenk, R. L., Strasser, A., & Dewson, G. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.100 · Cited by 72 · see citing works

Structure-dependent inhibition of the ETS-family transcription factor PU.1 by novel heterocyclic diamidines

Munde, M., Wang, S., Kumar, A., Stephens, C. E., Farahat, A. A., Boykin, D. W., Wilson, W. D., & Poon, G. M. K. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt955 · Cited by 68 · see citing works

Designing helical peptide inhibitors of protein–protein interactions

Araghi, R. R., & Keating, A. E. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.04.001 · Cited by 64 · see citing works

Structure‐Guided Rational Design of α/β‐Peptide Foldamers with High Affinity for BCL‐2 Family Prosurvival Proteins

Smith, B. J., Lee, E. F., Checco, J. W., Evangelista, M., Gellman, S. H., & Fairlie, W. D. (2013) · ChemBioChem · doi:10.1002/cbic.201300351 · Cited by 65 · see citing works

Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

Lau, Y. H., de Andrade, P., Sköld, N., McKenzie, G. J., Venkitaraman, A. R., Verma, C. S., Lane, D. P., & Spring, D. R. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00742e · Cited by 59 · see citing works

Macropinocytosis as a Key Determinant of Peptidomimetic Uptake in Cancer Cells

Yoo, D. Y., Barros, S. A., Brown, G. C., Rabot, C., Bar‐Sagi, D., & Arora, P. S. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c02109 · Cited by 58 · see citing works

Cell-Permeable Stapled Peptides Based on HIV-1 Integrase Inhibitors Derived from HIV-1 Gene Products

Nomura, W., Aikawa, H., Ohashi, N., Urano, E., Métifiot, M., Fujino, M., Maddali, K., Ozaki, T., Nozue, A., Narumi, T., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400495h · Cited by 56 · see citing works

Crystal Structures of Stapled and Hydrogen Bond Surrogate Peptides Targeting a Fully Buried Protein–Helix Interaction

Douse, C. H., Maas, S. J., Thomas, J. C., Garnett, J. A., Sun, Y., Cota, E., & Tate, E. W. (2014) · ACS Chemical Biology · doi:10.1021/cb500271c · Cited by 56 · see citing works

BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association

Dengler, M. A., Robin, A. Y., Gibson, L., Li, X., Sandow, J. J., Iyer, S., Webb, A. I., Westphal, D., Dewson, G., & Adams, J. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.040 · Cited by 56 · see citing works

Designing stapled peptides to inhibit protein‐protein interactions: An analysis of successes in a rapidly changing field

Bluntzer, M. T. J., O’Connell, J. P., BAKER, T. S., Michel, J., & Hulme, A. N. (2020) · Peptide Science · doi:10.1002/pep2.24191 · Cited by 56 · see citing works

Monosubstituted alkenyl amino acids for peptide “stapling”

Yeo, D. J., Warriner, S. L., & Wilson, A. J. (2013) · Chemical Communications · doi:10.1039/c3cc45231j · Cited by 54 · see citing works

TCTP contains a BH3-like domain, which instead of inhibiting, activates Bcl-xL

Thébault, S., Agez, M., Chi, X., Stojko, J., Cura, V., Telerman, S. B., Maillet, L., Gautier, F., Billas, I. M. L., Birck, C., et al. (2016) · Scientific Reports · doi:10.1038/srep19725 · Cited by 51 · see citing works

Ensemble Properties of Bax Determine Its Function

Robin, A. Y., Iyer, S., Birkinshaw, R. W., Sandow, J. J., Wardak, A. Z., Luo, C. S., Shi, M. X., Webb, A. I., Czabotar, P. E., Kluck, R. M., et al. (2018) · Structure · doi:10.1016/j.str.2018.07.006 · Cited by 49 · see citing works

Bh3 induced conformational changes in B cl‐ X l revealed by crystal structure and comparative analysis

Rajan, S. S., Choi, M., Baek, K., & Yoon, H. S. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24816 · Cited by 47 · see citing works

Dynamic Docking of Conformationally Constrained Macrocycles: Methods and Applications

Allen, S. E., Dokholyan, N. V., & Bowers, A. A. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00663 · Cited by 46 · see citing works

Design of Cell-Permeable Stapled Peptides as HIV-1 Integrase Inhibitors

Long, Y., Huang, S.-X., Zawahir, Z., Xu, Z.-L., Li, H., Sanchez, T. W., Zhi, Y., Houwer, S. D., Christ, F., Debyser, Z., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4006516 · Cited by 48 · see citing works

Strategies to Develop Inhibitors of Motif-Mediated Protein-Protein Interactions as Drug Leads

Corbi‐Verge, C., Garton, M., Nim, S., & Kim, P. M. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104805 · Cited by 48 · see citing works

hBfl-1/hNOXA Interaction Studies Provide New Insights on the Role of Bfl-1 in Cancer Cell Resistance and for the Design of Novel Anticancer Agents

Barile, E., Marconi, G. D., De, S. K., Baggio, C., Gambini, L., Salem, A. F., Kashyap, M. K., Castro, J. E., Kipps, T. J., & Pellecchia, M. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00962 · Cited by 47 · see citing works

Mechanistic validation of a clinical lead stapled peptide that reactivates p53 by dual HDM2 and HDMX targeting

Wachter, F., Morgan, A. M., Godes, M., Mourtada, R., Bird, G. H., & Walensky, L. D. (2016) · Oncogene · doi:10.1038/onc.2016.361 · Cited by 45 · see citing works

Rational design of stapled antimicrobial peptides

You, Y., Liu, H., Zhu, Y., & Zheng, H. (2023) · Amino Acids · doi:10.1007/s00726-023-03245-w · Cited by 45 · see citing works

Cellular Uptake and Ultrastructural Localization Underlie the Pro-apoptotic Activity of a Hydrocarbon-stapled BIM BH3 Peptide

Edwards, A., Wachter, F., Lammert, M., Huhn, A. J., Luccarelli, J., Bird, G. H., & Walensky, L. D. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00214 · Cited by 44 · see citing works

Short Antibacterial Peptides with Significantly Reduced Hemolytic Activity can be Identified by a Systematic l -to- d Exchange Scan of their Amino Acid Residues

Albada, B., Prochnow, P., Bobersky, S., Schäkermann, S., Bandow, J. E., & Metzler‐Nolte, N. (2013) · ACS Combinatorial Science · doi:10.1021/co400072q · Cited by 43 · see citing works

Stapled Vasoactive Intestinal Peptide (VIP) Derivatives Improve VPAC2Agonism and Glucose-Dependent Insulin Secretion

Giordanetto, F., Revell, J. D., Knerr, L., Hostettler, M., Paunovic, A., Priest, C., Janefeldt, A., & Gill, A. L. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml400257h · Cited by 42 · see citing works

Assessing the Efficacy of Mdm2/Mdm4-Inhibiting Stapled Peptides Using Cellular Thermal Shift Assays

Tan, B. X., Brown, C. J., Ferrer, F. J., Yuen, T. Y., Quah, S. T., Chan, B. H., Jansson, A. E., Teo, H., Nordlund, P., & Lane, D. P. (2015) · Scientific Reports · doi:10.1038/srep12116 · Cited by 40 · see citing works

BAX-Induced Apoptosis Can Be Initiated through a Conformational Selection Mechanism

Tsai, C.-J., Liu, S., Hung, C., Jhong, S.-R., Sung, T.-C., & Chiang, Y. (2014) · Structure · doi:10.1016/j.str.2014.10.016 · Cited by 40 · see citing works

Neue Modalitäten für schwierige Zielstrukturen in der Wirkstoffentwicklung

Valeur, E., Guéret, S. M., Adihou, H., Gopalakrishnan, R., Lemurell, M., Waldmann, H., Grossmann, T. N., & Plowright, A. T. (2017) · Angewandte Chemie · doi:10.1002/ange.201611914 · Cited by 40 · see citing works

A bicyclic peptide scaffold promotes phosphotyrosine mimicry and cellular uptake

Quartararo, J. S., Eshelman, M. R., Peraro, L., Yu, H., Baleja, J., Lin, Y., & Kritzer, J. A. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.09.050 · Cited by 39 · see citing works

Transcription factors and chromatin proteins as therapeutic targets in cancer

Johnston, S. J., & Carroll, J. S. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.02.002 · Cited by 39 · see citing works

Macrocyclization of an all- d linear α-helical peptide imparts cellular permeability

Kannan, S., Aronica, P. G. A., Ng, S., Lian, D. T. G., Frosi, Y., Chee, S. M. Q., Jiang, S., Yuen, T. Y., Sadruddin, A., Kaan, H. Y. K., et al. (2020) · Chemical Science · doi:10.1039/c9sc06383h · Cited by 38 · see citing works

Directed evolution of cyclic peptides for inhibition of autophagy

Gray, J. P., Uddin, M. N., Chaudhari, R. R., Sutton, M. N., Yang, H., Rask, P. J., Locke, H., Engel, B. J., Batistatou, N., Wang, J., et al. (2021) · Chemical Science · doi:10.1039/d0sc03603j · Cited by 38 · see citing works

Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides

Moreno‐Vargas, L. M., & Prada‐Gracia, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010059 · Cited by 39 · see citing works

Stapled peptides as a new technology to investigate protein–protein interactions in human platelets

Iegre, J., Ahmed, N. S., Gaynord, J. S., Wu, Y., Herlihy, K. M., Tan, Y. S., Pires, M. E. L., Jha, R., Lau, Y. H., Sore, H. F., et al. (2018) · Chemical Science · doi:10.1039/c8sc00284c · Cited by 34 · see citing works

Structural Details of BH3 Motifs and BH3-Mediated Interactions: an Updated Perspective

Sora, V., & Papaleo, E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.864874 · Cited by 32 · see citing works

Extrapyramidal side effects caused by fluphenazine decanoate in a horse

Kauffman, V. G., Soma, L. R., Divers, T. J., & Perkons, S. Z. (1989) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.1989.195.08.1128 · Cited by 32 · see citing works

Oxime Side‐Chain Cross‐Links in an α‐Helical Coiled‐Coil Protein: Structure, Thermodynamics, and Folding‐Templated Synthesis of Bicyclic Species

Haney, C. M., & Horne, W. S. (2013) · Chemistry - A European Journal · doi:10.1002/chem.201300506 · Cited by 31 · see citing works

Orthogonal functionalisation of α-helix mimetics

Barnard, A., Long, K., Yeo, D. J., Miles, J. A., Azzarito, V., Burslem, G. M., Prabhakaran, P., Edwards, T. A., & Wilson, A. J. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00915k · Cited by 30 · see citing works

Enhancing Specific Disruption of Intracellular Protein Complexes by Hydrocarbon Stapled Peptides Using Lipid Based Delivery

Thean, D., Ebo, J. S., Luxton, T., Lee, X. C., Yuen, T. Y., Ferrer, F. J., Johannes, C. W., Lane, D. P., & Brown, C. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-01712-5 · Cited by 30 · see citing works

Pharmacological Targeting of Executioner Proteins: Controlling Life and Death

Pogmore, J. P., Uehling, D., & Andrews, D. W. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02200 · Cited by 28 · see citing works

Dual-Purpose Linker for Alpha Helix Stabilization and Imaging Agent Conjugation to Glucagon-Like Peptide-1 Receptor Ligands

Zhang, L., Navaratna, T. A., Liao, J., & Thurber, G. M. (2015) · Bioconjugate Chemistry · doi:10.1021/bc500584t · Cited by 27 · see citing works

Further Insights into the Effects of Pre-organizing the BimBH3 Helix

Okamoto, T., Segal, D., Zobel, K., Fedorova, A. V., Yang, H. J., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2014) · ACS Chemical Biology · doi:10.1021/cb400638p · Cited by 27 · see citing works

Stapled Peptides: Providing the Best of Both Worlds in Drug Development

Xie, X., Gao, L., Shull, A. Y., & Teng, Y. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0102 · Cited by 27 · see citing works

Absence of a Stable Secondary Structure Is Not a Limitation for Photoswitchable Inhibitors of β-Arrestin/β-Adaptin 2 Protein-Protein Interaction

Martín‐Quirós, A., Nevola, L., Eckelt, K., Madurga, S., Gorostiza, P., & Giralt, E. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.10.022 · Cited by 21 · see citing works

Consideration of Binding Kinetics in the Design of Stapled Peptide Mimics of the Disordered Proteins Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 and Eukaryotic Translation Initiation Factor 4G

Gallagher, E. E., Song, J. M., Menon, A., Mishra, L. D., Chmiel, A. F., & Garner, A. L. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00068 · Cited by 24 · see citing works

Regulation of protein–protein interactions using stapled peptides

Jamieson, A. G., & Robertson, N. (2015) · Reports in Organic Chemistry · doi:10.2147/roc.s68161 · Cited by 23 · see citing works

Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction

Strizhak, A. V., Babii, O., Afonin, S., Bakanovich, I., Panteļejevs, T., Xu, W., Fowler, E., Eapen, R., Sharma, K., Platonov, M. O., et al. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00831a · Cited by 22 · see citing works

Rational Design of a 310‐Helical PIP‐Box Mimetic Targeting PCNA, the Human Sliding Clamp

Wegener, K. L., McGrath, A. E., Dixon, N. E., Oakley, A. J., Scanlon, D. B., Abell, A. D., & Bruning, J. B. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201801734 · Cited by 20 · see citing works

Structural and ITC Characterization of Peptide‐Protein Binding: Thermodynamic Consequences of Cyclization Constraints, a Case Study on Vascular Endothelial Growth Factor Ligands

Gaucher, J., Reille‐Seroussi, M., & Broussy, S. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202200465 · Cited by 19 · see citing works

Comparison of hydrocarbon-and lactam-bridged cyclic peptides as dimerization inhibitors of Leishmania infantum trypanothione reductase

Sánchez‐Murcia, P. A., Ruiz‐Santaquiteria, M., Toro-Londoño, M., de Lucio, H., Jiménez, M. A., Gago, F., Jiménez-Ruı́z, A., Camarasa, M., & Velázquez, S. (2015) · RSC Advances · doi:10.1039/c5ra06853c · Cited by 19 · see citing works

Discovery, X-ray structure and CPP-conjugation enabled uptake of p53/MDM2 macrocyclic peptide inhibitors

Schneider, A. F. L., Kallen, J. A., Ottl, J., Reid, P., Ripoche, S., Ruetz, S., Stachyra, T., Hintermann, S., Dumelin, C. E., Hackenberger, C. P. R., et al. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00056j · Cited by 19 · see citing works

Cyclic peptides discriminate BCL-2 and its clinical mutants from BCL-XL by engaging a single-residue discrepancy

Li, F., Liu, J.-J., Liu, C., Liu, Z., Peng, X., Huang, Y., Chen, X., Sun, X., Wang, S., Chen, W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45848-1 · Cited by 18 · see citing works

Development of recombinant protein-based nanoparticle systems for inducing tumor cell apoptosis: In vitro evaluation of their cytotoxic and apoptotic effects on cancer cells

Kaplan, Ö., Gök, M. K., Pekmez, M., Tayhan, S. E., Özgümüş, S., Gökçe, İ., & Arda, N. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.105565 · Cited by 17 · see citing works

Preparing Samples for Crystallization of Bcl-2 Family Complexes

Kvansakul, M., & Czabotar, P. E. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3581-9_16 · Cited by 17 · see citing works

Biophysical Characterization of Pro-apoptotic BimBH3 Peptides Reveals an Unexpected Capacity for Self-Association

Assafa, T. E., Nandi, S., Śmiłowicz, D., Galazzo, L., Teucher, M., Elsner, C., Pütz, S., Bleicken, S., Robin, A. Y., Westphal, D., et al. (2020) · Structure · doi:10.1016/j.str.2020.09.002 · Cited by 16 · see citing works

Small molecules targeting Mcl-1: the search for a silver bullet in cancer therapy

Nhu, D., Lessène, G., Huang, D. C. S., & Burns, C. J. (2016) · MedChemComm · doi:10.1039/c5md00582e · Cited by 16 · see citing works

Mapping the BH3 Binding Interface of Bcl-xL, Bcl-2, and Mcl-1 Using Split-Luciferase Reassembly

Campbell, S., Carlson, K. J., Buchholz, C. J., Helmers, M. R., & Ghosh, I. (2015) · Biochemistry · doi:10.1021/bi501505y · Cited by 16 · see citing works

Cellular Uptake and Ultrastructural Localization Underlie the Pro-apoptotic Activity of a Hydrocarbon-stapled BIM BH3 Peptide

Edwards, A., Wachter, F., Lammert, M., Huhn, A. J., Luccarelli, J., Bird, G. H., & Walensky, L. D. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00214 · Cited by 44 · see citing works

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 · see citing works

Molecular dynamics simulations of pro-apoptotic BH3 peptide helices in aqueous medium: relationship between helix stability and their binding affinities to the anti-apoptotic protein Bcl-XL

Lama, D., & Sankararamakrishnan, R. (2011) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-011-9428-y · Cited by 27 · 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

Amphiphilic peptides containing alternating α-aminoxy acids and α-amino acids to mimic the α-helix of bak BH3 domain and disulfide bond as covalent linkage for stabilizing 7/8 helix

Zhang, T. (2011) · doi:10.5353/th_b4786940