Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

Cell Death

Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651

Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626

In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse

Schwarze, S. R., Ho, A. L., Vocero-Akbani, A. M., & Dowdy, S. F. (1999) · Science · doi:10.1126/science.285.5433.1569 · Cited by 2,418

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

The third helix of the Antennapedia homeodomain translocates through biological membranes.

Derossi, D., Joliot, A., Chassaing, G., & Prochiantz, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34080-2 · Cited by 2,034

Involvement of the bcl -2 Gene in Human Follicular Lymphoma

Tsujimoto, Y., Cossman, J., Jaffe, E. S., & Croce, C. M. (1985) · Science · doi:10.1126/science.3874430 · Cited by 1,787

Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis

Wadia, J. S., Stan, R. V., & Dowdy, S. F. (2004) · Nature Medicine · doi:10.1038/nm996 · Cited by 1,647

Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science · doi:10.1126/science.275.5302.983 · Cited by 1,476

X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

Muchmore, S. W., Sattler, M., Liang, H., Meadows, R. P., Harlan, J. E., Yoon, H. S., Nettesheim, D. G., Chang, B. S., Thompson, C. B., Wong, S., et al. (1996) · Nature · doi:10.1038/381335a0 · Cited by 1,467

Inhibition of p53 inhibitors: progress, challenges and perspectives

Sanz, G., Singh, M., Peuget, S., & Selivanova, G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz075 · Cited by 140

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

Targeting intracellular protein–protein interactions with cell-permeable cyclic peptides

Qian, Z., Dougherty, P. G., & Pei, D. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.03.011 · Cited by 138

Determinants of BH3 Binding Specificity for Mcl-1 versus Bcl-xL

Dutta, S., Gullà, S. V., Chen, T. S., Fire, E., Grant, R. A., & Keating, A. E. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.058 · Cited by 139

Asymmetric triplex metallohelices with high and selective activity against cancer cells

Faulkner, A. D., Kaner, R. A., Abdallah, Q., Clarkson, G. J., Fox, D. J., Gurnani, P., Howson, S. E., Phillips, R. M., Roper, D. I., Simpson, D. H., et al. (2014) · Nature Chemistry · doi:10.1038/nchem.2024 · Cited by 136

Morphoregulation of avian beaks: Comparative mapping of growth zone activities and morphological evolution

Wu, P., Jiang, T., Shen, J., Widelitz, R. B., & Chuong, C. (2006) · Developmental Dynamics · doi:10.1002/dvdy.20825 · Cited by 135

Role and potential for therapeutic targeting of MYB in leukemia

Pattabiraman, D. R., & Gonda, T. J. (2012) · Leukemia · doi:10.1038/leu.2012.225 · Cited by 138

HtrA Serine Proteases as Potential Therapeutic Targets in Cancer

CHIEN, J. R., Campioni, M., Shridhar, V., & Baldi, A. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909788486704 · Cited by 135

A Thiol–Ene Coupling Approach to Native Peptide Stapling and Macrocyclization

Wang, Y., & Chou, D. H. (2015) · Angewandte Chemie · doi:10.1002/ange.201503975 · Cited by 134

Pharmacological manipulation of Bcl-2 family members to control cell death

Letai, A. G. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26250 · Cited by 134

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 137

Strained Cyclic Disulfides Enable Cellular Uptake by Reacting with the Transferrin Receptor

Abegg, D., Gasparini, G. M., Hoch, D. G., Shuster, A., Bartolami, E., Matile, S., & Adibekian, A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09643 · Cited by 134

Peptoid Macrocycles: Making the Rounds with Peptidomimetic Oligomers

Yoo, B., Shin, S. B. Y., Huang, M. L., & Kirshenbaum, K. (2010) · Chemistry - A European Journal · doi:10.1002/chem.200903549 · Cited by 136

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 133

Structural Basis of Enhanced Binding of Extended and Helically Constrained Peptide Epitopes of the Broadly Neutralizing HIV-1 Antibody 4E10

Cardoso, R. M. F., Brunel, F. M., Ferguson, S., Zwick, M. B., Burton, D. R., Dawson, P. E., & Wilson, I. A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.088 · Cited by 131

Protein surface recognition and proteomimetics: mimics of protein surface structure and function

Fletcher, S., & Hamilton, A. D. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.10.006 · Cited by 129

Bridged β3-Peptide Inhibitors of p53-hDM2 Complexation: Correlation between Affinity and Cell Permeability

Bautista, A. D., Appelbaum, J., Craig, C. J., Michel, J., & Schepartz, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910715u · Cited by 130

Ablation of oncogenic ALK is a viable therapeutic approach for anaplastic large-cell lymphomas

Piva, R., Chiarle, R., Manazza, A. D., Taulli, R., Simmons, W. R., Ambrogio, C., d’Escamard, V., Pellegrino, E., Ponzetto, C., Palestro, G., et al. (2005) · Blood · doi:10.1182/blood-2005-05-2125 · Cited by 128

Turning off Transcription of the bcl-2 Gene by Stabilizing the bcl-2 Promoter Quadruplex with Quindoline Derivatives

Wang, X., Ou, T., Lu, Y., Zeng, L. Q., Zheng, X., Chen, X., Tan, J., Huang, S., An, L., Li, D., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100445e · Cited by 127

Double Strain‐Promoted Macrocyclization for the Rapid Selection of Cell‐Active Stapled Peptides

Lau, Y. H., Wu, Y., Rossmann, M., Tan, B. X., de Andrade, P., Tan, Y. S., Verma, C. S., McKenzie, G. J., Venkitaraman, A. R., Hyvönen, M., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508416 · Cited by 128

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 131

Novel Pyrrolopyrimidine-Based α-Helix Mimetics: Cell-Permeable Inhibitors of Protein−Protein Interactions

Lee, J. H., Zhang, Q., Jo, S., Chai, S. C., Oh, M., Im, W., Lu, H., & Lim, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108230s · Cited by 126

A new HDL mimetic peptide that stimulates cellular cholesterol efflux with high efficiency greatly reduces atherosclerosis in mice

Bielicki, J. K., Zhang, H., Cortez, Y., Zheng, Y. Y., Narayanaswami, V., Patel, A., Johansson, J., & Azhar, S. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m003665 · Cited by 126

Design and synthesis of α-helical peptides and mimetics

Garner, J., & Harding, M. M. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b710425a · Cited by 129

Mitochondria as targets for chemotherapy

Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0323-0 · Cited by 127

Targeted Radionuclide Therapy - An Overview

Dash, A. K., Knapp, F. F., & Pillai, M. (2013) · Current Radiopharmaceuticals · doi:10.2174/18744710113066660023 · Cited by 133

Protein–protein interactions as targets for small-molecule therapeutics in cancer

White, A. W., Westwell, A. D., & Brahemi, G. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399408000641 · Cited by 122

Targeted induction of apoptosis for cancer therapy: current progress and prospects

Bremer, E., van Dam, G., Kroesen, B. J., de Leij, L., & Helfrich, W. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.06.002 · Cited by 121

Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not ‘Diffusion-Limited’

Rogers, J. M., Steward, A., & Clarke, J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja309527h · Cited by 126

Histidine–Iridium(III) Coordination-Based Peptide Luminogenic Cyclization and Cyclo-RGD Peptides for Cancer-Cell Targeting

Ma, X., Jia, J., Cao, R., Wang, X., & Hao, F. (2014) · Journal of the American Chemical Society · doi:10.1021/ja511656q · Cited by 120

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

Influenza A Virus Entry Inhibitors Targeting the Hemagglutinin

Yang, J. W., Li, M., Shen, X., & Liu, S. (2013) · Viruses · doi:10.3390/v5010352 · Cited by 119

Non‐peptidic small molecule inhibitors against Bcl‐2 for cancer therapy

Azmi, A. S., & Mohammad, R. M. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21567 · Cited by 119

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 124

Fluorescence Correlation Spectroscopy Reveals Highly Efficient Cytosolic Delivery of Certain Penta-Arg Proteins and Stapled Peptides

LaRochelle, J. R., Cobb, G., Steinauer, A., Rhoades, E. R., & Schepartz, A. (2015) · Journal of the American Chemical Society · doi:10.1021/ja510391n · Cited by 124

“Doubly Orthogonal” Labeling of Peptides and Proteins

Tessier, R., Ceballos, J., Guidotti, N., Simonet‐Davin, R., Fierz, B., & Waser, J. (2019) · Chem · doi:10.1016/j.chempr.2019.06.022 · Cited by 118

Targeting BCL2-Proteins for the Treatment of Solid Tumours

Vogler, M. (2014) · Advances in Medicine · doi:10.1155/2014/943648 · Cited by 121

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 122

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

A Left‐Handed Solution to Peptide Inhibition of the p53–MDM2 Interaction

Liu, M., Pazgier, M., Li, C., Yuan, W., Li, C., & Lu, W. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000329 · Cited by 115

MOrPH-PhD: An Integrated Phage Display Platform for the Discovery of Functional Genetically Encoded Peptide Macrocycles

Owens, A. E., Iannuzzelli, J. A., Gu, Y., & Fasan, R. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b00927 · Cited by 116

Targeting Apoptotic Pathways in Cancer Cells

Denicourt, C., & Dowdy, S. F. (2004) · Science · doi:10.1126/science.1102974 · Cited by 114

Regulators of apoptosis: suitable targets for immune therapy of cancer

Andersen, M. H., Becker, J. C., & Straten, P. T. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1717 · Cited by 114

Identification of Anticancer Peptides from Bovine Milk Proteins and Their Potential Roles in Management of Cancer: A Critical Review

Sah, B. N. P., Vasiljevic, T., McKechnie, S., & Donkor, O. N. (2015) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12126 · Cited by 114

Divergent unprotected peptide macrocyclisation by palladium-mediated cysteine arylation

Rojas, A. J., Zhang, C., Vinogradova, E. V., Buchwald, N. H., Reilly, J., Pentelute, B. L., & Buchwald, S. L. (2017) · Chemical Science · doi:10.1039/c6sc05454d · Cited by 112

Using Peptidomimetics and Constrained Peptides as Valuable Tools for Inhibiting Protein–Protein Interactions

Robertson, N., & Spring, D. R. (2018) · Molecules · doi:10.3390/molecules23040959 · Cited by 116

Targeting BCL‐2 family proteins to overcome drug resistance in non‐small cell lung cancer

Wesarg, E., Hoffarth, S., Wiewrodt, R. G., Kröll, M., Biesterfeld, S., Huber, C., & Schüler, M. (2007) · International Journal of Cancer · doi:10.1002/ijc.22977 · Cited by 112

Targeting Multiple Arms of the Apoptotic Regulatory Machinery

Dai, Y., & Grant, S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0082 · Cited by 112

New Frontiers in Druggability

Kozakov, D., Hall, D. R., Napoleon, R. L., Yueh, C., Whitty, A., & Vajda, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00586 · Cited by 111

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 113

ER Stress Signaling and the BCL-2 Family of Proteins: From Adaptation to Irreversible Cellular Damage

Hetz, C. A. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1793 · Cited by 113

Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells

Wink, G., Ryan, J. A., Gullà, S. V., Letai, A. G., & Keating, A. E. (2014) · ACS Chemical Biology · doi:10.1021/cb500340w · Cited by 116

Overcoming apoptosis deficiency of melanoma—Hope for new therapeutic approaches

Eberle, J., Kurbanov, B. M., Hossini, A. M., Trefzer, U., & Fecker, L. F. (2007) · Drug Resistance Updates · doi:10.1016/j.drup.2007.09.001 · Cited by 112

Recent Trends in Cyclic Peptides as Therapeutic Agents and Biochemical Tools

Choi, J., & Joo, S. H. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.082 · Cited by 112

Targeting Bcl-2 for cancer therapy

Zhang, L., Lu, Z., & Zhao, X. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188569 · Cited by 114

Therapeutic Applications of Cell-Penetrating Peptides

Johnson, R. M., Harrison, S. D., & Maclean, D. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-919-2_38 · Cited by 109

Gain of Interaction with IRS1 by p110α-Helical Domain Mutants Is Crucial for Their Oncogenic Functions

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

The Role of BH3-Only Proteins in Tumor Cell Development, Signaling, and Treatment

Elkholi, R., Floros, K. V., & Chipuk, J. E. (2011) · Genes & Cancer · doi:10.1177/1947601911417177 · Cited by 114

Peptiderive server: derive peptide inhibitors from protein–protein interactions

Sedan, Y., Marcu, O., Lyskov, S., & Schueler‐Furman, O. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw385 · Cited by 109

Paclitaxel Reduces Axonal Bclw to Initiate IP3R1-Dependent Axon Degeneration

Pease-Raissi, S. E., Pazyra‐Murphy, M. F., Li, Y., Wachter, F., Fukuda, Y., Fenstermacher, S. J., Barclay, L. A., Bird, G. H., Walensky, L. D., & Segal, R. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.034 · Cited by 109

Advances in Peptide Pharmaceuticals

Stevenson, C. L. (2009) · Current Pharmaceutical Biotechnology · doi:10.2174/138920109787048634 · Cited by 108

Anti-Apoptosis Mechanisms in Malignant Gliomas

Ziegler, D. S., Kung, A. L., & Kieran, M. W. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.13.9717 · Cited by 110

From DARPins to LoopDARPins: Novel LoopDARPin Design Allows the Selection of Low Picomolar Binders in a Single Round of Ribosome Display

Schilling, J., Schöppe, J., & Plückthun, A. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.026 · Cited by 112

Targeting Protein–Protein Interactions and Fragment-Based Drug Discovery

Valkov, E., Sharpe, T., Marsh, M., Greive, S., & Hyvönen, M. (2011) · Topics in Current Chemistry · doi:10.1007/128_2011_265 · Cited by 107

Backbone‐Enabled Directional Peptide Macrocyclization through Late‐Stage Palladium‐Catalyzed δ‐C(sp2)−H Olefination

Bai, Z., Cai, C., Yu, Z.-L., & Wang, H. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201807953 · Cited by 107

Emerging Bcl-2 inhibitors for the treatment of cancer

Azmi, A. S., Wang, Z. P., Philip, P. A., Mohammad, R. M., & Sarkar, F. H. (2010) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.2010.515210 · Cited by 105

Late‐Stage Peptide Macrocyclization by Palladium‐Catalyzed Site‐Selective C−H Olefination of Tryptophan

Bai, Z., Cai, C., Sheng, W., Ren, Y., & Wang, H. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202007226 · Cited by 106

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

Rapid biocompatible macrocyclization of peptides with decafluoro-diphenylsulfone

Kalhor‐Monfared, S., Jafari, M. R., Patterson, J. T., Kitov, P. I., Dwyer, J. J., Nuss, J. M., & Derda, R. (2016) · Chemical Science · doi:10.1039/c5sc03856a · Cited by 105

Motif mediated protein-protein interactions as drug targets

Corbi‐Verge, C., & Kim, P. M. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-016-0131-4 · Cited by 106

Bioorthogonal Reactions of Triarylphosphines and Related Analogues

Heiss, T. K., Dorn, R. S., & Prescher, J. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00014 · Cited by 104

High Specificity in Protein Recognition by Hydrogen‐Bond‐Surrogate α‐Helices: Selective Inhibition of the p53/MDM2 Complex

Henchey, L. K., Porter, J. R., Ghosh, I., & Arora, P. S. (2010) · ChemBioChem · doi:10.1002/cbic.201000378 · Cited by 104

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 103

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Haase, H. S., Peterson‐Kaufman, K. J., Levengood, S. K. L., Checco, J. W., Murphy, W. L., & Gellman, S. H. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302469a · Cited by 101

Evaluation and critical assessment of putative MCL-1 inhibitors

Varadarajan, S., Vogler, M., Butterworth, M., Dinsdale, D. D., Walensky, L. D., & Cohen, G. M. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.79 · Cited by 101

Targeting Mcl-1 and other Bcl-2 family member proteins in cancer therapy

Yamaguchi, R., Lartigue, L., & Perkins, G. A. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.10.009 · Cited by 102

Intracellular Delivery of a Proapoptotic Peptide via Conjugation to a RAFT Synthesized Endosomolytic Polymer

Duvall, C. L., Convertine, A. J., Benoit, D. S. W., Hoffman, A. S., & Stayton, P. S. (2009) · Molecular Pharmaceutics · doi:10.1021/mp9002267 · Cited by 100

Light‐Regulated Stapled Peptides to Inhibit Protein–Protein Interactions Involved in Clathrin‐Mediated Endocytosis

Nevola, L., Martín‐Quirós, A., Eckelt, K., Camarero, N., Tosi, S., Llobet, A., Giralt, E., & Gorostiza, P. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303324 · Cited by 100

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Meisel, C. T., Porcheri, C., & Mitsiadis, T. A. (2020) · Cells · doi:10.3390/cells9081879 · Cited by 103

Apoptosis and Pharmacological Therapies for Targeting Thereof for Cancer Therapeutics

Singh, V., Khurana, A., Navik, U., Allawadhi, P., Bharani, K. K., & Weiskirchen, R. (2022) · Sci · doi:10.3390/sci4020015 · Cited by 102

Modulating apoptosis as a target for effective therapy

Fleischer, A., Ghadiri, A., Dessauge, F., Duhamel, M., Rebollo, M. P., Alvarez-Franco, F., & Rebollo, A. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.07.013 · Cited by 101

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Matsunaga, T., Fukai, F., Miura, S., Nakane, Y., Owaki, T., Kodama, H., Tanaka, M., Nagaya, T., Takimoto, R., Takayama, T., et al. (2007) · Leukemia · doi:10.1038/sj.leu.2405017 · Cited by 100

Expanding the Cancer Arsenal with Targeted Therapies: Disarmament of the Antiapoptotic Bcl-2 Proteins by Small Molecules

Yap, J. L., Chen, L., Lanning, M. E., & Fletcher, S. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01888 · Cited by 99

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Alavi, S. E., Cabot, P. J., & Moyle, P. M. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00308 · Cited by 100

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Xu, S., Tan, P., Tang, Q., Wang, T., Ding, Y., Fu, H., Zhang, Y., Zhou, C., Song, M., Tang, Q., et al. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.145923 · Cited by 103

On-resin peptide macrocyclization using thiol–ene click chemistry

Aimetti, A. A., Shoemaker, R. L., Lin, C., & Anseth, K. S. (2010) · Chemical Communications · doi:10.1039/c001375g · Cited by 100

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Shang, Y., Zhi, D., Feng, G., Wang, Z., Mao, D., Guo, S., Liu, R., Liu, L., Zhang, S., Sun, S., et al. (2019) · Nano Letters · doi:10.1021/acs.nanolett.8b04406 · Cited by 98

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 98

Development of Peptidomimetic Inhibitors of the ERG Gene Fusion Product in Prostate Cancer

Wang, X., Qiao, Y., Asangani, I. A., Ateeq, B., Poliakov, A., Cieslik, M. P., Pitchiaya, S., Chakravarthi, B. V. S. K., Cao, X., Jing, X., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.02.017 · Cited by 96

Reversible Photocontrol of DNA Binding by a Designed GCN4-bZIP Protein

Woolley, G. A., Jaikaran, A. S. I., Berezovski, M. V., Calarco, J. P., Krylov, S. N., Smart, O. S., & Kumita, J. R. (2006) · Biochemistry · doi:10.1021/bi060142r · Cited by 96

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

Targeting BAX to drug death directly

Walensky, L. D. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0306-6 · Cited by 95

Condensation of 2-((Alkylthio)(aryl)methylene)malononitrile with 1,2-Aminothiol as a Novel Bioorthogonal Reaction for Site-Specific Protein Modification and Peptide Cyclization

Zheng, X., Li, Z., Gao, W., Meng, X., Li, X., Luk, L. Y. P., Zhao, Y., Tsai, Y., & Wu, C. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11875 · Cited by 96

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 98

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 99

TNF‐related apoptosis‐inducing ligand as a therapeutic agent in autoimmunity and cancer

Cretney, E., Shanker, A., Yagita∥, H., Smyth, M. J., & Sayers, T. J. (2006) · Immunology and Cell Biology · doi:10.1111/j.1440-1711.2005.01413.x · Cited by 97

Bax activation by Bim?

Czabotar, P. E., Colman, P. M., & Huang, D. C. S. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.83 · Cited by 95

Back to the future: Ribonuclease A

Marshall, G. R., Feng, J. A., & Kuster, D. J. (2007) · Biopolymers · doi:10.1002/bip.20845 · Cited by 97

Stapling of unprotected helical peptides via photo-induced intramolecular thiol–yne hydrothiolation

Tian, Y., Li, J., Zhao, H., Zeng, X., Wang, D., Liu, Q., Niu, X., Huang, X., Xu, N., & Li, Z. (2016) · Chemical Science · doi:10.1039/c6sc00106h · Cited by 96

Precision medicine by designer interference peptides: applications in oncology and molecular therapeutics

Sorolla, A., Wang, E., Golden, E., Duffy, C., Henriques, S. T., Redfern, A. D., & Blancafort, P. (2019) · Oncogene · doi:10.1038/s41388-019-1056-3 · Cited by 100

Anti-Leukemic Potency of Stapled BH3 Helices Correlates with Their Capacity for Bifunctional Activation of Apoptotic Pathways.

Walensky, L. D., Pitter, K. L., Morash, J. G., Verdine, G. L., & Korsmeyer, S. J. (2006) · Blood · doi:10.1182/blood.v108.11.711.711

Abstract SY37-01: Dissecting the canonical and noncanonical interactions of the BCL-2 family for therapeutic benefit

Walensky, L. D. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-sy37-01

Dissecting the BCL‐2 family interaction network with stapled peptides: mechanistic insights and pharmacologic opportunities

Walensky, L. D. (2012) · The FASEB Journal · doi:10.1096/fasebj.26.1_supplement.220.1

Abstract 4611: Multimodal activation of apoptosis by a hydrocarbon-stapled PUMA BH3 helix.

Edwards, A., Gavathiotis, E., LaBelle, J. L., Braun, C. R., Opoku-Nsiah, K., Bird, G. H., & Walensky, L. D. (2013) · Cancer Research · doi:10.1158/1538-7445.am2013-4611 · Cited by 1

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 99