Design and Structure of Stapled Peptides Binding to Estrogen Receptors

Molecular basis of agonism and antagonism in the oestrogen receptor

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The druggable genome

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The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen

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Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ

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Estrogen receptors: how do they signal and what are their targets

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

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An All-Hydrocarbon Cross-Linking System for Enhancing the Helicity and Metabolic Stability of Peptides

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Structure and specificity of nuclear receptor–coactivator interactionsPreprint

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Direct inhibition of the NOTCH transcription factor complex

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Hormone-Dependent Coactivator Binding to a Hydrophobic Cleft on Nuclear Receptors

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Highly Efficient Synthesis of Covalently Cross-Linked Peptide Helices by Ring-Closing Metathesis

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Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide

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Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors

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The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer

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Peptide Antagonists of the Human Estrogen Receptor

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Dissection of the LXXLL Nuclear Receptor-Coactivator Interaction Motif Using Combinatorial Peptide Libraries: Discovery of Peptide Antagonists of Estrogen Receptors α and β

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Single Turn Peptide Alpha Helices with Exceptional Stability in Water

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A Cell-penetrating Helical Peptide as a Potential HIV-1 Inhibitor

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Defining the "S" in SERMs

Katzenellenbogen, B. S., & Katzenellenbogen, B. S. (2002) · Science · doi:10.1126/science.1070442 · Cited by 179 · see citing works

Interaction of Transcriptional Intermediary Factor 2 Nuclear Receptor Box Peptides with the Coactivator Binding Site of Estrogen Receptor α

Wärnmark, A., Treuter, E., Gustafsson, J.-Α., Hubbard, R. E., Brzozowski, A. M., & Pike, A. C. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200764200 · Cited by 173 · see citing works

NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

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Novel Selective Inhibitors of the Interaction of Individual Nuclear Hormone Receptors with a Mutually Shared Steroid Receptor Coactivator 2

Geistlinger, T. R., & Guy, R. K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0348391 · Cited by 94 · see citing works

Potent Inhibitors of LXXLL‐Based Protein–Protein Interactions

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Differential interaction of steroid hormone receptors with LXXLL motifs in SRC-1a depends on residues flanking the motif

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Ser-884 Adjacent to the LXXLL Motif of Coactivator TRBP Defines Selectivity for ERs and TRs

Ko, L., Cardona, G. R., Iwasaki, T., Bramlett, K. S., Burris, T. P., & Chin, W. W. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.1.0755 · Cited by 46 · see citing works

Ligand-Selective Inhibition of the Interaction of Steroid Receptor Coactivators and Estrogen Receptor Isoforms

Geistlinger, T., McReynolds, A. C., & Guy, R. K. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.01.016 · Cited by 45 · see citing works

Magic bullets in nature's arsenal

Kritzer, J. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.407 · Cited by 34 · see citing works

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 · 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

Structure 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 · see citing works

Constrained Peptides with Target‐Adapted Cross‐Links as Inhibitors of a Pathogenic Protein–Protein Interaction

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 · see citing works

Proline primed helix length as a modulator of the nuclear receptor-coactivator interaction

Fuchs, S., Nguyen, H. D., Phan, T. T. P., Burton, M. F., Nieto, L., de Vries-van Leeuwen, I. J., Schmidt, A., Goodarzifard, M., Agten, S. M., Rose, R., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja311748r · Cited by 43 · see citing works

A “cross-stitched” peptide with improved helicity and proteolytic stability

Speltz, T. E., Mayne, C. G., Fanning, S. W., Siddiqui, Z., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob00790j · Cited by 39 · see citing works

PRIC295, a Nuclear Receptor Coactivator, Identified from PPAR-Interacting Cofactor Complex

Pyper, S. R., Viswakarma, N., Jia, Y., Zhu, Y., Fondell, J. D., & Reddy, J. K. (2010) · PPAR Research · doi:10.1155/2010/173907 · Cited by 15 · see citing works

Expression and function of nuclear receptor co-activator 4: evidence of a potential role independent of co-activator activity

Kollara, A., & Brown, T. J. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1000-y · Cited by 53 · see citing works

Tissue- and Nuclear Receptor-Specific Function of the C-Terminal LXXLL Motif of Coactivator NCoA6/AIB3 in Mice

Li, Q., CHU, M., & Xu, J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00451-07 · Cited by 32 · see citing works

Bcl3 Interacts Cooperatively with Peroxisome Proliferator-Activated Receptor Gamma (PPARγ) Coactivator 1α To Coactivate Nuclear Receptors Estrogen-Related Receptor α and PPARα

Yang, J., Williams, R. S., & Kelly, D. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01669-08 · Cited by 41 · see citing works

TRRAP as a hepatic coactivator of LXR and FXR function

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