Coiled-Coil Design: Updated and Upgraded

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Probing Designability via a Generalized Model of Helical Bundle Geometry

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Peptide and Protein Building Blocks for Synthetic Biology: From Programming Biomolecules to Self-Organized Biomolecular Systems

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A Periodic Table of Coiled-Coil Protein Structures

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Installing hydrolytic activity into a completely de novo protein framework

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In Situ Modification of Plain Liposomes with Lipidated Coiled Coil Forming Peptides Induces Membrane Fusion

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Extended knobs-into-holes packing in classical and complex coiled-coil assemblies☆

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Squaring the Circle in Peptide Assembly: From Fibers to Discrete Nanostructures by de Novo Design

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Synthetic biology through biomolecular design and engineering

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Local and macroscopic electrostatic interactions in single α-helices

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Engineered Coiled-Coil Protein Microfibers

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Extremely Thermostabilizing Core Mutations in Coiled-Coil Mimetic Proteins of HIV-1 gp41 Produce Diverse Effects on Target Binding but Do Not Affect Their Inhibitory Activity

Cano‐Muñoz, M., Cesaro, S., Morel, B., Lucas, J., Moog, C., & Conejero‐Lara, F. (2021) · Biomolecules · doi:10.3390/biom11040566 · Cited by 40 · see citing works

Functional and Structural Roles of Coiled Coils

Hartmann, M. D. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-49674-0_3 · Cited by 37 · see citing works

Guiding Biomolecular Interactions in Cells Using de Novo Protein–Protein Interfaces

Smith, A. J., Thomas, F., Shoemark, D. K., Woolfson, D. N., & Savery, N. J. (2019) · ACS Synthetic Biology · doi:10.1021/acssynbio.8b00501 · Cited by 37 · see citing works

De novo design of a reversible phosphorylation-dependent switch for membrane targeting

Harrington, L., Fletcher, J. M., Heermann, T., Woolfson, D., & Schwille, P. (2021) · Nature Communications · doi:10.1038/s41467-021-21622-5 · Cited by 31 · see citing works

Rational design of new materials using recombinant structural proteins: Current state and future challenges

Sutherland, T. D., Huson, M. G., & Rapson, T. D. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.10.012 · Cited by 33 · see citing works

Conformational Dynamics of Asparagine at Coiled-Coil Interfaces

Thomas, F., Niitsu, A., Oregioni, A., Bartlett, G. J., & Woolfson, D. N. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00848 · Cited by 33 · see citing works

Protein‐Based Controllable Nanoarchitectonics for Desired Applications

Li, L., Zhang, Y., Wu, Y., Wang, Z., Cui, W., Zhang, C., Wang, J., Liu, Y., & Yang, P. (2024) · Advanced Functional Materials · doi:10.1002/adfm.202315509 · Cited by 31 · see citing works

CCDC85B promotes non‐small cell lung cancer cell proliferation and invasion

Feng, Y., Gao, Y., Yu, J., Jiang, G., Zhang, X., Lin, X., Han, Q., Rong, X., Xu, H., Li, Q., et al. (2018) · Molecular Carcinogenesis · doi:10.1002/mc.22914 · Cited by 30 · see citing works

A library of coiled-coil domains: from regular bundles to peculiar twists

Szczepaniak, K., Bukala, A., Neto, A. M. D. S., Ludwiczak, J., & Dunin-Horkawicz, S. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa1041 · Cited by 30 · see citing works

Assembly of transmembrane pores from mirror-image peptides

Smrithi Krishnan, R., Jana, K., Shaji, A. H., Nair, K. S., Das, A. D., Vikraman, D., Bajaj, H., Kleinekathöfer, U., & Mahendran, K. R. (2022) · Nature Communications · doi:10.1038/s41467-022-33155-6 · Cited by 29 · see citing works

Recent research of peptide-based hydrogel in nervous regeneration

Xie, C., Chen, Y., Wang, L., Liao, K., Xue, B., Han, Y., Li, L., & Jiang, Q. Y. (2024) · Bioactive Materials · doi:10.1016/j.bioactmat.2024.06.013 · Cited by 29 · see citing works

De Novo Designed α‐Helical Coiled‐Coil Peptides as Scaffolds for Chemical Reactions

Rink, W. M., & Thomas, F. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201802849 · Cited by 29 · see citing works

Construction of Targeting-Peptide-Based Imaging Reagents and Their Application in Bioimaging

Zhang, L., Wang, X., Zhao, J., Sun, B., & Wang, W. (2023) · Chemical & Biomedical Imaging · doi:10.1021/cbmi.3c00104 · Cited by 28 · see citing works

Metal ion–regulated assembly of designed modular protein cages

Aupič, J., Lapenta, F., Strmšek, Ž., Merljak, E., Plaper, T., & Jerala, R. (2022) · Science Advances · doi:10.1126/sciadv.abm8243 · Cited by 22 · see citing works

Engineered Coiled-Coil Protein for Delivery of Inverse Agonist for Osteoarthritis

Yin, L., Agustinus, A. S., Yuvienco, C., Minashima, T., Schnabel, N. L., Kirsch, T., & Montclare, J. K. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b00158 · Cited by 25 · see citing works

Structural resolution of switchable states of a de novo peptide assembly

Dawson, W., Lang, E. J. M., Rhys, G. G., Shelley, K., Williams, C., Brady, R., Crump, M., Mulholland, A., & Woolfson, D. (2021) · Nature Communications · doi:10.1038/s41467-021-21851-8 · Cited by 24 · see citing works

Structural determinants of coiled coil mechanics

López‐García, P., Goktas, M., Bergues-Pupo, A. E., Koksch, B., Silva, D. V., & Blank, K. G. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp00665f · Cited by 25 · see citing works

From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles

Naudin, E. A., Albanese, K. I., Smith, A. J., Mylemans, B., Baker, E. G., Weiner, O. D., Andrews, D. M., Tigue, N. J., Savery, N. J., & Woolfson, D. N. (2022) · Chemical Science · doi:10.1039/d2sc04479j · Cited by 23 · see citing works

Critical assessment of coiled-coil predictions based on protein structure data

Simm, D., Hatje, K., Waack, S., & Kollmar, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-91886-w · Cited by 24 · see citing works

Self-Assembling Peptides as an Emerging Platform for the Treatment of Metabolic Syndrome

Díaz, L., Ruiz‐Pacheco, J. A., Elsawy, M. A., Reyes-Martínez, J. E., & Enríquez-Rodríguez, A. I. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s278189 · Cited by 23 · see citing works

De Novo Designed Protein-Interaction Modules for In-Cell Applications

Edgell, C. L., Smith, A. J., Beesley, J. L., Savery, N. J., & Woolfson, D. N. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00453 · Cited by 23 · see citing works

Early eukaryotic origins and metazoan elaboration of MAPR family proteins

Hehenberger, E., Eitel, M., Fortunato, S., Miller, D. J., Keeling, P. J., & Cahill, M. A. (2020) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2020.106814 · Cited by 23 · see citing works

Synthetic biology principles for the design of protein with novel structures and functions

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Designed folding pathway of modular coiled-coil-based proteins

Aupič, J., Strmšek, Ž., Lapenta, F., Pahovnik, D., Pisanski, T., Drobnak, I., Ljubetič, A., & Jerala, R. (2021) · Nature Communications · doi:10.1038/s41467-021-21185-5 · Cited by 23 · see citing works

Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers

Miller, J. G., Hughes, S. A., Modlin, C., & Conticello, V. P. (2022) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583522000014 · Cited by 22 · see citing works

Applying graph theory to protein structures: an Atlas of coiled coils

Heal, J. W., Bartlett, G. J., Wood, C. W., Thomson, A. R., & Woolfson, D. N. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty347 · Cited by 22 · see citing works

Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast

Popelka, H., Reinhart, E. F., Metur, S. P., Leary, K. A., Ragusa, M. J., & Klionsky, D. J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166809 · Cited by 22 · see citing works

Death at a funeral: Activation of the dead enzyme, MLKL, to kill cells by necroptosis

Davies, K. A., Czabotar, P. E., & Murphy, J. M. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102891 · Cited by 22 · see citing works

Engineering β-Sheet Peptide Coassemblies for Biomaterial Applications

Wong, K. M., Robang, A. S., Lint, A. H., Wang, Y., Dong, X. Y., Xiao, X., Seroski, D. T., Liu, R., Shao, Q., Hudalla, G. A., et al. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c04873 · Cited by 20 · see citing works

Coiled-Coil N21 of Hpa1 in Xanthomonas oryzae pv. oryzae Promotes Plant Growth, Disease Resistance and Drought Tolerance in Non-Hosts via Eliciting HR and Regulation of Multiple Defense Response Genes

Ji, Z., Yu, M., Ding, Y.-Y., Li, J., Zhu, F., He, J., & Yang, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010203 · Cited by 19 · see citing works

Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier

Dhankher, A., Lv, W., Studstill, W. T., & Champion, J. A. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.09.026 · Cited by 18 · see citing works

Computational Prediction of Coiled–Coil Protein Gelation Dynamics and Structure

Britton, D., Christians, L. F., Liu, C., Legocki, J., Xiao, Y., Meleties, M., Yang, L., Cammer, M., Jia, S., Zhang, Z., et al. (2023) · Biomacromolecules · doi:10.1021/acs.biomac.3c00968 · Cited by 18 · see citing works

Design of Coiled-Coil Protein Nanostructures for Therapeutics and Drug Delivery

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Hierarchical approach for the rational construction of helix-containing nanofibrils using α,β-peptides

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Crystal Structure of de Novo Designed Coiled-Coil Protein Origami Triangle

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Self-assembly of repeat proteins: Concepts and design of new interfaces

Sánchez‐deAlcázar, D., Mejías, S. H., Castillo, K. P. E., Sot, B., & Cortajarena, A. L. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.09.002 · Cited by 16 · see citing works

Robust De Novo-Designed Homotetrameric Coiled Coils

Edgell, C. L., Savery, N. J., & Woolfson, D. N. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00082 · Cited by 15 · see citing works

Making or Breaking Metal‐Dependent Catalytic Activity: The Role of Stammers in Designed Three‐Stranded Coiled Coils

Pinter, T. B. J., Manickas, E. C., Tolbert, A. E., Koebke, K. J., Deb, A., Penner‐Hahn, J. E., & Pecoraro, V. L. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202008356 · Cited by 15 · see citing works

Grass‐specific ABERRANT MICROSPORE DEVELOPMENT 1 is required for maintaining pollen fertility in rice

Zou, T., Xiong, P., Zhou, F., Zhou, D., Chen, H., Li, G., Peng, K., Zheng, K., Han, Y., Zhang, K., et al. (2022) · The Plant Journal · doi:10.1111/tpj.15921 · Cited by 14 · see citing works

Designed alpha-helical barrels for charge-selective peptide translocation

Smrithi Krishnan, R., Puthumadathil, N., Shaji, A. H., Kumar, K. S., Mohan, G., & Mahendran, K. R. (2020) · Chemical Science · doi:10.1039/d0sc04856a · Cited by 12 · see citing works

Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation

Cringoli, M. C., & Marchesan, S. (2023) · Molecules · doi:10.3390/molecules28134970 · Cited by 12 · see citing works

Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications.

Winter, D. L., Iranmanesh, H., Clark, D., & Glover, D. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00208 · Cited by 10 · see citing works

<scp> CC ⁺ </scp> : A searchable database of validated coiled coils in <scp>PDB</scp> structures and <scp>AlphaFold2</scp> models

Kumar, P., Petrenas, R., Dawson, W. M., Schweke, H., Levy, E. D., & Woolfson, D. N. (2023) · Protein Science · doi:10.1002/pro.4789 · Cited by 11 · see citing works

Designed Complex Peptide‐Based Adaptive Systems: A Bottom‐Up Approach

Kassem, S., & Ulijn, R. V. (2022) · ChemSystemsChem · doi:10.1002/syst.202200040 · Cited by 11 · see citing works

Preorganized cyclic modules facilitate the self-assembly of protein nanostructures

Snoj, J., Lapenta, F., & Jerala, R. (2024) · Chemical Science · doi:10.1039/d3sc06658d · Cited by 10 · see citing works

How Coiled-Coil Assemblies Accommodate Multiple Aromatic Residues

Rhys, G. G., Dawson, W., Beesley, J. L., Martin, F. J. O., Brady, R. L., Thomson, A. R., & Woolfson, D. N. (2021) · Biomacromolecules · doi:10.1021/acs.biomac.1c00131 · Cited by 10 · see citing works

Heterogeneous protein co-assemblies with tunable functional domain stoichiometry

Farhadi, S. A., Restuccia, A., Sorrentino, A. D., Cruz-Sánchez, A., & Hudalla, G. A. (2021) · Molecular Systems Design & Engineering · doi:10.1039/d1me00083g · Cited by 10 · see citing works

Assembly of peptide nanostructures with controllable sizes

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Creation of artificial protein–protein interactions using α-helices as interfaces

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Repurposing Peptide Nanomaterials as Synthetic Biomolecular Condensates in Bacteria

Tomares, D. T., Whitlock, S., Mann, M. D., DiBernardo, E. F., & Childers, W. S. (2022) · ACS Synthetic Biology · doi:10.1021/acssynbio.2c00078 · Cited by 8 · see citing works

Expanding the versatility of natural and de novo designed coiled coils and helical bundles.

ElGamacy, M., & Alvarez, B. H. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.03.011 · Cited by 6 · see citing works

Identification of novel functional mini-receptors by combinatorial screening of split-WW domains

Neitz, H., Paul, N. B., Häge, F. R., Lindner, C., Graebner, R., Kovermann, M., & Thomas, F. (2022) · Chemical Science · doi:10.1039/d2sc01078j · Cited by 8 · see citing works

Effect of the Aspect Ratio of Coiled-Coil Protein Carriers on Cellular Uptake

Nakayama, N., Takaoka, S., Ota, M., Takagaki, K., & Sano, K. (2018) · Langmuir · doi:10.1021/acs.langmuir.8b02616 · Cited by 8 · see citing works

Rational Design of Phosphorylation-Responsive Coiled Coil-Peptide Assemblies

Thompson, H. F., Beesley, J., Langlands, H. D., Edgell, C., Savery, N., & Woolfson, D. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00064 · Cited by 6 · see citing works

Design and Evolution of Enhanced Peptide–Peptide Ligation for Modular Transglutaminase Assembly

Keeble, A. H., Wood, D. P., & Howarth, M. R. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00122 · Cited by 7 · see citing works

Distribution of disease-causing germline mutations in coiled-coils implies an important role of their N-terminal region

Kálmán, Z. E., Mészáros, B., Gáspári, Z., & Dobson, L. (2020) · Scientific Reports · doi:10.1038/s41598-020-74354-9 · Cited by 7 · see citing works

Exploring Highly Conserved Regions of SARS-CoV-2 Spike S2 Subunit as Targets for Fusion Inhibition Using Chimeric Proteins

Polo-Megías, D., Cano‐Muñoz, M., Berruezo, A. G., Laumond, G., Moog, C., & Conejero‐Lara, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415511 · Cited by 7 · see citing works

Folding-Assisted Peptide Disulfide Formation and Dimerization

Victorio, C. G., & Sawyer, N. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.3c00268 · Cited by 7 · see citing works

Genetically Fusing Order‐Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials

Patkar, S. S., Wang, B., Mosquera, A. M., & Kiick, K. L. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202400582 · Cited by 7 · see citing works

Conformational control in a photoswitchable coiled coil

Torner, J. M., & Arora, P. S. (2021) · Chemical Communications · doi:10.1039/d0cc08318f · Cited by 7 · see citing works

Decoration of Coiled-Coil Peptides with N-Cysteine Peptide Thioesters As Cyclic Peptide Precursors Using Copper-Catalyzed Azide–Alkyne Cycloaddition (CuAAC) Click Reaction

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Biomolecular Structures: Prediction, Identification and Analyses

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Design and Synthesis of Crosslinked Helix Dimers as Protein Tertiary Structure Mimics

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Equipping Coiled-Coil Peptide Dimers With Furan Warheads Reveals Novel Cross-Link Partners

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Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions

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High Molecular Weight Protein-Like Semiflexible Chains via Bioorthogonal Polymerization of Coiled-Coil Peptides

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De Novo Design of Iron–Sulfur Proteins

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Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils

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