Prof. Dr. Michael Nash

Boult, S., Pacak, P., Yang, B., Liu, H., Vogel, V., & Nash, M. A. (2025). Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization. 16. https://doi.org/10.1038/s41467-025-62427-0

Sun, Y., Li, J., Vanella, R., Liu, H., Liu, Z., & Nash, M. A. (2025). Engineering Mechanostable Anticalin Scaffolds to Enhance Particle Adhesion and Targeting of CTLA‐4 Under Shear Stress [Journal-article]. Angewandte Chemie, 137(38). https://doi.org/10.1002/ange.202504483

Kueng, Christoph, Dalkiran, Alperen, Vanella, Rosario, Oyarzun, Diego, & Nash, Michael A. (2025). Discovery of Electron Hole-hopping Redox Mutations in Myoglobin by Deep Mutational Learning [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2025.08.27.672588

Marfoglia, M., Dumas, L., Yang, B. S., Oggier, A., Pedraza, M., Hijazi, M., Larabi, A. N., Lau, K., Pojer, F., Nash, M. A., & Barth, P. (2025). Molecular characterization of an adhesion GPCR signal transduction [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2025.08.14.670383

Sun, Y., Bertschi, A., Urosev, I., Kang, S., Vanella, R., & Nash, M. A. (2025). Enzyme-responsive Hemostatic Elastin-like Polypeptides for Fibrin Stabilization and Enhanced Coagulation in Thrombocytopenia [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2025.07.11.664375

Vanella, Rosario, Boult, Sean, Kueng, Christoph, & Nash, Michael. (2025). Decoding Substrate Specificity in a Promiscuous Biocatalyst by Enzyme Proximity Sequencing [Posted-content]. In BioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2025.07.10.664162

Küng, C., Protsenko, O., Vanella, R., & Nash, M. A. (2025). Deep mutational scanning reveals a de novo disulfide bond and combinatorial mutations for engineering thermostable myoglobin. 34. https://doi.org/10.1002/pro.70112

Fernández de Santaella, J., Koch, N. G., Widmer, L., & Nash, M. A. (2025). Amber Codon Mutational Scanning and Bioorthogonal PEGylation for Epitope Mapping of Antibody Binding Sites on Human Arginase-1. 20. https://doi.org/10.1021/acschembio.4c00692

Vanella, Rosario, Küng, Christoph, Schoepfer, Alexandre A., Doffini, Vanni, Ren, Jin, & Nash, Michael A. (2024). Understanding activity-stability tradeoffs in biocatalysts by enzyme proximity sequencing. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-45630-3

Yang, Byeongseon, Gomes, Diego E. B., Liu, Zhaowei, Santos, Mariana Sá, Li, Jiajun, Bernardi, Rafael C., & Nash, Michael A. (2024). Engineering the Mechanical Stability of a Therapeutic Complex between Affibody and Programmed Death-Ligand 1 by Anchor Point Selection [Journal-article]. ACS Nano, 18(46), 31912–31922. https://doi.org/10.1021/acsnano.4c09220

Boult, S., Pacak, P., Yang, B., Liu, H., Vogel, V., & Nash, M. A. (2024). Force-dependent Reorganization and Mechanostability of the Izumo1:Juno Complex Involved in Human Fertilization [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.10.17.618658

Doffini, V., & Nash, M. A. (2024). Impact of Interval Censoring on Data Accuracy and Machine Learning Performance in Biological High-Throughput Screening [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.09.25.615059

Heiniger, Malvina, Vanella, Rosario, Walsh-Korb, Zarah, & Nash, Michael A. (2024). Functionalized Polysaccharides Improve Sensitivity of Tyramide/Peroxidase Proximity Labeling Assays through Electrostatic Interactions. ACS Biomaterials Science and Engineering, 10(9), 5869–5880. https://doi.org/10.1021/acsbiomaterials.4c00895

Gomes, Diego E. B., Yang, Byeongseon, Vanella, Rosario, Nash, Michael A., & Bernardi, Rafael C. (2024). Integrating Dynamic Network Analysis with AI for Enhanced Epitope Prediction in PD-L1:Affibody Interactions [Journal-article]. Journal of the American Chemical Society, 146(34), 23842–23853. https://doi.org/10.1021/jacs.4c05869

Fernández de Santaella, J., Koch, N. G., Widmer, L., & Nash, M. A. (2024). Amber Codon Mutational Scanning and Bioorthogonal PEGylation for Epitope Mapping of Antibody Binding Sites on Human Arginase-1 [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.08.20.608740

Sun, Y., Li, J., Vanella, R., Liu, H., Liu, Z., & Nash, M. A. (2024). Engineering Mechanostable Anticalin Scaffolds to Enhance Particle Adhesion and Targeting of CTLA-4 under Shear Stress [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.08.16.608260

Yang, B., Gomes, D. E. B., Liu, Z., Santos, M. S., Li, J., Bernardi, R. C., & Nash, M. A. (2024). Engineering the Mechanical Stability of a Therapeutic Affibody/PD-L1 Complex by Anchor Point Selection [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.05.21.595133

Liu, Zhaowei, Liu, Haipei, Vera, Andrés M., Yang, Byeongseon, Tinnefeld, Philip, & Nash, Michael A. (2024). Engineering an artificial catch bond using mechanical anisotropy [Journal-article]. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-46858-9

Heiniger, Malvina, Vanella, Rosario, Walsh-Korb, Zarah, & Nash, Michael A. (2024). Functionalized polysaccharides improve sensitivity of tyramide/peroxidase proximity labeling assays through electrostatic interactions. In ChemRXiv. Cambridge University Press. https://doi.org/10.26434/chemrxiv-2024-crr79

Kueng, Christoph, Protsenko, Olena, Vanella, Rosario, & Nash, Michael. (2024). Decoding Stability and Epistasis in Human Myoglobin by Deep Mutational Scanning and Codon-level Machine Learning. In Biorxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.02.24.581358

Lopez-Morales, J., Vanella, R., Appelt, E. A., Whillock, S., Paulk, A. M., Shusta, E. V., Hackel, B. J., Liu, C. C., & Nash, M. A. (2023). Protein Engineering and High-Throughput Screening by Yeast Surface Display: Survey of Current Methods. 3. https://doi.org/10.1002/smsc.202300095

Doffini, V., Liu, H., Liu, Z., & Nash, M. A. (2023). Iterative Machine Learning for Classification and Discovery of Single-Molecule Unfolding Trajectories from Force Spectroscopy Data. 23. https://doi.org/10.1021/acs.nanolett.3c03026

Liu, Z., Liu, H., Vera, A. M., Yang, B., Tinnefeld, P., & Nash, M. A. (2023). Engineering an artificial catch bond using mechanical anisotropy [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2023.09.12.557335

Zarah Walsh-Korb, & Michael A. Nash. (2023, September 6). CatchGel—A Molecular to Macroscale Investigation of Catch Bond-Crosslinked Polysaccharide Hydrogels. 2022 MRS Fall Meeting.

Liu, H., Liu, Z., Sá Santos, M., & Nash, M. A. (2023). Direct Comparison of Lysine versus Site‐Specific Protein Surface Immobilization in Single‐Molecule Mechanical Assays** [Journal-article]. Angewandte Chemie, 135(32). https://doi.org/10.1002/ange.202304136

Koch, N. G., Goettig, P., Nash, M. A., Rappsilber, J., & Budisa, N. (2023). “Cold” Orthogonal Translation: A Psychrophilic Pyrrolysyl-tRNA Synthetase Boosts Genetic Code Expansion in E. coli [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2023.05.23.541947

Lopez-Morales, Joanan, Vanella, Rosario, Utzinger, Tamara, Schittny, Valentin, Hirsiger, Julia, Osthoff, Michael, Berger, Christoph T., Guri, Yakir, & Nash, Michael A. (2023). Multiplexed on-yeast serological assay for immune escape screening of SARS-CoV-2 variants. iScience, 26(5). https://doi.org/10.1016/j.isci.2023.106648

Fernández De Santaella, Jaime, Ren, Jin, Vanella, Rosario, & Nash, Michael A. (2023). Enzyme Cascade with Horseradish Peroxidase Readout for High-Throughput Screening and Engineering of Human Arginase-1 [Journal-article]. Analytical Chemistry, 95(18), 7150–7157. https://doi.org/10.1021/acs.analchem.2c05429

Dumas, L., Marfoglia, M., Yang, B., Hijazi, M., Larabi, A. N., Lau, K., Pojer, F., Nash, M. A., & Barth, P. (2023). Uncovering and engineering the mechanical properties of the adhesion GPCR ADGRG1 GAIN domain [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2023.04.05.535724

Vanella, Rosario, Küng, Christoph, Schoepfer, Alexandre A., Doffini, Vanni, Ren, Jin, & Nash, Michael A. (2023). Understanding Activity-Stability Tradeoffs in Biocatalysts by Enzyme Proximity Sequencing [Posted-content]. In Biorxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2023.02.24.529916

Lopez-Morales, J., Vanella, R., Utzinger, T., Schittny, V., Hirsiger, J., Osthoff, M., Berger, C., Guri, Y., & Nash, M. A. (2023, February 18). Rapidly Adaptable Multiplexed Yeast Surface Display Serological Assay for Immune Escape Screening of SARS-CoV-2 Variants [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2023.02.17.23286074

Lopez-Morales, J., Vanella, R., Kovacevic, G., Santos, M. S., & Nash, M. A. (2023). Titrating Avidity of Yeast-Displayed Proteins Using a Transcriptional Regulator. 12. https://doi.org/10.1021/acssynbio.2c00351

Küng, Christoph, Vanella, Rosario, & Nash, Michael A. (2023). Directed evolution of Rhodotorula gracilisd-amino acid oxidase using single-cell hydrogel encapsulation and ultrahigh-throughput screening. Reaction Chemistry and Engineering, 8, 1960–1968. https://doi.org/10.1039/d3re00002h

Liu, Haipei, Liu, Zhaowei, Yang, Byeongseon, Lopez Morales, Joanan, & Nash, Michael A. (2022). Optimal Sacrificial Domains in Mechanical Polyproteins: S. epidermidis Adhesins Are Tuned for Work Dissipation. JACS Au, 2(6), 1417–1427. https://doi.org/10.1021/jacsau.2c00121

Liu, Zhaowei, Moreira, Rodrigo A., Dujmović, Ana, Liu, Haipei, Yang, Byeongseon, Poma, Adolfo B., & Nash, Michael A. (2022). Mapping Mechanostable Pulling Geometries of a Therapeutic Anticalin/CTLA-4 Protein Complex. Nano Letters, 22(1), 179–187. https://doi.org/10.1021/acs.nanolett.1c03584

Nash, Michael A. (2022). Elastin-like Polypeptides: Protein-based Polymers for Biopharmaceutical Development. Chimia, 76(5), 478–479. https://doi.org/10.2533/chimia.2022.478

Risser, Fanny, López-Morales, Joanan, & Nash, Michael A. (2022). Adhesive Virulence Factors of Staphylococcus aureus Resist Digestion by Coagulation Proteases Thrombin and Plasmin. ACS Bio & Med Chem Au, 2(6), 586–599. https://doi.org/10.1021/acsbiomedchemau.2c00042

Risser, Fanny, Urosev, Ivan, López-Morales, Joanan, Sun, Yang, & Nash, Michael A. (2022). Engineered Molecular Therapeutics Targeting Fibrin and the Coagulation System: a Biophysical Perspective. Biophysical Reviews, 14(2), 427–461. https://doi.org/10.1007/s12551-022-00950-w

Santos, Mariana Sá, Liu, Haipei, Schittny, Valentin, Vanella, Rosario, & Nash, Michael A. (2022). Correlating single-molecule rupture mechanics with cell population adhesion by yeast display. Biophysical reports, 2(1), None. https://doi.org/10.1016/j.bpr.2021.100035

Vanella, Rosario, Kovacevic, Gordana, Doffini, Vanni, de Santaella, Jaime Fernandez, & Nash, Michael A. (2022). High-throughput screening, next generation sequencing and machine learning: advanced methods in enzyme engineering. Chemical Communications, 58(15), 2455–2467. https://doi.org/10.1039/d1cc04635g

Liu, Z., Moreira, R. A., Dujmović, A., Liu, H., Yang, B., Poma, A. B., & Nash, M. A. (2021). Optimizing mechanostable anchor points of engineered lipocalin in complex with CTLA-4 [Posted-content]. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2021.03.09.434559

Huo, Zihe, Sá Santos, Mariana, Drenckhan, Astrid, Holland-Cunz, Stefan, Izbicki, Jakob R., Nash, Michael A., & Gros, Stephanie J. (2021). Metastatic Esophageal Carcinoma Cells Exhibit Reduced Adhesion Strength and Enhanced Thermogenesis. Cells, 10(5), 1213. https://doi.org/10.3390/cells10051213

Nash, Michael A. (2021). Scalable Online Learning in Physical Chemistry. Chimia, 75(1), 64–66. https://doi.org/10.2533/chimia.2021.64

Jensen, Mikkel Herholdt, Morris, Eliza J., Hai , Tran, Nash, Michael A., & Tan, Cheemeng. (2020). Stochastic ordering of complexoform protein assembly by genetic circuits. PLoS Computational Biology, 16(6), e1007997. https://doi.org/10.1371/journal.pcbi.1007997

Liu, Zhaowei, Liu, Haipei, Vera, Andres M., Bernardi, Rafael C., Tinnefeld, Philip, & Nash, Michael A. (2020). High force catch bond mechanism of bacterial adhesion in the human gut. Nature Communications, 11(1), 4321. https://doi.org/10.1038/s41467-020-18063-x

Nash, Michael A. (2020). Single-molecule and Single-cell Approaches in Molecular Bioengineering. Chimia, 74(9), 704–709. https://doi.org/10.2533/chimia.2020.704

Nash, Michael A. (2020). Zig Zag AFM Protocol Reveals New Intermediate Folding States of Bacteriorhodopsin. Biophysical journal, 118(3), 538–540. https://doi.org/10.1016/j.bpj.2019.12.004

Urosev, Ivan, Lopez Morales, Joanan, & Nash, Michael A. (2020). Phase Separation of Intrinsically Disordered Protein Polymers Mechanically Stiffens Fibrin Clots. Advanced Functional Materials, 30(51), 2005245. https://doi.org/10.1002/adfm.202005245

Yang, Byeongseon, Liu, Haipei, Liu, Zhaowei, Doenen, Regina, & Nash, Michael A. (2020). Influence of Fluorination on Single-Molecule Unfolding and Rupture Pathways of a Mechanostable Protein Adhesion Complex. Nano Letters, 20(12), 8940–8950. https://doi.org/10.1021/acs.nanolett.0c04178

Yang, Byeongseon, Liu, Zhaowei, Liu, Haipei, & Nash, Michael A. (2020). Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes. Frontiers in Molecular Biosciences, 7, 85. https://doi.org/10.3389/fmolb.2020.00085

Bernardi, Rafael C., Durner, Ellis, Schoeler, Constantin, Malinowska, Klara H., Carvalho, Bruna G., Bayer, Edward A., Luthey-Schulten, Zaida, Gaub, Hermann E., & Nash, Michael A. (2019). Mechanisms of Nanonewton Mechanostability in a Protein Complex Revealed by Molecular Dynamics Simulations and Single-Molecule Force Spectroscopy. Journal of the American Chemical Society, 141(37), 14752–14763. https://doi.org/10.1021/jacs.9b06776

Nash, Michael A., Liu, Haipei, & Schittny, Valentin. (2019). Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex. Nano letters, 19(8), 5524–5529. https://doi.org/10.1021/acs.nanolett.9b02062

Vanella, Rosario, Bazin, Alfred, Ta, Duy Tien, & Nash, Michael A. (2019). Genetically encoded stimuli-responsive cytoprotective hydrogel capsules for single cells provide novel genotype-phenotype linkage. Chemistry of Materials, 31(6), 1899–1907. https://doi.org/10.1021/acs.chemmater.8b04348

Vanella, Rosario, Ta, Duy Tien, & Nash, Michael A. (2019). Enzyme-mediated hydrogel encapsulation of single cells for high-throughput screening and directed evolution of oxidoreductases. Biotechnology and bioengineering, 116(8), 1878–1886. https://doi.org/10.1002/bit.27002

Gunnoo, Melissabye, Cazade, Pierre-André, Orlowski, Adam, Chwastyk, Mateusz, Liu, Haipei, Ta, Duy Tien, Cieplak, Marek, Nash, Michael, & Thompson, Damien. (2018). Steered molecular dynamics simulations reveal the role of Ca2+ in regulating mechanostability of cellulose-binding proteins. Physical Chemistry Chemical Physics, 20(35), 22674–22680. https://doi.org/10.1039/c8cp00925b

Lewis, Daniel D., Vanella, Rosario, Vo, Christopher, Rose, Lesilee, Nash, Michael, & Tan, Cheemeng. (2018). Engineered Stochastic Adhesion Between Microbes as a Protection Mechanism Against Environmental Stress. Cellular and Molecular Bioengineering, 11(5), 367–382. https://doi.org/10.1007/s12195-018-0552-9

Liu, Haipei, Ta, Duy Tien, & Nash, Michael A. (2018). Mechanical Polyprotein Assembly Using Sfp and Sortase‐Mediated Domain Oligomerization for Single‐Molecule Studies. Small Methods, 2(6), 1800039. https://doi.org/10.1002/smtd.201800039

Ta, Duy Tien, Vanella, Rosario, & Nash, Michael A. (2018). Bioorthogonal Elastin-like Polypeptide Scaffolds for Immunoassay Enhancement. ACS Applied Materials and Interfaces, 10(36), 30147–30154. https://doi.org/10.1021/acsami.8b10092

Durner, Ellis, Ott, Wolfgang, Nash, Michael A., & Gaub, Hermann E. (2017). Post-translational Sortase-mediated Attachment of High-strength Force Spectroscopy Handles. ACS Omega, 2(6), 3064–3069. https://doi.org/10.1021/acsomega.7b00478

Milles, Lukas Frederik, Bayer, Edward A., Nash, Michael A., & Gaub, Hermann E. (2017). Mechanical Stability of a High-Affinity Toxin Anchor from the Pathogen Clostridium perfringens. Journal of Physical Chemistry B, 121(15), 3620–3625. https://doi.org/10.1021/acs.jpcb.6b09593

Ott, Wolfgang, Jobst, Markus A., Bauer, Magnus S., Durner, Ellis, Milles, Lukas F., Nash, Michael A., & Gaub, Hermann E. (2017). Elastin-like Polypeptide Linkers for Single-Molecule Force Spectroscopy. ACS Nano, 11(6), 6346–6354. https://doi.org/10.1021/acsnano.7b02694

Ott, Wolfgang, Jobst, Markus A., Schoeler, Constantin, Gaub, Hermann E., & Nash, Michael A. (2017). Single-molecule force spectroscopy on polyproteins and receptor-ligand complexes: The current toolbox. Journal of Structural Biology, 197(1), 3–12. https://doi.org/10.1016/j.jsb.2016.02.011

Ta, Duy Tien, Vanella, Rosario, & Nash, Michael A. (2017). Magnetic Separation of Elastin-like Polypeptide Receptors for Enrichment of Cellular and Molecular Targets. Nano Letters, 17(12), 7932–7939. https://doi.org/10.1021/acs.nanolett.7b04318

Verdorfer, Tobias, Bernardi, Rafael C., Meinhold, Aylin, Ott, Wolfgang, Luthey-Schulten, Zaida, Nash, Michael A., & Gaub, Hermann E. (2017). Combining in Vitro and in Silico Single-Molecule Force Spectroscopy to Characterize and Tune Cellulosomal Scaffoldin Mechanics. Journal of the American Chemical Society, 139(49), 17841–17852. https://doi.org/10.1021/jacs.7b07574

Malinowska, Klara H, & Nash, Michael A. (2016). Enzyme- and affinity biomolecule-mediated polymerization systems for biological signal amplification and cell screening. Current Opinion in Biotechnology, 39, 68–75. https://doi.org/10.1016/j.copbio.2016.01.007

Nash, Michael A., & Shoseyov, Oded. (2016). Editorial overview: Nanobiotechnology at a crossroads: moving beyond proof of concept. Current Opinion in Biotechnology, 39, vii–vix. https://doi.org/10.1016/j.copbio.2016.04.024

Nash, Michael A., Smith, Steven P., Fontes, Carlos Mga, & Bayer, Edward A. (2016). Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes. Current Opinion in Structural Biology, 40, 89–96. https://doi.org/10.1016/j.sbi.2016.08.002

Ott, Wolfgang, Nicolaus, Thomas, Gaub, Hermann E., & Nash, Michael A. (2016). Sequence-Independent Cloning and Post-Translational Modification of Repetitive Protein Polymers through Sortase and Sfp-Mediated Enzymatic Ligation. Biomacromolecules, 17(4), 8–1330. https://doi.org/10.1021/acs.biomac.5b01726

Schoeler, Constantin, Verdorfer, Tobias, Gaub, Hermann E., & Nash, Michael A. (2016). Biasing effects of receptor-ligand complexes on protein-unfolding statistics. Physical review E, 94(4-1), 42412. https://doi.org/10.1103/physreve.94.042412