High-affinity binders selected from designed ankyrin repeat protein libraries

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

Molecular cloning: A laboratory manual

Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

MOLMOL: A program for display and analysis of macromolecular structures

Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,156

LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230

AMoRe: an automated package for molecular replacement

Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941

Tuning the Drug Efflux Activity of an ABC Transporter in vivo by in vitro Selected DARPin Binders

Seeger, M. A., Mittal, A., Velamakanni, S., Hohl, M., Schauer, S., Salaa, I., Grütter, M. G., & van Veen, H. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037845 · Cited by 26

Quantitative assessment of the structural bias in protein–protein interaction assays

Björklund, Å. K., Light, S., Hedin, L. E., & Elofsson, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800150 · Cited by 26

Inhibition of the MET Kinase Activity and Cell Growth in MET-Addicted Cancer Cells by Bi-Paratopic Linking

Andres, F., Iamele, L., Meyer, T., Stüber, J. C., Kast, F., Gherardi, E., Niemann, H. H., & Plückthun, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.03.024 · Cited by 26

Specific Inhibition of Caspase-3 by a Competitive DARPin: Molecular Mimicry between Native and Designed Inhibitors

Schroeder, T., Barandun, J., Flütsch, A., Briand, C., Mittl, P. R. E., & Grütter, M. G. (2013) · Structure · doi:10.1016/j.str.2012.12.011 · Cited by 26

Ribosome display of mammalian receptor domains

Schimmele, B., Gräfe, N., & Plückthun, A. (2005) · Protein Engineering Design and Selection · doi:10.1093/protein/gzi030 · Cited by 26

Engineering of non-natural receptors

Mathonet, P., & Fastrez, J. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.06.007 · Cited by 26

Structure-Based Rational Design of a Toll-like Receptor 4 (TLR4) Decoy Receptor with High Binding Affinity for a Target Protein

Han, J., Kim, H. J., Lee, S., Hong, S. P., Park, K., Jeon, Y. H., Kim, D., Cheong, H., & Kim, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030929 · Cited by 25

A Hot-Spot Motif Characterizes the Interface between a Designed Ankyrin-Repeat Protein and Its Target Ligand

Cheung, L. S.-L., Kanwar, M., Ostermeier, M., & Κωνσταντόπουλος, Κ. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.004 · Cited by 25

Structure of the MORN4/Myo3a Tail Complex Reveals MORN Repeats as Protein Binding Modules

Li, J., Liu, H., Raval, M. H., Wan, J., Yengo, C. M., Liu, W., & Zhang, M. (2019) · Structure · doi:10.1016/j.str.2019.06.004 · Cited by 24

Selection of human anti-CD28 scFvs from a T-NHL related scFv library using ribosome display

Rothe, A., Nathanielsz, A., Hosse, R. J., Oberhauser, F., von Strandmann, E. P., Engert, A., Hudson, P. J., & Power, B. E. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2007.05.012 · Cited by 25

NMR structure and dynamics of human ephrin‐B2 ectodomain: The functionally critical C‐D and G‐H loops are highly dynamic in solution

Ran, X., Qin, H., Liu, J., Fan, J., Shi, J., & Song, J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21999 · Cited by 25

De novo design of buttressed loops for sculpting protein functions

Jiang, H., Jude, K. M., Wu, K., Fallas, J. A., Ueda, G., Brunette, T., Hicks, D. R., Pyles, H., Yang, A., Carter, L. P., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01632-2 · Cited by 24

The high-affinity immunoglobulin E receptor as pharmacological target

Blank, U., Charles, N., & Benhamou, M. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.05.070 · Cited by 24

A Designed, Phase Changing RTX-Based Peptide for Efficient Bioseparations

Shur, O., Dooley, K., Blenner, M., Baltimore, M., & Banta, S. A. (2013) · BioTechniques · doi:10.2144/000114010 · Cited by 24

Creating novel proteins by combining design and selection

Grove, T. Ž., Hands, M. D., & Regan, L. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq015 · Cited by 24

Modular protein switches derived from antibody mimetic proteins

Nicholes, N., Date, A., Beaujean, P., Hauk, P., Kanwar, M., & Ostermeier, M. (2015) · Protein Engineering Design and Selection · doi:10.1093/protein/gzv062 · Cited by 24

Molecular and functional characterization of a novel splice variant of ANKHD1 that lacks the KH domain and its role in cell survival and apoptosisc

Miles, M. C., Janket, M. L., Wheeler, E. D. A., Chattopadhyay, A., Majumder, B., DeRicco, J. S., Schafer, E. A., & Ayyavoo, V. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04821.x · Cited by 24

A rapid, site-selective and efficient route to the dual modification of DARPins

Moody, P. R., Chudasama, V., Nathani, R. I., Maruani, A., Martin, S., Smith, M. E. B., & Caddick, S. (2014) · Chemical Communications · doi:10.1039/c4cc00053f · Cited by 22

Abicipar pegol: an investigational anti-VEGF agent for the treatment of wet age-related macular degeneration

Desideri, L. F., Traverso, C. E., & Nicolò, M. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2020.1772754 · Cited by 23

Structures of in Vitro Evolved Binding Sites on Neocarzinostatin Scaffold Reveal Unanticipated Evolutionary Pathways

Drevelle, A., Graille, M., Heyd, B., Sorel, I., Ulryck, N., Pecorari, F., Desmadril, M., TILBEURGH, H. V., & Minard, P. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.02.002 · Cited by 23

Current and investigational pharmacotherapeutic approaches for modulating retinal angiogenesis

Todorich, B., Yiu, G. C., & Hahn, P. (2014) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2014.890047 · Cited by 23

Designed ankyrin repeat protein binders for the crystallization of AcrB: Plasticity of the dominant interface

Monroe, N., Sennhauser, G., Seeger, M. A., Briand, C., & Grütter, M. G. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.01.014 · Cited by 23

A novel, smaller scaffold for Affitins: Showcase with binders specific for EpCAM

Kalichuk, V., Renodon‐Cornière, A., Béhar, G., Carrión, F., Obal, G., Maillasson, M., Mouratou, B., Véronique Préat, A., & Pecorari, F. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26463 · Cited by 23

In vitro assays for anticancer drug discovery???a novel approach based on engineered mammalian cell lines

Gonzalez‐Nicolini, V., & Fussenegger, M. (2005) · Anti-Cancer Drugs · doi:10.1097/00001813-200503000-00001 · Cited by 23

Improved Cancer Therapy and Molecular Imaging with Multivalent, Multispecific Antibodies

Sharkey, R. M., Rossi, E. A., Chang, C., & Goldenberg, D. M. (2010) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.2009.0690 · Cited by 21

Bioengineering of Bacteria To Assemble Custom-Made Polyester Affinity Resins

Hay, I. D., Du, J., Burr, N. S., & Rehm, B. H. A. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.02595-14 · Cited by 22

Programmable DARPin-based receptors for the detection of thrombotic markers

Strittmatter, T., Wang, Y., Bertschi, A., Scheller, L., Freitag, P. C., Ray, P. G., Stücheli, P., Schaefer, J. V., Reinberg, T., Tsakiris, D. A., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01095-3 · Cited by 22

FAP-retargeted Ad5 enables in vivo gene delivery to stromal cells in the tumor microenvironment

Hartmann, K. P., van Gogh, M., Freitag, P. C., Kast, F., Nagy‐Davidescu, G., Borsig, L., & Plückthun, A. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.08.018 · Cited by 22

Structural Model for the Interaction of a Designed Ankyrin Repeat Protein with the Human Epidermal Growth Factor Receptor 2

Epa, V. C., Dolezal, O., Doughty, L., Xiao, X., Jöst, C., Plückthun, A., & Adams, T. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059163 · Cited by 22

Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS

Brandstätter, L., Sokolová, L., Eicher, T., Seeger, M. A., Briand, C., Cha, H.-J., Cernescu, M., Bohnert, J. A., Kern, W. V., Brutschy, B., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.05.009 · Cited by 22

Tracking Molecular Recognition at the Atomic Level with a New Protein Scaffold Based on the OB-Fold

Steemson, J. D., Baake, M., Rakonjac, J., Arcus, V. L., & Liddament, M. T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086050 · Cited by 22

Ribosome Display with the PURE Technology

Ueda, T., Kanamori, T., & Ohashi, H. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-331-2_18 · Cited by 22

Structural analysis of biological targets by host:guest crystal lattice engineering

Erñst, P., Plückthun, A., & Mittl, P. R. E. (2019) · Scientific Reports · doi:10.1038/s41598-019-51017-y · Cited by 21

Unravelling Receptor and RGD Motif Dependence of Retargeted Adenoviral Vectors using Advanced Tumor Model Systems

Chernyavska, M., Schmid, M., Freitag, P. C., Palacio-Castañeda, V., Piruska, A., Huck, W. T. S., Plückthun, A., & Verdurmen, W. P. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-54939-9 · Cited by 22

Generation of Affibody® ligands binding interleukin‐2 receptor α/CD25

Grönwall, C., Snelders, E., Palm, A. J., Eriksson, F., Herne, N., & Ståhl, S. (2008) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20070261 · Cited by 22

Amyloid-β Peptide-specific DARPins as a Novel Class of Potential Therapeutics for Alzheimer Disease

Hanenberg, M., McAfoose, J., Kulic, L., Welt, T., Wirth, F., Parizek, P., Strobel, L., Cattepoel, S., Späni, C. B., Derungs, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564013 · Cited by 22

Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport

Cross, J. A., Chegkazi, M. S., Steiner, R. A., Woolfson, D. N., & Dodding, M. P. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.03.010 · Cited by 24

Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment

Parker, R. N., Mercedes-Camacho, A. Y., & Grove, T. Ž. (2014) · Protein Science · doi:10.1002/pro.2461 · Cited by 21

Broad-Specificity mRNA–rRNA Complementarity in Efficient Protein Translation

Barendt, P. A., Shah, N. A., Barendt, G. A., & Sarkar, C. A. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002598 · Cited by 21

Evolutionary mechanism as a template for protein engineering

Eisenbeis, S., & Höcker, B. (2010) · Journal of Peptide Science · doi:10.1002/psc.1233 · Cited by 21

Selection of single-chain variable fragments specific for Mycobacterium tuberculosis ESAT-6 antigen using ribosome display.

Ahangarzadeh, S., Bandehpour, M., & Kazemi, B. (2017) · PubMed Central · doi:10.22038/ijbms.2017.8363 · Cited by 21

An experimental framework for improved selection of binding proteins using SNAP display

Houlihan, G., Gatti‐Lafranconi, P., Kaltenbach, M., Lowe, D., & Hollfelder, F. (2014) · Journal of Immunological Methods · doi:10.1016/j.jim.2014.01.006 · Cited by 21

VLR Recognition of TLR5 Expands the Molecular Characterization of Protein Antigen Binding by Non-Ig-based Antibodies

Gunn, R. J., Herrin, B. R., Acharya, S., Cooper, M. D., & Wilson, I. A. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.016 · Cited by 20

Addressing the Protein Crystallization Bottleneck By Cocrystallization

Warke, A., & Momany, C. (2007) · Crystal Growth & Design · doi:10.1021/cg700702c · Cited by 20

Knowledge-based design of reagentless fluorescent biosensors from a designed ankyrin repeat protein

Brient‐Litzler, E., Plückthun, A., & Bedouelle, H. (2009) · Protein Engineering Design and Selection · doi:10.1093/protein/gzp074 · Cited by 20

Peptide Screening Using PURE Ribosome Display

Ohashi, H., Kanamori, T., Osada, E., Akbar, B. K., & Ueda, T. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-379-0_14 · Cited by 20

Catch and Release: Engineered Allosterically Regulated β-Roll Peptides Enable On/Off Biomolecular Recognition

Bulutoglu, B., Dooley, K., Szilvay, G. R., Blenner, M., & Banta, S. A. (2017) · ACS Synthetic Biology · doi:10.1021/acssynbio.7b00089 · Cited by 20

Nanomolar Protein–Protein Interaction Monitoring with a Label-Free Protein-Probe Technique

Valtonen, S., Vuorinen, E., Kariniemi, T., Eskonen, V., Quesne, J. P. C. L., Bushell, M., Härmä, H., & Kopra, K. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02823 · Cited by 20

Mass Discrimination in High-Mass MALDI-MS

Weidmann, S., Mikutis, G., Barylyuk, K. V., & Zenobi, R. (2013) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-013-0686-x · Cited by 20

A stringent test for hydrophobicity scales: Two proteins with 88% sequence identity but different structure and function

Kister, A. E., & Phillips, J. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803264105 · Cited by 20

Epitopes of Protein Binders Are Related to the Structural Flexibility of a Target Protein Surface

Kim, D., Choi, Y., & Kim, H. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01397 · Cited by 20

Homeostasis and dyshomeostasis of the retina

Zhang, C.-J., & Jin, Z. (2023) · Current Medicine · doi:10.1007/s44194-023-00021-6 · Cited by 25

Ribosome display enhanced by next generation sequencing: A tool to identify antibody-specific peptide ligands

Heyduk, E., & Heyduk, T. (2014) · Analytical Biochemistry · doi:10.1016/j.ab.2014.07.014 · Cited by 19

NextGen protein design

Sawyer, N., Speltz, E. B., & Regan, L. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130112 · Cited by 19

Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus

Karlsson, O. A., Ramirez, J., Öberg, D., Malmqvist, T., Engström, Å., Friberg, M., Celestine, N., Widersten, M., Travé, G., Nilsson, M. T. I., et al. (2015) · Scientific Reports · doi:10.1038/srep09382 · Cited by 19

Using thermal scanning assays to test protein-protein interactions of inner-ear cadherins

Choudhary, D., Kumar, A., Magliery, T. J., & Sotomayor, M. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189546 · Cited by 19

Investigating Biomolecular Interactions and Binding Properties Using SPR Biosensors

Navratilova, I. H., & Myszka, D. G. (2006) · Springer series on chemical sensors and biosensors · doi:10.1007/5346_018 · Cited by 19

Rearranging and concatenating a native RTX domain to understand sequence modularity

Shur, O., & Banta, S. A. (2012) · Protein Engineering Design and Selection · doi:10.1093/protein/gzs092 · Cited by 19

A DARPin targeting activated Mac-1 is a novel diagnostic tool and potential anti-inflammatory agent in myocarditis, sepsis and myocardial infarction

Siegel, P. M., Bojti, I., Bassler, N., Holien, J. K., Flierl, U., Wang, X., Waggershauser, P., Tonnar, X., Vedecnik, C., Lamprecht, C., et al. (2021) · Basic Research in Cardiology · doi:10.1007/s00395-021-00849-9 · Cited by 19

A Binding Free Energy Hot Spot in the Ankyrin Repeat Protein GABPβ Mediated Protein–Protein Interaction

Desrosiers, D. C., & Peng, Z.-Y. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.045 · Cited by 19

Designed Ankyrin Repeat Proteins: A New Class of Viral Entry Inhibitors

Walser, M., Mayor, J., & Rothenberger, S. (2022) · Viruses · doi:10.3390/v14102242 · Cited by 18

Biophysical Characterization Platform Informs Protein Scaffold Evolvability

Golinski, A. W., Holec, P. V., Mischler, K. M., & Hackel, B. J. (2019) · ACS Combinatorial Science · doi:10.1021/acscombsci.8b00182 · Cited by 18

Ribosome DisplayIn Vitro Selection of Protein-Protein Interactions

Amstutz, P., BINZ, H., Zahnd, C., & Plückthun, A. (2006) · Elsevier eBooks · doi:10.1016/b978-012164730-8/50061-7 · Cited by 18

Rapid Selection of High-Affinity Antibody scFv Fragments Using Ribosome Display

Dreier, B., & Plückthun, A. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8648-4_13 · Cited by 18

Avimers hold their own

Jeong, K. J., Mabry, R., & Georgiou, G. (2005) · Nature Biotechnology · doi:10.1038/nbt1205-1493 · Cited by 18

Structure of human mitochondrial pyruvate carrier MPC1 and MPC2 complex

Sun, Y., Wang, Y., Zheng, X., Li, D., Wang, R., Chen, B., Zhou, N., Ayala, A., Tu, B. P., & Qi, X. (2025) · Nature Communications · doi:10.1038/s41467-025-61939-z · Cited by 19

Engineering a Supersecreting Strain of Escherichia coli by Directed Coevolution of the Multiprotein Tat Translocation Machinery

Taw, M. N., Li, M., Kim, D., Rocco, M. A., Waraho‐Zhmayev, D., & DeLisa, M. P. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.1c00183 · Cited by 16

TCR mimic compounds for pHLA targeting with high potency modalities in oncology

Gerber, H., & Presta, L. G. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1027548 · Cited by 18

The CD33xCD123xCD70 Multispecific CD3-Engaging DARPin MP0533 Induces Selective T Cell–Mediated Killing of AML Leukemic Stem Cells

Bianchi, M., Reichen, C., Croset, A., Fischer, S., Eggenschwiler, A., Grübler, Y., Marpakwar, R., Looser, T., Spitzli, P., Herzog, C., et al. (2024) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-23-0692 · Cited by 17

Identification of repetitive units in protein structures with ReUPred

Hirsh, L., Piovesan, D., Paladin, L., & Tosatto, S. C. E. (2016) · Amino Acids · doi:10.1007/s00726-016-2187-2 · Cited by 17

Drug, delivery and devices for diabetic retinopathy (3Ds in DR)

Nirmal, J., Radhakrishnan, K., Moreno, M. R., Natarajan, J. V., Laude, A., Lim, T. H., Venkatraman, S. S., & Agrawal, R. V. (2016) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2016.1188800 · Cited by 17

Distinct conformations of the HIV-1 V3 loop crown are targetable for broad neutralization

Friedrich, N., Stiegeler, E., Glögl, M., Lemmin, T., Hansen, S., Kadelka, C., Wu, Y., Erñst, P., Maliqi, L., Foulkes, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27075-0 · Cited by 16

Pharmacological approaches to target type 2 cytokines in asthma

Guilleminault, L., Conde, E., & Reber, L. L. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108167 · Cited by 17

Nuclear myosin VI maintains replication fork stability

Shi, J., Hauschulte, K., Mikičić, I., Maharjan, S., Arz, V., Strauch, T., Heidelberger, J. B., Schaefer, J. V., Dreier, B., Plückthun, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39517-y · Cited by 17

Streamlined Protocol for mRNA Display

Barendt, P. A., Ng, D. T. W., McQuade, C. N., & Sarkar, C. A. (2013) · ACS Combinatorial Science · doi:10.1021/co300135r · Cited by 17

A Hybrid In Silico and Tumor-on-a-Chip Approach to Model Targeted Protein Behavior in 3D Microenvironments

Palacio-Castañeda, V., Dumas, S., Albrecht, P., Wijgers, T. J., Descroix, S., & Verdurmen, W. P. R. (2021) · Cancers · doi:10.3390/cancers13102461 · Cited by 19

Ensovibep, a novel trispecific DARPin candidate that protects against SARS-CoV-2 variantsPreprint

Rothenberger, S., Hurdiss, D. L., Walser, M., Malvezzi, F., Mayor, J., Ryter, S., Moreno, H., Liechti, N., Bosshart, A., Iss, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.03.429164 · Cited by 17

Designed Ankyrin Repeat Proteins as a tool box for analyzing p63

Strubel, A., Münick, P., Chaikuad, A., Dreier, B., Schaefer, J. V., Gebel, J., Osterburg, C., Tuppi, M., Schäfer, B., Knapp, S., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01030-y · Cited by 16

Selection of Anti-Sulfadimidine Specific ScFvs from a Hybridoma Cell by Eukaryotic Ribosome Display

Qi, Y., Wu, C., Zhang, S., Wang, Z., Huang, S., Dai, L., Wang, S., Xia, L., Wen, K., Cao, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006427 · Cited by 16

Affinity transfer to the archaeal extremophilic Sac7d protein by insertion of a CDR

Pacheco, S., Béhar, G., Maillasson, M., Mouratou, B., & Pecorari, F. (2014) · Protein Engineering Design and Selection · doi:10.1093/protein/gzu042 · Cited by 16

Alpha-helicoidal HEAT-like Repeat Proteins (αRep) Selected as Interactors of HIV-1 Nucleocapsid Negatively Interfere with Viral Genome Packaging and Virus Maturation

Hadpech, S., Nangola, S., Chupradit, K., Fanhchaksai, K., Furnon, W., Urvoas, A., Valerio‐Lepiniec, M., Minard, P., Boulanger, P. A., Hong, S. S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16451-w · Cited by 16

Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts

Ernst, P. J., Honegger, A., van der Valk, F., Ewald, C., Mittl, P. R. E., & Plückthun, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-52121-9 · Cited by 16

Ubiquitin is a versatile scaffold protein for the generation of molecules withde novobinding and advantageous drug‐like properties

Job, F., Settele, F., Lorey, S., Rundfeldt, C., Baumann, L., Beck‐Sickinger, A. G., Haupts, U. M., Lilie, H., & Bosse-Doenecke, E. (2015) · FEBS Open Bio · doi:10.1016/j.fob.2015.07.002 · Cited by 16

Targeted delivery and endosomal cellular uptake of DARPin-siRNA bioconjugates: Influence of linker stability on gene silencing

Lorenzer, C., Streußnig, S., Tot, E., Winkler, A.-M., Merten, H., Brandl, F., Sayers, E. J., Watson, P., Jones, A. T., Zangemeister‐Wittke, U., et al. (2019) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2019.05.015 · Cited by 16

Contributions of Conserved TPLH Tetrapeptides to the Conformational Stability of Ankyrin Repeat Proteins

Guo, Y. C., Yuan, C., Tian, F., Huang, K., Weghorst, C. M., Tsai, M., & Li, J. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.04.010 · Cited by 16

Targeted radionuclide therapy in head and neck cancer

Nestor, M. (2009) · Head & Neck · doi:10.1002/hed.21243 · Cited by 16

Designed Ankyrin Repeat Proteins as Anti‐Idiotypic‐Binding Molecules

Vogel, M., Gautschi, E., Baumann, M. J., Amstutz, P., Ruf, C., Kricek, F., & Stadler, B. M. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1398.002 · Cited by 16

A Bispecific Inhibitor of the EGFR/ADAM17 Axis Decreases Cell Proliferation and Migration of EGFR-Dependent Cancer Cells

Soto-Gamez, A., Chen, D., Nabuurs, A., Quax, W. J., Demaria, M., & Boersma, Y. L. (2020) · Cancers · doi:10.3390/cancers12020411 · Cited by 15

Characterization of Monobody Scaffold Interactions with Ligand via Force Spectroscopy and Steered Molecular Dynamics

Cheung, L. S.-L., Shea, D. J., Nicholes, N., Date, A., Ostermeier, M., & Konstantopoulos, K. (2015) · Scientific Reports · doi:10.1038/srep08247 · Cited by 15

Design Principles for SuCESsFul Biosensors: Specific Fluorophore/Analyte Binding and Minimization of Fluorophore/Scaffold Interactions

de Picciotto, S., Dickson, P., Traxlmayr, M. W., Marques, B. S., Socher, E. R., Zhao, S., Cheung, S., Kiefer, J. D., Wand, A. J., Griffith, L. G., et al. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.07.004 · Cited by 16

Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications

Bulutoglu, B., & Banta, S. A. (2017) · Toxins · doi:10.3390/toxins9090289 · Cited by 15

Construction of Covalent Membrane Protein Complexes and High-Throughput Selection of Membrane Mimics

Suk, J.-E., Situ, A. J., & Ulmer, T. S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja304247f · Cited by 15

Fast and global detection of periodic sequence repeats in large genomic resources

Mori, H., Evans-Yamamoto, D., Ishiguro, S., Tomita, M., & Yachie, N. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky890 · Cited by 14

A DARPin-based molecular toolset to probe gephyrin and inhibitory synapse biology

Campbell, B. F. N., Dittmann, A., Dreier, B., Plückthun, A., & Tyagarajan, S. K. (2022) · eLife · doi:10.7554/elife.80895 · Cited by 13

SIMS: A Hybrid Method for Rapid Conformational Analysis

Gipson, B. R., Moll, M., & Kavraki, L. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068826 · Cited by 15

A transcription blocker isolated from a designed repeat protein combinatorial library by in vivo functional screen

Tikhonova, E. B., Ethayathulla, A. S., Su, Y., Hariharan, P., Xie, S., & Guan, L. (2015) · Scientific Reports · doi:10.1038/srep08070 · Cited by 12

The application of helix fusion methods in structural biology

Kwon, N., Kim, Y., & Lee, J. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.12.007 · Cited by 14

Structural plasticity of a designer protein sheds light on β‐propeller protein evolution

Mylemans, B., Laier, I., Kamata, K., Akashi, S., Noguchi, H., Tame, J., & Voet, A. (2020) · The FEBS Journal · doi:10.1111/febs.15347 · Cited by 12

A Biotin Ligase-Based Assay for the Quantification of the Cytosolic Delivery of Therapeutic Proteins

Verdurmen, W. P. R., Mazlami, M., & Plückthun, A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6857-2_14 · Cited by 14

Design of Protein Logic Gate System Operating on Lipid Membranes

Omersa, N., Aden, S., Kisovec, M., Podobnik, M., & Anderluh, G. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00340 · Cited by 14

Designed to be stable: Crystal structure of a consensus ankyrin repeat protein

Kohl, A., Binz, H. K., Forrer, P., Stumpp, M. T., Plückthun, A., & Grütter, M. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337680100 · Cited by 279

Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries. Protein Eng Des Sel 19

Amstutz, P., Koch, H., Binz, H., & Deuber, S. A. (2006)

Designing Repeat Proteins: Well-expressed, Soluble and Stable Proteins from Combinatorial Libraries of Consensus Ankyrin Repeat Proteins

Binz, H. K., Stumpp, M. T., Forrer, P., Amstutz, P., & Plückthun, A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00896-9 · Cited by 589

Selection of binders and inhibitors from designed ankyrin repeat protein libraries

Amstutz, P. (2005) · Zurich Open Repository and Archive (University of Zurich) · doi:10.5167/uzh-163269

Functional Inhibition of Sugar Transport by a Designed Novel Protein

Tikhonova, E. B., Hariharan, P., Su, Y., Anowarul, A., & Guan, L. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.2080