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Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin
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Proteins can be designed that bind to specific patches on target proteins to alter their subsequent interactions.
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“Binders have been generated starting from several computationally identified hotspot residues, which were then used to guide the positioning of naturally occurring protein scaffolds5.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [5]
In the citing paper
“The design of proteins that bind to a specific site on the surface of a target protein using no information other than the three-dimensional structure of the target remains a challenge1–5.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [5]
In the citing paper
“The RIF approach improves on previous discrete interaction-sampling approaches5 by reducing the algorithmic complexity from O(N) or O(N2) to O(1) with respect to the number of side-chain–target interactions considered, thereby allowing for billions, rather than thousands, of potential interfaces to be considered.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [5]
In the citing paper
“Protein1,5, peptide36 and small-molecule inhibitors37 have been designed to bind to the stem region of group 1 HA and neutralize influenza A viruses, but none recognize the group 2 HA.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [5]
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PatchDock and SymmDock: servers for rigid and symmetric docking
Schneidman-Duhovny, D., Inbar, Y., Nussinov, R., & Wolfson, H. J. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki481 · Cited by 3,018
A Hot Spot of Binding Energy in a Hormone-Receptor Interface
Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,987
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
Kuhlman, B. A., Dantas, G. A., Ireton, G. C., Varani, G., Stoddard, B. L., & Baker, D. A. (2003) · Science · doi:10.1126/science.1089427 · Cited by 1,666
Self-citationAntibody Recognition of a Highly Conserved Influenza Virus Epitope
Ekiert, D. C., Bhabha, G., Elsliger, M.-A., Friesen, R. H. E., Jongeneelen, M., Throsby, M., Goudsmit, J., & Wilson, I. A. (2009) · Science · doi:10.1126/science.1171491 · Cited by 1,326
Self-citationGray, J. J., Moughon, S. E., Wang, C., Schueler‐Furman, O., Kuhlman, B. A., Rohl, C. A., & Baker, D. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00670-3 · Cited by 1,130
Self-citationSui, J., Hwang, W. C., Perez, S., Ge, W., Aird, D. R., Chen, L., Santelli, E., Stec, B., Cadwell, G., Ali, M., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1566 · Cited by 1,128
Clinical Aspects of Pandemic 2009 Influenza A (H1N1) Virus Infection
Writing Committee of the WHO Consultation on Clinical Aspects of Pandemic (H1N1) 2009 Influenza (2010) · New England Journal of Medicine · doi:10.1056/nejmra1000449 · Cited by 1,056
Macromolecular Modeling with Rosetta
Das, R., & Baker, D. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062906.171838 · Cited by 995
Self-citationIsolating and engineering human antibodies using yeast surface display
Chao, G., Lau, W. L., Hackel, B. J., Sazinsky, S. L., Lippow, S. M., & Wittrup, K. D. (2006) · Nature Protocols · doi:10.1038/nprot.2006.94 · Cited by 913
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Chen, T., Hong, L., Yudistyra, V., Vincoff, S., & Chatterjee, P. (2023) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2023.100496 · Cited by 18
Strategies to control the binding mode of de novo designed protein interactions
Der, B. S., & Kuhlman, B. A. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.04.010 · Cited by 19
Elucidation of potential sites for antibody engineering by fluctuation editing
Yanaka, S., Moriwaki, Y., Tsumoto, K., & Sugase, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-10246-9 · Cited by 19
Accurately Predicting Disordered Regions of Proteins Using Rosetta ResidueDisorder Application
Kim, S. S., Seffernick, J. T., & Lindert, S. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b01763 · Cited by 18
Linke, H., Höcker, B., Furuta, K., Forde, N. R., & Curmi, P. M. G. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00717-1 · Cited by 18
Deep Mutational Scanning of Viral Glycoproteins and Their Host Receptors
Narayanan, K. K., & Procko, E. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.636660 · Cited by 18
MHCEpitopeEnergy, a Flexible Rosetta-Based Biotherapeutic Deimmunization Platform
Yachnin, B. J., Mulligan, V. K., Khare, S. D., & Bailey‐Kellogg, C. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00056 · Cited by 20
Yusuf, M., Konc, J., Bing, C. S., Konc, J. T., Khairudin, N. B. A., Janežič, D., & Wahab, H. A. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci400421e · Cited by 19
An integrated device for the rapid and sensitive detection of the influenza hemagglutinin
Anderson, C. E., Buser, J. R., Fleming, A. M., Strauch, E., Ladd, P. D., Englund, J. A., Baker, D. A., & Yager, P. (2019) · Lab on a Chip · doi:10.1039/c8lc00691a · Cited by 18
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Eguchi, R. R., & Huang, P. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz650 · Cited by 20
Applications of Deep Mutational Scanning in Virology
Burton, T. D., & Eyre, N. S. (2021) · Viruses · doi:10.3390/v13061020 · Cited by 19
Aizner, Y., Sharabi, O., Shirian, J., Dakwar, G. R., Risman, M., Avraham, O., & Shifman, J. M. (2014) · Structure · doi:10.1016/j.str.2014.01.012 · Cited by 18
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Zhang, C., Shen, Q., Tang, B., & Lai, L. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305963 · Cited by 18
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Chen, C., Liu, L., Xiao, Y., Cui, S., Wang, J., & Jin, Q. (2017) · Journal of Virology · doi:10.1128/jvi.01850-17 · Cited by 18
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Hecht, M. H., Zarzhitsky, S., Karas, C., & Chari, S. L. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.11.009 · Cited by 17
Jiang, Q., Teufel, A., Jackson, E. L., & Wilke, C. O. (2018) · Genetics · doi:10.1534/genetics.118.300699 · Cited by 17
Carrique, L., Duyvesteyn, H. M. E., Malinauskas, T., Zhao, Y., Ren, J., Zhou, D., Walter, T. S., Radecke, J., Huo, J., Ruza, R. R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.13.249177 · Cited by 18
Zhang, C., Tang, B., Wang, Q., & Lai, L. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24611 · Cited by 17
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Carothers, J. M. (2013) · Systems and Synthetic Biology · doi:10.1007/s11693-013-9118-2 · Cited by 16
Lin, D., Li, F., Wu, Q., Xie, X., Wu, W., Wu, J., Chen, Q., Liu, S., & He, J. G. (2016) · Scientific Reports · doi:10.1038/srep22790 · Cited by 16
Mou, K. Y., Huang, P., Thomas, L. M., & Mayo, S. L. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.06.006 · Cited by 16
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Krause, J. C., & Crowe, J. E. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.aid-0021-2014 · Cited by 15
Amino-acid site variability among natural and designed proteins
Jackson, E. L., Ollikainen, N., Covert, A. W., Kortemme, T., & Wilke, C. O. (2013) · PeerJ · doi:10.7717/peerj.211 · Cited by 15
Tertiary motifs as building blocks for the design of protein‐binding peptides
Swanson, S., Sivaraman, V., Grigoryan, G., & Keating, A. E. (2022) · Protein Science · doi:10.1002/pro.4322 · Cited by 14
von Kreudenstein, T. S., Lario, P. I., & Dixit, S. B. (2013) · Methods · doi:10.1016/j.ymeth.2013.10.016 · Cited by 15
De novo design of immunoreactive conformation-specific HIV-1 epitopes based on Top7 scaffold
Viana, I. F. T., Soares, T. A., Lima, L. F. O., Marques, E. T. A., Krieger, M. A., Dhália, R., & Lins, R. D. (2013) · RSC Advances · doi:10.1039/c3ra41562g · Cited by 15
Jacchetti, E., Gabellieri, E., Cioni, P., Bizzarri, R., & Nifosı̀, R. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp01274d · Cited by 15
Zheng, F., Jiang, X., Wen, Y., Yang, Y., & Li, M. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.12.018 · Cited by 14
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London, N., & Ambroggio, X. I. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.03.012 · Cited by 14
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Ernst, P. J., Zosel, F., Reichen, C., Nettels, D., Schuler, B., & Plückthun, A. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.9b00928 · Cited by 14
Parzych, E. M., DiMenna, L. J., Latimer, B. P., Small, J. C., Kannan, S., Manson, B., Lasaro, M. O., Wherry, E. J., & Ertl, H. C. J. (2013) · BioMed Research International · doi:10.1155/2013/876314 · Cited by 14
Binding Affinities Controlled by Shifting Conformational Equilibria: Opportunities and Limitations
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Tlatli, R., Nozach, H., Collet, G., Beau, F., Vera, L., Stura, E. A., Dive, V., & Cuniasse, P. (2012) · FEBS Journal · doi:10.1111/febs.12056 · Cited by 13
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Pascha, M. N., Thijssen, V., Egido, J. E., Linthorst, M. W., van Lanen, J. H., van Dongen, D. A. A., Hopstaken, A. J. P., van Kuppeveld, F. J. M., Snijder, J., de Haan, C. A. M., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00040 · Cited by 11
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Zhou, H., Wu, H., Zhong, Z., Blasco, P., Zeng, J., Wang, J., Liu, H., & Li, X. (2025) · JACS Au · doi:10.1021/jacsau.5c01181 · Cited by 10
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Lopes, T. J. S., Shoemaker, J. E., Matsuoka, Y., Kawaoka, Y., & Kitano, H. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00186 · Cited by 11
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Choi, Y. S., Yoon, S., Kim, K. L., Yoo, J., Song, P., Kim, M., Shin, Y.-E., Yang, W. J., Noh, J.-E., Cho, H.-S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092513 · Cited by 10
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Metadata
- Authors
- Fleishman, S. J., Whitehead, T. A., Ekiert, D. C., Dreyfus, C., Corn, J. E., Strauch, E.-M., Wilson, I. A., & Baker, D.
- Affiliations
- University of Washington (US)
- Scripps Research Institute (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Fleishman, Sarel J.
- Whitehead, Timothy A.
- Ekiert, Damian C.
- Baker, David
- ORCID
- Venue
- Science
- Published
- 2011-05-13
- Volume
- 332
- Issue
- 6031
- Pages
- 816-821
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3164876
- OpenAlex
- W2049275721
- Cited by
- 585
- References
- 20
- Citations by year
- 2026: 15 · 2025: 23 · 2024: 22 · 2023: 26 · 2022: 21 · 2021: 28 · 2020: 24 · 2019: 41 · 2018: 32 · 2017: 44 · 2016: 42 · 2015: 37 · 2014: 61 · 2013: 87 · 2012: 62
- FWCI
- 29.89
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (Y1-CO-1020)
- National Institute of General Medical Sciences (Y1-GM-1104, GM080209, T32GM080209)
- National Institute of Allergy and Infectious Diseases (U54AI057141, P01AI058113, AI057141, AI058113)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- protein design, influenza hemagglutinin, affinity maturation
- MeSH terms
- Algorithms, Amino Acid Sequence, Binding Sites, Computer Simulation, Hydrogen Bonding, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Protein Conformation, Proteins, Software, Protein Engineering, Protein Structure, Secondary, Peptide Library, Hemagglutinin Glycoproteins, Influenza Virus, Computational Biology, Protein Interaction Domains and Motifs, Hydrophobic and Hydrophilic Interactions
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