Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications

Tiede, Christian; Tang, Anna A. S.; Deacon, Sarah E.; Mandal, Upasana; Nettleship, Joanne E.; Owen, Robin L.; George, Suja E.; Harrison, David J.; Owens, Raymond J.; Tomlinson, Darren C.; McPherson, Michael J.

doi:10.1093/protein/gzu007

Cited by 163Biochemical and Structural CharacterizationMonoclonal and Polyclonal Antibodies ResearchChemical Synthesis and Analysis

Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications

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Tiede, Christian, Tang, Anna A. S., Deacon, Sarah E., Mandal, Upasana, Nettleship, Joanne E., Owen, Robin L., George, Suja E., Harrison, David J. +3 more·2014·Protein Engineering, Design and Selection

DOI 10.1093/protein/gzu007PMC PMC4000234

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Abstract

We have designed a novel non-antibody scaffold protein, termed Adhiron, based on a phytocystatin consensus sequence. The Adhiron scaffold shows high thermal stability (Tm ca. 101°C), and is expressed well in Escherichia coli. We have determined the X-ray crystal structure of the Adhiron scaffold to 1.75 Å resolution revealing a compact cystatin-like fold. We have constructed a phage-display library in this scaffold by insertion of two variable peptide regions. The library is of high quality and complexity comprising 1.3 × 10(10) clones. To demonstrate library efficacy, we screened against the yeast Small Ubiquitin-like Modifier (SUMO). In selected clones, variable region 1 often contained sequences homologous to the known SUMO interactive motif (V/I-X-V/I-V/I). Four Adhirons were further characterised and displayed low nanomolar affinities and high specificity for yeast SUMO with essentially no cross-reactivity to human SUMO protein isoforms. We have identified binders against >100 target molecules to date including as examples, a fibroblast growth factor (FGF1), platelet endothelial cell adhesion molecule (PECAM-1; CD31), the SH2 domain Grb2 and a 12-aa peptide. Adhirons are highly stable and well expressed allowing highly specific binding reagents to be selected for use in molecular recognition applications.

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POI-targeting polypeptides can either be single chain antibodies (e.g. nanobodies) or a variety of synthetic polypeptide scaffolds that bind POIs such as monobodies, DARPINs, affimers, or Affibodies.
“These POI-targeting polypeptides can either be single chain antibodies (e.g. variable domains from camelid or shark-derived heavy chain only antibodies, nanobodies), or a variety of synthetic polypeptide scaffolds that bind POIs such as fibronectin type III domain-based monobodies [110, 111], designed ankyrin repeats (DARPINs) [112, 113], cystatin-derived affimers [114] or Affibodies derived from”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [114]

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Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
XDS
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
REFMAC 5 for the refinement of macromolecular crystal structures
Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M., Long, F., & Vagin, A. A. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911001314 · Cited by 8,385 · see citing works
Multiple sequence alignment with hierarchical clustering.
Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,575 · see citing works
Towards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511 · see citing works
Scaling and assessment of data quality
Evans, P. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905036693 · Cited by 4,391 · see citing works
Gene Splicing by Overlap Extension: Tailor-Made Genes Using the Polymerase Chain Reaction
Horton, R. M., Cai, Z., Ho, S. N., & Pease, L. R. (2013) · BioTechniques · doi:10.2144/000114017 · Cited by 1,292 · see citing works
Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains
Hoogenboom, H. R., Griffiths, A. D., Johnson, K. S., Chiswell, D. J., Hudson, P. J., & Winter, G. P. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.15.4133 · Cited by 1,019 · see citing works
Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides 1 1Edited by I. A. Wilson
Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A., & Virnekäs, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3444 · Cited by 728 · see citing works
The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.
Bode, W., Engh, R. A., Müsil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., & Türk, V. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03109.x · Cited by 591 · see citing works
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 · see citing works
Identification of a SUMO-binding motif that recognizes SUMO-modified proteins
Song, J., Durrin, L. K., Wilkinson, T. A., Krontiris, T. G., & Chen, Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403498101 · Cited by 588 · see citing works
The fibronectin type III domain as a scaffold for novel binding proteins
Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585 · see citing works
The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.
Stubbs, M. T., Laber, B., Bode, W., Huber, R., Jerala, R., Lenar≷cic̆, B., & Türk, V. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08321.x · Cited by 494 · see citing works
Introduction to current and future protein therapeutics: A protein engineering perspective
Carter, P. J. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.02.013 · Cited by 467 · see citing works
A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner
Schellenberger, V., Wang, C., Geething, N. C., Spink, B. J., Campbell, A., To, W., Scholle, M. D., Yin, Y., Yao, Y., Bogin, O., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1588 · Cited by 462 · see citing works
SUMO junction—what's your function?
Kerscher, O. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400980 · Cited by 418 · see citing works
A roadmap to generate renewable protein binders to the human proteome
Renewable Protein Binder Working Group, Colwill, K., & Gräslund, S. (2011) · Nature Methods · doi:10.1038/nmeth.1607 · Cited by 378 · see citing works
Consensus-derived structural determinants of the ankyrin repeat motif
Mosavi, L. K., Minor, D. L., & Peng, Z. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252537899 · Cited by 360 · see citing works
Sequence Statistics Reliably Predict Stabilizing Mutations in a Protein Domain
Steipe, B., Schiller, B., Plückthun, A., et al. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1434 · Cited by 349 · see citing works
Engineered protein scaffolds as next-generation antibody therapeutics
Gebauer, M., & Skerra, A. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.04.627 · Cited by 339 · see citing works
Alternative non-antibody scaffolds for molecular recognition
Skerra, A. (2007) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2007.04.010 · Cited by 300 · see citing works
A combinatorial library of an α-helical bacterial receptor domain
Nord, K., Nilsson, J., Nilsson, B., et al. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.6.601 · Cited by 287 · see citing works
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 · see citing works
Design of Stable α-Helical Arrays from an Idealized TPR Motif
Main, E. R. G., Xiong, Y., Cocco, M. J., D’Andrea, L. D., & Regan, L. (2003) · Structure · doi:10.1016/s0969-2126(03)00076-5 · Cited by 274 · see citing works
Efficient Selection of DARPins with Sub-nanomolar Affinities using SRP Phage Display
Steiner, D., Forrer, P., & Plückthun, A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.085 · Cited by 272 · see citing works
Small Ubiquitin-like Modifier (SUMO) Recognition of a SUMO Binding Motif
Song, J., Zhang, Z., Hu, W., & Chen, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507059200 · Cited by 264 · see citing works
A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization
Walter, T. S., Diprose, J. M., Mayo, C., Siebold, C., Pickford, M. G., Carter, L. G., Sutton, G. C., Berrow, N. S., Brown, J., Berry, I. M., et al. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905007808 · Cited by 246 · see citing works
Self-citation
From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase
Lehmann, M., Kostrewa, D., Wyss, M., et al. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.1.49 · Cited by 195 · see citing works
Folding and Unfolding Mechanism of Highly Stable Full-Consensus Ankyrin Repeat Proteins
Wetzel, S. K., Settanni, G., Kenig, M., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.046 · Cited by 179 · see citing works
A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain
Wojcik, J. B., Hantschel, O. D., Grebien, F., Kaupe, I., Bennett, K. L., Barkinge, J. L., Jones, R. B., Koide, A., Superti‐Furga, G., & Koide, S. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1793 · Cited by 165 · see citing works
Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis
Grebien, F., Hantschel, O. D., Wojcik, J. B., Kaupe, I., Kovačic, B., Wyrzucki, A. M., Gish, G. D., Cerny‐Reiterer, S., Koide, A., Beug, H., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.046 · Cited by 152 · see citing works
Design of a binding scaffold based on variable lymphocyte receptors of jawless vertebrates by module engineering
Lee, S., Park, K., Han, J., Lee, J., Kim, H. S., Hong, S. P., Heu, W., Kim, Y. J., Ha, J., Lee, S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113193109 · Cited by 146 · see citing works
Inhibition of Caspase-2 by a Designed Ankyrin Repeat Protein: Specificity, Structure, and Inhibition Mechanism
Schweizer, A., Roschitzki‐Voser, H., Amstutz, P., Briand, C., Gulotti-Georgieva, M., Prenosil, E., Binz, H. K., Capitani, G., Baici, A., Plückthun, A., et al. (2007) · Structure · doi:10.1016/j.str.2007.03.014 · Cited by 130 · see citing works
Three-Dimensional Solution Structure of Oryzacystatin-I, a Cysteine Proteinase Inhibitor of the Rice, Oryza sativa L. japonica,
Nagata, K., Kudo, N., Abe, K., Arai, S., & Tanokura, M. (2000) · Biochemistry · doi:10.1021/bi0006971 · Cited by 112 · see citing works
Poly-Small Ubiquitin-like Modifier (PolySUMO)-binding Proteins Identified through a String Search
Sun, H., & Hunter, T. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.410985 · Cited by 104 · see citing works
Novel protein scaffolds as emerging therapeutic proteins: from discovery to clinical proof-of-concept
Wurch, T., Pierré, A., & Depil, S. (2012) · Trends in biotechnology · doi:10.1016/j.tibtech.2012.07.006 · Cited by 102 · see citing works
Consensus Design of Repeat Proteins
Forrer, P., Binz, H. K., Stumpp, M. T., & Plückthun, A. (2004) · ChemBioChem · doi:10.1002/cbic.200300762 · Cited by 102 · see citing works
Antibodies to watch in 2010
Reichert, J. M. (2010) · mAbs · doi:10.4161/mabs.2.1.10677 · Cited by 91 · see citing works
Design of novel FN3 domains with high stability by a consensus sequence approach
Jacobs, S. A., Diem, M., Luo, J., et al. (2012) · Protein Engineering Design and Selection · doi:10.1093/protein/gzr064 · Cited by 84 · see citing works
Gene organization of oryzacystatin‐II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin‐I but different from those of animal cystatins
Kondo, H., Abe, K., Emori, Y., et al. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80090-p · Cited by 66 · see citing works
Designed Ankyrin Repeat Proteins (DARPins) as Novel Isoform-Specific Intracellular Inhibitors of c-Jun N-Terminal Kinases
Parizek, P., Kummer, L., Rube, P., Prinz, A., Herberg, F. W., & Plückthun, A. (2012) · ACS Chemical Biology · doi:10.1021/cb3001167 · Cited by 65 · see citing works
Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods
Komor, R. S., Romero, P. A., Xie, C. B., & Arnold, F. H. (2012) · Protein Engineering Design and Selection · doi:10.1093/protein/gzs058 · Cited by 64 · see citing works
Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design
Gilbreth, R. N., Truong, K., Madu, I. G., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102294108 · Cited by 61 · see citing works
Designed ankyrin repeat proteins: a novel tool for testing epidermal growth factor receptor 2 expression in breast cancer
Theurillat, J.-P. P., Dreier, B., Nagy‐Davidescu, G., et al. (2010) · Modern Pathology · doi:10.1038/modpathol.2010.103 · Cited by 45 · see citing works
Trinucleotide cassettes increase diversity of T7 phage-displayed peptide library
Krumpe, L. R. H., Schumacher, K. M., McMahon, J. B., et al. (2007) · BMC Biotechnology · doi:10.1186/1472-6750-7-65 · Cited by 39 · see citing works
Anticalins as an alternative to antibody technology
Schlehuber, S., & Skerra, A. (2005) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.5.11.1453 · Cited by 38 · see citing works
Role of SUMO:SIM-mediated protein–protein interaction in non-homologous end joining
Li, Y., Stark, J. M., Chen, D. J., et al. (2010) · Oncogene · doi:10.1038/onc.2010.108 · Cited by 32 · see citing works
Solution Structure of a Phytocystatin from Ananas comosus and Its Molecular Interaction with Papain
Irene, D., Chung, T., Chen, B.-J., Liu, T., Li, F., Tzen, J. T. C., Wang, C., & Chyan, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047865 · Cited by 17 · see citing works
Engineered protein inhibitors of proteases.
Nixon, A. E., & Wood, C. R. (2006) · PubMed · Cited by 16 · see citing works

Flagged first, then by citations

Research works printed but not linked: 51

Afonine P.V. Grosse-Kunstleve R.W. Echols N. Acta Crystallogr. D 2012 68 352 367 22505256 PMC3322595
Binz H.K. Stumpp M.T. Forrer P. Amstutz P. Pluckthun A. J. Mol. Biol. 2003 332 489 503 12948497
Bode W. Engh R. Musil D. Thiele U. Huber R. Karshikov A. Brzin J. Kos J. Turk V. EMBO J. 1988 7 2593 2599 3191914 PMC457133
Carter P.J. Exp. Cell Res. 2011 317 1261 1269 21371474
Colwill K. Graslund S. Renewable Prot Binder Working G. Nat. Methods 2011 8 551 558 21572409
Corpet F. Nucleic Acids Res 1988 16 10881 10890 2849754 PMC338945
Emsley P. Lohkamp B. Scott W.G. Cowtan K. Acta Crystallogr. D 2010 66 486 501 20383002 PMC2852313
Evans P.R. Acta Crystallogr. D 2006 62 72 82 16369096
Forrer P. Binz H.K. Stumpp M.T. Pluckthun A. Chembiochem 2004 5 183 189 14760739
Gebauer M. Skerra A. Curr. Opin. Chem. Biol. 2009 13 245 255 19501012
Gilbreth R.N. Truong K. Madu I. Koide A. Wojcik J.B. Li N.-S. Piccirilli J.A. Chen Y. Koide S. Proc. Natl. Acad. Sci. USA 2011 108 7751 7756 21518904 PMC3093456
Grebien F. Hantschel O. Wojcik J. Cell 2011 147 306 319 22000011 PMC3202669
Hoogenboom H.R. Griffiths A.D. Johnson K.S. Chiswell D.J. Hudson P. Winter G. Nucleic Acids Res. 1991 19 4133 4137 1908075 PMC328552
Horton R. Cai Z. Ho S. Pease L. Biotechniques 1990 8 528 535 2357375
Irene D. Chung T.-Y. Chen B.-J. Liu T.-H. Li F.-Y. Tzen J.T.C. Wang C.-I. Chyan C.L. PLoS ONE 2012 7 e47865 23139757 PMC3490968
Jacobs S.A. Diem M.D. Luo J. Teplyakov A. Obmolova G. Malia T. Gilliland G.L. O'Neil K.T. PEDS 2012 25 107 117 22240293
Kabsch W. Acta Crystallogr. D 2010 66 125 132 20124692 PMC2815665
Kerscher O. EMBO Rep. 2007 8 550 555 17545995 PMC2002525
Knappik A. Ge L.M. Honegger A. J. Mol. Biol. 2000 296 57 86 10656818
Kohl A. Binz H.K. Forrer P. Stumpp M.T. Pluckthun A. Grutter M.G. Proc. Natl Acad. Sci. USA 2003 100 1700 1705 12566564 PMC149896
Koide A. Bailey C.W. Huang X.L. Koide S. J. Mol. Biol. 1998 284 1141 1151 9837732
Komor R.S. Romero P.A. Xie C.B. Arnold F.H. PEDS 2012 25 827 833 22961332
Kondo H. Abe K. Emori Y. Arai S. FEBS Lett. 1991 278 87 90 1993479
Krumpe L.R. Schumacher K.M. McMahon J.B. Makowski L. Mori T. BMC Biotechnol. 2007 7 65 17919322 PMC2174457
Lee S.-C. Park K. Han J. Proc. Natl. Acad. Sci. USA 2012 109 3299 3304 22328160 PMC3295290
Lehmann M. Kostrewa D. Wyss M. Brugger R. D'Arcy A. Pasamontes L. van Loon A. Protein Eng 2000 13 49 57 10679530
Li Y.J. Stark J.M. Chen D.J. Ann D.K. Chen Y. Oncogene 2010 29 3509 3518 20400978 PMC2891878
Main E.R.G. Xiong Y. Cocco M.J. D'Andrea L. Regan L. Structure 2003 11 497 508 12737816
McCoy A.J. Grosse-Kunstleve R.W. Adams P.D. Winn M.D. Storoni L.C. Read R.J. J. Appl. Crystallogr. 2007 40 658 674 19461840 PMC2483472
Mosavi L.K. Minor D.L. Peng Z.Y. Proc. Natl Acad. Sci. USA 2002 99 16029 16034 12461176 PMC138559
Murshudov G.N. Skubak P. Lebedev A.A. Pannu N.S. Steiner R.A. Nicholls R.A. Winn M.D. Long F. Vagin A.A. Acta Crystallogr. D 2011 67 355 367 21460454 PMC3069751
Nagata K. Kudo N. Abe K. Arai S. Tanokura M. Biochemistry 2000 39 14753 14760 11101290
Nixon A.E. Wood C.R. Curr. Opin. Drug Discov. Develop. 2006 9 261 268 16566296
Nord K. Nilsson J. Nilsson B. Uhlen M. Nygren P.A. Protein Eng. 1995 8 601 608 8532685
Parizek P. Kummer L. Rube P. Prinz A. Herberg F.W. Plueckthun A. ACS Chem. Biol. 2012 7 1356 1366 22568706
Reichert J.M. MAbs 2010 2 84 100 20065640 PMC2828582
Schellenberger V. Wang C.-w. Geething N.C. Nat Biotechnol. 2009 27 1186 1190 19915550
Schlehuber S. Skerra A. Expert Opin. Biol. Ther. 2005 5 1453 1462 16255649
Schweizer A. Roschitzki-Voser H. Amstutz P. Structure 2007 15 625 636 17502107
Skerra A. Curr. Opin. Biotechnol. 2007 18 295 304 17643280
Song J. Durrin L.K. Wilkinson T.A. Krontiris T.G. Chen Y.A. Proc. Natl Acad. Sci. USA 2004 101 14373 14378 15388847 PMC521952
Song J. Zhang Z.M. Hu W.D. Chen Y. J. Biol. Chem. 2005 280 40122 40129 16204249
Steiner D. Forrer P. Plueckthun A. J. Mol. Biol. 2008 382 1211 1227 18706916
Steipe B. Schiller B. Pluckthun A. Steinbacher S. J. Mol. Biol. 1994 240 188 192 8028003
Stubbs M.T. Laber B. Bode W. Huber R. Jerala R. Lenarcic B. Turk V. EMBO J. 1990 9 1939 1947 2347312 PMC551902
Sun H. Hunter T. J. Biol. Chem. 2012 287 42071 42083 23086935 PMC3516753
Theurillat J.-P. Dreier B. Nagy-Davidescu G. Seifert B. Behnke S. Zuerrer-Haerdi U. Ingold F. Plueckthun A. Moch H. Mod. Pathol. 2010 23 1289 1297 20495541
Walter T.S. Diprose J.M. Mayo C.J. Acta Crystallogr. D 2005 61 651 657 15930615 PMC7159505
Wetzel S.K. Settanni G. Kenig M. Binz H.K. Pluckthun A. J. Mol. Biol. 2008 376 241 257 18164721
Wojcik J. Hantschel O. Grebien F. Nat. Struct. Mol. Biol. 2010 17 519 U173 20357770 PMC2926940
Wurch T. Pierre A. Depil S. Trends Biotechnol. 2012 30 575 582 22944617

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Authors: Tiede, C., Tang, A. A. S., Deacon, S. E., Mandal, U., Nettleship, J. E., Owen, R. L., George, S. E., Harrison, D. J., Owens, R. J., Tomlinson, D. C., & McPherson, M. J.
Affiliations: University of Leeds (GB)
Rutherford Appleton Laboratory (GB)
Diamond Light Source (GB)
Corresponding author: Tomlinson, Darren C.
McPherson, Michael J.
ORCID: Tiede, Christian
Tang, Anna A. S.
Deacon, Sarah E.
Mandal, Upasana
Nettleship, Joanne E.
Owen, Robin L.
Harrison, David J.
Owens, Raymond J.
Tomlinson, Darren C.
McPherson, Michael J.
Venue: Protein Engineering, Design and Selection
Publisher: Oxford University Press (OUP)
Published: 2014-03-25
Volume: 27
Issue: 5
Pages: 145-155
ISSN: 0269-2139 (ISSN-L)
1741-0134
1741-0126
DOI: 10.1093/protein/gzu007
PMC: PMC4000234
OpenAlex: W2141002805
Cited by: 163
References: 51
Citations by year: 2026: 6 · 2025: 9 · 2024: 9 · 2023: 16 · 2022: 13 · 2021: 16 · 2020: 21 · 2019: 17 · 2018: 12 · 2017: 20 · 2016: 8 · 2015: 11 · 2014: 4
FWCI: 5.88
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
Locations: Protein Engineering Design and Selection (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
University of Huddersfield Repository (University of Huddersfield) (acceptedVersion, other-oa)
White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
Funders: Wellcome Trust (/WT088908/Z/09/Z, 088908/Z/09/Z)
University of Leeds
Directorate for Biological Sciences
Medical Research Council (MR/K018779/1)
Engineering and Physical Sciences Research Council (088908/Z/09/Z, WT 088908/Z/09/Z)
Biotechnology and Biological Sciences Research Council (24/G15882)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
Keywords: phage display library, thermal stability, SUMO, protein-protein binding, fibroblast growth factor 1, CD31, Grb2 SH2 domain, molecular recognition, X-ray crystal structure
MeSH terms: Amino Acid Sequence, Base Sequence, Humans, Models, Molecular, Molecular Sequence Data, Peptides, Temperature, Protein Engineering, Cystatins, Consensus Sequence, Protein Structure, Secondary, Peptide Library, SUMO-1 Protein, Protein Stability

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Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications

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