Teaching an old scaffold new tricks: monobodies constructed using alternative surfaces of the FN3 scaffold.
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Shohei Koide | John B Wojcik | A. Koide | S. Koide | R. Gilbreth | Robert J. Hoey | Robert J Hoey | Akiko Koide | Ryan N Gilbreth | John Wojcik
[1] H. Hogrefe,et al. A bacteriophage lambda vector for the cloning and expression of immunoglobulin Fab fragments on the surface of filamentous phage. , 1993, Gene.
[2] S. Koide. Design And Engineering Of Synthetic Binding Proteins Using Nonantibody Scaffolds , 2009 .
[3] Frederic A. Fellouse,et al. High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries. , 2007, Journal of molecular biology.
[4] Sachdev S Sidhu,et al. Synthetic therapeutic antibodies , 2006, Nature chemical biology.
[5] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[6] A. Plückthun,et al. High-affinity binders selected from designed ankyrin repeat protein libraries , 2004, Nature Biotechnology.
[7] Shohei Koide,et al. Exploring the capacity of minimalist protein interfaces: interface energetics and affinity maturation to picomolar KD of a single-domain antibody with a flat paratope. , 2007, Journal of molecular biology.
[8] A. Skerra. Alternative non-antibody scaffolds for molecular recognition. , 2007, Current opinion in biotechnology.
[9] Shohei Koide,et al. A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain , 2010, Nature Structural &Molecular Biology.
[10] David W. Colby,et al. A disulfide-free single-domain V(L) intrabody with blocking activity towards huntingtin reveals a novel mode of epitope recognition. , 2011, Journal of molecular biology.
[11] R. Poljak,et al. Three-dimensional structure of immunoglobulins. , 1979, Annual review of biochemistry.
[12] J. Richardson,et al. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[13] S. Sidhu,et al. Phage display for selection of novel binding peptides. , 2000, Methods in enzymology.
[14] D. Leahy,et al. All Mammalian Hedgehog Proteins Interact with Cell Adhesion Molecule, Down-regulated by Oncogenes (CDO) and Brother of CDO (BOC) in a Conserved Manner* , 2010, The Journal of Biological Chemistry.
[15] David Reverter,et al. Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex , 2005, Nature.
[16] Bruce A. Johnson,et al. NMR View: A computer program for the visualization and analysis of NMR data , 1994, Journal of biomolecular NMR.
[17] Corella S. Casas-Delucchi,et al. Modulation of protein properties in living cells using nanobodies , 2010, Nature Structural &Molecular Biology.
[18] K D Wittrup,et al. Yeast surface display for directed evolution of protein expression, affinity, and stability. , 2000, Methods in enzymology.
[19] T. T. Wu,et al. Length distribution of CDRH3 in antibodies , 1993, Proteins.
[20] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[21] Shohei Koide,et al. Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design , 2011, Proceedings of the National Academy of Sciences.
[22] Andreas Plückthun,et al. Engineered proteins as specific binding reagents. , 2005, Current opinion in biotechnology.
[23] A. Plückthun,et al. Engineering novel binding proteins from nonimmunoglobulin domains , 2005, Nature Biotechnology.
[24] Arash Bahrami,et al. Probabilistic Interaction Network of Evidence Algorithm and its Application to Complete Labeling of Peak Lists from Protein NMR Spectroscopy , 2009, PLoS Comput. Biol..
[25] I. Korndörfer,et al. Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin. , 2003, Journal of molecular biology.
[26] Peter Briggs,et al. A graphical user interface to the CCP4 program suite. , 2003, Acta crystallographica. Section D, Biological crystallography.
[27] Arne Skerra,et al. Construction of an Artificial Receptor Protein (“Anticalin”) Based on the Human Apolipoprotein D , 2004, Chembiochem : a European journal of chemical biology.
[28] L. Bloom,et al. FN3: a new protein scaffold reaches the clinic. , 2009, Drug discovery today.
[29] A. Koide,et al. The fibronectin type III domain as a scaffold for novel binding proteins. , 1998, Journal of molecular biology.
[30] A. Brunger. Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.
[31] A. Koide,et al. Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain. , 2007, Methods in molecular biology.
[32] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[33] John B Wojcik,et al. Accelerating phage-display library selection by reversible and site-specific biotinylation. , 2009, Protein engineering, design & selection : PEDS.
[34] S. Koide,et al. NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-sheet , 1998, Journal of biomolecular NMR.
[35] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[36] Shohei Koide,et al. The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. , 2009, ACS chemical biology.
[37] Shohei Koide,et al. A Dominant Conformational Role for Amino Acid Diversity in Minimalist Protein-protein Interfaces Nih Public Access Introduction , 2022 .
[38] Lode Wyns,et al. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme , 1996, Nature Structural Biology.
[39] M. Tatham,et al. Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9* , 2001, The Journal of Biological Chemistry.
[40] L. Wyns,et al. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[41] A. Koide,et al. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. , 2001, Biochemistry.
[42] E Ruoslahti,et al. Crystal structure of the tenth type III cell adhesion module of human fibronectin. , 1994, Journal of molecular biology.
[43] M. Uhlén,et al. Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain , 1997, Nature Biotechnology.
[44] A. Skerra,et al. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[45] Shohei Koide,et al. High-affinity single-domain binding proteins with a binary-code interface , 2007, Proceedings of the National Academy of Sciences.
[46] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[47] K. Wittrup,et al. Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display. , 2004, Nucleic acids research.
[48] A. Kapila,et al. Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling. , 2008, Journal of molecular biology.
[49] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[50] S. Muyldermans,et al. Naturally occurring antibodies devoid of light chains , 1993, Nature.
[51] Susan Jones,et al. ProtorP: a protein-protein interaction analysis server , 2009, Bioinform..