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Volumn 5, Issue 1, 2015, Pages 60-75

Artificial affinity proteins as ligands of immunoglobulins

Author keywords

Affibody; Affitin; Alternative scaffold protein; CBM; DARPin; Fc; Immunoglobulin; Knottin; Monobody

Indexed keywords

ANKYRIN; ANKYRIN REPEAT PROTEIN; CARBOHYDRATE BINDING PROTEIN; FIBRONECTIN BINDING PROTEIN; KNOTTIN; OMALIZUMAB; PEGDINETANIB; PROTEIN G; SCAFFOLD PROTEIN; STAPHYLOCOCCUS PROTEIN A; UNCLASSIFIED DRUG; IMMUNOGLOBULIN; LIGAND; PROTEIN;

EID: 84990306240     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5010060     Document Type: Review
Times cited : (25)

References (85)
  • 1
    • 34447527576 scopus 로고    scopus 로고
    • Affinity-based methodologies and ligands for antibody purification: Advances and perspectives
    • Roque, A. C.; Silva, C. S.; Taipa, M. A. Affinity-based methodologies and ligands for antibody purification: Advances and perspectives. J. Chromatogr. A 2007, 1160, 44-55.
    • (2007) J. Chromatogr. A , vol.1160 , pp. 44-55
    • Roque, A.C.1    Silva, C.S.2    Taipa, M.A.3
  • 2
    • 0021276488 scopus 로고
    • Purification and some properties of streptococcal protein G, a novel IgG-binding reagent
    • Bjorck, L.; Kronvall, G. Purification and some properties of streptococcal protein G, a novel IgG-binding reagent. J. Immunol. 1984, 133, 969-974.
    • (1984) J. Immunol , vol.133 , pp. 969-974
    • Bjorck, L.1    Kronvall, G.2
  • 3
    • 0023853713 scopus 로고
    • Protein L. A novel bacterial cell wall protein with affinity for Ig L chains
    • Bjorck, L. Protein L. A novel bacterial cell wall protein with affinity for Ig L chains. J. Immunol. 1988, 140, 1194-1197.
    • (1988) J. Immunol , vol.140 , pp. 1194-1197
    • Bjorck, L.1
  • 4
    • 0013992053 scopus 로고
    • Protein A from S. aureus. I. Pseudo-immune reaction with human globulin
    • Forsgren, A.; Sjoquist, J. "Protein A" from S. aureus. I. Pseudo-immune reaction with human globulin. J. Immunol. 1966, 97, 822-827.
    • (1966) J. Immunol , vol.97 , pp. 822-827
    • Forsgren, A.1    Sjoquist, J.2
  • 5
    • 0343962157 scopus 로고    scopus 로고
    • Stability towards alkaline conditions can be engineered into a protein ligand
    • Gulich, S.; Linhult, M.; Nygren, P.; Uhlen, M.; Hober, S. Stability towards alkaline conditions can be engineered into a protein ligand. J. Biotechnol. 2000, 80, 169-178.
    • (2000) J. Biotechnol , vol.80 , pp. 169-178
    • Gulich, S.1    Linhult, M.2    Nygren, P.3    Uhlen, M.4    Hober, S.5
  • 6
    • 0037412172 scopus 로고    scopus 로고
    • Engineering streptococcal protein G for increased alkaline stability
    • Gulich, S.; Linhult, M.; Stahl, S.; Hober, S. Engineering streptococcal protein G for increased alkaline stability. Protein Eng. 2002, 15, 835-842.
    • (2002) Protein Eng , vol.15 , pp. 835-842
    • Gulich, S.1    Linhult, M.2    Stahl, S.3    Hober, S.4
  • 7
    • 1842530550 scopus 로고    scopus 로고
    • Improving the tolerance of a protein a analogue to repeated alkaline exposures using a bypass mutagenesis approach
    • Linhult, M.; Gulich, S.; Graslund, T.; Simon, A.; Karlsson, M.; Sjoberg, A.; Nord, K.; Hober, S. Improving the tolerance of a protein a analogue to repeated alkaline exposures using a bypass mutagenesis approach. Proteins 2004, 55, 407-416.
    • (2004) Proteins , vol.55 , pp. 407-416
    • Linhult, M.1    Gulich, S.2    Graslund, T.3    Simon, A.4    Karlsson, M.5    Sjoberg, A.6    Nord, K.7    Hober, S.8
  • 8
    • 41549104499 scopus 로고    scopus 로고
    • Design of stability at extreme alkaline pH in streptococcal protein G
    • Palmer, B.; Angus, K.; Taylor, L.; Warwicker, J.; Derrick, J. P. Design of stability at extreme alkaline pH in streptococcal protein G. J. Biotechnol. 2008, 134, 222-230.
    • (2008) J. Biotechnol , vol.134 , pp. 222-230
    • Palmer, B.1    Angus, K.2    Taylor, L.3    Warwicker, J.4    Derrick, J.P.5
  • 9
    • 34547849601 scopus 로고    scopus 로고
    • Fragments of protein A eluted during protein A affinity chromatography
    • Carter-Franklin, J. N.; Victa, C.; McDonald, P.; Fahrner, R. Fragments of protein A eluted during protein A affinity chromatography. J. Chromatogr. A 2007, 1163, 105-111.
    • (2007) J. Chromatogr. A , vol.1163 , pp. 105-111
    • Carter-Franklin, J.N.1    Victa, C.2    McDonald, P.3    Fahrner, R.4
  • 10
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes, J.; Pluckthun, A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. USA 1997, 94, 4937-4942.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Pluckthun, A.2
  • 11
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 1985, 228, 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 12
    • 1642493921 scopus 로고    scopus 로고
    • Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data
    • Zheng, D.; Aramini, J. M.; Montelione, G. T. Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data. Protein Sci. 2004, 13, 549-554.
    • (2004) Protein Sci , vol.13 , pp. 549-554
    • Zheng, D.1    Aramini, J.M.2    Montelione, G.T.3
  • 15
    • 0030050396 scopus 로고    scopus 로고
    • 2. 0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D. J.; Aukhil, I.; Erickson, H. P. 2. 0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996, 84, 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 16
    • 34548522063 scopus 로고    scopus 로고
    • Alternative non-antibody scaffolds for molecular recognition
    • Skerra, A. Alternative non-antibody scaffolds for molecular recognition. Curr. Opin. Biotechnol. 2007, 18, 295-304.
    • (2007) Curr. Opin. Biotechnol , vol.18 , pp. 295-304
    • Skerra, A.1
  • 17
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer, M.; Skerra, A. Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 2009, 13, 245-255.
    • (2009) Curr. Opin. Chem. Biol , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 18
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz, H. K.; Amstutz, P.; Pluckthun, A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat. Biotechnol. 2005, 23, 1257-1268.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 19
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • Binz, H. K.; Pluckthun, A. Engineered proteins as specific binding reagents. Curr. Opin. Biotechnol. 2005, 16, 459-469.
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 459-469
    • Binz, H.K.1    Pluckthun, A.2
  • 20
    • 84904321648 scopus 로고    scopus 로고
    • Engineered proteins with desired specificity: DARPins, other alternative scaffolds and bispecific IgGs
    • Jost, C.; Pluckthun, A. Engineered proteins with desired specificity: DARPins, other alternative scaffolds and bispecific IgGs. Curr. Opin. Struct. Biol. 2014, 27, 102-112.
    • (2014) Curr. Opin. Struct. Biol , vol.27 , pp. 102-112
    • Jost, C.1    Pluckthun, A.2
  • 21
    • 0021328728 scopus 로고
    • Complete sequence of the staphylococcal gene encoding protein A. A gene evolved through multiple duplications
    • Uhlen, M.; Guss, B.; Nilsson, B.; Gatenbeck, S.; Philipson, L.; Lindberg, M. Complete sequence of the staphylococcal gene encoding protein A. A gene evolved through multiple duplications. J. Biol. Chem. 1984, 259, 1695-1702.
    • (1984) J. Biol. Chem , vol.259 , pp. 1695-1702
    • Uhlen, M.1    Guss, B.2    Nilsson, B.3    Gatenbeck, S.4    Philipson, L.5    Lindberg, M.6
  • 23
    • 0028982245 scopus 로고
    • A combinatorial library of an helical bacterial receptor domain
    • Nord, K.; Nilsson, J.; Nilsson, B.; Uhlen, M.; Nygren, P. A. A combinatorial library of an helical bacterial receptor domain. Protein Eng. 1995, 8, 601-608.
    • (1995) Protein Eng , vol.8 , pp. 601-608
    • Nord, K.1    Nilsson, J.2    Nilsson, B.3    Uhlen, M.4    Nygren, P.A.5
  • 24
    • 80054079725 scopus 로고    scopus 로고
    • Ribosome display selection of a murine IgG1 Fab binding affibody molecule allowing species selective recovery of monoclonal antibodies
    • Grimm, S.; Yu, F.; Nygren, P. A. Ribosome display selection of a murine IgG1 Fab binding affibody molecule allowing species selective recovery of monoclonal antibodies. Mol. Biotechnol. 2011, 48, 263-276.
    • (2011) Mol. Biotechnol , vol.48 , pp. 263-276
    • Grimm, S.1    Yu, F.2    Nygren, P.A.3
  • 28
  • 30
    • 77953130101 scopus 로고    scopus 로고
    • Affibody molecules: Engineered proteins for therapeutic, diagnostic and biotechnological applications
    • Löfblom, J.; Feldwisch, J.; Tolmachev, V.; Carlsson, J.; Ståhl, S.; Frejd, F. Y. Affibody molecules: Engineered proteins for therapeutic, diagnostic and biotechnological applications. FEBS Lett. 2010, 584, 2670-2680.
    • (2010) FEBS Lett , vol.584 , pp. 2670-2680
    • Löfblom, J.1    Feldwisch, J.2    Tolmachev, V.3    Carlsson, J.4    Ståhl, S.5    Frejd, F.Y.6
  • 32
    • 0036275295 scopus 로고    scopus 로고
    • Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A
    • Ronnmark, J.; Gronlund, H.; Uhlen, M.; Nygren, P. A. Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A. Eur. J. Biochem. 2002, 269, 2647-2655.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2647-2655
    • Ronnmark, J.1    Gronlund, H.2    Uhlen, M.3    Nygren, P.A.4
  • 33
    • 0032826457 scopus 로고    scopus 로고
    • Staphylococcal surface display of immunoglobulin A (IgA)-and IgE-specific in vitro-selected binding proteins (affibodies) based on Staphylococcus aureus protein A
    • Gunneriusson, E.; Samuelson, P.; Ringdahl, J.; Gronlund, H.; Nygren, P. A.; Stahl, S. Staphylococcal surface display of immunoglobulin A (IgA)-and IgE-specific in vitro-selected binding proteins (affibodies) based on Staphylococcus aureus protein A. Appl. Environ. Microbiol. 1999, 65, 4134-4140.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 4134-4140
    • Gunneriusson, E.1    Samuelson, P.2    Ringdahl, J.3    Gronlund, H.4    Nygren, P.A.5    Stahl, S.6
  • 34
    • 79957773363 scopus 로고    scopus 로고
    • Highly stable binding proteins derived from the hyperthermophilic Sso7d scaffold
    • Gera, N.; Hussain, M.; Wright, R. C.; Rao, B. M. Highly stable binding proteins derived from the hyperthermophilic Sso7d scaffold. J. Mol. Biol. 2011, 409, 601-616.
    • (2011) J. Mol. Biol , vol.409 , pp. 601-616
    • Gera, N.1    Hussain, M.2    Wright, R.C.3    Rao, B.M.4
  • 35
    • 84868711258 scopus 로고    scopus 로고
    • Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold
    • Gera, N.; Hill, A. B.; White, D. P.; Carbonell, R. G.; Rao, B. M. Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold. PLOS ONE 2012, 7, e48928.
    • (2012) PLOS ONE , vol.7
    • Gera, N.1    Hill, A.B.2    White, D.P.3    Carbonell, R.G.4    Rao, B.M.5
  • 36
    • 84875580431 scopus 로고    scopus 로고
    • Scaffold diversification enhances effectiveness of a superlibrary of hyperthermophilic proteins
    • Hussain, M.; Gera, N.; Hill, A. B.; Rao, B. M. Scaffold diversification enhances effectiveness of a superlibrary of hyperthermophilic proteins. ACS Synth. Biol. 2013, 2, 6-13.
    • (2013) ACS Synth. Biol , vol.2 , pp. 6-13
    • Hussain, M.1    Gera, N.2    Hill, A.B.3    Rao, B.M.4
  • 39
    • 51349091340 scopus 로고    scopus 로고
    • Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display
    • Steiner, D.; Forrer, P.; Pluckthun, A. Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display. J. Mol. Biol. 2008, 382, 1211-1227.
    • (2008) J. Mol. Biol , vol.382 , pp. 1211-1227
    • Steiner, D.1    Forrer, P.2    Pluckthun, A.3
  • 41
    • 79958110928 scopus 로고    scopus 로고
    • Inhibition of ongoing allergic reactions using a novel anti-IgE DARPin-Fc fusion protein
    • Eggel, A.; Buschor, P.; Baumann, M. J.; Amstutz, P.; Stadler, B. M.; Vogel, M. Inhibition of ongoing allergic reactions using a novel anti-IgE DARPin-Fc fusion protein. Allergy 2011, 66, 961-968.
    • (2011) Allergy , vol.66 , pp. 961-968
    • Eggel, A.1    Buschor, P.2    Baumann, M.J.3    Amstutz, P.4    Stadler, B.M.5    Vogel, M.6
  • 42
    • 18544368988 scopus 로고    scopus 로고
    • New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold
    • Souriau, C.; Chiche, L.; Irving, R.; Hudson, P. New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold. Biochemistry 2005, 44, 7143-7155.
    • (2005) Biochemistry , vol.44 , pp. 7143-7155
    • Souriau, C.1    Chiche, L.2    Irving, R.3    Hudson, P.4
  • 43
    • 77954757013 scopus 로고    scopus 로고
    • Stability and CDR composition biases enrich binder functionality landscapes
    • Hackel, B. J.; Ackerman, M. E.; Howland, S. W.; Wittrup, K. D. Stability and CDR composition biases enrich binder functionality landscapes. J. Mol. Biol. 2010, 401, 84-96.
    • (2010) J. Mol. Biol , vol.401 , pp. 84-96
    • Hackel, B.J.1    Ackerman, M.E.2    Howland, S.W.3    Wittrup, K.D.4
  • 44
    • 77954626231 scopus 로고    scopus 로고
    • The full amino acid repertoire is superior to serine/tyrosine for selection of high affinity immunoglobulin G binders from the fibronectin scaffold
    • Hackel, B. J.; Wittrup, K. D. The full amino acid repertoire is superior to serine/tyrosine for selection of high affinity immunoglobulin G binders from the fibronectin scaffold. Protein Eng. Des. Sel. 2010, 23, 211-219.
    • (2010) Protein Eng. Des. Sel , vol.23 , pp. 211-219
    • Hackel, B.J.1    Wittrup, K.D.2
  • 47
    • 53549101897 scopus 로고    scopus 로고
    • Artificial binding proteins (Affitins) as probes for conformational changes in secretin PulD
    • Krehenbrink, M.; Chami, M.; Guilvout, I.; Alzari, P. M.; Pecorari, F.; Pugsley, A. P. Artificial binding proteins (Affitins) as probes for conformational changes in secretin PulD. J. Mol. Biol. 2008, 383, 1058-1068.
    • (2008) J. Mol. Biol , vol.383 , pp. 1058-1068
    • Krehenbrink, M.1    Chami, M.2    Guilvout, I.3    Alzari, P.M.4    Pecorari, F.5    Pugsley, A.P.6
  • 48
    • 84909582000 scopus 로고    scopus 로고
    • Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability
    • Béhar, G.; Pacheco, S.; Maillasson, M.; Mouratou, B.; Pecorari, F. Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability. J. Biotechnol. 2014, 192A, 123-129.
    • (2014) J. Biotechnol , vol.192 A , pp. 123-129
    • Béhar, G.1    Pacheco, S.2    Maillasson, M.3    Mouratou, B.4    Pecorari, F.5
  • 49
    • 0030582620 scopus 로고    scopus 로고
    • Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d
    • McCrary, B. S.; Edmondson, S. P.; Shriver, J. W. Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d. J. Mol. Biol. 1996, 264, 784-805.
    • (1996) J. Mol. Biol , vol.264 , pp. 784-805
    • McCrary, B.S.1    Edmondson, S.P.2    Shriver, J.W.3
  • 50
    • 0034986024 scopus 로고    scopus 로고
    • DNA binding proteins Sac7d and Sso7d from Sulfolobus
    • Edmondson, S. P.; Shriver, J. W. DNA binding proteins Sac7d and Sso7d from Sulfolobus. Methods Enzymol. 2001, 334, 129-145.
    • (2001) Methods Enzymol , vol.334 , pp. 129-145
    • Edmondson, S.P.1    Shriver, J.W.2
  • 52
    • 84873284075 scopus 로고    scopus 로고
    • Avidity-mediated virus separation using a hyperthermophilic affinity ligand
    • Hussain, M.; Lockney, D.; Wang, R.; Gera, N.; Rao, B. M. Avidity-mediated virus separation using a hyperthermophilic affinity ligand. Biotechnol. Prog. 2013, 29, 237-246.
    • (2013) Biotechnol. Prog , vol.29 , pp. 237-246
    • Hussain, M.1    Lockney, D.2    Wang, R.3    Gera, N.4    Rao, B.M.5
  • 53
    • 58149503629 scopus 로고    scopus 로고
    • Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane
    • Buddelmeijer, N.; Krehenbrink, M.; Pecorari, F.; Pugsley, A. P. Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane. J. Bacteriol. 2009, 191, 161-168.
    • (2009) J. Bacteriol , vol.191 , pp. 161-168
    • Buddelmeijer, N.1    Krehenbrink, M.2    Pecorari, F.3    Pugsley, A.P.4
  • 55
  • 57
    • 33645457940 scopus 로고    scopus 로고
    • Evolution of a carbohydrate binding module into a protein-specific binder
    • Gunnarsson, L. C.; Dexlin, L.; Karlsson, E. N.; Holst, O.; Ohlin, M. Evolution of a carbohydrate binding module into a protein-specific binder. Biomol. Eng. 2006, 23, 111-117.
    • (2006) Biomol. Eng , vol.23 , pp. 111-117
    • Gunnarsson, L.C.1    Dexlin, L.2    Karlsson, E.N.3    Holst, O.4    Ohlin, M.5
  • 58
    • 33845934490 scopus 로고    scopus 로고
    • Ankyrin repeat: A unique motif mediating protein-protein interactions
    • Li, J.; Mahajan, A.; Tsai, M. D. Ankyrin repeat: A unique motif mediating protein-protein interactions. Biochemistry 2006, 45, 15168-15178.
    • (2006) Biochemistry , vol.45 , pp. 15168-15178
    • Li, J.1    Mahajan, A.2    Tsai, M.D.3
  • 59
    • 0042780350 scopus 로고    scopus 로고
    • 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.; Pluckthun, A. Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 2003, 332, 489-503.
    • (2003) J. Mol. Biol , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Pluckthun, A.5
  • 60
    • 84892544158 scopus 로고    scopus 로고
    • From DARPins to LoopDARPins: Novel LoopDARPin design allows the selection of low picomolar binders in a single round of ribosome display
    • Schilling, J.; Schöppe, J.; Plückthun, A. From DARPins to LoopDARPins: Novel LoopDARPin design allows the selection of low picomolar binders in a single round of ribosome display. J. Mol. Biol. 2014, 426, 691-721.
    • (2014) J. Mol. Biol , vol.426 , pp. 691-721
    • Schilling, J.1    Schöppe, J.2    Plückthun, A.3
  • 64
    • 21744440783 scopus 로고    scopus 로고
    • Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins
    • Amstutz, P.; Binz, H. K.; Parizek, P.; Stumpp, M. T.; Kohl, A.; Grutter, M. G.; Forrer, P.; Pluckthun, A. Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins. J. Biol. Chem. 2005, 280, 24715-24722.
    • (2005) J. Biol. Chem , vol.280 , pp. 24715-24722
    • Amstutz, P.1    Binz, H.K.2    Parizek, P.3    Stumpp, M.T.4    Kohl, A.5    Grutter, M.G.6    Forrer, P.7    Pluckthun, A.8
  • 65
    • 33845939857 scopus 로고    scopus 로고
    • Selection and characterisation of HER2-binding designed ankyrin repeat proteins
    • Zahnd, C.; Pecorari, F.; Straumann, N.; Wyler, E.; Pluckthun, A. Selection and characterisation of HER2-binding designed ankyrin repeat proteins. J. Biol. Chem. 2006, 281, 9.
    • (2006) J. Biol. Chem , vol.281
    • Zahnd, C.1    Pecorari, F.2    Straumann, N.3    Wyler, E.4    Pluckthun, A.5
  • 68
    • 78751503899 scopus 로고    scopus 로고
    • A novel fusion toxin derived from an EpCAM-specific designed ankyrin repeat protein has potent antitumor activity
    • Martin-Killias, P.; Stefan, N.; Rothschild, S.; Pluckthun, A.; Zangemeister-Wittke, U. A novel fusion toxin derived from an EpCAM-specific designed ankyrin repeat protein has potent antitumor activity. Clin. Cancer Res. 2011, 17, 100-110.
    • (2011) Clin. Cancer Res , vol.17 , pp. 100-110
    • Martin-Killias, P.1    Stefan, N.2    Rothschild, S.3    Pluckthun, A.4    Zangemeister-Wittke, U.5
  • 70
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot
    • Colgrave, M. L.; Craik, D. J. Thermal, chemical, and enzymatic stability of the cyclotide kalata B1: The importance of the cyclic cystine knot. Biochemistry 2004, 43, 5965-5975.
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 71
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded sheet in toxic and inhibitory polypeptides
    • Pallaghy, P. K.; Nielsen, K. J.; Craik, D. J.; Norton, R. S. A common structural motif incorporating a cystine knot and a triple-stranded sheet in toxic and inhibitory polypeptides. Protein Sci. 1994, 3, 1833-1839.
    • (1994) Protein Sci , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 72
    • 0033543156 scopus 로고    scopus 로고
    • Min-21 and min-23, the smallest peptides that fold like a cystine-stabilized sheet motif: Design, solution structure, and thermal stability
    • Heitz, A.; le-Nguyen, D.; Chiche, L. Min-21 and min-23, the smallest peptides that fold like a cystine-stabilized sheet motif: Design, solution structure, and thermal stability. Biochemistry 1999, 38, 10615-10625.
    • (1999) Biochemistry , vol.38 , pp. 10615-10625
    • Heitz, A.1    le-Nguyen, D.2    Chiche, L.3
  • 73
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide, A.; Bailey, C. W.; Huang, X.; Koide, S. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 1998, 284, 1141-1151.
    • (1998) J. Mol. Biol , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 75
    • 84855802142 scopus 로고    scopus 로고
    • Teaching an old scaffold new tricks: Monobodies constructed using alternative surfaces of the FN3 scaffold
    • Koide, A.; Wojcik, J.; Gilbreth, R. N.; Hoey, R. J.; Koide, S. Teaching an old scaffold new tricks: Monobodies constructed using alternative surfaces of the FN3 scaffold. J. Mol. Biol. 2012, 415, 393-405.
    • (2012) J. Mol. Biol , vol.415 , pp. 393-405
    • Koide, A.1    Wojcik, J.2    Gilbreth, R.N.3    Hoey, R.J.4    Koide, S.5
  • 76
    • 48749101428 scopus 로고    scopus 로고
    • Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling
    • Hackel, B. J.; Kapila, A.; Wittrup, K. D. Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling. J. Mol. Biol. 2008, 381, 1238-1252.
    • (2008) J. Mol. Biol , vol.381 , pp. 1238-1252
    • Hackel, B.J.1    Kapila, A.2    Wittrup, K.D.3
  • 77
    • 34547457742 scopus 로고    scopus 로고
    • Monobodies: Antibody mimics based on the scaffold of the fibronectin type III domain
    • Koide, A.; Koide, S. Monobodies: Antibody mimics based on the scaffold of the fibronectin type III domain. Methods Mol. Biol. 2007, 352, 95-109.
    • (2007) Methods Mol. Biol , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 80
    • 84892615437 scopus 로고    scopus 로고
    • Computational design of a pH-sensitive IgG binding protein
    • Strauch, E. M.; Fleishman, S. J.; Baker, D. Computational design of a pH-sensitive IgG binding protein. Proc. Natl. Acad. Sci. USA 2014, 111, 675-680.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 675-680
    • Strauch, E.M.1    Fleishman, S.J.2    Baker, D.3
  • 81
    • 0029120867 scopus 로고
    • Tendamistat as a scaffold for conformationally constrained phage peptide libraries
    • McConnell, S. J.; Hoess, R. H. Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J. Mol. Biol. 1995, 250, 460-470.
    • (1995) J. Mol. Biol , vol.250 , pp. 460-470
    • McConnell, S.J.1    Hoess, R.H.2
  • 83
    • 0032956429 scopus 로고    scopus 로고
    • Engineering a regulatable enzyme for homogeneous immunoassays
    • Legendre, D.; Soumillion, P.; Fastrez, J. Engineering a regulatable enzyme for homogeneous immunoassays. Nat. Biotechnol. 1999, 17, 67-72.
    • (1999) Nat. Biotechnol , vol.17 , pp. 67-72
    • Legendre, D.1    Soumillion, P.2    Fastrez, J.3
  • 85
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein interactions
    • Lu, Z.; Murray, K. S.; van Cleave, V.; LaVallie, E. R.; Stahl, M. L.; McCoy, J. M. Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein interactions. Nat. Biotechnol. 1995, 13, 366-372.
    • (1995) Nat. Biotechnol , vol.13 , pp. 366-372
    • Lu, Z.1    Murray, K.S.2    van Cleave, V.3    LaVallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.