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Volumn 14, Issue 19-20, 2009, Pages 949-955

FN3: a new protein scaffold reaches the clinic

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CERTOLIZUMAB PEGOL; CT 322; FIBRONECTIN; FIBRONECTIN TYPE 3; IRINOTECAN; UNCLASSIFIED DRUG;

EID: 70349314669     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2009.06.007     Document Type: Review
Times cited : (102)

References (48)
  • 1
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., et al. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284 (1998) 1141-1151
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1
  • 2
    • 34548522063 scopus 로고    scopus 로고
    • Alternative non-antibody scaffolds for molecular recognition
    • Skerra A. Alternative non-antibody scaffolds for molecular recognition. Curr. Opin. Biotechnol. 18 (2007) 295-304
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 295-304
    • Skerra, A.1
  • 3
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M., and Skerra A. Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 13 (2009) 1-11
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 1-11
    • Gebauer, M.1    Skerra, A.2
  • 4
    • 33751347582 scopus 로고    scopus 로고
    • Biopharmaceutical drug discovery using novel protein scaffolds
    • Gill D.S., and Damle N.K. Biopharmaceutical drug discovery using novel protein scaffolds. Curr. Opin. Biotechnol. 17 (2006) 653-658
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 653-658
    • Gill, D.S.1    Damle, N.K.2
  • 5
    • 33646191863 scopus 로고    scopus 로고
    • Ig-like domains on bacteriophages: a tale of promiscuity and deceit
    • Fraser J.S., et al. Ig-like domains on bacteriophages: a tale of promiscuity and deceit. J. Mol. Biol. 59 (2006) 496-507
    • (2006) J. Mol. Biol. , vol.59 , pp. 496-507
    • Fraser, J.S.1
  • 6
    • 0028216926 scopus 로고
    • Crystal structure of the tenth type III cell adhesion module of human fibronectin
    • Dickinson C.D., et al. Crystal structure of the tenth type III cell adhesion module of human fibronectin. J. Mol. Biol. 236 (1994) 1079-1092
    • (1994) J. Mol. Biol. , vol.236 , pp. 1079-1092
    • Dickinson, C.D.1
  • 7
    • 0028997623 scopus 로고
    • Interactions between type III domains in the 110 kDa cell-binding fragment of fibronectin
    • Litvinovich S.V., and Ingham K.C. Interactions between type III domains in the 110 kDa cell-binding fragment of fibronectin. J. Mol. Biol. 248 (1995) 611-626
    • (1995) J. Mol. Biol. , vol.248 , pp. 611-626
    • Litvinovich, S.V.1    Ingham, K.C.2
  • 8
    • 0035793212 scopus 로고    scopus 로고
    • The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold
    • Cota E., et al. The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold. J. Mol. Biol. 305 (2001) 1185-1194
    • (2001) J. Mol. Biol. , vol.305 , pp. 1185-1194
    • Cota, E.1
  • 9
    • 27944505913 scopus 로고    scopus 로고
    • Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors
    • Wang X., et al. Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors. Science 310 (2005) 1159-1163
    • (2005) Science , vol.310 , pp. 1159-1163
    • Wang, X.1
  • 10
    • 0028032203 scopus 로고
    • The x-ray structure of a growth hormone-prolactin receptor complex
    • Somers W., et al. The x-ray structure of a growth hormone-prolactin receptor complex. Nature 372 (1994) 478-481
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1
  • 11
    • 47049105753 scopus 로고    scopus 로고
    • A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces
    • Gilbreth R.N., et al. A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces. J. Mol. Biol. 381 (2008) 407-418
    • (2008) J. Mol. Biol. , vol.381 , pp. 407-418
    • Gilbreth, R.N.1
  • 12
    • 34848892716 scopus 로고    scopus 로고
    • D of a single-domain antibody
    • D of a single-domain antibody. J. Mol. Biol. 373 (2007) 941-953
    • (2007) J. Mol. Biol. , vol.373 , pp. 941-953
    • Koide, A.1
  • 13
    • 33847103076 scopus 로고    scopus 로고
    • Maturation of shark single-domain (IgNAR) antibodies: evidence for induced-fit binding
    • Stanfield R.L., et al. Maturation of shark single-domain (IgNAR) antibodies: evidence for induced-fit binding. J. Mol. Biol. 367 (2007) 358-372
    • (2007) J. Mol. Biol. , vol.367 , pp. 358-372
    • Stanfield, R.L.1
  • 14
    • 35748949254 scopus 로고    scopus 로고
    • Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition
    • Henderson K.L., et al. Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure 15 (2007) 1452-1466
    • (2007) Structure , vol.15 , pp. 1452-1466
    • Henderson, K.L.1
  • 15
    • 34547457742 scopus 로고    scopus 로고
    • Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain
    • Koide A., and Koide S. Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain. Methods Mol. Biol. 352 (2007) 95-109
    • (2007) Methods Mol. Biol. , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 16
    • 0037022351 scopus 로고    scopus 로고
    • Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor
    • Koide A., et al. Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1253-1258
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1253-1258
    • Koide, A.1
  • 17
    • 0037424598 scopus 로고    scopus 로고
    • Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human alphavbeta3 integrin
    • Richards J., et al. Engineered fibronectin type III domain with a RGDWXE sequence binds with enhanced affinity and specificity to human alphavbeta3 integrin. J. Mol. Biol. 326 (2003) 1475-1488
    • (2003) J. Mol. Biol. , vol.326 , pp. 1475-1488
    • Richards, J.1
  • 18
    • 34247098240 scopus 로고    scopus 로고
    • Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies
    • Lipovsek D., et al. Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies. J. Mol. Biol. 368 (2007) 1024-1041
    • (2007) J. Mol. Biol. , vol.368 , pp. 1024-1041
    • Lipovsek, D.1
  • 19
    • 3042633729 scopus 로고    scopus 로고
    • Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain
    • Karatan E., et al. Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain. Chem. Biol. 11 (2004) 835-844
    • (2004) Chem. Biol. , vol.11 , pp. 835-844
    • Karatan, E.1
  • 20
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu L., et al. Directed evolution of high-affinity antibody mimics using mRNA display. Chem. Biol. 9 (2002) 933-942
    • (2002) Chem. Biol. , vol.9 , pp. 933-942
    • Xu, L.1
  • 21
    • 43149097838 scopus 로고    scopus 로고
    • Simple method for production of randomized human tenth fibronectin domain III libraries for use in combinatorial screening procedures
    • Garcia-Ibilcieta D., et al. Simple method for production of randomized human tenth fibronectin domain III libraries for use in combinatorial screening procedures. Biotechniques 44 (2008) 559-562
    • (2008) Biotechniques , vol.44 , pp. 559-562
    • Garcia-Ibilcieta, D.1
  • 22
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • Koide A., et al. High-affinity single-domain binding proteins with a binary-code interface. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 6632-6637
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6632-6637
    • Koide, A.1
  • 23
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • Huang J., et al. Design of protein function leaps by directed domain interface evolution. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 6578-6583
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6578-6583
    • Huang, J.1
  • 24
    • 33646740974 scopus 로고    scopus 로고
    • Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro
    • Getmanova E.V., et al. Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro. Chem. Biol. 13 (2006) 549-556
    • (2006) Chem. Biol. , vol.13 , pp. 549-556
    • Getmanova, E.V.1
  • 25
    • 33847268834 scopus 로고    scopus 로고
    • Design, expression, and stability of a diverse protein library based on the human fibronectin type III domain
    • Olson C.A., and Roberts R.W. Design, expression, and stability of a diverse protein library based on the human fibronectin type III domain. Protein Sci. 16 (2007) 476-484
    • (2007) Protein Sci. , vol.16 , pp. 476-484
    • Olson, C.A.1    Roberts, R.W.2
  • 26
    • 18044391361 scopus 로고    scopus 로고
    • Covalent DNA display as a novel tool for directed evolution of proteins in vitro
    • Bertschinger J., and Neri D. Covalent DNA display as a novel tool for directed evolution of proteins in vitro. Protein Eng. Des. Sel. 17 (2004) 699-707
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 699-707
    • Bertschinger, J.1    Neri, D.2
  • 27
    • 48749101428 scopus 로고    scopus 로고
    • Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling
    • Hackel B.J., et al. Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling. J. Mol. Biol. 381 (2008) 1238-1252
    • (2008) J. Mol. Biol. , vol.381 , pp. 1238-1252
    • Hackel, B.J.1
  • 28
    • 53149108997 scopus 로고    scopus 로고
    • mRNA display selection of a high-affinity, modification-specific phospho-IκBα-binding fibronectin
    • Olson C.A., et al. mRNA display selection of a high-affinity, modification-specific phospho-IκBα-binding fibronectin. ACS Chem. Biol. 3 (2008) 480-485
    • (2008) ACS Chem. Biol. , vol.3 , pp. 480-485
    • Olson, C.A.1
  • 29
    • 66949181440 scopus 로고    scopus 로고
    • Label-free, electrical detection of the SARS virus N-protein with nanowire biosensors utilizing antibody mimics as capture probes
    • Ishikawa F.N., et al. Label-free, electrical detection of the SARS virus N-protein with nanowire biosensors utilizing antibody mimics as capture probes. ACSNano 3 (2009) 1219-1224
    • (2009) ACSNano , vol.3 , pp. 1219-1224
    • Ishikawa, F.N.1
  • 30
    • 34848905895 scopus 로고    scopus 로고
    • Conformational dynamics in loop swap mutants of homologous fibronectin type III domains
    • Siggers K., et al. Conformational dynamics in loop swap mutants of homologous fibronectin type III domains. Biophys. J. 93 (2007) 2447-2456
    • (2007) Biophys. J. , vol.93 , pp. 2447-2456
    • Siggers, K.1
  • 31
    • 36549021676 scopus 로고    scopus 로고
    • Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain
    • Billings K.S., et al. Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. J. Mol. Biol. 375 (2008) 560-571
    • (2008) J. Mol. Biol. , vol.375 , pp. 560-571
    • Billings, K.S.1
  • 32
    • 0036940153 scopus 로고    scopus 로고
    • Exploring the potential of the monobody scaffold: effects of loop elongation on the stability of a fibronectin type III domain
    • Batori V., et al. Exploring the potential of the monobody scaffold: effects of loop elongation on the stability of a fibronectin type III domain. Protein Eng. 12 (2002) 1015-1020
    • (2002) Protein Eng. , vol.12 , pp. 1015-1020
    • Batori, V.1
  • 33
    • 33646560366 scopus 로고    scopus 로고
    • Conformation-specific affinity purification of proteins using engineered binding proteins: application to the estrogen receptor
    • Huang J., et al. Conformation-specific affinity purification of proteins using engineered binding proteins: application to the estrogen receptor. Protein Expr. Purif. 47 (2006) 348-354
    • (2006) Protein Expr. Purif. , vol.47 , pp. 348-354
    • Huang, J.1
  • 34
    • 24044445550 scopus 로고    scopus 로고
    • Antibody mimics based on human fibronectin type three domain engineered for thermostability and high-affinity binding to vascular endothelial growth factor receptor two
    • Parker M.H., et al. Antibody mimics based on human fibronectin type three domain engineered for thermostability and high-affinity binding to vascular endothelial growth factor receptor two. Protein Eng. Des. Sel. 18 (2005) 435-444
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 435-444
    • Parker, M.H.1
  • 35
    • 67650555401 scopus 로고    scopus 로고
    • mRNA display of fibronectin-based intrabodies that detect and inhibit SARS-COV N protein
    • http://www.jbc.org/cgi/doi/10.1074/jbc.M901547200
    • Liao H.I., et al. mRNA display of fibronectin-based intrabodies that detect and inhibit SARS-COV N protein. J. Biol. Chem. (2009) http://www.jbc.org/cgi/doi/10.1074/jbc.M901547200
    • (2009) J. Biol. Chem.
    • Liao, H.I.1
  • 36
    • 27644468373 scopus 로고    scopus 로고
    • High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement
    • Dutta S., et al. High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement. Protein Sci. 14 (2005) 2838-2848
    • (2005) Protein Sci. , vol.14 , pp. 2838-2848
    • Dutta, S.1
  • 37
    • 1542409973 scopus 로고    scopus 로고
    • Accelerated screening of phage-display output with alkaline phosphatase fusions
    • Han Z., et al. Accelerated screening of phage-display output with alkaline phosphatase fusions. Comb. Chem. High Throughput Screen. 7 (2004) 55-62
    • (2004) Comb. Chem. High Throughput Screen. , vol.7 , pp. 55-62
    • Han, Z.1
  • 38
    • 0036645674 scopus 로고    scopus 로고
    • In vitro selection of fibronectin gain-of-function mutations
    • Tani P.H., et al. In vitro selection of fibronectin gain-of-function mutations. Biochem. J. X 365 (2004) 287-294
    • (2004) Biochem. J. X , vol.365 , pp. 287-294
    • Tani, P.H.1
  • 39
    • 3142685154 scopus 로고    scopus 로고
    • In-vitro protein evolution by ribosome display and mRNA display
    • Lipovsek D., and Plückthun A. In-vitro protein evolution by ribosome display and mRNA display. J. Immunol. Methods 290 (2004) 51-67
    • (2004) J. Immunol. Methods , vol.290 , pp. 51-67
    • Lipovsek, D.1    Plückthun, A.2
  • 40
    • 35848950756 scopus 로고    scopus 로고
    • Fibronectin type III domain based monobody with high avidity
    • Duan J., et al. Fibronectin type III domain based monobody with high avidity. Biochemistry 46 (2007) 12656-12664
    • (2007) Biochemistry , vol.46 , pp. 12656-12664
    • Duan, J.1
  • 41
    • 70349339836 scopus 로고    scopus 로고
    • Camphausen, Ray et al. Adnexus. Targeted therapeutics based on engineered proteins for tyrosine kinases receptors, including igf-ir. WO2008066752 (A2)
    • Camphausen, Ray et al. Adnexus. Targeted therapeutics based on engineered proteins for tyrosine kinases receptors, including igf-ir. WO2008066752 (A2)
  • 42
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A., et al. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry 40 (2001) 10326-10333
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1
  • 44
    • 60549096767 scopus 로고    scopus 로고
    • The Adnectin CT-322 is a novel VEGF receptor 2 inhibitor that decreases tumor burden in an orthotopic mouse model of pancreatic cancer
    • 10.1186/1471-2407-8-352
    • Dineen S.P., et al. The Adnectin CT-322 is a novel VEGF receptor 2 inhibitor that decreases tumor burden in an orthotopic mouse model of pancreatic cancer. BMC Cancer (2008). http://www.biomedcentral.com 10.1186/1471-2407-8-352
    • (2008) BMC Cancer
    • Dineen, S.P.1
  • 45
    • 84882538118 scopus 로고    scopus 로고
    • Abstract
    • Sweeney C.J., et al. Abstract. J. Clin. Oncol. 26 20 Suppl. (2008) 2523
    • (2008) J. Clin. Oncol. , vol.26 , Issue.20 SUPPL , pp. 2523
    • Sweeney, C.J.1
  • 46
    • 62549160588 scopus 로고    scopus 로고
    • First-in-class, first-in-human phase I results of targeted agents: Highlights of the 2008 American Society of Clinical Oncology Meeting
    • 10.1186/1756-8722-1-20
    • Molckovsky A., and Siu L.L. First-in-class, first-in-human phase I results of targeted agents: Highlights of the 2008 American Society of Clinical Oncology Meeting. J. Hematol. Oncol. (2008). http://www.jhoonline.org 10.1186/1756-8722-1-20
    • (2008) J. Hematol. Oncol.
    • Molckovsky, A.1    Siu, L.L.2
  • 47
    • 4344634877 scopus 로고    scopus 로고
    • Pharmacokinetic aspects of biotechnology products
    • Tang L., et al. Pharmacokinetic aspects of biotechnology products. J. Pharm. Sci. 93 (2004) 2184-2204
    • (2004) J. Pharm. Sci. , vol.93 , pp. 2184-2204
    • Tang, L.1
  • 48
    • 0036796777 scopus 로고    scopus 로고
    • Efficacy of a novel PEGylated humanized anti-TNF fragment (CDP870) in patients with rheumatoid arthritis: a phase II double-blinded, randomized, dose-escalating trial
    • Choy E.H., et al. Efficacy of a novel PEGylated humanized anti-TNF fragment (CDP870) in patients with rheumatoid arthritis: a phase II double-blinded, randomized, dose-escalating trial. Rheumatology (Oxford) 41 (2002) 1133-1137
    • (2002) Rheumatology (Oxford) , vol.41 , pp. 1133-1137
    • Choy, E.H.1


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