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Volumn 209, Issue 5, 2015, Pages 633-644

Nanobodies and recombinant binders in cell biology

Author keywords

[No Author keywords available]

Indexed keywords

NANOBODY; REAGENT; RECOMBINANT ANTIBODY;

EID: 84945195539     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201409074     Document Type: Review
Times cited : (176)

References (130)
  • 1
    • 84892960113 scopus 로고    scopus 로고
    • Probing the N-terminal ß-sheet conversion in the crystal structure of the human prion protein bound to a nanobody
    • Abskharon, R.N., G. Giachin, A. Wohlkonig, S.H. Soror, E. Pardon, G. Legname, and J. Steyaert. 2014. Probing the N-terminal ß-sheet conversion in the crystal structure of the human prion protein bound to a nanobody. J. Am. Chem. Soc. 136:937-944. http://dx.doi.org/10.1021/ja407527p
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 937-944
    • Abskharon, R.N.1    Giachin, G.2    Wohlkonig, A.3    Soror, S.H.4    Pardon, E.5    Legname, G.6    Steyaert, J.7
  • 2
    • 84889586902 scopus 로고    scopus 로고
    • Synthetic antibody technologies
    • Adams, J.J., and S.S. Sidhu. 2014. Synthetic antibody technologies. Curr. Opin. Struct. Biol. 24:1-9. http://dx.doi.org/10.1016/j.sbi.2013.11.003
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 1-9
    • Adams, J.J.1    Sidhu, S.S.2
  • 3
    • 77649148783 scopus 로고    scopus 로고
    • Functional diversity of ankyrin repeats in microbial proteins
    • Al-Khodor, S., C.T. Price, A. Kalia, and Y. Abu Kwaik. 2010. Functional diversity of ankyrin repeats in microbial proteins. Trends Microbiol. 18:132-139. http://dx.doi.org/10.1016/j.tim.2009.11.004
    • (2010) Trends Microbiol. , vol.18 , pp. 132-139
    • Al-Khodor, S.1    Price, C.T.2    Kalia, A.3    Abu Kwaik, Y.4
  • 6
    • 0033515005 scopus 로고    scopus 로고
    • Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
    • Beste, G., F.S. Schmidt, T. Stibora, and A. Skerra. 1999. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl. Acad. Sci. USA. 96:1898-1903. http://dx.doi.org/10.1073/pnas.96.5.1898
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 1898-1903
    • Beste, G.1    Schmidt, F.S.2    Stibora, T.3    Skerra, A.4
  • 7
    • 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., M.T. Stumpp, P. Forrer, P. Amstutz, and A. Plückthun. 2003. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332:489-503. http://dx.doi.org/10.1016/S0022-2836(03)00896-9
    • (2003) J. Mol. Biol. , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 8
    • 0036517707 scopus 로고    scopus 로고
    • Self-immobilizing recombinant antibody fragments for immunoaffinity chromatography: generic, parallel, and scalable protein purification
    • Blank, K., P. Lindner, B. Diefenbach, and A. Plückthun. 2002. Self-immobilizing recombinant antibody fragments for immunoaffinity chromatography: generic, parallel, and scalable protein purification. Protein Expr. Purif. 24:313-322. http://dx.doi.org/10.1006/prep.2001.1575
    • (2002) Protein Expr. Purif. , vol.24 , pp. 313-322
    • Blank, K.1    Lindner, P.2    Diefenbach, B.3    Plückthun, A.4
  • 9
    • 33947155314 scopus 로고    scopus 로고
    • Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage
    • Bowley, D.R., A.F. Labrijn, M.B. Zwick, and D.R. Burton. 2007. Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage. Protein Eng. Des. Sel. 20:81-90. http://dx.doi.org/10.1093/protein/gzl057
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 81-90
    • Bowley, D.R.1    Labrijn, A.F.2    Zwick, M.B.3    Burton, D.R.4
  • 10
    • 84923206397 scopus 로고    scopus 로고
    • Reproducibility: Standardize antibodies used in research
    • Bradbury, A., and A. Plückthun. 2015. Reproducibility: Standardize antibodies used in research. Nature. 518:27-29. http://dx.doi.org/10.1038/518027a
    • (2015) Nature. , vol.518 , pp. 27-29
    • Bradbury, A.1    Plückthun, A.2
  • 12
    • 84866702125 scopus 로고    scopus 로고
    • Quantitative live imaging of endogenous DNA replication in mammalian cells
    • Burgess, A., T. Lorca, and A. Castro. 2012. Quantitative live imaging of endogenous DNA replication in mammalian cells. PLoS ONE. 7:e45726. http://dx.doi.org/10.1371/journal.pone.0045726
    • (2012) PLoS ONE. , vol.7
    • Burgess, A.1    Lorca, T.2    Castro, A.3
  • 13
    • 77955823113 scopus 로고    scopus 로고
    • Plasma proteome profiling reveals biomarker patterns associated with prognosis and therapy selection in glioblastoma multiforme patients
    • Carlsson, A., O. Persson, J. Ingvarsson, B. Widegren, L. Salford, C.A. Borrebaeck, and C. Wingren. 2010. Plasma proteome profiling reveals biomarker patterns associated with prognosis and therapy selection in glioblastoma multiforme patients. Proteomics Clin. Appl. 4:591-602. http://dx.doi.org/10.1002/prca.200900173
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 591-602
    • Carlsson, A.1    Persson, O.2    Ingvarsson, J.3    Widegren, B.4    Salford, L.5    Borrebaeck, C.A.6    Wingren, C.7
  • 14
    • 79955747971 scopus 로고    scopus 로고
    • Serum protein profiling of systemic lupus erythematosus and systemic sclerosis using recombinant antibody microarrays
    • M110.005033
    • Carlsson, A., D.M. Wuttge, J. Ingvarsson, A.A. Bengtsson, G. Sturfelt, C.A. Borrebaeck, and C. Wingren. 2011. Serum protein profiling of systemic lupus erythematosus and systemic sclerosis using recombinant antibody microarrays. Mol. Cell. Proteomics. 10:M110.005033. http://dx.doi.org/10.1074/mcp.M110.005033
    • (2011) Mol. Cell. Proteomics. , vol.10
    • Carlsson, A.1    Wuttge, D.M.2    Ingvarsson, J.3    Bengtsson, A.A.4    Sturfelt, G.5    Borrebaeck, C.A.6    Wingren, C.7
  • 15
    • 84871231720 scopus 로고    scopus 로고
    • Targeted manipulation of heterochromatin rescues MeCP2 Rett mutants and re-establishes higher order chromatin organization
    • Casas-Delucchi, C.S., A. Becker, J.J. Bolius, and M.C. Cardoso. 2012. Targeted manipulation of heterochromatin rescues MeCP2 Rett mutants and re-establishes higher order chromatin organization. Nucleic Acids Res. 40:e176. http://dx.doi.org/10.1093/nar/gks784
    • (2012) Nucleic Acids Res. , vol.40
    • Casas-Delucchi, C.S.1    Becker, A.2    Bolius, J.J.3    Cardoso, M.C.4
  • 16
    • 84855425542 scopus 로고    scopus 로고
    • Fluorescent fusion protein knockout mediated by anti-GFP nanobody
    • Caussinus, E., O. Kanca, and M. Affolter. 2012. Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nat. Struct. Mol. Biol. 19:117-121. http://dx.doi.org/10.1038/nsmb.2180
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 117-121
    • Caussinus, E.1    Kanca, O.2    Affolter, M.3
  • 18
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. The packing of variable domains
    • Chothia, C., J. Novotnỳ, R. Bruccoleri, and M. Karplus. 1985. Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186:651-663. http://dx.doi.org/10.1016/0022-2836(85)90137-8
    • (1985) J. Mol. Biol. , vol.186 , pp. 651-663
    • Chothia, C.1    Novotnỳ, J.2    Bruccoleri, R.3    Karplus, M.4
  • 19
    • 79959851876 scopus 로고    scopus 로고
    • A roadmap to generate renewable protein binders to the human proteome
    • Colwill, K., Renewable Protein Binder Working Group, and S. Gräslund. 2011. A roadmap to generate renewable protein binders to the human proteome. Nat. Methods. 8:551-558. http://dx.doi.org/10.1038/nmeth.1607
    • (2011) Nat. Methods. , vol.8 , pp. 551-558
    • Colwill, K.1    Gräslund, S.2
  • 20
  • 21
    • 34247580832 scopus 로고    scopus 로고
    • JNK pathway: diseases and therapeutic potential
    • Cui, J., M. Zhang, Y.Q. Zhang, and Z.H. Xu. 2007. JNK pathway: diseases and therapeutic potential. Acta Pharmacol. Sin. 28:601-608. http://dx.doi.org/10.1111/j.1745-7254.2007.00579.x
    • (2007) Acta Pharmacol. Sin. , vol.28 , pp. 601-608
    • Cui, J.1    Zhang, M.2    Zhang, Y.Q.3    Xu, Z.H.4
  • 23
    • 77952022366 scopus 로고    scopus 로고
    • Application of protein engineering to enhance crystallizability and improve crystal properties
    • Derewenda, Z.S. 2010. Application of protein engineering to enhance crystallizability and improve crystal properties. Acta Crystallogr. D Biol. Crystallogr. 66:604-615. http://dx.doi.org/10.1107/S090744491000644X
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 604-615
    • Derewenda, Z.S.1
  • 26
    • 84894986114 scopus 로고    scopus 로고
    • Structure-guided engineering of Anticalins with improved binding behavior and biochemical characteristics for application in radio-immuno imaging and/or therapy
    • Eggenstein, E., A. Eichinger, H.J. Kim, and A. Skerra. 2014. Structure-guided engineering of Anticalins with improved binding behavior and biochemical characteristics for application in radio-immuno imaging and/or therapy. J. Struct. Biol. 185:203-214. http://dx.doi.org/10.1016/j.jsb.2013.03.009
    • (2014) J. Struct. Biol. , vol.185 , pp. 203-214
    • Eggenstein, E.1    Eichinger, A.2    Kim, H.J.3    Skerra, A.4
  • 28
    • 0037468685 scopus 로고    scopus 로고
    • A novel strategy to design binding molecules harnessing the modular nature of repeat proteins
    • Forrer, P., M.T. Stumpp, H.K. Binz, and A. Plückthun. 2003. A novel strategy to design binding molecules harnessing the modular nature of repeat proteins. FEBS Lett. 539:2-6. http://dx.doi.org/10.1016/S0014-5793(03)00177-7
    • (2003) FEBS Lett. , vol.539 , pp. 2-6
    • Forrer, P.1    Stumpp, M.T.2    Binz, H.K.3    Plückthun, A.4
  • 29
    • 63349087781 scopus 로고    scopus 로고
    • A versatile non-radioactive assay for DNA methyltransferase activity and DNA binding
    • Frauer, C., and H. Leonhardt. 2009. A versatile non-radioactive assay for DNA methyltransferase activity and DNA binding. Nucleic Acids Res. 37:e22. http://dx.doi.org/10.1093/nar/gkn1029
    • (2009) Nucleic Acids Res. , vol.37
    • Frauer, C.1    Leonhardt, H.2
  • 32
    • 84873414124 scopus 로고    scopus 로고
    • Combinatorial design of an Anticalin directed against the extra-domain b for the specific targeting of oncofetal fibronectin
    • Gebauer, M., A. Schiefner, G. Matschiner, and A. Skerra. 2013. Combinatorial design of an Anticalin directed against the extra-domain b for the specific targeting of oncofetal fibronectin. J. Mol. Biol. 425:780-802. http://dx.doi.org/10.1016/j.jmb.2012.12.004
    • (2013) J. Mol. Biol. , vol.425 , pp. 780-802
    • Gebauer, M.1    Schiefner, A.2    Matschiner, G.3    Skerra, A.4
  • 33
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good, M.C., J.G. Zalatan, and W.A. Lim. 2011. Scaffold proteins: hubs for controlling the flow of cellular information. Science. 332:680-686. http://dx.doi.org/10.1126/science.1198701
    • (2011) Science. , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 34
    • 34047244187 scopus 로고    scopus 로고
    • A novel, non-immunogenic Fyn SH3-derived binding protein with tumor vascular targeting properties
    • Grabulovski, D., M. Kaspar, and D. Neri. 2007. A novel, non-immunogenic Fyn SH3-derived binding protein with tumor vascular targeting properties. J. Biol. Chem. 282:3196-3204. http://dx.doi.org/10.1074/jbc.M609211200
    • (2007) J. Biol. Chem. , vol.282 , pp. 3196-3204
    • Grabulovski, D.1    Kaspar, M.2    Neri, D.3
  • 40
    • 84923108892 scopus 로고    scopus 로고
    • Multiplex single-molecule interaction profiling of DNA-barcoded proteins
    • Gu, L., C. Li, J. Aach, D.E. Hill, M. Vidal, and G.M. Church. 2014. Multiplex single-molecule interaction profiling of DNA-barcoded proteins. Nature. 515:554-557. http://dx.doi.org/10.1038/nature13761
    • (2014) Nature. , vol.515 , pp. 554-557
    • Gu, L.1    Li, C.2    Aach, J.3    Hill, D.E.4    Vidal, M.5    Church, G.M.6
  • 44
    • 0034524838 scopus 로고    scopus 로고
    • Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features
    • Harmsen, M.M., R.C. Ruuls, I.J. Nijman, T.A. Niewold, L.G. Frenken, and B. de Geus. 2000. Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. Mol. Immunol. 37:579-590. http://dx.doi.org/10.1016/S0161-5890(00)00081-X
    • (2000) Mol. Immunol. , vol.37 , pp. 579-590
    • Harmsen, M.M.1    Ruuls, R.C.2    Nijman, I.J.3    Niewold, T.A.4    Frenken, L.G.5    de Geus, B.6
  • 46
    • 84886668282 scopus 로고    scopus 로고
    • Visualization and targeted disruption of protein interactions in living cells
    • Herce, H.D., W. Deng, J. Helma, H. Leonhardt, and M.C. Cardoso. 2013. Visualization and targeted disruption of protein interactions in living cells. Nat. Commun. 4:2660. http://dx.doi.org/10.1038/ncomms3660
    • (2013) Nat. Commun. , vol.4 , pp. 2660
    • Herce, H.D.1    Deng, W.2    Helma, J.3    Leonhardt, H.4    Cardoso, M.C.5
  • 47
    • 21444439732 scopus 로고    scopus 로고
    • Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity
    • Hoet, R.M., E.H. Cohen, R.B. Kent, K. Rookey, S. Schoonbroodt, S. Hogan, L. Rem, N. Frans, M. Daukandt, H. Pieters, et al. 2005. Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity. Nat. Biotechnol. 23:344-348. http://dx.doi.org/10.1038/nbt1067
    • (2005) Nat. Biotechnol. , vol.23 , pp. 344-348
    • Hoet, R.M.1    Cohen, E.H.2    Kent, R.B.3    Rookey, K.4    Schoonbroodt, S.5    Hogan, S.6    Rem, L.7    Frans, N.8    Daukandt, M.9    Pieters, H.10
  • 48
    • 0346965990 scopus 로고    scopus 로고
    • Expression of GFP-actin leads to failure of nuclear elongation and cytokinesis in Tetrahymena thermophila
    • Hosein, R.E., S.A. Williams, K. Haye, and R.H. Gavin. 2003. Expression of GFP-actin leads to failure of nuclear elongation and cytokinesis in Tetrahymena thermophila. J. Eukaryot. Microbiol. 50:403-408. http://dx.doi.org/10.1111/j.1550-7408.2003.tb00261.x
    • (2003) J. Eukaryot. Microbiol. , vol.50 , pp. 403-408
    • Hosein, R.E.1    Williams, S.A.2    Haye, K.3    Gavin, R.H.4
  • 49
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a ß-hairpin in monomeric Alzheimer's amyloid-ß peptide inhibits amyloid formation
    • Hoyer, W., C. Grönwall, A. Jonsson, S. Ståhl, and T. Härd. 2008. Stabilization of a ß-hairpin in monomeric Alzheimer's amyloid-ß peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. USA. 105:5099-5104. http://dx.doi.org/10.1073/pnas.0711731105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 5099-5104
    • Hoyer, W.1    Grönwall, C.2    Jonsson, A.3    Ståhl, S.4    Härd, T.5
  • 50
    • 84555177672 scopus 로고    scopus 로고
    • SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells
    • Hussain, A.F., F. Kampmeier, V. von Felbert, H.F. Merk, M.K. Tur, and S. Barth. 2011. SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells. Bioconjug. Chem. 22:2487-2495. http://dx.doi.org/10.1021/bc200304k
    • (2011) Bioconjug. Chem. , vol.22 , pp. 2487-2495
    • Hussain, A.F.1    Kampmeier, F.2    von Felbert, V.3    Merk, H.F.4    Tur, M.K.5    Barth, S.6
  • 53
    • 0037225784 scopus 로고    scopus 로고
    • Immunomodulation of enzyme function in plants by single-domain antibody fragments
    • Jobling, S.A., C. Jarman, M.M. Teh, N. Holmberg, C. Blake, and M.E. Verhoeyen. 2003. Immunomodulation of enzyme function in plants by single-domain antibody fragments. Nat. Biotechnol. 21:77-80. http://dx.doi.org/10.1038/nbt772
    • (2003) Nat. Biotechnol. , vol.21 , pp. 77-80
    • Jobling, S.A.1    Jarman, C.2    Teh, M.M.3    Holmberg, N.4    Blake, C.5    Verhoeyen, M.E.6
  • 55
    • 66149167323 scopus 로고    scopus 로고
    • Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase
    • Kampmeier, F., M. Ribbert, T. Nachreiner, S. Dembski, F. Beaufils, A. Brecht, and S. Barth. 2009. Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase. Bioconjug. Chem. 20:1010-1015. http://dx.doi.org/10.1021/bc9000257
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1010-1015
    • Kampmeier, F.1    Ribbert, M.2    Nachreiner, T.3    Dembski, S.4    Beaufils, F.5    Brecht, A.6    Barth, S.7
  • 56
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler, A., S. Gendreizig, T. Gronemeyer, H. Pick, H. Vogel, and K. Johnsson. 2003. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21:86-89. http://dx.doi.org/10.1038/nbt765
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 57
    • 80052976954 scopus 로고    scopus 로고
    • ChIP-Seq: technical considerations for obtaining high-quality data
    • Kidder, B.L., G. Hu, and K. Zhao. 2011. ChIP-Seq: technical considerations for obtaining high-quality data. Nat. Immunol. 12:918-922. http://dx.doi.org/10.1038/ni.2117
    • (2011) Nat. Immunol. , vol.12 , pp. 918-922
    • Kidder, B.L.1    Hu, G.2    Zhao, K.3
  • 58
    • 84855999851 scopus 로고    scopus 로고
    • Rapid identification of recombinant Fabs that bind to membrane proteins
    • Kim, J., R.M. Stroud, and C.S. Craik. 2011. Rapid identification of recombinant Fabs that bind to membrane proteins. Methods. 55:303-309. http://dx.doi.org/10.1016/j.ymeth.2011.09.012
    • (2011) Methods. , vol.55 , pp. 303-309
    • Kim, J.1    Stroud, R.M.2    Craik, C.S.3
  • 60
    • 78549278144 scopus 로고    scopus 로고
    • Eradication of B-lineage cells and regression of lymphoma in a patient treated with autologous T cells genetically engineered to recognize CD19
    • Kochenderfer, J.N., W.H. Wilson, J.E. Janik, M.E. Dudley, M. Stetler-Stevenson, S.A. Feldman, I. Maric, M. Raffeld, D.A. Nathan, B.J. Lanier, et al. 2010. Eradication of B-lineage cells and regression of lymphoma in a patient treated with autologous T cells genetically engineered to recognize CD19. Blood. 116:4099-4102. http://dx.doi.org/10.1182/blood-2010-04-281931
    • (2010) Blood. , vol.116 , pp. 4099-4102
    • Kochenderfer, J.N.1    Wilson, W.H.2    Janik, J.E.3    Dudley, M.E.4    Stetler-Stevenson, M.5    Feldman, S.A.6    Maric, I.7    Raffeld, M.8    Nathan, D.A.9    Lanier, B.J.10
  • 61
  • 62
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide, A., C.W. Bailey, X. Huang, and S. Koide. 1998. The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol. 284:1141-1151. http://dx.doi.org/10.1006/jmbi.1998.2238
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 63
    • 0037022351 scopus 로고    scopus 로고
    • Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor
    • Koide, A., S. Abbatiello, L. Rothgery, and S. Koide. 2002. Probing protein conformational changes in living cells by using designer binding proteins: application to the estrogen receptor. Proc. Natl. Acad. Sci. USA. 99:1253-1258. http://dx.doi.org/10.1073/pnas.032665299
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 1253-1258
    • Koide, A.1    Abbatiello, S.2    Rothgery, L.3    Koide, S.4
  • 64
    • 84855802142 scopus 로고    scopus 로고
    • Teaching an old scaffold new tricks: monobodies constructed using alternative surfaces of the FN3 scaffold
    • Koide, A., J. Wojcik, R.N. Gilbreth, R.J. Hoey, and S. Koide. 2012. Teaching an old scaffold new tricks: monobodies constructed using alternative surfaces of the FN3 scaffold. J. Mol. Biol. 415:393-405. http://dx.doi.org/10.1016/j.jmb.2011.12.019
    • (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
  • 65
    • 0041819708 scopus 로고    scopus 로고
    • Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region
    • Korndörfer, I.P., G. Beste, and A. Skerra. 2003. Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins. 53:121-129. http://dx.doi.org/10.1002/prot.10497
    • (2003) Proteins. , vol.53 , pp. 121-129
    • Korndörfer, I.P.1    Beste, G.2    Skerra, A.3
  • 66
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov, K.V., E. Pardon, J. Steyaert, and W.G. Hol. 2009. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure. 17:255-265. http://dx.doi.org/10.1016/j.str.2008.11.011
    • (2009) Structure. , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 67
    • 0029646090 scopus 로고
    • The use of antibody fragments for crystallization and structure determinations
    • Kovari, L.C., C. Momany, and M.G. Rossmann. 1995. The use of antibody fragments for crystallization and structure determinations. Structure. 3:1291-1293. http://dx.doi.org/10.1016/S0969-2126(01)00266-0
    • (1995) Structure. , vol.3 , pp. 1291-1293
    • Kovari, L.C.1    Momany, C.2    Rossmann, M.G.3
  • 68
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy, H., and E. Gouaux. 2012. X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature. 481:469-474. http://dx.doi.org/10.1038/nature10737
    • (2012) Nature. , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 73
    • 33845934490 scopus 로고    scopus 로고
    • Ankyrin repeat: a unique motif mediating protein-protein interactions
    • Li, J., A. Mahajan, and M.D. Tsai. 2006. Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry. 45:15168-15178. http://dx.doi.org/10.1021/bi062188q
    • (2006) Biochemistry. , vol.45 , pp. 15168-15178
    • Li, J.1    Mahajan, A.2    Tsai, M.D.3
  • 74
    • 84894534641 scopus 로고    scopus 로고
    • Synthetic biology in mammalian cells: next generation research tools and therapeutics
    • Lienert, F., J.J. Lohmueller, A. Garg, and P.A. Silver. 2014. Synthetic biology in mammalian cells: next generation research tools and therapeutics. Nat. Rev. Mol. Cell Biol. 15:95-107. http://dx.doi.org/10.1038/nrm3738
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 95-107
    • Lienert, F.1    Lohmueller, J.J.2    Garg, A.3    Silver, P.A.4
  • 78
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: natural single-domain antibodies
    • Muyldermans, S. 2013. Nanobodies: natural single-domain antibodies. Annu. Rev. Biochem. 82:775-797. http://dx.doi.org/10.1146/annurev-biochem-063011-092449
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 79
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., T. Atarhouch, J. Saldanha, J.A. Barbosa, and R. Hamers. 1994. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7:1129-1135. http://dx.doi.org/10.1093/protein/7.9.1129
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 80
    • 4644266043 scopus 로고    scopus 로고
    • Activation of endogenous Cdc42 visualized in living cells
    • Nalbant, P., L. Hodgson, V. Kraynov, A. Toutchkine, and K.M. Hahn. 2004. Activation of endogenous Cdc42 visualized in living cells. Science. 305:1615-1619. http://dx.doi.org/10.1126/science.1100367
    • (2004) Science. , vol.305 , pp. 1615-1619
    • Nalbant, P.1    Hodgson, L.2    Kraynov, V.3    Toutchkine, A.4    Hahn, K.M.5
  • 81
    • 0034161488 scopus 로고    scopus 로고
    • Camel heavychain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
    • Nguyen, V.K., R. Hamers, L. Wyns, and S. Muyldermans. 2000. Camel heavychain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire. EMBO J. 19:921-930. http://dx.doi.org/10.1093/emboj/19.5.921
    • (2000) EMBO J. , vol.19 , pp. 921-930
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 82
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an a-helical bacterial receptor domain
    • Nord, K., E. Gunneriusson, J. Ringdahl, S. Ståhl, M. Uhlén, and P.A. Nygren. 1997. Binding proteins selected from combinatorial libraries of an a-helical bacterial receptor domain. Nat. Biotechnol. 15:772-777. http://dx.doi.org/10.1038/nbt0897-772
    • (1997) Nat. Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Ståhl, S.4    Uhlén, M.5    Nygren, P.A.6
  • 83
    • 0028991525 scopus 로고
    • Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • Ostermeier, C., S. Iwata, B. Ludwig, and H. Michel. 1995. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat. Struct. Biol. 2:842-846. http://dx.doi.org/10.1038/nsb1095-842
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 842-846
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 84
    • 84877121241 scopus 로고    scopus 로고
    • Generating conformation-specific synthetic antibodies to trap proteins in selected functional states
    • Paduch, M., A. Koide, S. Uysal, S.S. Rizk, S. Koide, and A.A. Kossiakoff. 2013. Generating conformation-specific synthetic antibodies to trap proteins in selected functional states. Methods. 60:3-14. http://dx.doi.org/10.1016/j.ymeth.2012.12.010
    • (2013) Methods. , vol.60 , pp. 3-14
    • Paduch, M.1    Koide, A.2    Uysal, S.3    Rizk, S.S.4    Koide, S.5    Kossiakoff, A.A.6
  • 86
    • 84862014201 scopus 로고    scopus 로고
    • Designed ankyrin repeat proteins (DARPins) as novel isoform-specific intracellular inhibitors of c-Jun N-terminal kinases
    • Parizek, P., L. Kummer, P. Rube, A. Prinz, F.W. Herberg, and A. Plückthun. 2012. Designed ankyrin repeat proteins (DARPins) as novel isoform-specific intracellular inhibitors of c-Jun N-terminal kinases. ACS Chem. Biol. 7:1356-1366. http://dx.doi.org/10.1021/cb3001167
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1356-1366
    • Parizek, P.1    Kummer, L.2    Rube, P.3    Prinz, A.4    Herberg, F.W.5    Plückthun, A.6
  • 87
    • 39149098445 scopus 로고    scopus 로고
    • Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core
    • Parmeggiani, F., R. Pellarin, A.P. Larsen, G. Varadamsetty, M.T. Stumpp, O. Zerbe, A. Caflisch, and A. Plückthun. 2008. Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core. J. Mol. Biol. 376:1282-1304. http://dx.doi.org/10.1016/j.jmb.2007.12.014
    • (2008) J. Mol. Biol. , vol.376 , pp. 1282-1304
    • Parmeggiani, F.1    Pellarin, R.2    Larsen, A.P.3    Varadamsetty, G.4    Stumpp, M.T.5    Zerbe, O.6    Caflisch, A.7    Plückthun, A.8
  • 89
    • 84934439360 scopus 로고    scopus 로고
    • Fluorescent protein specific Nanotraps to study protein-protein interactions and histone-tail peptide binding
    • Pichler, G., H. Leonhardt, and U. Rothbauer. 2012. Fluorescent protein specific Nanotraps to study protein-protein interactions and histone-tail peptide binding. Methods Mol. Biol. 911:475-483.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 475-483
    • Pichler, G.1    Leonhardt, H.2    Rothbauer, U.3
  • 90
    • 84920848625 scopus 로고    scopus 로고
    • Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy
    • Plückthun, A. 2015. Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy. Annu. Rev. Pharmacol. Toxicol. 55:489-511. http://dx.doi.org/10.1146/annurev-pharmtox-010611-134654
    • (2015) Annu. Rev. Pharmacol. Toxicol. , vol.55 , pp. 489-511
    • Plückthun, A.1
  • 91
    • 80052709792 scopus 로고    scopus 로고
    • Magnetosome expression of functional camelid antibody fragments (nanobodies) in Magnetospirillum gryphiswaldense
    • Pollithy, A., T. Romer, C. Lang, F.D. Muller, J. Helma, H. Leonhardt, U. Rothbauer, and D. Schuler. 2011. Magnetosome expression of functional camelid antibody fragments (nanobodies) in Magnetospirillum gryphiswaldense. Appl. Environ. Microbiol. 77:6165-6171. http://dx.doi.org/10.1128/AEM.05282-11
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 6165-6171
    • Pollithy, A.1    Romer, T.2    Lang, C.3    Muller, F.D.4    Helma, J.5    Leonhardt, H.6    Rothbauer, U.7    Schuler, D.8
  • 96
    • 84861979783 scopus 로고    scopus 로고
    • A simple, versatile method for GFP-based super-resolution microscopy via nanobodies
    • Ries, J., C. Kaplan, E. Platonova, H. Eghlidi, and H. Ewers. 2012. A simple, versatile method for GFP-based super-resolution microscopy via nanobodies. Nat. Methods. 9:582-584. http://dx.doi.org/10.1038/nmeth.1991
    • (2012) Nat. Methods. , vol.9 , pp. 582-584
    • Ries, J.1    Kaplan, C.2    Platonova, E.3    Eghlidi, H.4    Ewers, H.5
  • 98
    • 39749193861 scopus 로고    scopus 로고
    • A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
    • Rothbauer, U., K. Zolghadr, S. Muyldermans, A. Schepers, M.C. Cardoso, and H. Leonhardt. 2008. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteomics. 7:282-289. http://dx.doi.org/10.1074/mcp.M700342-MCP200
    • (2008) Mol. Cell. Proteomics. , vol.7 , pp. 282-289
    • Rothbauer, U.1    Zolghadr, K.2    Muyldermans, S.3    Schepers, A.4    Cardoso, M.C.5    Leonhardt, H.6
  • 100
    • 77954995399 scopus 로고    scopus 로고
    • A guide to super-resolution fluorescence microscopy
    • Schermelleh, L., R. Heintzmann, and H. Leonhardt. 2010. A guide to super-resolution fluorescence microscopy. J. Cell Biol. 190:165-175. http://dx.doi.org/10.1083/jcb.201002018
    • (2010) J. Cell Biol. , vol.190 , pp. 165-175
    • Schermelleh, L.1    Heintzmann, R.2    Leonhardt, H.3
  • 102
    • 84892930656 scopus 로고    scopus 로고
    • Design, construction, and characterization of a second-generation DARP in library with reduced hydrophobicity
    • Seeger, M.A., R. Zbinden, A. Flütsch, P.G. Gutte, S. Engeler, H. Roschitzki-Voser, and M.G. Grütter. 2013. Design, construction, and characterization of a second-generation DARP in library with reduced hydrophobicity. Protein Sci. 22:1239-1257. http://dx.doi.org/10.1002/pro.2312
    • (2013) Protein Sci. , vol.22 , pp. 1239-1257
    • Seeger, M.A.1    Zbinden, R.2    Flütsch, A.3    Gutte, P.G.4    Engeler, S.5    Roschitzki-Voser, H.6    Grütter, M.G.7
  • 103
    • 33846363597 scopus 로고    scopus 로고
    • Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors
    • Sennhauser, G., P. Amstutz, C. Briand, O. Storchenegger, and M.G. Grütter. 2007. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 5:e7. http://dx.doi.org/10.1371/journal.pbio.0050007
    • (2007) PLoS Biol. , vol.5
    • Sennhauser, G.1    Amstutz, P.2    Briand, C.3    Storchenegger, O.4    Grütter, M.G.5
  • 104
    • 78650414170 scopus 로고    scopus 로고
    • Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography
    • Serrière, J., J.M. Dugua, M. Bossus, B. Verrier, R. Haser, P. Gouet, and C. Guillon. 2011. Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. J. Mol. Biol. 405:33-42. http://dx.doi.org/10.1016/j.jmb.2010.10.033
    • (2011) J. Mol. Biol. , vol.405 , pp. 33-42
    • Serrière, J.1    Dugua, J.M.2    Bossus, M.3    Verrier, B.4    Haser, R.5    Gouet, P.6    Guillon, C.7
  • 105
    • 84883770456 scopus 로고    scopus 로고
    • Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains
    • Sha, F., E.B. Gencer, S. Georgeon, A. Koide, N. Yasui, S. Koide, and O. Hantschel. 2013. Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains. Proc. Natl. Acad. Sci. USA. 110:14924-14929. http://dx.doi.org/10.1073/pnas.1303640110
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 14924-14929
    • Sha, F.1    Gencer, E.B.2    Georgeon, S.3    Koide, A.4    Yasui, N.5    Koide, S.6    Hantschel, O.7
  • 106
    • 28644436100 scopus 로고    scopus 로고
    • Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains
    • Silverman, J., Q. Liu, A. Bakker, W. To, A. Duguay, B.M. Alba, R. Smith, A. Rivas, P. Li, H. Le, et al. 2005. Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains. Nat. Biotechnol. 23:1556-1561. http://dx.doi.org/10.1038/nbt1166
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1556-1561
    • Silverman, J.1    Liu, Q.2    Bakker, A.3    To, W.4    Duguay, A.5    Alba, B.M.6    Smith, R.7    Rivas, A.8    Li, P.9    Le, H.10
  • 107
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
    • Sims, J.J., F. Scavone, E.M. Cooper, L.A. Kane, R.J. Youle, J.D. Boeke, and R.E. Cohen. 2012. Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Nat. Methods. 9:303-309. http://dx.doi.org/10.1038/nmeth.1888
    • (2012) Nat. Methods. , vol.9 , pp. 303-309
    • Sims, J.J.1    Scavone, F.2    Cooper, E.M.3    Kane, L.A.4    Youle, R.J.5    Boeke, J.D.6    Cohen, R.E.7
  • 108
    • 77953616095 scopus 로고    scopus 로고
    • Monoclonal antibody MN423 as a stable mold facilitates structure determination of disordered tau protein
    • Skrabana, R., R. Dvorsky, J. Sevcik, and M. Novak. 2010. Monoclonal antibody MN423 as a stable mold facilitates structure determination of disordered tau protein. J. Struct. Biol. 171:74-81. http://dx.doi.org/10.1016/j.jsb.2010.02.016
    • (2010) J. Struct. Biol. , vol.171 , pp. 74-81
    • Skrabana, R.1    Dvorsky, R.2    Sevcik, J.3    Novak, M.4
  • 109
    • 0032571365 scopus 로고    scopus 로고
    • Small binding proteins selected from a combinatorial repertoire of knottins displayed on phage
    • Smith, G.P., S.U. Patel, J.D. Windass, J.M. Thornton, G. Winter, and A.D. Griffiths. 1998. Small binding proteins selected from a combinatorial repertoire of knottins displayed on phage. J. Mol. Biol. 277:317-332. http://dx.doi.org/10.1006/jmbi.1997.1621
    • (1998) J. Mol. Biol. , vol.277 , pp. 317-332
    • Smith, G.P.1    Patel, S.U.2    Windass, J.D.3    Thornton, J.M.4    Winter, G.5    Griffiths, A.D.6
  • 110
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli, S., A. Desmyter, C.T. Verrips, H.J. de Haard, S. Moineau, and C. Cambillau. 2006. Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13:85-89. http://dx.doi.org/10.1038/nsmb1029
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    de Haard, H.J.4    Moineau, S.5    Cambillau, C.6
  • 112
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg, E.J., and R.A. Mariuzza. 2002. Molecular recognition in antibody-antigen complexes. Adv. Protein Chem. 61:119-160.
    • (2002) Adv. Protein Chem. , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 113
    • 84882792150 scopus 로고    scopus 로고
    • A nanobody-based system using fluorescent proteins as scaffolds for cell-specific gene manipulation
    • Tang, J.C., T. Szikra, Y. Kozorovitskiy, M. Teixiera, B.L. Sabatini, B. Roska, and C.L. Cepko. 2013. A nanobody-based system using fluorescent proteins as scaffolds for cell-specific gene manipulation. Cell. 154:928-939. http://dx.doi.org/10.1016/j.cell.2013.07.021
    • (2013) Cell. , vol.154 , pp. 928-939
    • Tang, J.C.1    Szikra, T.2    Kozorovitskiy, Y.3    Teixiera, M.4    Sabatini, B.L.5    Roska, B.6    Cepko, C.L.7
  • 114
    • 33750287537 scopus 로고    scopus 로고
    • Improving solubility and refolding efficiency of human V(H)s by a novel mutational approach
    • Tanha, J., T.D. Nguyen, A. Ng, S. Ryan, F. Ni, and R. Mackenzie. 2006. Improving solubility and refolding efficiency of human V(H)s by a novel mutational approach. Protein Eng. Des. Sel. 19:503-509. http://dx.doi.org/10.1093/protein/gzl037
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 503-509
    • Tanha, J.1    Nguyen, T.D.2    Ng, A.3    Ryan, S.4    Ni, F.5    Mackenzie, R.6
  • 116
    • 46449122768 scopus 로고    scopus 로고
    • Toward chaperone-assisted crystallography: protein engineering enhancement of crystal packing and X-ray phasing capabilities of a camelid single-domain antibody (VHH) scaffold
    • Tereshko, V., S. Uysal, A. Koide, K. Margalef, S. Koide, and A.A. Kossiakoff. 2008. Toward chaperone-assisted crystallography: protein engineering enhancement of crystal packing and X-ray phasing capabilities of a camelid single-domain antibody (VHH) scaffold. Protein Sci. 17:1175-1187. http://dx.doi.org/10.1110/ps.034892.108
    • (2008) Protein Sci. , vol.17 , pp. 1175-1187
    • Tereshko, V.1    Uysal, S.2    Koide, A.3    Margalef, K.4    Koide, S.5    Kossiakoff, A.A.6
  • 118
    • 84877897559 scopus 로고    scopus 로고
    • A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties
    • Tiller, T., I. Schuster, D. Deppe, K. Siegers, R. Strohner, T. Herrmann, M. Berenguer, D. Poujol, J. Stehle, Y. Stark, et al. 2013. A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties. MAbs. 5:445-470. http://dx.doi.org/10.4161/mabs.24218
    • (2013) MAbs. , vol.5 , pp. 445-470
    • Tiller, T.1    Schuster, I.2    Deppe, D.3    Siegers, K.4    Strohner, R.5    Herrmann, T.6    Berenguer, M.7    Poujol, D.8    Stehle, J.9    Stark, Y.10
  • 119
    • 0037427330 scopus 로고    scopus 로고
    • Solvent-sensitive dyes to report protein conformational changes in living cells
    • Toutchkine, A., V. Kraynov, and K. Hahn. 2003. Solvent-sensitive dyes to report protein conformational changes in living cells. J. Am. Chem. Soc. 125:4132-4145. http://dx.doi.org/10.1021/ja0290882
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4132-4145
    • Toutchkine, A.1    Kraynov, V.2    Hahn, K.3
  • 122
  • 123
    • 0031267747 scopus 로고    scopus 로고
    • Comparison of llama VH sequences from conventional and heavy chain antibodies
    • Vu, K.B., M.A. Ghahroudi, L. Wyns, and S. Muyldermans. 1997. Comparison of llama VH sequences from conventional and heavy chain antibodies. Mol. Immunol. 34:1121-1131. http://dx.doi.org/10.1016/S0161-5890(97)00146-6
    • (1997) Mol. Immunol. , vol.34 , pp. 1121-1131
    • Vu, K.B.1    Ghahroudi, M.A.2    Wyns, L.3    Muyldermans, S.4
  • 124
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther, T.C., and M. Mann. 2010. Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 190:491-500. http://dx.doi.org/10.1083/jcb.201004052
    • (2010) J. Cell Biol. , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 125
    • 0033571383 scopus 로고    scopus 로고
    • High thermal stability is essential for tumor targeting of antibody fragments: engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment
    • Willuda, J., A. Honegger, R. Waibel, P.A. Schubiger, R. Stahel, U. Zangemeister-Wittke, and A. Plückthun. 1999. High thermal stability is essential for tumor targeting of antibody fragments: engineering of a humanized anti-epithelial glycoprotein-2 (epithelial cell adhesion molecule) single-chain Fv fragment. Cancer Res. 59:5758-5767.
    • (1999) Cancer Res. , vol.59 , pp. 5758-5767
    • Willuda, J.1    Honegger, A.2    Waibel, R.3    Schubiger, P.A.4    Stahel, R.5    Zangemeister-Wittke, U.6    Plückthun, A.7
  • 126
    • 34748919097 scopus 로고    scopus 로고
    • Design of recombinant antibody microarrays for complex proteome analysis: choice of sample labeling-tag and solid support
    • Wingren, C., J. Ingvarsson, L. Dexlin, D. Szul, and C.A. Borrebaeck. 2007. Design of recombinant antibody microarrays for complex proteome analysis: choice of sample labeling-tag and solid support. Proteomics. 7:3055-3065. http://dx.doi.org/10.1002/pmic.200700025
    • (2007) Proteomics. , vol.7 , pp. 3055-3065
    • Wingren, C.1    Ingvarsson, J.2    Dexlin, L.3    Szul, D.4    Borrebaeck, C.A.5
  • 128
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Wörn, A., and A. Plückthun. 2001. Stability engineering of antibody single-chain Fv fragments. J. Mol. Biol. 305:989-1010. http://dx.doi.org/10.1006/jmbi.2000.4265
    • (2001) J. Mol. Biol. , vol.305 , pp. 989-1010
    • Wörn, A.1    Plückthun, A.2
  • 129
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Zhou, Y., J.H. Morais-Cabral, A. Kaufman, and R. MacKinnon. 2001. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature. 414:43-48. http://dx.doi.org/10.1038/35102009
    • (2001) Nature. , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 130
    • 84934444389 scopus 로고    scopus 로고
    • Case study on live cell apoptosis-assay using lamin-chromobody cell-lines for high-content analysis
    • Zolghadr, K., J. Gregor, H. Leonhardt, and U. Rothbauer. 2012. Case study on live cell apoptosis-assay using lamin-chromobody cell-lines for high-content analysis. Methods Mol. Biol. 911:569-575.
    • (2012) Methods Mol. Biol. , vol.911 , pp. 569-575
    • Zolghadr, K.1    Gregor, J.2    Leonhardt, H.3    Rothbauer, U.4


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