메뉴 건너뛰기




Volumn 372, Issue 1, 2007, Pages 172-185

Affilin-Novel Binding Molecules Based on Human γ-B-Crystallin, an All β-Sheet Protein

Author keywords

de novo binding; intrinsic stability; scaffold; structure; B crystallin

Indexed keywords

BINDING PROTEIN; CRYSTALLIN; GAMMA B CRYSTALLIN; IMMUNOGLOBULIN G; PROTEIN AFFILIN; UNCLASSIFIED DRUG;

EID: 34547663529     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.045     Document Type: Article
Times cited : (54)

References (65)
  • 1
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James L.C., Roversi P., and Tawfik D.S. Antibody multispecificity mediated by conformational diversity. Science 299 (2003) 1362-1367
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 2
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D.R., and Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA 93 (1996) 7-12
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 4
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl Acad. Sci. USA 44 (1958) 98-104
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 5
    • 0032981632 scopus 로고    scopus 로고
    • Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: implications for the protein docking problem
    • Jackson R.M. Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: implications for the protein docking problem. Protein Sci. 8 (1999) 603-613
    • (1999) Protein Sci. , vol.8 , pp. 603-613
    • Jackson, R.M.1
  • 6
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 7
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • Binz H.K., and Pluckthun A. Engineered proteins as specific binding reagents. Curr. Opin. Biotechnol. 16 (2005) 459-469
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 459-469
    • Binz, H.K.1    Pluckthun, A.2
  • 8
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • Hey T., Fiedler E., Rudolph R., and Fiedler M. Artificial, non-antibody binding proteins for pharmaceutical and industrial applications. Trends Biotechnol. 23 (2005) 514-522
    • (2005) Trends Biotechnol. , vol.23 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 9
    • 0033865190 scopus 로고    scopus 로고
    • Engineered protein scaffolds for molecular recognition
    • Skerra A. Engineered protein scaffolds for molecular recognition. J. Mol. Recognit. 13 (2000) 167-187
    • (2000) J. Mol. Recognit. , vol.13 , pp. 167-187
    • Skerra, A.1
  • 10
    • 0033515005 scopus 로고    scopus 로고
    • Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
    • Beste G., Schmidt F.S., Stibora T., and Skerra A. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl Acad. Sci. USA 96 (1999) 1898-1903
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1898-1903
    • Beste, G.1    Schmidt, F.S.2    Stibora, T.3    Skerra, A.4
  • 11
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., Bailey C.W., Huang X., and Koide S. 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    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 12
    • 0041819708 scopus 로고    scopus 로고
    • Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region
    • Korndorfer I.P., Beste G., and Skerra A. Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins: Struct. Funct. Genet. 53 (2003) 121-129
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 121-129
    • Korndorfer, I.P.1    Beste, G.2    Skerra, A.3
  • 13
    • 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., and Pluckthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332 (2003) 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
  • 14
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord K., Gunneriusson E., Ringdahl J., Stahl S., Uhlen M., and Nygren P.A. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nature Biotechnol. 15 (1997) 772-777
    • (1997) Nature Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Stahl, S.4    Uhlen, M.5    Nygren, P.A.6
  • 16
    • 0028138405 scopus 로고
    • Grafting of a high-affinity Zn(II)-binding site on the beta-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification
    • Müller H.N., and Skerra A. Grafting of a high-affinity Zn(II)-binding site on the beta-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification. Biochemistry 33 (1994) 14126-14135
    • (1994) Biochemistry , vol.33 , pp. 14126-14135
    • Müller, H.N.1    Skerra, A.2
  • 17
    • 0029050766 scopus 로고
    • Scorpion toxins as natural scaffolds for protein engineering
    • Vita C., Roumestand C., Toma F., and Menez A. Scorpion toxins as natural scaffolds for protein engineering. Proc. Natl Acad. Sci. USA 92 (1995) 6404-6408
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6404-6408
    • Vita, C.1    Roumestand, C.2    Toma, F.3    Menez, A.4
  • 18
    • 0034669782 scopus 로고    scopus 로고
    • Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold
    • Lehtio J., Teeri T.T., and Nygren P.A. Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold. Proteins: Struct. Funct. Genet. 41 (2000) 316-322
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 316-322
    • Lehtio, J.1    Teeri, T.T.2    Nygren, P.A.3
  • 19
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: structure, stability, and function
    • Jaenicke R., and Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36 (2001) 435-499
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 20
    • 0030067190 scopus 로고    scopus 로고
    • Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles
    • Jaenicke R. Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles. FASEB J. 10 (1996) 84-92
    • (1996) FASEB J. , vol.10 , pp. 84-92
    • Jaenicke, R.1
  • 21
    • 0030513191 scopus 로고    scopus 로고
    • An eye lens protein-water structure: 1.2 angstrom resolution structure of gamma B-crystallin at 150K
    • Kumaraswamy V.S., Lindley P.F., Slingsby C., and Glover I.D. An eye lens protein-water structure: 1.2 angstrom resolution structure of gamma B-crystallin at 150K. Acta Crystallog. sect. D 52 (1996) 611-622
    • (1996) Acta Crystallog. sect. D , vol.52 , pp. 611-622
    • Kumaraswamy, V.S.1    Lindley, P.F.2    Slingsby, C.3    Glover, I.D.4
  • 22
    • 0025339471 scopus 로고
    • Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens
    • Rudolph R., Siebendritt R., Nesslauer G., Sharma A.K., and Jaenicke R. Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens. Proc. Natl Acad. Sci. USA 87 (1990) 4625-4629
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5
  • 23
    • 0025670590 scopus 로고
    • Limited proteolysis of gamma II-crystallin from calf eye lens. Physicochemical studies on the N-terminal domain and the intact two-domain protein
    • Sharma A.K., Minke-Gogl V., Gohl P., Siebendritt R., Jaenicke R., and Rudolph R. Limited proteolysis of gamma II-crystallin from calf eye lens. Physicochemical studies on the N-terminal domain and the intact two-domain protein. Eur. J. Biochem. 194 (1990) 603-609
    • (1990) Eur. J. Biochem. , vol.194 , pp. 603-609
    • Sharma, A.K.1    Minke-Gogl, V.2    Gohl, P.3    Siebendritt, R.4    Jaenicke, R.5    Rudolph, R.6
  • 24
    • 0028104494 scopus 로고
    • Eye-lens proteins: structure, superstructure, stability, genetics
    • Jaenicke R. Eye-lens proteins: structure, superstructure, stability, genetics. Naturwissenschaften 81 (1994) 423-429
    • (1994) Naturwissenschaften , vol.81 , pp. 423-429
    • Jaenicke, R.1
  • 25
    • 11844265970 scopus 로고    scopus 로고
    • Protein sequence randomization: efficient estimation of protein stability using knowledge-based potentials
    • Wiederstein M., and Sippl M.J. Protein sequence randomization: efficient estimation of protein stability using knowledge-based potentials. J. Mol. Biol. 345 (2005) 1199-1212
    • (2005) J. Mol. Biol. , vol.345 , pp. 1199-1212
    • Wiederstein, M.1    Sippl, M.J.2
  • 26
    • 0035976524 scopus 로고    scopus 로고
    • Regulation of cell survival by secreted proneurotrophins
    • Lee R., Kermani P., Teng K.K., and Hempstead B.L. Regulation of cell survival by secreted proneurotrophins. Science 294 (2001) 1945-1948
    • (2001) Science , vol.294 , pp. 1945-1948
    • Lee, R.1    Kermani, P.2    Teng, K.K.3    Hempstead, B.L.4
  • 27
    • 10744219632 scopus 로고    scopus 로고
    • Sortilin is essential for proNGF-induced neuronal cell death
    • Nykjaer A., Lee R., Teng K.K., Jansen P., Madsen P., Nielsen M.S., et al. Sortilin is essential for proNGF-induced neuronal cell death. Nature 427 (2004) 843-848
    • (2004) Nature , vol.427 , pp. 843-848
    • Nykjaer, A.1    Lee, R.2    Teng, K.K.3    Jansen, P.4    Madsen, P.5    Nielsen, M.S.6
  • 28
    • 0030752436 scopus 로고    scopus 로고
    • Melanoma-inhibiting activity, a novel serum marker for progression of malignant melanoma
    • Bosserhoff A.K., Kaufmann M., Kaluza B., Bartke I., Zirngibl H., Hein R., et al. Melanoma-inhibiting activity, a novel serum marker for progression of malignant melanoma. Cancer Res. 57 (1997) 3149-3153
    • (1997) Cancer Res. , vol.57 , pp. 3149-3153
    • Bosserhoff, A.K.1    Kaufmann, M.2    Kaluza, B.3    Bartke, I.4    Zirngibl, H.5    Hein, R.6
  • 29
    • 0030789317 scopus 로고    scopus 로고
    • Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens
    • Palme S., Slingsby C., and Jaenicke R. Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens. Protein Sci. 6 (1997) 1529-1536
    • (1997) Protein Sci. , vol.6 , pp. 1529-1536
    • Palme, S.1    Slingsby, C.2    Jaenicke, R.3
  • 30
    • 0037449865 scopus 로고    scopus 로고
    • Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins
    • Salim A., and Zaidi Z.H. Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins. Biochem. Biophys. Res. Commun. 300 (2003) 624-630
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 624-630
    • Salim, A.1    Zaidi, Z.H.2
  • 31
    • 3142677981 scopus 로고    scopus 로고
    • Binding proteins from alternative scaffolds
    • Nygren P.A., and Skerra A. Binding proteins from alternative scaffolds. J. Immunol. Methods 290 (2004) 3-28
    • (2004) J. Immunol. Methods , vol.290 , pp. 3-28
    • Nygren, P.A.1    Skerra, A.2
  • 32
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu L., Aha P., Gu K., Kuimelis R.G., Kurz M., Lam T., 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    Aha, P.2    Gu, K.3    Kuimelis, R.G.4    Kurz, M.5    Lam, T.6
  • 33
    • 0029120867 scopus 로고
    • Tendamistat as a scaffold for conformationally constrained phage peptide libraries
    • McConnell S.J., and Hoess R.H. Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J. Mol. Biol. 250 (1995) 460-470
    • (1995) J. Mol. Biol. , vol.250 , pp. 460-470
    • McConnell, S.J.1    Hoess, R.H.2
  • 34
    • 0142184270 scopus 로고    scopus 로고
    • Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering
    • Sandstrom K., Xu Z., Forsberg G., and Nygren P.A. Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering. Protein Eng. 16 (2003) 691-697
    • (2003) Protein Eng. , vol.16 , pp. 691-697
    • Sandstrom, K.1    Xu, Z.2    Forsberg, G.3    Nygren, P.A.4
  • 36
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • Jung S., Honegger A., and Pluckthun A. Selection for improved protein stability by phage display. J. Mol. Biol. 294 (1999) 163-180
    • (1999) J. Mol. Biol. , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Pluckthun, A.3
  • 37
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains
    • Ewert S., Cambillau C., Conrath K., and Pluckthun A. Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains. Biochemistry 41 (2002) 3628-3636
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1    Cambillau, C.2    Conrath, K.3    Pluckthun, A.4
  • 39
    • 0037359054 scopus 로고    scopus 로고
    • Rapid method for measuring ScFv thermal stability by yeast surface display
    • Orr B.A., Carr L.M., Wittrup K.D., Roy E.J., and Kranz D.M. Rapid method for measuring ScFv thermal stability by yeast surface display. Biotechnol. Prog. 19 (2003) 631-638
    • (2003) Biotechnol. Prog. , vol.19 , pp. 631-638
    • Orr, B.A.1    Carr, L.M.2    Wittrup, K.D.3    Roy, E.J.4    Kranz, D.M.5
  • 40
    • 0037007445 scopus 로고    scopus 로고
    • Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant-a so-called 'anticalin'-using a molecular random approach
    • Schlehuber S., and Skerra A. Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant-a so-called 'anticalin'-using a molecular random approach. Biophys. Chem. 96 (2002) 213-228
    • (2002) Biophys. Chem. , vol.96 , pp. 213-228
    • Schlehuber, S.1    Skerra, A.2
  • 41
    • 0034646561 scopus 로고    scopus 로고
    • A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin
    • Schlehuber S., Beste G., and Skerra A. A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin. J. Mol. Biol. 297 (2000) 1105-1120
    • (2000) J. Mol. Biol. , vol.297 , pp. 1105-1120
    • Schlehuber, S.1    Beste, G.2    Skerra, A.3
  • 42
    • 0023718830 scopus 로고
    • Specific binding characteristics of high affinity monoclonal antidigitoxin antibodies
    • Collignon A., Geniteau-Legendre M., Sandre C., Quero A.M., and Labarre C. Specific binding characteristics of high affinity monoclonal antidigitoxin antibodies. Hybridoma 7 (1988) 355-366
    • (1988) Hybridoma , vol.7 , pp. 355-366
    • Collignon, A.1    Geniteau-Legendre, M.2    Sandre, C.3    Quero, A.M.4    Labarre, C.5
  • 43
    • 0141572471 scopus 로고    scopus 로고
    • Emerging trends in the synthesis and improvement of hapten-specific recombinant antibodies
    • Yau K.Y., Lee H., and Hall J.C. Emerging trends in the synthesis and improvement of hapten-specific recombinant antibodies. Biotechnol. Advan. 21 (2003) 599-637
    • (2003) Biotechnol. Advan. , vol.21 , pp. 599-637
    • Yau, K.Y.1    Lee, H.2    Hall, J.C.3
  • 44
    • 33845993299 scopus 로고    scopus 로고
    • Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening
    • Kawe M., Forrer P., Amstutz P., and Pluckthun A. Isolation of intracellular proteinase inhibitors derived from designed ankyrin repeat proteins by genetic screening. J. Biol. Chem. 281 (2006) 40252-40263
    • (2006) J. Biol. Chem. , vol.281 , pp. 40252-40263
    • Kawe, M.1    Forrer, P.2    Amstutz, P.3    Pluckthun, A.4
  • 45
    • 33845939857 scopus 로고    scopus 로고
    • Selection and characterization of Her2 binding-designed ankyrin repeat proteins
    • Zahnd C., Pecorari F., Straumann N., Wyler E., and Pluckthun A. Selection and characterization of Her2 binding-designed ankyrin repeat proteins. J. Biol. Chem. 281 (2006) 35167-35175
    • (2006) J. Biol. Chem. , vol.281 , pp. 35167-35175
    • Zahnd, C.1    Pecorari, F.2    Straumann, N.3    Wyler, E.4    Pluckthun, A.5
  • 46
  • 47
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu L., Aha P., Gu K., Kuimelis R.G., Kurz M., Lam T., 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    Aha, P.2    Gu, K.3    Kuimelis, R.G.4    Kurz, M.5    Lam, T.6
  • 48
    • 0037391745 scopus 로고    scopus 로고
    • Recombinant antibodies for cancer diagnosis and therapy
    • Souriau C., and Hudson P.J. Recombinant antibodies for cancer diagnosis and therapy. Expert Opin. Biol. Ther. 3 (2003) 305-318
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 305-318
    • Souriau, C.1    Hudson, P.J.2
  • 49
    • 20844463814 scopus 로고    scopus 로고
    • A general method for greatly improving the affinity of antibodies by using combinatorial libraries
    • Rajpal A., Beyaz N., Haber L., Cappuccilli G., Yee H., Bhatt R.R., et al. A general method for greatly improving the affinity of antibodies by using combinatorial libraries. Proc. Natl Acad. Sci. USA 102 (2005) 8466-8471
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8466-8471
    • Rajpal, A.1    Beyaz, N.2    Haber, L.3    Cappuccilli, G.4    Yee, H.5    Bhatt, R.R.6
  • 50
    • 24344495780 scopus 로고    scopus 로고
    • Alternative views of functional protein binding epitopes obtained by combinatorial shotgun scanning mutagenesis
    • Pal G., Fong S.Y., Kossiakoff A.A., and Sidhu S.S. Alternative views of functional protein binding epitopes obtained by combinatorial shotgun scanning mutagenesis. Protein Sci. 14 (2005) 2405-2413
    • (2005) Protein Sci. , vol.14 , pp. 2405-2413
    • Pal, G.1    Fong, S.Y.2    Kossiakoff, A.A.3    Sidhu, S.S.4
  • 51
    • 9144234724 scopus 로고    scopus 로고
    • A fully human monoclonal antibody to the insulin-like growth factor I receptor blocks ligand-dependent signaling and inhibits human tumor growth in vivo
    • Burtrum D., Zhu Z., Lu D., Anderson D.M., Prewett M., Pereira D.S., et al. A fully human monoclonal antibody to the insulin-like growth factor I receptor blocks ligand-dependent signaling and inhibits human tumor growth in vivo. Cancer Res. 63 (2003) 8912-8921
    • (2003) Cancer Res. , vol.63 , pp. 8912-8921
    • Burtrum, D.1    Zhu, Z.2    Lu, D.3    Anderson, D.M.4    Prewett, M.5    Pereira, D.S.6
  • 52
    • 0141866900 scopus 로고    scopus 로고
    • Human combinatorial Fab library yielding specific and functional antibodies against the human fibroblast growth factor receptor 3
    • Rauchenberger R., Borges E., Thomassen-Wolf E., Rom E., Adar R., Yaniv Y., et al. Human combinatorial Fab library yielding specific and functional antibodies against the human fibroblast growth factor receptor 3. J. Biol. Chem. 278 (2003) 38194-38205
    • (2003) J. Biol. Chem. , vol.278 , pp. 38194-38205
    • Rauchenberger, R.1    Borges, E.2    Thomassen-Wolf, E.3    Rom, E.4    Adar, R.5    Yaniv, Y.6
  • 53
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder E.T., Midelfort K.S., and Wittrup K.D. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc. Natl Acad. Sci. USA 97 (2000) 10701-10705
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 54
    • 0027930862 scopus 로고
    • Association constants of monoclonal antibodies for hapten: heterogeneity of frequency distribution and possible relationship with hapten molecular weight
    • Chappey O., Debray M., Niel E., and Scherrmann J.M. Association constants of monoclonal antibodies for hapten: heterogeneity of frequency distribution and possible relationship with hapten molecular weight. J. Immunol. Methods 24 (1994) 219-225
    • (1994) J. Immunol. Methods , vol.24 , pp. 219-225
    • Chappey, O.1    Debray, M.2    Niel, E.3    Scherrmann, J.M.4
  • 56
    • 0031917485 scopus 로고    scopus 로고
    • Engineering the steroid-specificity of an anti-17β-estradiol Fab by random mutagenesis and competitive phage panning
    • Saviranta P., Pajunen M., Jauria P., Karp M., Pettersson K., Mantsala P., and Lovgren T. Engineering the steroid-specificity of an anti-17β-estradiol Fab by random mutagenesis and competitive phage panning. Protein Eng. 11 (1998) 143-152
    • (1998) Protein Eng. , vol.11 , pp. 143-152
    • Saviranta, P.1    Pajunen, M.2    Jauria, P.3    Karp, M.4    Pettersson, K.5    Mantsala, P.6    Lovgren, T.7
  • 57
  • 59
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton T. (Ed), Oxford University Press, Oxford
    • Pace C.N., and Scholtz J.M. Measuring the conformational stability of a protein. In: Creighton T. (Ed). Protein Structure: A Practical Approach. 2nd edit. vol. 75 (1997), Oxford University Press, Oxford 299-322
    • (1997) Protein Structure: A Practical Approach. 2nd edit. , vol.75 , pp. 299-322
    • Pace, C.N.1    Scholtz, J.M.2
  • 60
    • 0002452464 scopus 로고
    • Proceedings of the CCP4 study weekend
    • Lawyer L., Isaacs N., and Bailey S. (Eds), Daresbury Laboratory, Warrington, UK
    • Otwinowski Z. Proceedings of the CCP4 study weekend. In: Lawyer L., Isaacs N., and Bailey S. (Eds). Proceedings of the CCP4 Study Weekend (1993), Daresbury Laboratory, Warrington, UK 56-62
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 62
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A 50 (1994) 157-163
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 63
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S., and Kjelgaard M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallog. sect. A 47 (1991) 100-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 100-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjelgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.