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Volumn 138, Issue 3, 2002, Pages 171-186

Antiferritin VL homodimer binds human spleen ferritin with high specificity

Author keywords

Antibody light chain; Antiferritin antibody; CDR loops; Model structures; VL domain; X ray structure

Indexed keywords

DIMER; FERRITIN; FERRITIN ANTIBODY; LYSOZYME;

EID: 18644361957     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00015-1     Document Type: Article
Times cited : (10)

References (72)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams, P.D., Pannu, N.S., Read, R.J., Brünger, A.T., 1997. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA 94, 5018-5023.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 2
    • 0032942076 scopus 로고    scopus 로고
    • Extending the limits of molecular replacement through combined simulated annealing and maximum-likelihood refinement
    • Adams, P.D., Pannu, N.S., Read, R.J., Brünger, A.T., 1999. Extending the limits of molecular replacement through combined simulated annealing and maximum-likelihood refinement. Acta Crystallogr. D 55, 181-190.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 181-190
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 3
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani, B., Lesk, A.M., Chothia, C., 1997. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273, 927-948.
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 6
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J., 1993. ALSCRIPT: A tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 10
    • 0031586001 scopus 로고    scopus 로고
    • Stabilization of a recombinant Fv fragment by base-loop interconnection and VH-VL permutation
    • Brinkmann, U., Di Carlo, A., Vasmatzis, G., Kurochkina, N., Beers, R., Lee, B., Pastan, I., 1997. Stabilization of a recombinant Fv fragment by base-loop interconnection and VH-VL permutation. J. Mol. Biol. 268, 107-117.
    • (1997) J. Mol. Biol. , vol.268 , pp. 107-117
    • Brinkmann, U.1    Di Carlo, A.2    Vasmatzis, G.3    Kurochkina, N.4    Beers, R.5    Lee, B.6    Pastan, I.7
  • 11
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T., 1992. Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 12
    • 0031569392 scopus 로고    scopus 로고
    • New applications of simulated annealing in X-ray crystallography and solution NMR
    • Brünger, A.T., Adams, P.D., Rice, L.M., 1997. New applications of simulated annealing in X-ray crystallography and solution NMR. Structure 5, 325-336.
    • (1997) Structure , vol.5 , pp. 325-336
    • Brünger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 13
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T., Krukowski, A., Erickson, J.W., 1990. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A 46, 585-593.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 14
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J., Karplus, M., 1987. Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 15
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia, C., Lesk, A.M., 1987. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 16
    • 0024429683 scopus 로고
    • Development of an immunoassay for all human isoferritins, its application to serum ferritin evaluation
    • Cozzi, A., Levi, S., Bazzagaluppi, E., Ruggeri, G., Arosio, P., 1989. Development of an immunoassay for all human isoferritins, its application to serum ferritin evaluation. Clin. Chim. Acta 184, 197-206.
    • (1989) Clin. Chim. Acta , vol.184 , pp. 197-206
    • Cozzi, A.1    Levi, S.2    Bazzagaluppi, E.3    Ruggeri, G.4    Arosio, P.5
  • 17
    • 0029746203 scopus 로고    scopus 로고
    • Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved protein stability
    • Davies, J., Riechmann, L., 1996. Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved protein stability. Protein Eng. 9, 531-537.
    • (1996) Protein Eng. , vol.9 , pp. 531-537
    • Davies, J.1    Riechmann, L.2
  • 20
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber, R., Malia, M., Pfitzinger, I., Plückthun, A., 1990. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry 29, 1362-1367.
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Plückthun, A.4
  • 21
    • 0028856717 scopus 로고
    • Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain
    • Helms, L.R., Wetzel, R., 1995. Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain. Protein Sci. 4, 2073-2081.
    • (1995) Protein Sci. , vol.4 , pp. 2073-2081
    • Helms, L.R.1    Wetzel, R.2
  • 23
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig, M., Darimont, B., Sterner, R., Kirschner, K., Jansonius, J.N., 1995. 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability. Structure 3, 1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 24
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel, A., Kim, S.-H., Brünger, A.T., 1992. Model bias in macromolecular crystal structures. Acta Crystallogr. A 48, 851-858.
    • (1992) Acta Crystallogr. A , vol.48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brünger, A.T.3
  • 25
    • 0030855425 scopus 로고    scopus 로고
    • The three-dimensional structure of a T-cell antigen receptor Vα Vβ heterodimer reveals a novel arrangement of the Vβ domain
    • Housset, D., Mazza, G., Grégoire, C., Piras, C., Malissen, B., Fontecilla-Camps, J.C., 1997. The three-dimensional structure of a T-cell antigen receptor Vα Vβ heterodimer reveals a novel arrangement of the Vβ domain. EMBO J. 16, 4205-4216.
    • (1997) EMBO J. , vol.16 , pp. 4205-4216
    • Housset, D.1    Mazza, G.2    Grégoire, C.3    Piras, C.4    Malissen, B.5    Fontecilla-Camps, J.C.6
  • 26
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle, M.R., Helms, L.R., Li, L., Chan, W., Wetzel, R., 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. USA 91, 5446-5450.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 28
    • 0001817941 scopus 로고    scopus 로고
    • Comparison of protein three-dimensional structures
    • Higgins, D., Taylor, W. (Eds.). Oxford University Press, Oxford
    • Johnson, M.S., Lehtonen, J.V., 2000. Comparison of protein three-dimensional structures. In: Higgins, D., Taylor, W. (Eds.), Bioinformatics: Sequence, Structure, and Databanks. Oxford University Press, Oxford, pp. 15-50.
    • (2000) Bioinformatics: Sequence, Structure, and Databanks , pp. 15-50
    • Johnson, M.S.1    Lehtonen, J.V.2
  • 29
    • 0029884429 scopus 로고    scopus 로고
    • Discrimination of common protein folds: Applications of structural information to sequence/structure comparisons
    • Johnson, M.S., May, A.C.W., Rodionov, M.A., Overington, J.P., 1996. Discrimination of common protein folds: Applications of structural information to sequence/structure comparisons. Methods Enzymol. 266, 575-598.
    • (1996) Methods Enzymol. , vol.266 , pp. 575-598
    • Johnson, M.S.1    May, A.C.W.2    Rodionov, M.A.3    Overington, J.P.4
  • 30
    • 0027361123 scopus 로고
    • A structural basis for the comparison of sequences: An evaluation of scoring methodologies
    • Johnson, M.S., Overington, J.P., 1993. A structural basis for the comparison of sequences: An evaluation of scoring methodologies. J. Mol. Biol. 233, 716-738.
    • (1993) J. Mol. Biol. , vol.233 , pp. 716-738
    • Johnson, M.S.1    Overington, J.P.2
  • 31
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones, P.T., Dear, P.H., Foote, J., Neuberger, M.S., Winter, G., 1986. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321, 522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A., Jaenicke, R., 1995. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246, 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 35
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J., 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 36
    • 0032144264 scopus 로고    scopus 로고
    • Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity
    • Kravchuk, Z.I., Chumanevich, A.A., Vlasov, A.P., Martsev, S.P., 1998. Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity. J. Immunol. Methods 217, 131-141.
    • (1998) J. Immunol. Methods , vol.217 , pp. 131-141
    • Kravchuk, Z.I.1    Chumanevich, A.A.2    Vlasov, A.P.3    Martsev, S.P.4
  • 37
  • 38
    • 0032478777 scopus 로고    scopus 로고
    • Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments
    • Lawrence, L.J., Kortt, A.A., Iliades, P., Tulloch, P.A., Hudson, P.J., 1998. Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett. 425, 479-484.
    • (1998) FEBS Lett. , vol.425 , pp. 479-484
    • Lawrence, L.J.1    Kortt, A.A.2    Iliades, P.3    Tulloch, P.A.4    Hudson, P.J.5
  • 40
    • 0034636843 scopus 로고    scopus 로고
    • The antiferritin single-chain Fv fragment is a functional protein with properties of a partially structured state: Comparison with the completely folded VL domain
    • Martsev, S.P., Chumanevich, A.A., Vlasov, A.P., Dubnovitsky, A.P., Tsybovsky, Y.I., Deyev, S.M., Cozzi, A., Arosio, P., Kravchuk, Z.I., 2000. The antiferritin single-chain Fv fragment is a functional protein with properties of a partially structured state: Comparison with the completely folded VL domain. Biochemistry 39, 8047-8057.
    • (2000) Biochemistry , vol.39 , pp. 8047-8057
    • Martsev, S.P.1    Chumanevich, A.A.2    Vlasov, A.P.3    Dubnovitsky, A.P.4    Tsybovsky, Y.I.5    Deyev, S.M.6    Cozzi, A.7    Arosio, P.8    Kravchuk, Z.I.9
  • 42
    • 0028892153 scopus 로고
    • Modification of monoclonal and polyclonal IgG with palladium (II) coproporphyrin I: Stimulatory and inhibitory functional effects induced by two different methods
    • Martsev, S.P., Preygerzon, V.A., Mel'nikova, Y.I., Kravchuk, Z.I., Ponomarev, G.V., Lunev, V.E., Savitsky, A.P., 1995. Modification of monoclonal and polyclonal IgG with palladium (II) coproporphyrin I: Stimulatory and inhibitory functional effects induced by two different methods. J. Immunol. Methods 186, 293-304.
    • (1995) J. Immunol. Methods , vol.186 , pp. 293-304
    • Martsev, S.P.1    Preygerzon, V.A.2    Mel'nikova, Y.I.3    Kravchuk, Z.I.4    Ponomarev, G.V.5    Lunev, V.E.6    Savitsky, A.P.7
  • 43
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W., 1968. Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 44
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A., Bacon, D.J., 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 45
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • Morea, V., Tramontano, A., Rustici, M., Chothia, C., Lesk, A.M., 1998. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275, 269-294.
    • (1998) J. Mol. Biol. , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properites of hydrocarbons
    • Nicholls, A., Sharp, K.A., Honing, B., 1991. Protein folding and association: Insights from the interfacial and thermodynamic properites of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honing, B.3
  • 47
    • 0026438116 scopus 로고
    • Electrostatic fields in antibodies and antibody/antigen complexes
    • Novotný, J., Sharp, K., 1992. Electrostatic fields in antibodies and antibody/antigen complexes. Prog. Biophys. Mol. Biol. 58, 203-224.
    • (1992) Prog. Biophys. Mol. Biol. , vol.58 , pp. 203-224
    • Novotný, J.1    Sharp, K.2
  • 48
    • 0032568959 scopus 로고    scopus 로고
    • Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure predictions
    • Oliva, B., Bates, P.A., Querol, E., Avilés, F.X., Sternberg, M.J.E., 1998. Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure predictions. J. Mol. Biol. 279, 1193-1210.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1193-1210
    • Oliva, B.1    Bates, P.A.2    Querol, E.3    Avilés, F.X.4    Sternberg, M.J.E.5
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Procession of X-ray diffraction data collected in oscillation mode
    • Carter Jr., C.W., Sweet, R.M. (Eds.), Academic Press, New York
    • Otwinowski, Z., Minor, W., 1997. Procession of X-ray diffraction data collected in oscillation mode. In: Carter Jr., C.W., Sweet, R.M. (Eds.), Macromolecular Crystallography, Part A, vol. 276. Academic Press, New York, pp. 307-326.
    • (1997) Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N.S., Read, R.J., 1996. Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668.
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 52
    • 0031776392 scopus 로고    scopus 로고
    • Reengineering immunoglobulin domain interactions by introduction of charged residues
    • Raffen, R., Stevens, P.W., Boogaard, C., Schiffer, M., Stevens, F.J., 1998. Reengineering immunoglobulin domain interactions by introduction of charged residues. Protein Eng. 11, 303-309.
    • (1998) Protein Eng. , vol.11 , pp. 303-309
    • Raffen, R.1    Stevens, P.W.2    Boogaard, C.3    Schiffer, M.4    Stevens, F.J.5
  • 53
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J., 1986. Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 54
    • 0028070557 scopus 로고
    • Torsion angle dynamics reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L.M., Brünger, A.T., 1994. Torsion angle dynamics reduced variable conformational sampling enhances crystallographic structure refinement. Proteins: Struct. Funct. Genet. 19, 277-290.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 55
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann, M.G., Moras, D., Olsen, K.W., 1974. Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 56
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial restraints
    • Šali, A., Blundell, T.L., 1993. Comparative modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 57
    • 0029896617 scopus 로고    scopus 로고
    • An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases
    • Salminen, T., Teplyakov, A., Kankare, J., Cooperman, B.S., Lahti, R., Goldman, A., 1996. An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases. Protein Sci. 5, 1014-1025.
    • (1996) Protein Sci. , vol.5 , pp. 1014-1025
    • Salminen, T.1    Teplyakov, A.2    Kankare, J.3    Cooperman, B.S.4    Lahti, R.5    Goldman, A.6
  • 58
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio, P., Levi, A., Cozzi, A., Rovida, E., Alberitini, A., Arosio, P., 1993. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268, 12744-12748.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, A.2    Cozzi, A.3    Rovida, E.4    Alberitini, A.5    Arosio, P.6
  • 59
    • 0017076856 scopus 로고
    • Binding of 2,4-dinitrophenyl derivatives by the light chain dimer obtained from immunoglobulin A produced by MOPC-315 mouse myeloma
    • Schechter, I., Ziv, E., Licht, A., 1976. Binding of 2,4-dinitrophenyl derivatives by the light chain dimer obtained from immunoglobulin A produced by MOPC-315 mouse myeloma. Biochemistry 15
    • (1976) Biochemistry , vol.15
    • Schechter, I.1    Ziv, E.2    Licht, A.3
  • 60
    • 0033058759 scopus 로고    scopus 로고
    • H3-rules: Identification for CDR-H3 structures in antibodies
    • Shirai, H., Kidera, A., Nakamura, H., 1999. H3-rules: Identification for CDR-H3 structures in antibodies. FEBS Lett. 455, 188-197.
    • (1999) FEBS Lett. , vol.455 , pp. 188-197
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 61
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra, A., Plückthun, A., 1988. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240, 1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Plückthun, A.2
  • 64
    • 0023809071 scopus 로고
    • A diffusion limited reaction theory for a microtiter plate assay
    • Stenberg, M., Wertehn, M., Theander, S., Bygren, H., 1988. A diffusion limited reaction theory for a microtiter plate assay. J. Immunol. Methods 112, 23-29.
    • (1988) J. Immunol. Methods , vol.112 , pp. 23-29
    • Stenberg, M.1    Wertehn, M.2    Theander, S.3    Bygren, H.4
  • 65
    • 0025775997 scopus 로고
    • Bence Jones proteins: A powerful tool for the fundamental study of protein chemistry and pathophysiology
    • Stevens, B.J., Solomon, A., Schiffer, M., 1991. Bence Jones proteins: A powerful tool for the fundamental study of protein chemistry and pathophysiology. Biochemistry 30, 6803-6805.
    • (1991) Biochemistry , vol.30 , pp. 6803-6805
    • Stevens, B.J.1    Solomon, A.2    Schiffer, M.3
  • 66
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilágyi, A., Závodszky, P., 2000. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey. Structure 8, 493-504.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilágyi, A.1    Závodszky, P.2
  • 67
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward, E.S., Güssow, D., Griffiths, A.D., Jones, P.T., Winter, G., 1989. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341, 544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Güssow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 68
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I.A., Stanfield, R.L., 1994. Antibody-antigen interactions: New structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 69
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, ion pairs
    • Vogt, G., Woell, S., Argos, P., 1997. Protein thermal stability, hydrogen bonds, ion pairs. J. Mol. Biol. 269.
    • (1997) J. Mol. Biol. , pp. 269
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 70
    • 0025609563 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G., 1990. WHAT IF: A molecular modeling and drug design program. Protein Eng. 4, 221-223.
    • (1990) Protein Eng. , vol.4 , pp. 221-223
    • Vriend, G.1
  • 72
    • 0026684815 scopus 로고
    • Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms
    • Yokota, T., Milenic, D.E., Whitlow, M., Schlom, J., 1992. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res. 52, 3402-3408.
    • (1992) Cancer Res. , vol.52 , pp. 3402-3408
    • Yokota, T.1    Milenic, D.E.2    Whitlow, M.3    Schlom, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.