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Volumn 42, Issue 6, 2003, Pages 1517-1528

Structure-based improvement of the biophysical properties of immunoglobulin VH domains with a generalizable approach

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BINDING ENERGY; CONFORMATIONS; GENETIC ENGINEERING; HYDROPHOBICITY; IMMUNOLOGY; MOLECULAR BIOLOGY; MOLECULAR STRUCTURE;

EID: 0037452533     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026448p     Document Type: Article
Times cited : (96)

References (42)
  • 2
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber, R., Malia, M., Pfitzinger, I., and 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
  • 5
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta, E. V., Raines, R. T., Plückthun, A., and Wittrup, K. D. (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments, Nat. Biotechnol. 16, 773-777.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Plückthun, A.3    Wittrup, K.D.4
  • 7
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Wörn, A., and Plückthun, A. (2001) Stability engineering of antibody single-chain Fv fragments, J. Mol. Biol. 305, 989-1010.
    • (2001) J. Mol. Biol. , vol.305 , pp. 989-1010
    • Wörn, A.1    Plückthun, A.2
  • 9
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba, L., Honegger, A., Krebber, C., and Plückthun, A. (1997) Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment, Protein Eng. 10, 435-444.
    • (1997) Protein Eng. , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Plückthun, A.4
  • 10
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behavior of ScFv fragments: Identification, classification, and improvement by protein engineering
    • Wörn, A., and Plückthun, A. (1999) Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering, Biochemistry 38, 8739-8750.
    • (1999) Biochemistry , vol.38 , pp. 8739-8750
    • Wörn, A.1    Plückthun, A.2
  • 11
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human variable antibody domains
    • Ewert, S., Huber, T., Honegger, A., and Plückthun, A. (2003) Biophysical properties of human variable antibody domains, J. Mol. Biol. 325, 531-553.
    • (2003) J. Mol. Biol. , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Plückthun, A.4
  • 12
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann, H., and Plückthun, A. (1998) Selection for a periplasmic factor improving phage display and functional periplasmic expression, Nat. Biotechnol. 16, 376-380.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Plückthun, A.2
  • 13
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cisprolines
    • Bothmann, H., and Plückthun, A. (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cisprolines, J. Biol. Chem. 275, 17100-17105.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Plückthun, A.2
  • 14
    • 0030916353 scopus 로고    scopus 로고
    • Two amino acid mutations in an antihuman CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity
    • Kipriyanov, S. M., Moldenhauer, G., Martin, A. C., Kupriyanova, O. A., and Little, M. (1997) Two amino acid mutations in an antihuman CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity, Protein Eng. 10, 445-453.
    • (1997) Protein Eng. , vol.10 , pp. 445-453
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Martin, A.C.3    Kupriyanova, O.A.4    Little, M.5
  • 15
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik, A., and Plückthun, A. (1995) Engineered turns of a recombinant antibody improve its in vivo folding, Protein Eng. 8, 81-89.
    • (1995) Protein Eng. , vol.8 , pp. 81-89
    • Knappik, A.1    Plückthun, A.2
  • 16
    • 0030912095 scopus 로고    scopus 로고
    • Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in Escherichia coli
    • Forsberg, G., Forsgren, M., Jaki, M., Norin, M., Sterky, C., Enhorning, A., Larsson, K., Ericsson, M., and Björk, P. (1997) Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in Escherichia coli, J. Biol. Chem. 272, 12430-12436.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12430-12436
    • Forsberg, G.1    Forsgren, M.2    Jaki, M.3    Norin, M.4    Sterky, C.5    Enhorning, A.6    Larsson, K.7    Ericsson, M.8    Björk, P.9
  • 17
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber, V., Plückthun, A., and Schmid, F. X. (1998) Selecting proteins with improved stability by a phage-based method, Nat. Biotechnol. 16, 955-960.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 955-960
    • Sieber, V.1    Plückthun, A.2    Schmid, F.X.3
  • 18
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • Jung, S., Honegger, A., and Plückthun, A. (1999) Selection for improved protein stability by phage display, J. Mol. Biol. 294, 163-180.
    • (1999) J. Mol. Biol. , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Plückthun, A.3
  • 20
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilizing mutations in a protein domain
    • Steipe, B., Schiller, B., Plückthun, A., and Steinbacher, S. (1994) Sequence statistics reliably predict stabilizing mutations in a protein domain, J. Mol. Biol. 240, 188-192.
    • (1994) J. Mol. Biol. , vol.240 , pp. 188-192
    • Steipe, B.1    Schiller, B.2    Plückthun, A.3    Steinbacher, S.4
  • 21
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A., and Virnekäs, B. (2000) Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides, J. Mol. Biol. 296, 57-86.
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6    Hoess, A.7    Wölle, J.8    Plückthun, A.9    Virnekäs, B.10
  • 23
    • 0035793214 scopus 로고    scopus 로고
    • The scFv fragment of the antibody hu4D5-8: Evidence for early premature domain interaction in refolding
    • Jäger, M., Gehrig, P., and Plückthun, A. (2001) The scFv fragment of the antibody hu4D5-8: evidence for early premature domain interaction in refolding, J. Mol. Biol. 305, 1111-1129.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1111-1129
    • Jäger, M.1    Gehrig, P.2    Plückthun, A.3
  • 24
    • 0027978869 scopus 로고
    • Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors
    • Karlsson, R. (1994) Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors, Anal. Biochem. 221, 142-151.
    • (1994) Anal. Biochem. , vol.221 , pp. 142-151
    • Karlsson, R.1
  • 25
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: Large differences from values determined from binding kinetics
    • Nieba, L., Krebber, A., and Plückthun, A. (1996) Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics, Anal. Biochem. 234, 155-165.
    • (1996) Anal. Biochem. , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Plückthun, A.3
  • 26
    • 0032564346 scopus 로고    scopus 로고
    • Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries
    • Hanes, J., Jermutus, L., Weber-Bornhauser, S., Bosshard, H. R., and Plückthun, A. (1998) Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries, Proc. Natl. Acad. Sci. U.S.A. 95, 14130-14135.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14130-14135
    • Hanes, J.1    Jermutus, L.2    Weber-Bornhauser, S.3    Bosshard, H.R.4    Plückthun, A.5
  • 27
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins, Biophys. J. 66, 482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 28
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 29
    • 0345044918 scopus 로고    scopus 로고
    • Domain interactions in antibody Fv and scFv fragments: Effects on unfolding kinetics and equilibria
    • Jäger, M., and Plückthun, A. (1999) Domain interactions in antibody Fv and scFv fragments: effects on unfolding kinetics and equilibria, FEBS Lett. 462, 307-312.
    • (1999) FEBS Lett. , vol.462 , pp. 307-312
    • Jäger, M.1    Plückthun, A.2
  • 30
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 31
    • 0030581145 scopus 로고    scopus 로고
    • The use of amino acid patterns of classified helices and strands in secondary structure prediction
    • Zhu, Z. Y., and Blundell, T. L. (1996) The use of amino acid patterns of classified helices and strands in secondary structure prediction, J. Mol. Biol. 260, 261-276.
    • (1996) J. Mol. Biol. , vol.260 , pp. 261-276
    • Zhu, Z.Y.1    Blundell, T.L.2
  • 32
    • 0035827218 scopus 로고    scopus 로고
    • The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains
    • Honegger, A., and Plückthun, A. (2001) The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains, J. Mol. Biol. 309, 687-699.
    • (2001) J. Mol. Biol. , vol.309 , pp. 687-699
    • Honegger, A.1    Plückthun, A.2
  • 33
    • 0035827172 scopus 로고    scopus 로고
    • Yet another numbering scheme for immunoglobulin variable domains: An automatic modeling and analysis tool
    • Honegger, A., and Plückthun, A. (2001) Yet another numbering scheme for immunoglobulin variable domains: An automatic modeling and analysis tool, J. Mol. Biol. 309, 657-670.
    • (2001) J. Mol. Biol. , vol.309 , pp. 657-670
    • Honegger, A.1    Plückthun, A.2
  • 34
    • 0035827149 scopus 로고    scopus 로고
    • The importance of framework residues H6, H7 and H10 in antibody heavy chains: Experimental evidence for a new structural subclassification of antibody VH domain
    • Jung, S., Spinelli, S., Schimmele, B., Honegger, A., Pugliese, L., Cambillau, C., and Plückthun, A. (2001) The importance of framework residues H6, H7 and H10 in antibody heavy chains: experimental evidence for a new structural subclassification of antibody VH domain, J. Mol. Biol. 309, 701-716.
    • (2001) J. Mol. Biol. , vol.309 , pp. 701-716
    • Jung, S.1    Spinelli, S.2    Schimmele, B.3    Honegger, A.4    Pugliese, L.5    Cambillau, C.6    Plückthun, A.7
  • 38
    • 0026673067 scopus 로고
    • By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro
    • Hoogenboom, H. R., and Winter, G. (1992) By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro, J. Mol. Biol. 227, 381-388.
    • (1992) J. Mol. Biol. , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 42
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 29-32, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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