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Volumn 12, Issue 12, 2003, Pages 2732-2747

C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer

Author keywords

ANS; Assembly; Folding; Hydrophobic interactions; P22 tailspike

Indexed keywords

OLIGOMER; PROTEIN; PROTEIN P22; UNCLASSIFIED DRUG;

EID: 0242336022     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03150303     Document Type: Article
Times cited : (21)

References (61)
  • 1
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization
    • Bachinger, H.P., Bruckner, P., Timpl, R., Prockop, D.J., and Engel, J. 1980. Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur. J. Biochem. 106: 619-632.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 619-632
    • Bachinger, H.P.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 2
    • 0027178317 scopus 로고
    • Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme
    • Baldwin, T.O., Ziegler, M.M., Chaffotte, A.F., and Goldberg, M.E. 1993. Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme. J. Biol. Chem. 268: 10766-10772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10766-10772
    • Baldwin, T.O.1    Ziegler, M.M.2    Chaffotte, A.F.3    Goldberg, M.E.4
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P.B., and Steitz, T.A. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289: 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 4
    • 0029031409 scopus 로고
    • Mutations that stabilize folding intermediates of phage P22 tailspike protein: Folding in vivo and in vitro, stability, and structural context
    • Beibinger, M., Lee, S.C., Steinbacher, S., Reinemer, P., Huber, R., Yu, M.-H., and Seckler, R. 1995. Mutations that stabilize folding intermediates of phage P22 tailspike protein: Folding in vivo and in vitro, stability, and structural context. J. Mol. Biol. 249: 185-194.
    • (1995) J. Mol. Biol. , vol.249 , pp. 185-194
    • Beibinger, M.1    Lee, S.C.2    Steinbacher, S.3    Reinemer, P.4    Huber, R.5    Yu, M.-H.6    Seckler, R.7
  • 5
    • 0037161301 scopus 로고    scopus 로고
    • Characterization of the protrimer intermediate in the folding pathway of the interdigitated β-helix tailspike protein
    • Benton, C.B., King, J., and Clark, P.L. 2002. Characterization of the protrimer intermediate in the folding pathway of the interdigitated β-helix tailspike protein. Biochemistry 41: 5093-5103.
    • (2002) Biochemistry , vol.41 , pp. 5093-5103
    • Benton, C.B.1    King, J.2    Clark, P.L.3
  • 6
    • 0031854135 scopus 로고    scopus 로고
    • Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation
    • Betts, S.D. and King, J. 1998. Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation. Protein Sci. 7: 1516-1523.
    • (1998) Protein Sci. , vol.7 , pp. 1516-1523
    • Betts, S.D.1    King, J.2
  • 7
    • 0027509618 scopus 로고
    • Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro
    • Brunschier, R., Danner, M., and Seckler, R. 1993. Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J. Biol. Chem. 268: 2767-2772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2767-2772
    • Brunschier, R.1    Danner, M.2    Seckler, R.3
  • 8
    • 0035961347 scopus 로고    scopus 로고
    • Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases
    • Buevich, A. and Baum, J. 2001. Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 356: 159-168.
    • (2001) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.356 , pp. 159-168
    • Buevich, A.1    Baum, J.2
  • 9
    • 0036892063 scopus 로고    scopus 로고
    • Interdependent interactions between TFIIB, TATA binding protein, and DNA
    • Buratowski, R.M., Downs, J., and Buratowski, S. 2002. Interdependent interactions between TFIIB, TATA binding protein, and DNA. Mol. Cell. Biol. 22: 8735-8743.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8735-8743
    • Buratowski, R.M.1    Downs, J.2    Buratowski, S.3
  • 10
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P., Stetefeld, J., and Strelkov, S.V. 2001. Coiled coils: A highly versatile protein folding motif. Trends Cell Biol. 11: 82-88.
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 11
    • 0036307698 scopus 로고    scopus 로고
    • Improving coiled-coil stability by optimizing ionic interactions
    • Burkhard, P., Ivaninskii, S., and Lustig, A. 2002. Improving coiled-coil stability by optimizing ionic interactions. J. Mol. Biol. 318: 901-910.
    • (2002) J. Mol. Biol. , vol.318 , pp. 901-910
    • Burkhard, P.1    Ivaninskii, S.2    Lustig, A.3
  • 12
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • Capaldi, A.P., Kleanthous, C., and Radford, S.E. 2002. Im7 folding mechanism: Misfolding on a path to the native state. Nat. Struct. Biol. 9: 209-216.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 13
    • 0035816546 scopus 로고    scopus 로고
    • A newly synthesized, ribosome-bound polypeptide chain adopts conformation dissimilar from early in vitro refolding intermediates
    • Clark, P.L. and King, J. 2001. A newly synthesized, ribosome-bound polypeptide chain adopts conformation dissimilar from early in vitro refolding intermediates. J. Biol. Chem. 276: 25411-25420.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25411-25420
    • Clark, P.L.1    King, J.2
  • 14
    • 0242290827 scopus 로고    scopus 로고
    • Non-native interactions between cysteines direct productive assembly of P22 tailspike protein
    • in press
    • Danek, B.L. and Robinson, A.S. 2003. Non-native interactions between cysteines direct productive assembly of P22 tailspike protein. Biophys. J. 85: (in press)
    • (2003) Biophys. J. , vol.85
    • Danek, B.L.1    Robinson, A.S.2
  • 15
    • 0027370268 scopus 로고
    • Mechanism of phage P22 tailspike folding mutations
    • Danner, M. and Seckler, R. 1993. Mechanism of phage P22 tailspike folding mutations. Protein Sci. 2: 1869-1881.
    • (1993) Protein Sci. , vol.2 , pp. 1869-1881
    • Danner, M.1    Seckler, R.2
  • 16
    • 0027165264 scopus 로고
    • Folding and assembly of phage P22 tailspike protein lacking N-terminal, head-binding domain
    • Danner, M., Fuchs, A., Miller, S., and Seckler, R. 1993. Folding and assembly of phage P22 tailspike protein lacking N-terminal, head-binding domain. Eur. J. Biochem. 215: 653-661.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 653-661
    • Danner, M.1    Fuchs, A.2    Miller, S.3    Seckler, R.4
  • 17
    • 0025821345 scopus 로고
    • In vitro folding pathway of phage P22 tailspike protein
    • Fuchs, A., Seiderer, C., and Seckler, R. 1991. In vitro folding pathway of phage P22 tailspike protein. Biochemistry 30: 6598-6604.
    • (1991) Biochemistry , vol.30 , pp. 6598-6604
    • Fuchs, A.1    Seiderer, C.2    Seckler, R.3
  • 18
    • 0032506048 scopus 로고    scopus 로고
    • Mechanism of folding of the dimeric core domain of Escherichia coli Trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate
    • Gloss, L.M. and Matthews, C.R. 1998. Mechanism of folding of the dimeric core domain of Escherichia coli Trp repressor: A nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry 37: 15990-15999.
    • (1998) Biochemistry , vol.37 , pp. 15990-15999
    • Gloss, L.M.1    Matthews, C.R.2
  • 19
    • 0019474427 scopus 로고
    • Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30°C
    • Goldenberg, D.P. and King, J. 1981. Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30°C. J. Mol. Biol. 145: 633-651.
    • (1981) J. Mol. Biol. , vol.145 , pp. 633-651
    • Goldenberg, D.P.1    King, J.2
  • 20
    • 1542563859 scopus 로고
    • Trimeric intermediate in the in vivo folding and subunit assembly of the tailspike endorhamnosidase of bacteriophage P22
    • -. 1982. Trimeric intermediate in the in vivo folding and subunit assembly of the tailspike endorhamnosidase of bacteriophage P22. Proc. Natl. Acad. Sci. 79: 3403-3407.
    • (1982) Proc. Natl. Acad. Sci. , vol.79 , pp. 3403-3407
  • 21
    • 0011191567 scopus 로고
    • Genetic analysis of the folding pathway for the tailspike protein of phage P22
    • Goldenberg, D., Smith, D.H., and King, J. 1983. Genetic analysis of the folding pathway for the tailspike protein of phage P22. Proc. Natl. Acad. Sci. 80: 7060-7064.
    • (1983) Proc. Natl. Acad. Sci. , vol.80 , pp. 7060-7064
    • Goldenberg, D.1    Smith, D.H.2    King, J.3
  • 22
    • 0023883586 scopus 로고
    • Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation a model for inclusion body formation
    • Haase-Pettingell, C. and King, J. 1988. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation a model for inclusion body formation. J. Biol. Chem. 263: 4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.1    King, J.2
  • 23
    • 0035104501 scopus 로고    scopus 로고
    • Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike
    • Haase-Pettingell, C., Betts, S.D., Raso, S.W., Stuart, L., Robinson, A., and King, J. 2000. Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike. Protein Sci. 10: 397-410.
    • (2000) Protein Sci. , vol.10 , pp. 397-410
    • Haase-Pettingell, C.1    Betts, S.D.2    Raso, S.W.3    Stuart, L.4    Robinson, A.5    King, J.6
  • 24
    • 0031048105 scopus 로고    scopus 로고
    • Roles of hydrogen bonding residues in the interaction between the α and β subunits in the tryptophan synthase complex
    • Hiraga, K. and Yutani, K. 1997. Roles of hydrogen bonding residues in the interaction between the α and β subunits in the tryptophan synthase complex. J. Biol. Chem. 272: 4935-4940.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4935-4940
    • Hiraga, K.1    Yutani, K.2
  • 25
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. 1987. Folding and association of proteins. Prog. Biophys. Mol. Biol. 49: 117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 26
    • 0039792280 scopus 로고    scopus 로고
    • Getting a grip: Polymerases and their substrate complexes
    • Jager, J. and Pata, J.D. 1999. Getting a grip: Polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 9: 21-28.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 21-28
    • Jager, J.1    Pata, J.D.2
  • 27
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J. and Chothia, C. 1990. The structure of protein-protein recognition sites. J. Biol. Chem. 265: 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 28
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction: Nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus
    • Kang, K.I., Devin, J., Cadepond, F., Jibard, N., Guiochon-Mantel, A., Baulieu, E.E., and Catelli, M.G. 1994. In vivo functional protein-protein interaction: Nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus. Proc. Natl. Acad. Sci. 91: 340-344.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 340-344
    • Kang, K.I.1    Devin, J.2    Cadepond, F.3    Jibard, N.4    Guiochon-Mantel, A.5    Baulieu, E.E.6    Catelli, M.G.7
  • 29
    • 0038532258 scopus 로고    scopus 로고
    • Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
    • Kim, Y.S., Randolph, T.W., Manning, M.C., Stevens, F.J., and Carpenter, J.F. 2003. Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 278: 10842-10850.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10842-10850
    • Kim, Y.S.1    Randolph, T.W.2    Manning, M.C.3    Stevens, F.J.4    Carpenter, J.F.5
  • 30
    • 0022482647 scopus 로고
    • Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase
    • King, J. and Yu, M.-H. 1986. Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase. Methods Enzymol. 131: 250-266.
    • (1986) Methods Enzymol. , vol.131 , pp. 250-266
    • King, J.1    Yu, M.-H.2
  • 31
    • 0034492510 scopus 로고    scopus 로고
    • β-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike
    • Kreisberg, J.F., Betts, S.D., and King, J. 2000. β-Helix core packing within the triple-stranded oligomerization domain of the P22 tailspike. Protein Sci. 9: 2338-2343.
    • (2000) Protein Sci. , vol.9 , pp. 2338-2343
    • Kreisberg, J.F.1    Betts, S.D.2    King, J.3
  • 32
    • 0036127119 scopus 로고    scopus 로고
    • The inter-digitated β-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization
    • Kreisberg, J.F., Betts, S.D., Haase-Pettingell, C., and King, J. 2002. The inter-digitated β-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization. Protein Sci. 11: 820-830.
    • (2002) Protein Sci. , vol.11 , pp. 820-830
    • Kreisberg, J.F.1    Betts, S.D.2    Haase-Pettingell, C.3    King, J.4
  • 33
    • 0035857484 scopus 로고    scopus 로고
    • Oligomerization of Escherichia coli enterotoxin b through its C-terminal hydrophobic α-helix
    • Labrie, V., Harel, J., and Dubreuil, J.D. 2001. Oligomerization of Escherichia coli enterotoxin b through its C-terminal hydrophobic α-helix. Biochim. Biophys. Acta 1535: 128-133.
    • (2001) Biochim. Biophys. Acta , vol.1535 , pp. 128-133
    • Labrie, V.1    Harel, J.2    Dubreuil, J.D.3
  • 34
    • 0037420910 scopus 로고    scopus 로고
    • Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates
    • Lefebvre, B.G. and Robinson, A.S. 2003. Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates. Biotechnol. Bioeng. 82: 595-604.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 595-604
    • Lefebvre, B.G.1    Robinson, A.S.2
  • 35
    • 0035805556 scopus 로고    scopus 로고
    • Importance of homodimerization for the in vivo function of yeast RNA triphosphatase
    • Lehman, K., Ho, C.K., and Shuman, S. 2001. Importance of homodimerization for the in vivo function of yeast RNA triphosphatase. J. Biol. Chem. 276: 14996-15002.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14996-15002
    • Lehman, K.1    Ho, C.K.2    Shuman, S.3
  • 36
    • 0025908547 scopus 로고
    • The tryptophan synthase α2 β2 complex. Cleavage of a flexible loop in the αsubunit alters allosteric properties
    • Miles, E.W. 1991. The tryptophan synthase α2 β2 complex. Cleavage of a flexible loop in the αsubunit alters allosteric properties. J. Biol. Chem. 266: 10715-10718.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10715-10718
    • Miles, E.W.1
  • 37
    • 0029204814 scopus 로고
    • Tryptophan synthase. Structure, function, and protein engineering
    • -. 1995. Tryptophan synthase. Structure, function, and protein engineering. Subcell. Biochem. 24: 207-254.
    • (1995) Subcell. Biochem. , vol.24 , pp. 207-254
  • 38
    • 0023072042 scopus 로고
    • Tryptophan synthase from Escherichia coli and Salmonella typhimurium
    • Miles, E.W., Bauerle, R., and Ahmed, S.A. 1987. Tryptophan synthase from Escherichia coli and Salmonella typhimurium. Methods Enzymol. 142: 398-414.
    • (1987) Methods Enzymol. , vol.142 , pp. 398-414
    • Miles, E.W.1    Bauerle, R.2    Ahmed, S.A.3
  • 39
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M.E., Brown, B.M., Waldburger, C.D., and Sauer, R.T. 1995. P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34: 13914-13919.
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 40
    • 0024846203 scopus 로고
    • The structure of interfaces between subunits of dimeric and tetrameric proteins
    • Miller, S. 1989. The structure of interfaces between subunits of dimeric and tetrameric proteins. Protein Eng. 3: 77-83.
    • (1989) Protein Eng. , vol.3 , pp. 77-83
    • Miller, S.1
  • 41
    • 0032560643 scopus 로고    scopus 로고
    • A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated β-helix domain
    • Miller, S., Schuler, B., and Seckler, R. 1998. A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated β-helix domain. Biochemistry 37: 9160-9168.
    • (1998) Biochemistry , vol.37 , pp. 9160-9168
    • Miller, S.1    Schuler, B.2    Seckler, R.3
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 44
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • Reinisch, K.M., Nibert, M.L., and Harrison, S.C. 2000. Structure of the reovirus core at 3.6 Å resolution. Nature 404: 960-967.
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 45
    • 0030900095 scopus 로고    scopus 로고
    • Disulphide-bonded intermediate on the folding and assembly pathway of a nondisulphide bonded protein
    • Robinson, A.S. and King, J. 1997. Disulphide-bonded intermediate on the folding and assembly pathway of a nondisulphide bonded protein. Nat. Struct. Biol. 4: 450-455.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 450-455
    • Robinson, A.S.1    King, J.2
  • 47
    • 0023942827 scopus 로고
    • Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant
    • Sargent, D., Benevides, J.M., Yu, M.H., King, J., and Thomas Jr., G.J., 1988. Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant. J. Mol. Biol. 199: 491-502.
    • (1988) J. Mol. Biol. , vol.199 , pp. 491-502
    • Sargent, D.1    Benevides, J.M.2    Yu, M.H.3    King, J.4    Thomas Jr., G.J.5
  • 48
    • 0028036622 scopus 로고
    • Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide
    • Sather, S. and King, J. 1994. Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. J. Biol. Chem. 269: 25268-25276.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25268-25276
    • Sather, S.1    King, J.2
  • 49
    • 0032516802 scopus 로고    scopus 로고
    • P22 tailspike folding mutants revisited: Effects on the thermodynamic stability of the isolated β-helix domain
    • Schuler, B. and Seckler, R. 1998. P22 tailspike folding mutants revisited: Effects on the thermodynamic stability of the isolated β-helix domain. J. Mol. Biol. 281: 227-234.
    • (1998) J. Mol. Biol. , vol.281 , pp. 227-234
    • Schuler, B.1    Seckler, R.2
  • 50
    • 0024971016 scopus 로고
    • Reconstitution of the thermostable trimeric phage P22 tailspike from denatured chains in vitro
    • Seckler, R., Fuchs, A., King, J., and Jaenicke, R. 1989. Reconstitution of the thermostable trimeric phage P22 tailspike from denatured chains in vitro. J. Biol. Chem. 264: 11750-11753.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11750-11753
    • Seckler, R.1    Fuchs, A.2    King, J.3    Jaenicke, R.4
  • 51
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
    • Smith, T.J., Olson, N.H., Cheng, R.H., Chase, E.S., and Baker, T.S. 1993. Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc. Natl. Acad. Sci. 90: 7015-7018.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 52
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • Smith, T.J., Schmidt, T., Fang, J., Wu, J., Siuzdak, G., and Stanley, C.A. 2002. The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J. Mol. Biol. 318: 765-777.
    • (2002) J. Mol. Biol. , vol.318 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 53
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation
    • Souillac, P.O., Uversky, V.N., Millett, I.S., Khurana, R., Doniach, S., and Fink, A.L. 2002. Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. J. Biol. Chem. 277: 12666-12679.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 54
    • 0028943183 scopus 로고
    • Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tail spike polypeptide chains
    • Speed, M., Wang, D.I.C., and King, J. 1995. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tail spike polypeptide chains. Protein Sci. 4: 900-908.
    • (1995) Protein Sci. , vol.4 , pp. 900-908
    • Speed, M.1    Wang, D.I.C.2    King, J.3
  • 55
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R., and Reinemer, P. 1994. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265: 383-385.
    • (1994) Science , vol.265 , pp. 383-385
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 56
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R., and Huber, R. 1997. Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267: 865-880.
    • (1997) J. Mol. Biol. , vol.267 , pp. 865-880
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 57
    • 0036088114 scopus 로고    scopus 로고
    • α-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: Implications for preventing irreversible thermal denaturation
    • Tanksale, A., Ghatge, M., and Deshpande, V. 2002. α-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: Implications for preventing irreversible thermal denaturation. Protein Sci. 11: 1720-1728.
    • (2002) Protein Sci. , vol.11 , pp. 1720-1728
    • Tanksale, A.1    Ghatge, M.2    Deshpande, V.3
  • 58
    • 0035128334 scopus 로고    scopus 로고
    • In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins
    • Tellinghuisen, T.L., Perera, R., and Kuhn, R.J. 2001. In vitro assembly of Sindbis virus core-like particles from cross-linked dimers of truncated and mutant capsid proteins. J. Virol. 75: 2810-2817.
    • (2001) J. Virol. , vol.75 , pp. 2810-2817
    • Tellinghuisen, T.L.1    Perera, R.2    Kuhn, R.J.3
  • 59
    • 0033613385 scopus 로고    scopus 로고
    • A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • Van Raaij, M.J., Mitraki, A., Lavigne, G., and Cusack, S. 1999. A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature 401: 935-938.
    • (1999) Nature , vol.401 , pp. 935-938
    • Van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 60
    • 0023834933 scopus 로고
    • Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein
    • Yu, M.-H. and King, J. 1988. Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein. J. Biol. Chem. 263: 1424-1431.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1424-1431
    • Yu, M.-H.1    King, J.2
  • 61
    • 0034927421 scopus 로고    scopus 로고
    • The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly
    • Zhou, J. and Weiner, H. 2001. The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly. Protein Sci. 10: 1490-1497.
    • (2001) Protein Sci. , vol.10 , pp. 1490-1497
    • Zhou, J.1    Weiner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.