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Volumn 6, Issue 4, 1998, Pages 421-427

Morphology of protein-protein interfaces

Author keywords

Oligomeric protein; Protein folding; Protein interface

Indexed keywords


EID: 0032522670     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00044-6     Document Type: Article
Times cited : (208)

References (32)
  • 1
    • 0000986242 scopus 로고
    • Quaternary structure of proteins
    • Neurath, H. & Hill, R.L., eds., Academic Press, N.Y.
    • Klotz, I.M., Darnall, D.W. & Langerman, N.R. (1975). Quaternary structure of proteins. In The Proteins (Neurath, H. & Hill, R.L., eds.), pp. 293-411. Academic Press, N.Y.
    • (1975) The Proteins , pp. 293-411
    • Klotz, I.M.1    Darnall, D.W.2    Langerman, N.R.3
  • 2
    • 0027499733 scopus 로고
    • Soluble proteins: Size, shape and function
    • Goodsell, D.S. & Olson, A.J. (1993). Soluble proteins: size, shape and function. Trends Biochem. Sci. 18, 65-68.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 65-68
    • Goodsell, D.S.1    Olson, A.J.2
  • 3
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia, C. & Janin, J. (1975). Principles of protein-protein recognition. Nature 256, 705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 4
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S. & Chothia, C. (1988). Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 5
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos, P. (1988). An investigation of protein subunit and domain interfaces. Protein Eng. 2, 101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 6
    • 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
  • 7
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J. & 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
  • 8
    • 0026079134 scopus 로고
    • Distribution and complementarity of hydropathy in multisubunit proteins
    • Korn, A.P. & Burnett, R.M. (1991). Distribution and complementarity of hydropathy in multisubunit proteins. Proteins 9, 37-55.
    • (1991) Proteins , vol.9 , pp. 37-55
    • Korn, A.P.1    Burnett, R.M.2
  • 9
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S. & Thornton, J.M. (1995). Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Molec. Biol. 63, 31-65.
    • (1995) Prog. Biophys. Molec. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 10
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S. & Thornton, J.M. (1996). Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93, 13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 11
    • 0029988383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Architectures and interactions in protein-protein interfaces and in protein cores
    • Tsai, G-J., Lin, S.L., Wolfson, H.J. & Nussinov, R. (1996). Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Crit. Rev. Biochem. Molec. Biol. 31, 127-152.
    • (1996) Crit. Rev. Biochem. Molec. Biol. , vol.31 , pp. 127-152
    • Tsai, G.-J.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 12
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interactions sites using surface patches
    • Jones, S. & Thornton, J.M. (1997). Analysis of protein-protein interactions sites using surface patches. J. Mol. Biol. 272, 121-132.
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 13
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, G-J., Lin, S.L., Wolfson, H.J. & Nussinov, R. (1997). Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci. 6, 53-64.
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, G.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 14
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu, D., Lin, S.L. & Nussinov, R. (1997). Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J. Mol. Biol. 265, 68-84.
    • (1997) J. Mol. Biol. , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 15
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 16
    • 0029906944 scopus 로고    scopus 로고
    • A method for detecting hydrophobic patches on protein surfaces
    • Lijnzaad, P., Berendsen, H.J.C. & Argos, P. (1996). A method for detecting hydrophobic patches on protein surfaces. Proteins 26, 192-203.
    • (1996) Proteins , vol.26 , pp. 192-203
    • Lijnzaad, P.1    Berendsen, H.J.C.2    Argos, P.3
  • 17
    • 0030997363 scopus 로고    scopus 로고
    • Hydrophobic patches on protein subunit interfaces: Characteristics and prediction
    • Lijnzaad, P. & Argos, P. (1997). Hydrophobic patches on protein subunit interfaces: characteristics and prediction. Proteins 28, 333-343.
    • (1997) Proteins , vol.28 , pp. 333-343
    • Lijnzaad, P.1    Argos, P.2
  • 18
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M.J., Choe, S. & Eisenberg, D. (1994). Domain swapping: entangling alliances between proteins. Proc. Natl. Acad. Sci. USA 91, 3127-3131.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 19
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M.J., Schlunegger, M.P. & Eisenberg, D. (1995). 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4, 2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 20
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M.P., Bennett, M.J. & Eisenberg, D. (1997). Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Prot. Chem. 50, 61-1 22.
    • (1997) Adv. Prot. Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 21
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard, S.J. & Argos, P. (1994). Cavities and packing at protein interfaces. Protein Sci. 3, 2194-2206.
    • (1994) Protein Sci. , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 22
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson, L. & Eisenberg, D. (1992). Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci. 1, 227-235.
    • (1992) Protein Sci. , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 23
    • 0030756203 scopus 로고    scopus 로고
    • Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and to protein-protein association
    • Tsai, C.-J. & Nussinov, R. (1997). Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association. Protein Sci. 6, 1426-1437.
    • (1997) Protein Sci. , vol.6 , pp. 1426-1437
    • Tsai, C.-J.1    Nussinov, R.2
  • 24
    • 0022384676 scopus 로고
    • The second translation of the genetic message: Protein folding and assembly
    • Goldberg, M.E. (1985). The second translation of the genetic message: protein folding and assembly. Trends Biochem. Sci. 10, 388-391.
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 388-391
    • Goldberg, M.E.1
  • 25
    • 0027491549 scopus 로고
    • Refolding of brain-derived neurotrophic factor from guanidine hydrochloride: Kinetic trapping in a collapsed form which is incompetent for dimerization
    • Philo, J.S., Rosenfeld, R., Arakawa, T., Wen, J. & Narhi, L.O. (1993). Refolding of brain-derived neurotrophic factor from guanidine hydrochloride: kinetic trapping in a collapsed form which is incompetent for dimerization. Biochemistry 32, 1081 2-10818.
    • (1993) Biochemistry , vol.32 , pp. 10812-10818
    • Philo, J.S.1    Rosenfeld, R.2    Arakawa, T.3    Wen, J.4    Narhi, L.O.5
  • 27
    • 0030858236 scopus 로고    scopus 로고
    • Role of quaternary structure in the stability of dimeric proteins: The case of ascorbate oxidase
    • Mei, G., Di Venere, A., Buganza, M., Vecchini, P., Rosato, N. & FinazziAgro, A. (1997). Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase. Biochemistry 36, 10917-10922.
    • (1997) Biochemistry , vol.36 , pp. 10917-10922
    • Mei, G.1    Di Venere, A.2    Buganza, M.3    Vecchini, P.4    Rosato, N.5    Finazziagro, A.6
  • 28
    • 0025125731 scopus 로고
    • Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: Characterization of a monomeric intermediate
    • Herald, M. & Kirschner, K. (1990). Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. Biochemistry 29, 1907-1913.
    • (1990) Biochemistry , vol.29 , pp. 1907-1913
    • Herald, M.1    Kirschner, K.2
  • 29
    • 0026541905 scopus 로고
    • Dissociation of a native dimer into a molten globule monomer
    • Silva, J.L., Silveira, C.F., Correia, A. & Pontes, L. (1992). Dissociation of a native dimer into a molten globule monomer. J. Mol. Biol. 223, 545-555.
    • (1992) J. Mol. Biol. , vol.223 , pp. 545-555
    • Silva, J.L.1    Silveira, C.F.2    Correia, A.3    Pontes, L.4
  • 30
    • 0019642282 scopus 로고
    • Evidence for an intermediate in the denaturation and assembly of phosphoglucose isomerase
    • Blackburn, M.N. & Noltmann, E.A. (1981). Evidence for an intermediate in the denaturation and assembly of phosphoglucose isomerase. Arch. Biochem. Biophys. 212, 162-169.
    • (1981) Arch. Biochem. Biophys. , vol.212 , pp. 162-169
    • Blackburn, M.N.1    Noltmann, E.A.2
  • 31
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner, M.F., Oison, A.J. & Spehner, J.-C. (1996). Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38, 305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Oison, A.J.2    Spehner, J.-C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.