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Volumn 325, Issue 5, 2003, Pages 991-1018

Structural characterisation and functional significance of transient protein-protein interactions

Author keywords

Homologous dimer; Interface structure; Physiological control; Protein protein interaction; Transient oligomerisation

Indexed keywords

CADHERIN; CILIARY NEUROTROPHIC FACTOR; CYCLIN A; CYCLIN DEPENDENT KINASE 2; CYTOCHROME C; DIMER; DNA BINDING PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; GALECTIN 1; GLYCOPROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; INTERLEUKIN 8; KARYOPHERIN BETA; MONOCYTE CHEMOTACTIC PROTEIN 1; MONOMER; NEUTROPHIL CYTOSOL FACTOR 2 PROTEIN; OLIGOMER; PHOSDUCIN; PROTEIN; PROTEIN CDC42; RAC PROTEIN; RAF PROTEIN; RAN PROTEIN; RAS PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; STEM CELL FACTOR; STROMAL CELL DERIVED FACTOR 1ALPHA; TRANSDUCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 0037474541     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01281-0     Document Type: Article
Times cited : (509)

References (103)
  • 1
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod J., Changeux J., Jacob F. Allosteric proteins and cellular control systems. J. Mol. Biol. 6:1963;306-329.
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.2    Jacob, F.3
  • 2
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H., Henrick K., Thornton J.M. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins: Struct. Funct. Genet. 41:2000;47-57.
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 3
    • 0035853028 scopus 로고    scopus 로고
    • Identification of protein oligomerisation states by analysis of interface conservation
    • Elcock A.H., McCammon J.A. Identification of protein oligomerisation states by analysis of interface conservation. Proc. Natl Acad. Sci. USA. 98:2001;2990-2994.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2990-2994
    • Elcock, A.H.1    McCammon, J.A.2
  • 4
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • Valdar W.S., Thornton J.M. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins: Struct. Funct. Genet. 42:2001;108-124.
    • (2001) Proteins: Struct. Funct. Genet. , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 5
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller S., Lesk A.M., Janin J., Chothia C. The accessible surface area and stability of oligomeric proteins. Nature. 328:1987;834-836.
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 6
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J., Miller S., Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204:1988;155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 7
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos P. An investigation of protein subunit and domain interfaces. Protein Eng. 2:1988;101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 8
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones S., Thornton J.M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63:1995;31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 10
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S., Thornton J.M. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272:1997;121-132.
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 11
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique
    • Tsai C.J., Lin S.L., Wolfson H.J., Nussinov R. A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique. J. Mol. Biol. 260:1996;604-620.
    • (1996) J. Mol. Biol. , vol.260 , pp. 604-620
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 12
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D., Tsai C.J., Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng. 10:1997;999-1012.
    • (1997) Protein Eng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 13
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte L.L., Chothia C., Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285:1999;2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 14
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucl. Acids Res. 28:2000;45-48.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 16
  • 17
    • 0035659985 scopus 로고    scopus 로고
    • The many faces of Ras: Recognition of small GTP-binding proteins
    • Corbett K.D., Alber T. The many faces of Ras: recognition of small GTP-binding proteins. Trends Biochem. Sci. 26:2001;710-716.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 710-716
    • Corbett, K.D.1    Alber, T.2
  • 18
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3
    • Sakurai K., Oobatake M., Goto Y. Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3. Protein Sci. 10:2001;2325-2335.
    • (2001) Protein Sci. , vol.10 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 19
    • 0030305457 scopus 로고    scopus 로고
    • R: A language for data analysis and graphics
    • Ihaka R., Gentleman R. R: a language for data analysis and graphics. J. Comput. Graphical Stat. 5:1996;299-314.
    • (1996) J. Comput. Graphical Stat. , vol.5 , pp. 299-314
    • Ihaka, R.1    Gentleman, R.2
  • 20
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerisation
    • Xu D., Tsai C.J., Nussinov R. Mechanism and evolution of protein dimerisation. Protein Sci. 7:1998;533-544.
    • (1998) Protein Sci. , vol.7 , pp. 533-544
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 21
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K., Thornton J.M. PQS: a protein quaternary structure file server. Trends Biochem. Sci. 23:1998;358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 24
    • 0035942317 scopus 로고    scopus 로고
    • Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions
    • Laurence J.S., Blanpain C., De Leener A., Parmentier M., LiWang P.J. Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions. Biochemistry. 40:2001;4990-4999.
    • (2001) Biochemistry , vol.40 , pp. 4990-4999
    • Laurence, J.S.1    Blanpain, C.2    De Leener, A.3    Parmentier, M.4    LiWang, P.J.5
  • 25
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
    • Mondragon A., Subbiah S., Almo S.C., Drottar M., Harrison S.C. Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J. Mol. Biol. 205:1989;189-200.
    • (1989) J. Mol. Biol. , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrison, S.C.5
  • 26
    • 0024961623 scopus 로고
    • Structure of phage 434 Cro protein at 2.35 Å resolution
    • Mondragon A., Wolberger C., Harrison S.C. Structure of phage 434 Cro protein at 2.35 Å resolution. J. Mol. Biol. 205:1989;179-188.
    • (1989) J. Mol. Biol. , vol.205 , pp. 179-188
    • Mondragon, A.1    Wolberger, C.2    Harrison, S.C.3
  • 27
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • Tegoni M., Ramoni R., Bignetti E., Spinelli S., Cambillau C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Struct. Biol. 3:1996;863-867.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 28
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerisation and L-arginine binding domain of the arginine repressor of Escherichia coli
    • Van Duyne G.D., Ghosh G., Maas W.K., Sigler P.B. Structure of the oligomerisation and L-arginine binding domain of the arginine repressor of Escherichia coli. J. Mol. Biol. 256:1996;377-391.
    • (1996) J. Mol. Biol. , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 30
    • 0032709317 scopus 로고    scopus 로고
    • Factors affecting the dissociation and aggregation of human interferon gamma
    • Zlateva T., Boteva R., Salvato B., Tsanev R. Factors affecting the dissociation and aggregation of human interferon gamma. Int. J. Biol. Macromol. 26:1999;357-362.
    • (1999) Int. J. Biol. Macromol. , vol.26 , pp. 357-362
    • Zlateva, T.1    Boteva, R.2    Salvato, B.3    Tsanev, R.4
  • 31
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: Implications for structure rearrangements in the helicase hexamer
    • Weigelt J., Brown S.E., Miles C.S., Dixon N.E., Otting G. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Struct. Fold. Des. 7:1999;681-690.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 32
    • 0034719111 scopus 로고    scopus 로고
    • Oligomerisation properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein
    • Clements A., Johnston K., Mazzarelli J.M., Ricciardi R.P., Marmorstein R. Oligomerisation properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein. Biochemistry. 39:2000;16033-16045.
    • (2000) Biochemistry , vol.39 , pp. 16033-16045
    • Clements, A.1    Johnston, K.2    Mazzarelli, J.M.3    Ricciardi, R.P.4    Marmorstein, R.5
  • 33
    • 0034719101 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium of normal and modified beta A3-crystallins: Experimental determination and molecular modeling
    • Sergeev Y.V., Wingfield P.T., Hejtmancik J.F. Monomer-dimer equilibrium of normal and modified beta A3-crystallins: experimental determination and molecular modeling. Biochemistry. 39:2000;15799-15806.
    • (2000) Biochemistry , vol.39 , pp. 15799-15806
    • Sergeev, Y.V.1    Wingfield, P.T.2    Hejtmancik, J.F.3
  • 34
    • 0035816541 scopus 로고    scopus 로고
    • Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans
    • Parfenyev A.N., Salminen A., Halonen P., Hachimori A., Baykov A.A., Lahti R. Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans. J. Biol. Chem. 276:2001;24511-24518.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24511-24518
    • Parfenyev, A.N.1    Salminen, A.2    Halonen, P.3    Hachimori, A.4    Baykov, A.A.5    Lahti, R.6
  • 35
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature. 415:2002;141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5    Bauer, A.6
  • 36
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature. 415:2002;180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6
  • 37
    • 0028230082 scopus 로고
    • Dissociation of enzyme oligomers: A mechanism for allosteric regulation
    • Traut T.W. Dissociation of enzyme oligomers: a mechanism for allosteric regulation. Crit. Rev. Biochem. Mol. Biol. 29:1994;125-163.
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 125-163
    • Traut, T.W.1
  • 38
  • 39
    • 0034657260 scopus 로고    scopus 로고
    • Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases
    • Stroppolo M.E., Malvezzi-Campeggi F., Mei G., Rosato N., Desideri A. Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases. Arch. Biochem. Biophys. 377:2000;215-218.
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 215-218
    • Stroppolo, M.E.1    Malvezzi-Campeggi, F.2    Mei, G.3    Rosato, N.4    Desideri, A.5
  • 40
    • 0029967362 scopus 로고    scopus 로고
    • SRS: Information retrieval system for molecular biology data banks
    • Etzold T., Ulyanov A., Argos P. SRS: information retrieval system for molecular biology data banks. Methods Enzymol. 266:1996;114-128.
    • (1996) Methods Enzymol. , vol.266 , pp. 114-128
    • Etzold, T.1    Ulyanov, A.2    Argos, P.3
  • 41
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • Dasgupta S., Iyer G.H., Bryant S.H., Lawrence C.E., Bell J.A. Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins: Struct. Funct. Genet. 28:1997;494-514.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Bryant, S.H.3    Lawrence, C.E.4    Bell, J.A.5
  • 42
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 44
    • 0034687127 scopus 로고    scopus 로고
    • Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: Analysis of cro dimerisation from nanomolar to micromolar concentrations
    • Darling P.J., Holt J.M., Ackers G.K. Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerisation from nanomolar to micromolar concentrations. Biochemistry. 39:2000;11500-11507.
    • (2000) Biochemistry , vol.39 , pp. 11500-11507
    • Darling, P.J.1    Holt, J.M.2    Ackers, G.K.3
  • 45
    • 0029093731 scopus 로고
    • Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers
    • Tao X., Zeng H.Y., Murphy J.R. Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers. Proc. Natl Acad. Sci. USA. 92:1995;6803-6807.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6803-6807
    • Tao, X.1    Zeng, H.Y.2    Murphy, J.R.3
  • 46
    • 0031573470 scopus 로고    scopus 로고
    • The role of DNA in the mechanism of NFkappaB dimer formation: Crystal structures of the dimerisation domains of the p50 and p65 subunits
    • Huang D.B., Huxford T., Chen Y.Q., Ghosh G. The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerisation domains of the p50 and p65 subunits. Structure. 5:1997;1427-1436.
    • (1997) Structure , vol.5 , pp. 1427-1436
    • Huang, D.B.1    Huxford, T.2    Chen, Y.Q.3    Ghosh, G.4
  • 48
    • 0031913371 scopus 로고    scopus 로고
    • IL-8 derivatives with a reduced potential to form homodimers are fully active in vitro and in vivo
    • Horcher M., Rot A., Aschauer H., Besemer J. IL-8 derivatives with a reduced potential to form homodimers are fully active in vitro and in vivo. Cytokine. 10:1998;1-12.
    • (1998) Cytokine , vol.10 , pp. 1-12
    • Horcher, M.1    Rot, A.2    Aschauer, H.3    Besemer, J.4
  • 49
    • 0028362141 scopus 로고
    • Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B
    • Schnitzel W., Monschein U., Besemer J. Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B. J. Leukoc. Biol. 55:1994;763-770.
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 763-770
    • Schnitzel, W.1    Monschein, U.2    Besemer, J.3
  • 50
    • 0028102938 scopus 로고
    • Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations
    • Burrows S.D., Doyle M.L., Murphy K.P., Franklin S.G., White J.R., Brooks I., et al. Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations. Biochemistry. 33:1994;12741-12745.
    • (1994) Biochemistry , vol.33 , pp. 12741-12745
    • Burrows, S.D.1    Doyle, M.L.2    Murphy, K.P.3    Franklin, S.G.4    White, J.R.5    Brooks, I.6
  • 52
  • 53
    • 0030683638 scopus 로고    scopus 로고
    • Solution structure and basis for functional activity of stromal cell-derived factor-1; Dissociation of CXCR4 activation from binding and inhibition of HIV-1
    • Crump M.P., Gong J.H., Loetscher P., Rajarathnam K., Amara A., Arenzana-Seisdedos F., et al. Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J. 16:1997;6996-7007.
    • (1997) EMBO J. , vol.16 , pp. 6996-7007
    • Crump, M.P.1    Gong, J.H.2    Loetscher, P.3    Rajarathnam, K.4    Amara, A.5    Arenzana-Seisdedos, F.6
  • 55
    • 0029131699 scopus 로고
    • A dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer
    • Zhang Y., Rollins B.J. A dominant negative inhibitor indicates that monocyte chemoattractant protein 1 functions as a dimer. Mol. Cell Biol. 15:1995;4851-4855.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4851-4855
    • Zhang, Y.1    Rollins, B.J.2
  • 56
    • 0030597050 scopus 로고    scopus 로고
    • Structural characterisation of a monomeric chemokine: Monocyte chemoattractant protein-3
    • Kim K.S., Rajarathnam K., Clark-lewis I., Sykes B.D. Structural characterisation of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Letters. 395:1996;277-282.
    • (1996) FEBS Letters , vol.395 , pp. 277-282
    • Kim, K.S.1    Rajarathnam, K.2    Clark-lewis, I.3    Sykes, B.D.4
  • 58
    • 0028797816 scopus 로고
    • Spontaneous dissociation-association of monomers of the human-stem-cell-factor dimer
    • Lu H.S., Chang W.C., Mendiaz E.A., Mann M.B., Langley K.E., Hsu Y.R. Spontaneous dissociation-association of monomers of the human-stem-cell-factor dimer. Biochem. J. 305:1995;563-568.
    • (1995) Biochem. J. , vol.305 , pp. 563-568
    • Lu, H.S.1    Chang, W.C.2    Mendiaz, E.A.3    Mann, M.B.4    Langley, K.E.5    Hsu, Y.R.6
  • 59
    • 0030939956 scopus 로고    scopus 로고
    • The majority of stem cell factor exists as monomer under physiological conditions. Implications for dimerisation mediating biological activity
    • Hsu Y.R., Wu G.M., Mendiaz E.A., Syed R., Wypych J., Toso R., et al. The majority of stem cell factor exists as monomer under physiological conditions. Implications for dimerisation mediating biological activity. J. Biol. Chem. 272:1997;6406-6415.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6406-6415
    • Hsu, Y.R.1    Wu, G.M.2    Mendiaz, E.A.3    Syed, R.4    Wypych, J.5    Toso, R.6
  • 60
    • 0029046795 scopus 로고
    • Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing
    • McDonald N.Q., Panayotatos N., Hendrickson W.A. Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing. EMBO J. 14:1995;2689-2699.
    • (1995) EMBO J. , vol.14 , pp. 2689-2699
    • McDonald, N.Q.1    Panayotatos, N.2    Hendrickson, W.A.3
  • 61
    • 0030824193 scopus 로고    scopus 로고
    • Comparison of solution properties of human and rat ciliary neurotrophic factor
    • Narhi L.O., Rosenfeld R., Shimamoto G., Lee R., Hawkins N., Li T., et al. Comparison of solution properties of human and rat ciliary neurotrophic factor. J. Pept. Res. 50:1997;300-309.
    • (1997) J. Pept. Res. , vol.50 , pp. 300-309
    • Narhi, L.O.1    Rosenfeld, R.2    Shimamoto, G.3    Lee, R.4    Hawkins, N.5    Li, T.6
  • 62
    • 0013881729 scopus 로고
    • An equilibrium ultracentrifuge study of the self-association of bovine insulin
    • Jeffrey P.D., Coates J.H. An equilibrium ultracentrifuge study of the self-association of bovine insulin. Biochemistry. 5:1966;489-498.
    • (1966) Biochemistry , vol.5 , pp. 489-498
    • Jeffrey, P.D.1    Coates, J.H.2
  • 63
    • 0013913179 scopus 로고
    • Relationship of structure to biological activity of insulin as revealed by degradative studies
    • Carpenter F.H. Relationship of structure to biological activity of insulin as revealed by degradative studies. Am. J. Med. 40:1966;750-758.
    • (1966) Am. J. Med. , vol.40 , pp. 750-758
    • Carpenter, F.H.1
  • 64
    • 0032981135 scopus 로고    scopus 로고
    • MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimics the c4 Dihemic cytochrome domain association
    • Brown K., Nurizzo D., Besson S., Shepard W., Moura J., et al. MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimics the c4 Dihemic cytochrome domain association. J. Mol. Biol. 289:1999;1017-1028.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1017-1028
    • Brown, K.1    Nurizzo, D.2    Besson, S.3    Shepard, W.4    Moura, J.5
  • 65
    • 0022517026 scopus 로고
    • Ligand-controlled dissociation of Chromatium vinosum cytochrome c′
    • Doyle M.L., Gill S.J., Cusanovich M.A. Ligand-controlled dissociation of Chromatium vinosum cytochrome c′ Biochemistry. 25:1986;2509-2516.
    • (1986) Biochemistry , vol.25 , pp. 2509-2516
    • Doyle, M.L.1    Gill, S.J.2    Cusanovich, M.A.3
  • 66
    • 0027380310 scopus 로고
    • Atomic structure of a cytochrome c′ with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution
    • Ren Z., Meyer T., McRee D.E. Atomic structure of a cytochrome c′ with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution. J. Mol. Biol. 234:1993;433-445.
    • (1993) J. Mol. Biol. , vol.234 , pp. 433-445
    • Ren, Z.1    Meyer, T.2    McRee, D.E.3
  • 67
    • 0015242015 scopus 로고
    • Molecular weights of some cytochromes cc′
    • Cusanovich M.A. Molecular weights of some cytochromes cc′ Biochim. Biophys. Acta. 236:1971;238-241.
    • (1971) Biochim. Biophys. Acta , vol.236 , pp. 238-241
    • Cusanovich, M.A.1
  • 68
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer
    • Uhrinova S., Smith M.H., Jameson G.B., Uhrin D., Sawyer L., Barlow P.N. Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer. Biochemistry. 39:2000;3565-3574.
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 69
    • 0029102907 scopus 로고
    • Crystal structure and subunit dynamics of the abalone sperm lysin dimer: Egg envelopes dissociate dimers, the monomer is the active species
    • Shaw A., Fortes P.A., Stout C.D., Vacquier V.D. Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species. J. Cell Biol. 130:1995;1117-1125.
    • (1995) J. Cell Biol. , vol.130 , pp. 1117-1125
    • Shaw, A.1    Fortes, P.A.2    Stout, C.D.3    Vacquier, V.D.4
  • 71
    • 0035852805 scopus 로고    scopus 로고
    • Dimerisation and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar E., Kleinman B., Imhoff D., Li M., Hays T.S., Hare M. Dimerisation and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry. 40:2001;1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 72
    • 0034663733 scopus 로고    scopus 로고
    • Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes
    • Bianchet M.A., Ahmed H., Vasta G.R., Amzel L.M. Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes. Proteins. 40:2000;378-388.
    • (2000) Proteins , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 73
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., Record M.T. jr. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:1994;777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record M.T., Jr.2
  • 74
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • Rittinger K., Walker P.A., Eccleston J.F., Smerdon S.J., Gamblin S.J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature. 389:1997;758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 75
    • 0030759770 scopus 로고    scopus 로고
    • Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
    • Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., et al. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature. 388:1997;693-697.
    • (1997) Nature , vol.388 , pp. 693-697
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Nurmahomed, K.4    Owen, D.5    Laue, E.6
  • 79
    • 0032541137 scopus 로고    scopus 로고
    • The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation
    • Rudolph M.G., Bayer P., Abo A., Kuhlmann J., Vetter I.R., Wittinghofer A. The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. J. Biol. Chem. 273:1998;18067-18076.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18067-18076
    • Rudolph, M.G.1    Bayer, P.2    Abo, A.3    Kuhlmann, J.4    Vetter, I.R.5    Wittinghofer, A.6
  • 81
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1 A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1 A and a GTP analogue. Nature. 375:1995;554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 82
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • Stewart M., Kent H.M., McCoy A.J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J. Mol. Biol. 277:1998;635-646.
    • (1998) J. Mol. Biol. , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 83
    • 0034007087 scopus 로고    scopus 로고
    • Dissecting the interactions between NTF2, RanGDP, and the nucleoporin XFXFG repeats
    • Chaillan-Huntington C., Braslavsky C.V., Kuhlmann J., Stewart M. Dissecting the interactions between NTF2, RanGDP, and the nucleoporin XFXFG repeats. J. Biol. Chem. 275:2000;5874-5879.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5874-5879
    • Chaillan-Huntington, C.1    Braslavsky, C.V.2    Kuhlmann, J.3    Stewart, M.4
  • 84
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature. 398:1999;39-46.
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 85
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3 Å resolution
    • Vetter I.R., Arndt A., Kutay U., Gorlich D., Wittinghofer A. Structural view of the Ran-Importin beta interaction at 2.3 Å resolution. Cell. 97:1999;635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 86
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Gorlich D., Pante N., Kutay U., Aebi U., Bischoff F.R. Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 15:1996;5584-5594.
    • (1996) EMBO J. , vol.15 , pp. 5584-5594
    • Gorlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 87
  • 88
    • 0033231561 scopus 로고    scopus 로고
    • The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1
    • Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K., Hakoshima T. The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol. Cell. 4:1999;793-803.
    • (1999) Mol. Cell , vol.4 , pp. 793-803
    • Maesaki, R.1    Ihara, K.2    Shimizu, T.3    Kuroda, S.4    Kaibuchi, K.5    Hakoshima, T.6
  • 89
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • Ostermeier C., Brunger A.T. Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell. 96:1999;363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 90
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylake D.K., Rossman K.L., Sondek J. Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature. 408:2000;682-688.
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 91
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)
    • Renault L., Kuhlmann J., Henkel A., Wittinghofer A. Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell. 105:2001;245-255.
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 93
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution
    • Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R. The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution. Nature. 379:1996;511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 94
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4-activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis
    • Tesmer J.J., Berman D.M., Gilman A.G., Sprang S.R. Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell. 89:1997;251-261.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 95
    • 0029861417 scopus 로고    scopus 로고
    • The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis
    • Berman D.M., Kozasa T., Gilman A.G. The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis. J. Biol. Chem. 271:1996;27209-27212.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27209-27212
    • Berman, D.M.1    Kozasa, T.2    Gilman, A.G.3
  • 96
    • 0028237708 scopus 로고
    • Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
    • Lambright D.G., Noel J.P., Hamm H.E., Sigler P.B. Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Nature. 369:1994;621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 97
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin
    • Gaudet R., Bohm A., Sigler P.B. Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. Cell. 87:1996;577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 98
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell. 85:1996;931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 99
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee C.H., Leung B., Lemmon M.A., Zheng J., Cowburn D., Kuriyan J., Saksela K. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14:1995;5006-5015.
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Leung, B.2    Lemmon, M.A.3    Zheng, J.4    Cowburn, D.5    Kuriyan, J.6    Saksela, K.7
  • 101
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S., Pavletich N.P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science. 274:1996;1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 102
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch M., Chinardet N., Mourey L., Birck C., Samama J.P. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nature Struct. Biol. 5:1998;25-29.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 25-29
    • Welch, M.1    Chinardet, N.2    Mourey, L.3    Birck, C.4    Samama, J.P.5
  • 103
    • 0028869205 scopus 로고
    • The response regulators CheB and CheY exhibit competitive binding to the kinase CheA
    • Li J., Swanson R.V., Simon M.I., Weis R.M. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry. 34:1995;14626-14636.
    • (1995) Biochemistry , vol.34 , pp. 14626-14636
    • Li, J.1    Swanson, R.V.2    Simon, M.I.3    Weis, R.M.4


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