메뉴 건너뛰기




Volumn 50, Issue , 1997, Pages 61-122

Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly

Author keywords

[No Author keywords available]

Indexed keywords

CD2 ANTIGEN; CRYSTALLIN; CYCLIN DEPENDENT KINASE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DIMER; DIPHTHERIA TOXIN; GLYOXALASE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 1BETA CONVERTING ENZYME; INTERLEUKIN 5; MONOMER; POLYMER; RIBONUCLEASE; SERINE PROTEINASE INHIBITOR;

EID: 0030770294     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0065-3233(08)60319-8     Document Type: Review
Times cited : (281)

References (137)
  • 1
    • 0030067028 scopus 로고    scopus 로고
    • High-resolution structure of an engineered cro monomer shows changes in conformation relative to the native dimer
    • Albright, R. A., Mossing, M. C., and Matthews, B. W. (1996). High-resolution structure of an engineered cro monomer shows changes in conformation relative to the native dimer. Biochemistry 35, 735-742.
    • (1996) Biochemistry , vol.35 , pp. 735-742
    • Albright, R.A.1    Mossing, M.C.2    Matthews, B.W.3
  • 2
    • 0019456340 scopus 로고
    • Structure of the cro repressor from bacteriophage lambda and its interaction with DNA
    • Anderson, W. F., Ohlendorf, D. H., Takeda, Y., and Matthwes, B. W. (1981). Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Nature 290, 754-758.
    • (1981) Nature , vol.290 , pp. 754-758
    • Anderson, W.F.1    Ohlendorf, D.H.2    Takeda, Y.3    Matthwes, B.W.4
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0029034120 scopus 로고
    • Crystal structure of the human cell cycle protein CksHs1: Single domain fold with similarity to kinase N-lobe domain
    • Arvai, A. S., Bourne, Y., Hickey, M. J., and Tainer, J. A. (1995). Crystal structure of the human cell cycle protein CksHs1: Single domain fold with similarity to kinase N-lobe domain. J. Mol. Biol. 249, 835-842.
    • (1995) J. Mol. Biol. , vol.249 , pp. 835-842
    • Arvai, A.S.1    Bourne, Y.2    Hickey, M.J.3    Tainer, J.A.4
  • 5
    • 0026597011 scopus 로고
    • β-Sheet rearrangements: Serpins and beyond
    • Banzon, J. A., and Kelly, J. W. (1992). β-Sheet rearrangements: serpins and beyond. Protein Eng. 5, 113-115.
    • (1992) Protein Eng. , vol.5 , pp. 113-115
    • Banzon, J.A.1    Kelly, J.W.2
  • 7
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell, C. E., and Eisenberg, D. (1996). Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochemistry 35, 1137-1149.
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 8
    • 0028077639 scopus 로고
    • Refined structure of monomeric diphtheria toxin at 2.3 Å resolution
    • Bennett, M. J., and Eisenberg, D. (1994). Refined structure of monomeric diphtheria toxin at 2.3 Å resolution. Protein Sci. 3, 1464-1475.
    • (1994) Protein Sci. , vol.3 , pp. 1464-1475
    • Bennett, M.J.1    Eisenberg, D.2
  • 9
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M. J., Choe, S., and Eisenberg, D. (1994a). 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
  • 10
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2.0 Å resolution
    • Bennett, M. J., Choe, S., and Eisenberg, D. (1994b). Refined structure of dimeric diphtheria toxin at 2.0 Å resolution. Protein Sci. 3, 1444-1463.
    • (1994) Protein Sci. , vol.3 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 11
    • 0028865843 scopus 로고
    • Domain swapping: A mechanism for oligomer assembly
    • Bennett, M. J., Schlunegger, M. P., and Eisenberg, D. (1995). 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
  • 13
    • 0029858390 scopus 로고    scopus 로고
    • The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition
    • Bianchet, M. A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S. H., Monaco, H. L., and Amzel, L. M. (1996). The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Nature Struct. Biol. 3, 934-939.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 934-939
    • Bianchet, M.A.1    Bains, G.2    Pelosi, P.3    Pevsner, J.4    Snyder, S.H.5    Monaco, H.L.6    Amzel, L.M.7
  • 15
    • 0024510020 scopus 로고
    • Activation of interleukin-1β by a co-induced protease
    • Black, R. A., Kronheim, S. R., and Sleath, P. R. (1989). Activation of interleukin-1β by a co-induced protease. FEBS Lett. 247, 386-390.
    • (1989) FEBS Lett. , vol.247 , pp. 386-390
    • Black, R.A.1    Kronheim, S.R.2    Sleath, P.R.3
  • 16
    • 77956940788 scopus 로고
    • Pancreatic ribonucleases
    • (P. D. Boyer, ed.), Academic Press Inc., New York
    • Blackburn, P., and Moore, S. (1982). Pancreatic ribonucleases. In "The Enzymes" (P. D. Boyer, ed.), pp. 317-433. Academic Press Inc., New York.
    • (1982) The Enzymes , pp. 317-433
    • Blackburn, P.1    Moore, S.2
  • 17
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid-fibril is a continuous β-sheet helix
    • Blake, C., and Serpell, L. (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid-fibril is a continuous β-sheet helix. Structure 4, 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 20
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y., Watson, M. H., Hickey, M. J., Holmes, W., Rocque, W., Reed, S. I., and Tainer, J. A. (1996). Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 84, 863-874.
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1    Watson, M.H.2    Hickey, M.J.3    Holmes, W.4    Rocque, W.5    Reed, S.I.6    Tainer, J.A.7
  • 21
  • 22
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brunger, A. T., Krukowski, A., and Erickson, J. W. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A46, 585-593.
    • (1990) Acta Crystallogr. , vol.A46 , pp. 585-593
    • Brunger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 23
    • 0027171791 scopus 로고
    • Preparation of an affinity resin for odorants by coupling odorant binding protein from bovine nasal mucosa to Sepharose 4B
    • Bussolati, L., Ramoni, R., Grolli, S., Donofrio, G., and Bignetti, E. (1993). Preparation of an affinity resin for odorants by coupling odorant binding protein from bovine nasal mucosa to Sepharose 4B. J. Biotechnol. 30, 225-230.
    • (1993) J. Biotechnol. , vol.30 , pp. 225-230
    • Bussolati, L.1    Ramoni, R.2    Grolli, S.3    Donofrio, G.4    Bignetti, E.5
  • 25
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I - Evidence for gene duplication and 3D domain swapping
    • Cameron, A. D., Olin, B., Ridderstroem, M., Mannervik, B., and Jones, T. A. (1997). Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. EMBOJ. 16, 3386-3395.
    • (1997) EMBOJ. , vol.16 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderstroem, M.3    Mannervik, B.4    Jones, T.A.5
  • 26
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell, R. W., Evans, D. L., and Stein, P. E. (1991). Mobile reactive centre of serpins and the control of thrombosis. Nature 353, 576-578.
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.E.3
  • 27
    • 0028773279 scopus 로고
    • Biological implications of a 3 Å structure of dimeric antithrombin
    • Carrell, R. W., Stein, P. E., Fermi, G., and Wardell, M. R. (1994). Biological implications of a 3 Å structure of dimeric antithrombin. Structure 2, 257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 28
    • 0022511852 scopus 로고
    • Dimeric form of diphtheria toxin: Purification and characterization
    • Carroll, S. F., Barbieri, J. T., and Collier, R. J. (1986). Dimeric form of diphtheria toxin: purification and characterization. Biochemistry 25, 2425-2430.
    • (1986) Biochemistry , vol.25 , pp. 2425-2430
    • Carroll, S.F.1    Barbieri, J.T.2    Collier, R.J.3
  • 30
    • 36949079814 scopus 로고
    • Structure of bushy stunt virus
    • Casper, D. L. D. (1956). Structure of bushy stunt virus. Nature 177, 475-476.
    • (1956) Nature , vol.177 , pp. 475-476
    • Casper, D.L.D.1
  • 31
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Casper, D. L. D., and Klug, A. (1962). Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. Quant. Biol. 27, 1-24.
    • (1962) Cold Spring Harbor Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Casper, D.L.D.1    Klug, A.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography. Collaborative Computational Project
    • Number 4, SERC Daresbury Laboratory, England
    • CCP4 (1994). The CCP4 suite: programs for protein crystallography. Collaborative Computational Project, Number 4, SERC Daresbury Laboratory, England. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 36
    • 0021112585 scopus 로고
    • Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases
    • Chung, C. H., Ives, H. E., Almeda, S., and Goldberg, A. L. (1983). Purification from Escherichia coli of a periplasmic protein that is a potent inhibitor of pancreatic proteases. J. Biol. Chem. 258, 11032-11038.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11032-11038
    • Chung, C.H.1    Ives, H.E.2    Almeda, S.3    Goldberg, A.L.4
  • 37
    • 0016609883 scopus 로고
    • Diphtheria toxin: Mode of action and structure
    • Collier, R. J. (1975). Diphtheria toxin: mode of action and structure. Bacteriol. Rev. 39, 54-85.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 54-85
    • Collier, R.J.1
  • 39
    • 36949077319 scopus 로고
    • Structure of small viruses
    • Crick, F. H. C., and Watson, J. D. (1956). Structure of small viruses. Nature 177, 473-475.
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 40
    • 0030062246 scopus 로고    scopus 로고
    • Creation of a biologically active interleukin-5 monomer
    • Dickason, R. R., and Huston, D. P. (1996). Creation of a biologically active interleukin-5 monomer. Nature 379, 652-655.
    • (1996) Nature , vol.379 , pp. 652-655
    • Dickason, R.R.1    Huston, D.P.2
  • 41
    • 0029146293 scopus 로고
    • Hints on the evolutionary design of a dimeric RNase with special bioactions
    • Di Donato, A., Cafaro, V., Romeo, I., and D'Alessio, G. (1995). Hints on the evolutionary design of a dimeric RNase with special bioactions. Protein Sci. 4, 1470-1477.
    • (1995) Protein Sci. , vol.4 , pp. 1470-1477
    • Di Donato, A.1    Cafaro, V.2    Romeo, I.3    D'Alessio, G.4
  • 42
    • 0026320870 scopus 로고
    • Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor
    • Diederichs, K., Boone, T., and Karplus, P. A. (1991). Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor. Science 254, 1779-1782.
    • (1991) Science , vol.254 , pp. 1779-1782
    • Diederichs, K.1    Boone, T.2    Karplus, P.A.3
  • 43
    • 0028332528 scopus 로고
    • The decision to enter mitosis
    • Dunphy, W. G. (1994). The decision to enter mitosis. Trends Cell Biol. 4, 202-207.
    • (1994) Trends Cell Biol. , vol.4 , pp. 202-207
    • Dunphy, W.G.1
  • 44
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D., and McLachlan, A. D. (1986). Solvation energy in protein folding and binding. Nature 319, 199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 45
    • 0000152788 scopus 로고
    • Interpretation of protein folding and binding with atomic solvation parameters
    • Eisenberg, D., Wesson, M., and Yamashita, M. (1989). Interpretation of protein folding and binding with atomic solvation parameters. Chem. Scr. 29A, 217-221.
    • (1989) Chem. Scr. , vol.29 A , pp. 217-221
    • Eisenberg, D.1    Wesson, M.2    Yamashita, M.3
  • 47
    • 0029644478 scopus 로고
    • The cell cycle and sucl: From structure to function?
    • Endicott, J. A., and Nurse, P. (1995). The cell cycle and sucl: from structure to function? Structure 3, 321-325.
    • (1995) Structure , vol.3 , pp. 321-325
    • Endicott, J.A.1    Nurse, P.2
  • 51
    • 0029001848 scopus 로고
    • Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH
    • Gouet, P., Jouve, H.-M., and Dideberg, O. (1995). Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J. Mol. Biol. 249, 933-954.
    • (1995) J. Mol. Biol. , vol.249 , pp. 933-954
    • Gouet, P.1    Jouve, H.-M.2    Dideberg, O.3
  • 53
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
    • Han, S., Eltis, L. D., Timmis, K. N., Muchmore, S. W., and Bolin, J. T. (1995). Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 54
    • 0027197493 scopus 로고
    • Diabodies: Small bivalent and bispecific antibody fragments
    • Holliger, P., Prospero, T., and Winter G. (1990). Diabodies: Small bivalent and bispecific antibody fragments. Proc. Natl. Acad. Sci. USA 90, 6444-6448.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 55
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • Horton, N., and Lewis, M. (1992). Calculation of the free energy of association for protein complexes. Protein Sci. 1, 169-181.
    • (1992) Protein Sci. , vol.1 , pp. 169-181
    • Horton, N.1    Lewis, M.2
  • 56
    • 0027768579 scopus 로고
    • Braking the cycle
    • Hunter, T. (1993). Braking the cycle. Cell 75, 839-841.
    • (1993) Cell , vol.75 , pp. 839-841
    • Hunter, T.1
  • 57
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle, M. R., Helms, L. R., Li, L., Chan, W., and 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
  • 58
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 59
    • 0014670538 scopus 로고
    • The formation and properties of dimers of the tryptophan synthetase a subunit of Escherichia coli
    • Jackson, D. A., and Yanofsky, C. (1969). The formation and properties of dimers of the tryptophan synthetase a subunit of Escherichia coli. J. Biol. Chem. 244, 4526-4538.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4526-4538
    • Jackson, D.A.1    Yanofsky, C.2
  • 60
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, A., and 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, A.2    Chothia, C.3
  • 61
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 62
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K., and Stuart, D. I. (1992). Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 63
    • 0023747338 scopus 로고
    • Bovine endothelial cell plasminogen activator inhibitor. Purification and heat activation
    • Katagiri, K., Okada, K., Hattori, H., and Yano, M. (1988). Bovine endothelial cell plasminogen activator inhibitor. Purification and heat activation. Eur. J. Biochem. 176, 81-87.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 81-87
    • Katagiri, K.1    Okada, K.2    Hattori, H.3    Yano, M.4
  • 64
    • 0025895787 scopus 로고
    • Vitronectin governs the interactions between plasminogen activator inhibitor 1 and tissue-type plasminogen activator
    • Keijer, J., Ehrlich, H. J., Linders, M., Preissner, K. T., and Pannekoek, H. (1991). Vitronectin governs the interactions between plasminogen activator inhibitor 1 and tissue-type plasminogen activator. J. Biol. Chem. 266, 10700-10707.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10700-10707
    • Keijer, J.1    Ehrlich, H.J.2    Linders, M.3    Preissner, K.T.4    Pannekoek, H.5
  • 65
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behaviour
    • Kelly, J. W. (1996). Alternative conformations of amyloidogenic proteins govern their behaviour. Curr. Opin. Struct. Biol. 6, 11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 69
    • 0003890119 scopus 로고
    • (A. Kornberg and T. Baker, eds.). Freeman, New York
    • Kornberg, A., and Baker, T. (1992). In "DNA Replication" (A. Kornberg and T. Baker, eds.). Freeman, New York.
    • (1992) DNA Replication
    • Kornberg, A.1    Baker, T.2
  • 72
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (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.1
  • 74
    • 0027256201 scopus 로고
    • Three-dimensional structure of satellite tobacco mosaic virus at 2.9 Å resolution
    • Larson, S. B., Koszelak, S., Day, J., Greenwood, A., Dodds, J. A., and McPherson, A. (1993). Three-dimensional structure of satellite tobacco mosaic virus at 2.9 Å resolution. J. Mol. Biol. 231, 375-391.
    • (1993) J. Mol. Biol. , vol.231 , pp. 375-391
    • Larson, S.B.1    Koszelak, S.2    Day, J.3    Greenwood, A.4    Dodds, J.A.5    McPherson, A.6
  • 75
    • 0029882967 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)
    • Larsson, G., Svensson, L. A., and Nyman, P. O. (1996). Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nature Struct. Biol. 3, 532-538.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 532-538
    • Larsson, G.1    Svensson, L.A.2    Nyman, P.O.3
  • 76
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M., Jr., and Kato, I. (1980). Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 77
    • 0029669956 scopus 로고    scopus 로고
    • Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation
    • Li, J., Koni, P. A., and Ellar, D. J. (1996). Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation. J. Mol. Biol. 257, 129-152.
    • (1996) J. Mol. Biol. , vol.257 , pp. 129-152
    • Li, J.1    Koni, P.A.2    Ellar, D.J.3
  • 78
    • 0021747157 scopus 로고
    • 1-Proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • 1-Proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-556.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, J.4
  • 81
    • 0016206102 scopus 로고
    • Renaturation of Escherichia coli tryptophanase after exposure to 8M urea
    • London, J., Skrzynia, C., and Goldberg, M. E. (1974). Renaturation of Escherichia coli tryptophanase after exposure to 8M urea. Eur. J. Biochem. 47, 409-415.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.E.3
  • 82
    • 0024218965 scopus 로고
    • The evolution of lenticular proteins: The β- and γ-crystallin super gene family
    • Lubsen, N. H., Aarts, H. J. M., and Schoenmakers, J. G. G. (1988). The evolution of lenticular proteins: The β- and γ-crystallin super gene family. Prog. Biophys. Mol. Biol. 51, 47-76.
    • (1988) Prog. Biophys. Mol. Biol. , vol.51 , pp. 47-76
    • Lubsen, N.H.1    Aarts, H.J.M.2    Schoenmakers, J.G.G.3
  • 85
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen, S. L., Lai, Z., Miroy, G., Kelly, J. W., and Colon, W. (1995). Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34, 13527-13536.
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.3    Kelly, J.W.4    Colon, W.5
  • 86
    • 0025865926 scopus 로고
    • The sequence and reactive site of ecotin. A general inhibitor of pancreatic serine proteases from Escherichia coli
    • McGrath, M. E., Hines, W. M., Sakanari, J. A., Fletterick, R. J., and Craik, C. S. (1991). The sequence and reactive site of ecotin. A general inhibitor of pancreatic serine proteases from Escherichia coli. J. Biol. Chem. 266, 6620-6625.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6620-6625
    • McGrath, M.E.1    Hines, W.M.2    Sakanari, J.A.3    Fletterick, R.J.4    Craik, C.S.5
  • 87
    • 0028266885 scopus 로고
    • Macromolecular chelation as an improved mechanism of protease inhibition: Structure of the ecotin-trypsin complex
    • McGrath, M. E., Erpel, T., Bystroff, C., and Fletterick, R. J. (1994). Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex. EMBO J. 13, 1502-1507.
    • (1994) EMBO J. , vol.13 , pp. 1502-1507
    • McGrath, M.E.1    Erpel, T.2    Bystroff, C.3    Fletterick, R.J.4
  • 88
    • 0028912630 scopus 로고
    • Ecotin: Lessons on survival in a protease-filled world
    • McGrath, M. E., Gillmor, S. A., and Fletterick, R. J. (1995). Ecotin: Lessons on survival in a protease-filled world. Protein Sci. 4, 141-148.
    • (1995) Protein Sci. , vol.4 , pp. 141-148
    • McGrath, M.E.1    Gillmor, S.A.2    Fletterick, R.J.3
  • 89
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5
    • Milburn, M. V., Hassell, A. M., Lambert, M. H., Jordan, S. R., Proudfoot, A. E. I., Graber, P., and Wells, T. N. C. (1993). A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5. Nature 363, 172-176.
    • (1993) Nature , vol.363 , pp. 172-176
    • Milburn, M.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.I.5    Graber, P.6    Wells, T.N.C.7
  • 90
    • 0024671486 scopus 로고
    • Nucleotide sequence and translation of satellite tobacco mosaic virus-RNA
    • Mirkov, T. E., Mathews, D. M., Du Plessis, D. H., and Dodds, J. A. (1989). Nucleotide sequence and translation of satellite tobacco mosaic virus-RNA. Virology 170, 139-146.
    • (1989) Virology , vol.170 , pp. 139-146
    • Mirkov, T.E.1    Mathews, D.M.2    Du Plessis, D.H.3    Dodds, J.A.4
  • 91
    • 0026848943 scopus 로고
    • Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity
    • Monaco, H. L., and Zanotti, G. (1992). Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity. Biopolymers 32, 457-465.
    • (1992) Biopolymers , vol.32 , pp. 457-465
    • Monaco, H.L.1    Zanotti, G.2
  • 92
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D. O. (1995). Principles of CDK regulation. Nature 374, 131-133.
    • (1995) Nature , vol.374 , pp. 131-133
    • Morgan, D.O.1
  • 93
    • 0025712476 scopus 로고
    • Stable, monomeric variants of λ cro obtained by insertion of a designed β-hairpin sequence
    • Mossing, M. C., and Sauer, R. T. (1990). Stable, monomeric variants of λ cro obtained by insertion of a designed β-hairpin sequence. Science 250, 1712-1715.
    • (1990) Science , vol.250 , pp. 1712-1715
    • Mossing, M.C.1    Sauer, R.T.2
  • 96
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domain complexed with proline-rich peptides
    • Musacchio, A., Saraste, M., and Wilmanns, M. (1994). High-resolution crystal structures of tyrosine kinase SH3 domain complexed with proline-rich peptides. Nature Struct. Biol. 1, 546-551.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 97
    • 0028208249 scopus 로고
    • Pathogenic potential of human monoclonal immunoglobulin light chains: Relationship of in vitro aggregation to in vivo organ deposition
    • Myatt, E. A., Westholm, F. A., Weiss, D. T., Solomon, A., Schiffer, M., and Stevens, F. J. (1994). Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition. Proc. Natl. Acad. Sci. USA 91, 3034-3038.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3034-3038
    • Myatt, E.A.1    Westholm, F.A.2    Weiss, D.T.3    Solomon, A.4    Schiffer, M.5    Stevens, F.J.6
  • 98
    • 0029644408 scopus 로고
    • Crystal structure of the MS2 coat protein dimer: Implications for RNA binding and virus assembly
    • Ni, C.-Z., Syed, R., Kodandapani, R., Wickersham, J., Peabody, D. S., and Ely, K. R. (1995). Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly. Structure 3, 255-263.
    • (1995) Structure , vol.3 , pp. 255-263
    • Ni, C.-Z.1    Syed, R.2    Kodandapani, R.3    Wickersham, J.4    Peabody, D.S.5    Ely, K.R.6
  • 100
    • 0027482006 scopus 로고
    • Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control
    • Parge, H. E., Arvai, A. S., Murtari, D. J., Reed, S. I., and Tainer, J. A. (1993). Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control. Science 262, 387-395.
    • (1993) Science , vol.262 , pp. 387-395
    • Parge, H.E.1    Arvai, A.S.2    Murtari, D.J.3    Reed, S.I.4    Tainer, J.A.5
  • 101
    • 0028774708 scopus 로고
    • Crystal structure of a diabody, a bivalent antibody fragment
    • Perisic, O., Webb, P. A., Holliger, P., Winter, G., and Williams, R. L. (1994). Crystal structure of a diabody, a bivalent antibody fragment. Structure 2, 1217-1226.
    • (1994) Structure , vol.2 , pp. 1217-1226
    • Perisic, O.1    Webb, P.A.2    Holliger, P.3    Winter, G.4    Williams, R.L.5
  • 102
    • 0023802428 scopus 로고
    • Co-operativity in seminal ribonuclease function
    • Piccoli, R., Di Donato, A., and D'Alessio, G. (1988). Co-operativity in seminal ribonuclease function. Biochem. J. 253, 329-336.
    • (1988) Biochem. J. , vol.253 , pp. 329-336
    • Piccoli, R.1    Di Donato, A.2    D'Alessio, G.3
  • 104
    • 0025989905 scopus 로고
    • Cyclin-dependent kinases: A new cell cycle motif?
    • Pines, J., and Hunter, T. (1991). Cyclin-dependent kinases: a new cell cycle motif? Trends Cell Biol. 1, 117-121.
    • (1991) Trends Cell Biol. , vol.1 , pp. 117-121
    • Pines, J.1    Hunter, T.2
  • 105
    • 0028843420 scopus 로고
    • Single chain Fvs
    • Raag, R., and Whitlow, M. (1995). Single chain Fvs. FASEB J. 9, 73-80.
    • (1995) FASEB J. , vol.9 , pp. 73-80
    • Raag, R.1    Whitlow, M.2
  • 106
    • 0026620556 scopus 로고
    • The role of p34 kinases in the G1 to S-phase transition
    • Reed, S. I. (1992). The role of p34 kinases in the G1 to S-phase transition. Annu. Rev. Cell Biol. 8, 529-561.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 529-561
    • Reed, S.I.1
  • 107
    • 84965093921 scopus 로고
    • The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components
    • Richards, F. M., and Vithayathil, P. J. (1959). The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components. J. Biol. Chem. 234, 1459-1465.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1459-1465
    • Richards, F.M.1    Vithayathil, P.J.2
  • 108
    • 26844446997 scopus 로고
    • (F. M. Richards and H. W. Wyckoff, eds.). Clarendon Press, Oxford
    • Richards, F. M., and Wyckoff, H. W. (1973). In "Ribonuclease S" (F. M. Richards and H. W. Wyckoff, eds.). Clarendon Press, Oxford.
    • (1973) Ribonuclease S
    • Richards, F.M.1    Wyckoff, H.W.2
  • 110
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603
    • Satow, Y., Cohen, G. H., Padlan, E. A., and Davies, D. R. (1986). Phosphocholine binding immunoglobulin Fab McPC603. J. Mol. Biol. 190, 593-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 111
    • 0004153150 scopus 로고
    • (C. R. Cantor, ed.), 9th printing, Springer-Verlag, New York
    • Schulz, G. E., and Schirmer, R. H. (1979). In "Principles of Protein Structure" (C. R. Cantor, ed.), 9th printing, p. 69. Springer-Verlag, New York.
    • (1979) Principles of Protein Structure , pp. 69
    • Schulz, G.E.1    Schirmer, R.H.2
  • 113
    • 0027145507 scopus 로고
    • Cytokine structural taxonomy and mechanisms of receptor engagement
    • Sprang, S. R., and Bazan, J. F. (1993). Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol. 3, 815-826.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 815-826
    • Sprang, S.R.1    Bazan, J.F.2
  • 114
    • 0026426731 scopus 로고
    • Cell adhesion. Sticky sugars for selectins
    • Springer, T. A., and Lasky, L. A. (1991). Cell adhesion. Sticky sugars for selectins. Nature 349, 196-197.
    • (1991) Nature , vol.349 , pp. 196-197
    • Springer, T.A.1    Lasky, L.A.2
  • 116
    • 0023428040 scopus 로고
    • Complete-amino-acid sequence of bovine seminal ribonuclease, a dimeric protein from seminal plasma
    • Suzuki, H., Parente, A., Farina, B., Greco, L., La Montagna, R., and Leone, E. (1987). Complete-amino-acid sequence of bovine seminal ribonuclease, a dimeric protein from seminal plasma. Biol. Chem. Hoppe-Seyler 368, 1305-1312.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 1305-1312
    • Suzuki, H.1    Parente, A.2    Farina, B.3    Greco, L.4    La Montagna, R.5    Leone, E.6
  • 118
    • 0017759227 scopus 로고
    • Cro regulatory protein specified by bacteriophage λ
    • Takeda, Y., Folkmanis, A., and Echols, H. (1977). Cro regulatory protein specified by bacteriophage λ. J. Bial. Chem. 252, 6177-6183.
    • (1977) J. Bial. Chem. , vol.252 , pp. 6177-6183
    • Takeda, Y.1    Folkmanis, A.2    Echols, H.3
  • 119
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi, M. (1991). Cadherin cell adhesion receptors as a morphogenetic regulator. Science 251, 1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 120
    • 0023511451 scopus 로고
    • Molecular cloning and structure of the human interleukin-5 gene
    • Tanabe, T., Konishi, M., Mizuta, T., Noma, T., and Honjo, T. (1987). Molecular cloning and structure of the human interleukin-5 gene. J. Biol. Chem. 262, 16580-16584.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16580-16584
    • Tanabe, T.1    Konishi, M.2    Mizuta, T.3    Noma, T.4    Honjo, T.5
  • 121
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bonne odorant binding protein dimer
    • Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S., and Cambillau C. (1996). Domain swapping creates a third putative combining site in bonne odorant binding protein dimer. Nature Struct. Biol. 3, 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
  • 123
    • 0028171466 scopus 로고
    • Dimerization of βB2-crystallin: The role of the linker peptide and the N- and C-terminal extensions
    • Trinkl, S., Glockshuber, R., and Jaenicke, R. (1994). Dimerization of βB2-crystallin: The role of the linker peptide and the N- and C-terminal extensions. Protein Sci. 3, 1392-1400.
    • (1994) Protein Sci. , vol.3 , pp. 1392-1400
    • Trinkl, S.1    Glockshuber, R.2    Jaenicke, R.3
  • 124
    • 0013608322 scopus 로고
    • Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA
    • Tye, B. K., Nyman, P.-O., Lehman, I. R., Hochhauser, S., and Weiss, B. (1987). Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA. Proc. Natl. Acad. Sci. USA 74, 154-157.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 154-157
    • Tye, B.K.1    Nyman, P.-O.2    Lehman, I.R.3    Hochhauser, S.4    Weiss, B.5
  • 126
    • 0019499763 scopus 로고
    • Antitumoral action of bovine seminal ribonuclease
    • Vescia, S., and Tramontane, D. (1980). Antitumoral action of bovine seminal ribonuclease. Mol. Cell Biol. 36, 125-128.
    • (1980) Mol. Cell Biol. , vol.36 , pp. 125-128
    • Vescia, S.1    Tramontane, D.2
  • 127
    • 0018938880 scopus 로고
    • In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease
    • Vescia, S., Tramontano, D., Augusti-Tocco, G., and D'Alessio, G. (1980). In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease. Cancer Res. 40, 3740-3744.
    • (1980) Cancer Res. , vol.40 , pp. 3740-3744
    • Vescia, S.1    Tramontano, D.2    Augusti-Tocco, G.3    D'Alessio, G.4
  • 129
    • 0028074723 scopus 로고
    • Multivalent Fvs: Characterization of single-domain Fv oligomers and preparation of a bispecific Fv
    • Whitlow, M., Filpula, D., Rollence, M. L., Feng, S.-L., and Wood, J. F. (1994). Multivalent Fvs: characterization of single-domain Fv oligomers and preparation of a bispecific Fv. Protein Eng. 7, 1017-1026.
    • (1994) Protein Eng. , vol.7 , pp. 1017-1026
    • Whitlow, M.1    Filpula, D.2    Rollence, M.L.3    Feng, S.-L.4    Wood, J.F.5
  • 130
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for cell surface recognition
    • Williams, A. F., and Barclay, A. N. A. (1988). The immunoglobulin superfamily-domains for cell surface recognition. Annu. Rev. Immunol. 6, 381-406.
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-406
    • Williams, A.F.1    Barclay, A.N.A.2
  • 133
    • 0020478577 scopus 로고
    • The refined crystal structure of ribonuclease A at 2.0 Å resolution
    • Wlodawer, A., Bott, R., and Sjoelin, L. (1982). The refined crystal structure of ribonuclease A at 2.0 Å resolution. J. Biol. Chem. 257, 1325-1332.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1325-1332
    • Wlodawer, A.1    Bott, R.2    Sjoelin, L.3
  • 134
  • 135
    • 0029121068 scopus 로고
    • Free energy determinants of secondary structure formation: I. α-Helices
    • Yang, A.-S., and Honig, B. (1995a). Free energy determinants of secondary structure formation: I. α-Helices. J. Mol. Biol. 252, 351-365.
    • (1995) J. Mol. Biol. , vol.252 , pp. 351-365
    • Yang, A.-S.1    Honig, B.2
  • 136
    • 0029150955 scopus 로고
    • Free energy determinants of secondary structure formation: II. Antiparallel β-sheets
    • Yang, A.-S., and Honig, B. (1995b). Free energy determinants of secondary structure formation: II. Antiparallel β-sheets. J. Mol. Biol. 252, 366-376.
    • (1995) J. Mol. Biol. , vol.252 , pp. 366-376
    • Yang, A.-S.1    Honig, B.2
  • 137
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon γ
    • Zdanov, A., Schalk-Hihi, C., Gustchina, A., Tsang, M., Weatherbee, J., and Wlodawer, A. (1995). Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon γ. Structure 3, 591-601.
    • (1995) Structure , vol.3 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.