메뉴 건너뛰기




Volumn 85, Issue 6, 2003, Pages 3587-3599

A Perspective on Mechanisms of Protein Tetramer Formation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; TETRAMER;

EID: 0344119489     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74777-8     Document Type: Article
Times cited : (41)

References (55)
  • 3
    • 0019619407 scopus 로고
    • Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde
    • Bemhardt, G., R. Rudolph, and R. Jaenicke. 1981. Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde. Z. Naturforsch. [C]. 36:772-777.
    • (1981) Z. Naturforsch. [C] , vol.36 , pp. 772-777
    • Bemhardt, G.1    Rudolph, R.2    Jaenicke, R.3
  • 4
    • 0016140360 scopus 로고
    • Structure of human plasma prealbumin at 2.5 Å resolution. A preliminary report on the polypeptide chain conformation, quatemary structure and thyroxine binding
    • Blake, C. C., M. J. Geisow, I. D. Swan, C. Rerat, and B. Rerat. 1974. Structure of human plasma prealbumin at 2.5 Å resolution. A preliminary report on the polypeptide chain conformation, quatemary structure and thyroxine binding. J. Mol. Biol. 88:1-12.
    • (1974) J. Mol. Biol. , vol.88 , pp. 1-12
    • Blake, C.C.1    Geisow, M.J.2    Swan, I.D.3    Rerat, C.4    Rerat, B.5
  • 5
    • 2242480182 scopus 로고    scopus 로고
    • Kinetic analysis of R67 dihydrofolate reductase folding: From the unfolded monomer to the native tetramer
    • Bodenreider, C., N. Kellershohn, M. E. Goldberg, and A. Mejean. 2002. Kinetic analysis of R67 dihydrofolate reductase folding: from the unfolded monomer to the native tetramer. Biochemistry. 41:14988-14999.
    • (2002) Biochemistry , vol.41 , pp. 14988-14999
    • Bodenreider, C.1    Kellershohn, N.2    Goldberg, M.E.3    Mejean, A.4
  • 6
    • 0024432915 scopus 로고
    • Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli
    • Bras, G. L., W. Teschner, D. Deville-Bonne, and J. R. Garel. 1989. Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli. Biochemistry. 28:6836-6841.
    • (1989) Biochemistry , vol.28 , pp. 6836-6841
    • Bras, G.L.1    Teschner, W.2    Deville-Bonne, D.3    Garel, J.R.4
  • 7
    • 0016356440 scopus 로고
    • Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase
    • Buehner, M., G. C. Ford, K. W. Olsen, D. Moras, and M. G. Rossman. 1974. Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 90:25-49.
    • (1974) J. Mol. Biol. , vol.90 , pp. 25-49
    • Buehner, M.1    Ford, G.C.2    Olsen, K.W.3    Moras, D.4    Rossman, M.G.5
  • 8
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation-mediated protein-protein binding
    • Camacho, C. J., S. R. Kimura, C. DeLisi, and S. Vajda. 2000. Kinetics of desolvation-mediated protein-protein binding. Biophys. J. 78:1094-1105.
    • (2000) Biophys. J. , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    DeLisi, C.3    Vajda, S.4
  • 9
    • 0032981961 scopus 로고    scopus 로고
    • Free energy landscapes of encounter complexes in protein-protein association
    • Camacho, C. J., Z. Weng, S. Vajda, and C. DeLisi. 1999. Free energy landscapes of encounter complexes in protein-protein association. Biophys. J. 76:1166-1178.
    • (1999) Biophys. J. , vol.76 , pp. 1166-1178
    • Camacho, C.J.1    Weng, Z.2    Vajda, S.3    DeLisi, C.4
  • 10
    • 0016327034 scopus 로고
    • Structure of yeast phosphoglycerate mutase
    • Campbell, J. W., H. C. Watson, and G. I. Hodgson. 1974. Structure of yeast phosphoglycerate mutase. Nature. 250:301-303.
    • (1974) Nature , vol.250 , pp. 301-303
    • Campbell, J.W.1    Watson, H.C.2    Hodgson, G.I.3
  • 11
    • 0025779255 scopus 로고
    • Human platelet factor 4 subunit association/dissociation thermodynamics and kinetics
    • Chen, M. J., and K. H. Mayo. 1991. Human platelet factor 4 subunit association/dissociation thermodynamics and kinetics. Biochemistry. 30:6402-6411.
    • (1991) Biochemistry , vol.30 , pp. 6402-6411
    • Chen, M.J.1    Mayo, K.H.2
  • 12
    • 0000726661 scopus 로고
    • Kinetic analysis of irreversible consecutive reactions
    • Chien, J.-Y. 1948. Kinetic analysis of irreversible consecutive reactions. J. Am. Chem. Soc. 70:2256-2261.
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 2256-2261
    • Chien, J.-Y.1
  • 13
    • 0036193888 scopus 로고    scopus 로고
    • Potassium channel ontogeny
    • Deutsch, C. 2002. Potassium channel ontogeny. Annu. Rev. Physiol. 64: 19-46.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 19-46
    • Deutsch, C.1
  • 14
    • 0024506337 scopus 로고
    • Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN
    • Deville-Bonne, D., G. Le Bras, W. Teschner, and J. R. Garel. 1989. Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN. Biochemistry. 28:1917-1922.
    • (1989) Biochemistry , vol.28 , pp. 1917-1922
    • Deville-Bonne, D.1    Le Bras, G.2    Teschner, W.3    Garel, J.R.4
  • 15
    • 0036301867 scopus 로고    scopus 로고
    • Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution
    • Esposito, L., F. Sica, C. A. Raia, A. Giordano, M. Rossi, L. Mazzarella, and A. Zagari. 2002. Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution. J. Mol. Biol. 318:463-477.
    • (2002) J. Mol. Biol. , vol.318 , pp. 463-477
    • Esposito, L.1    Sica, F.2    Raia, C.A.3    Giordano, A.4    Rossi, M.5    Mazzarella, L.6    Zagari, A.7
  • 16
    • 0027522365 scopus 로고
    • The p53 protein is an unusually shaped tetramer that binds directly to DNA
    • Friedman, P. N., X. Chen, J. Bargonetti, and C. Prives. 1993. The p53 protein is an unusually shaped tetramer that binds directly to DNA. Proc. Natl. Acad. Sci. USA. 90:3319-3323.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3319-3323
    • Friedman, P.N.1    Chen, X.2    Bargonetti, J.3    Prives, C.4
  • 18
    • 0001067872 scopus 로고    scopus 로고
    • Mean-field kinetic modeling of polymerization: The Smoluchowski coagulation equation
    • Galina, H., and J. B. Lechowicz. 1998. Mean-field kinetic modeling of polymerization: the Smoluchowski coagulation equation. Adv. Polym. Sci. 137:135-172.
    • (1998) Adv. Polym. Sci. , vol.137 , pp. 135-172
    • Galina, H.1    Lechowicz, J.B.2
  • 19
    • 0021116789 scopus 로고
    • The dimeric intermediate on the pathway of reconstitution of lactate dehydrogenase is enzymatically active
    • Girg, R., R. Rudolph, and R. Jaenicke. 1983. The dimeric intermediate on the pathway of reconstitution of lactate dehydrogenase is enzymatically active. FEBS Lett. 163:132-135.
    • (1983) FEBS Lett. , vol.163 , pp. 132-135
    • Girg, R.1    Rudolph, R.2    Jaenicke, R.3
  • 21
    • 0021034261 scopus 로고
    • Kinetic analysis of the reconstitution pathway of lactate dehydrogenase using cross-linking with glutaraldehyde
    • Hermann, R., R. Jaenicke, and G. Kretsch. 1983a. Kinetic analysis of the reconstitution pathway of lactate dehydrogenase using cross-linking with glutaraldehyde. Naturwissenschaften. 70:517-518.
    • (1983) Naturwissenschaften , vol.70 , pp. 517-518
    • Hermann, R.1    Jaenicke, R.2    Kretsch, G.3
  • 22
    • 0021802560 scopus 로고
    • Evidence for active intermediates during the reconstitution of yeast phosphoglycerate mutase
    • Hermann, R., R. Jaenicke, and N. C. Price. 1985. Evidence for active intermediates during the reconstitution of yeast phosphoglycerate mutase. Biochemistry. 24:1817-1821.
    • (1985) Biochemistry , vol.24 , pp. 1817-1821
    • Hermann, R.1    Jaenicke, R.2    Price, N.C.3
  • 23
    • 0019616577 scopus 로고
    • Analysis of the reconstitution of oligomeric enzymes by cross-linking with glutaraldehyde: Kinetics of reassociation of lactic dehydrogenase
    • Hermann, R., R. Jaenicke, and R. Rudolph. 1981. Analysis of the reconstitution of oligomeric enzymes by cross-linking with glutaraldehyde: kinetics of reassociation of lactic dehydrogenase. Biochemistry. 20:5195-5201.
    • (1981) Biochemistry , vol.20 , pp. 5195-5201
    • Hermann, R.1    Jaenicke, R.2    Rudolph, R.3
  • 24
    • 0020197175 scopus 로고
    • The use of subunit hybridization to monitor the reassociation of porcine lactate dehydrogenase after acid dissociation
    • Hermann, R., R. Rudolph, and R. Jaenicke. 1982. The use of subunit hybridization to monitor the reassociation of porcine lactate dehydrogenase after acid dissociation. Hoppe Seylers Z. Physiol. Chem. 363:1259-1265.
    • (1982) Hoppe Seylers Z. Physiol. Chem. , vol.363 , pp. 1259-1265
    • Hermann, R.1    Rudolph, R.2    Jaenicke, R.3
  • 27
    • 0016164172 scopus 로고
    • Reassociation and reactivation of lactic dehydrogenase from the unfolded subunits
    • Jaenicke, R. 1974. Reassociation and reactivation of lactic dehydrogenase from the unfolded subunits. Eur. J. Biochem. 46:149-155.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 149-155
    • Jaenicke, R.1
  • 28
    • 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
  • 29
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke, R., and H. Lilie. 2000. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53:329-401.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 30
    • 0031010107 scopus 로고    scopus 로고
    • The kinetics of protein-protein recognition
    • Janin, J. 1997. The kinetics of protein-protein recognition. Proteins. 28: 153-161.
    • (1997) Proteins , vol.28 , pp. 153-161
    • Janin, J.1
  • 31
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim, J. J., M. Wang, and R. Paschke. 1993. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. USA. 90:7523-7527.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7523-7527
    • Kim, J.J.1    Wang, M.2    Paschke, R.3
  • 32
    • 0021342007 scopus 로고
    • Renaturation of the allosteric phosphofructokinase from Escherichia coli
    • Martel, A., and J. R. Garel. 1984. Renaturation of the allosteric phosphofructokinase from Escherichia coli. J. Biol. Chem. 259:4917-4921.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4917-4921
    • Martel, A.1    Garel, J.R.2
  • 33
    • 0032906377 scopus 로고    scopus 로고
    • Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
    • Mateu, M. G., M. M. Sanchez Del Pino, and A. R. Fersht. 1999. Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53. Nat. Struct. Biol. 6:191-198.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 191-198
    • Mateu, M.G.1    Sanchez Del Pino, M.M.2    Fersht, A.R.3
  • 34
    • 0025779730 scopus 로고
    • Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
    • Maury, C. P. 1991. Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J. Clin. Invest. 87:1195-1199.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1195-1199
    • Maury, C.P.1
  • 35
    • 33747646924 scopus 로고    scopus 로고
    • An overview of the potassium channel family
    • Miller, C. 2000. An overview of the potassium channel family. Genome Biol. 1:1-5.
    • (2000) Genome Biol. , vol.1 , pp. 1-5
    • Miller, C.1
  • 36
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation
    • Modler, A. J., K. Gast, G. Lutsch, and G. Damaschun. 2003. Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation. J. Mol. Biol. 325:135-148.
    • (2003) J. Mol. Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 39
    • 0028006337 scopus 로고
    • Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase 1
    • Ramaswamy, S., D. A. Kratzer, A. D. Hershey, P. H. Rogers, A. Amone, H. Eklund, and B. V. Plapp. 1994. Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase 1. J. Mol. Biol. 235:777-779.
    • (1994) J. Mol. Biol. , vol.235 , pp. 777-779
    • Ramaswamy, S.1    Kratzer, D.A.2    Hershey, A.D.3    Rogers, P.H.4    Amone, A.5    Eklund, H.6    Plapp, B.V.7
  • 40
    • 0026648514 scopus 로고
    • Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • Rehaber, V., and R. Jaenicke. 1992. Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. J. Biol. Chem. 267:10999-11006.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 41
    • 0027069576 scopus 로고
    • Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: Dissection of the stabilizing effects of coenzyme binding and subunit interaction
    • Risse, B., G. Stempfer, R. Rudolph, H. Mollering, and R. Jaenicke. 1992. Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: dissection of the stabilizing effects of coenzyme binding and subunit interaction. Protein Sci. 1:1699-1709.
    • (1992) Protein Sci. , vol.1 , pp. 1699-1709
    • Risse, B.1    Stempfer, G.2    Rudolph, R.3    Mollering, H.4    Jaenicke, R.5
  • 42
    • 0017744370 scopus 로고
    • Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media
    • Rudolph, R., I. Heider, E. Westhof, and R. Jaenicke. 1977. Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media. Biochemistry. 16:3384-3390.
    • (1977) Biochemistry , vol.16 , pp. 3384-3390
    • Rudolph, R.1    Heider, I.2    Westhof, E.3    Jaenicke, R.4
  • 43
    • 0017282438 scopus 로고
    • Kinetics of reassociation and reactivation of pig-muscle lactic dehydrogenase after acid dissociation
    • Rudolph, R., and R. Jaenicke. 1976. Kinetics of reassociation and reactivation of pig-muscle lactic dehydrogenase after acid dissociation. Eur. J. Biochem. 63:409-417.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 409-417
    • Rudolph, R.1    Jaenicke, R.2
  • 44
    • 0018788373 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 2. Reactivation of irreversibly denatured aggregates
    • Rudolph, R., G. Zettlmeissl, and R. Jaenicke. 1979. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 2. Reactivation of irreversibly denatured aggregates. Biochemistry. 18:5572-5575.
    • (1979) Biochemistry , vol.18 , pp. 5572-5575
    • Rudolph, R.1    Zettlmeissl, G.2    Jaenicke, R.3
  • 45
    • 0024974796 scopus 로고
    • Crystal structure of unliganded phosphofructokinase from Escherichia coli
    • Rypniewski, W. R., and P. R. Evans. 1989. Crystal structure of unliganded phosphofructokinase from Escherichia coli. J. Mol. Biol. 207:805-821.
    • (1989) J. Mol. Biol. , vol.207 , pp. 805-821
    • Rypniewski, W.R.1    Evans, P.R.2
  • 46
    • 0008194141 scopus 로고
    • On the use of "concentration-time" integrals in the solution of complex kinetic equations
    • Saville, B. 1971. On the use of "concentration-time" integrals in the solution of complex kinetic equations. J. Phys. Chem. 75:2215-2217.
    • (1971) J. Phys. Chem. , vol.75 , pp. 2215-2217
    • Saville, B.1
  • 47
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber, G. 2002. Kinetic studies of protein-protein interactions. Curr. Opin. Struct. Biol. 12:41-47.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 48
    • 0033605858 scopus 로고    scopus 로고
    • Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction
    • Schreiber, G., and T. Selzer. 1999. Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction. J. Mol. Biol. 287:409-419.
    • (1999) J. Mol. Biol. , vol.287 , pp. 409-419
    • Schreiber, G.1    Selzer, T.2
  • 49
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. 1998. The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8:447-453.
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 50
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of protein-protein interactions
    • Sheinerman, F. B., R. Norel, and B. Honig. 2000. Electrostatic aspects of protein-protein interactions. Curr. Opin. Struct. Biol. 10:153-159.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 51
    • 0017178879 scopus 로고
    • The refolding of lactate dehydrogenase subunits and their assembly to the functional tetramer
    • Tenenbaum-Bayer, H., and A. Levitzki. 1976. The refolding of lactate dehydrogenase subunits and their assembly to the functional tetramer. Biochim. Biophys. Acta. 445:261-279.
    • (1976) Biochim. Biophys. Acta , vol.445 , pp. 261-279
    • Tenenbaum-Bayer, H.1    Levitzki, A.2
  • 52
    • 0024519278 scopus 로고
    • Intermediates on the reassociation pathway of phosphofructokinase I from Escherichia coli
    • Teschner, W., and J. R. Garel. 1989. Intermediates on the reassociation pathway of phosphofructokinase I from Escherichia coli. Biochemistry. 28:1912-1916.
    • (1989) Biochemistry , vol.28 , pp. 1912-1916
    • Teschner, W.1    Garel, J.R.2
  • 54
    • 0038360689 scopus 로고    scopus 로고
    • Understanding the structure and function of catalases: Clues from molecular evolution and in vitro mutagenesis
    • Zamocky, M., and F. Koller. 1999. Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol. 72:19-66.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 19-66
    • Zamocky, M.1    Koller, F.2
  • 55
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., R. Rudolph, and R. Jaenicke. 1979. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry. 18:5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.