메뉴 건너뛰기




Volumn 25, Issue 3, 2000, Pages 150-153

Macromolecular interactions: Tracing the roots

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PROTEIN;

EID: 0034161474     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01550-4     Document Type: Note
Times cited : (124)

References (43)
  • 3
    • 0028839792 scopus 로고
    • T.H. Huxley and the 'protoplasmic theory of life': 100 years later
    • Welch G.R. T.H. Huxley and the 'protoplasmic theory of life': 100 years later. Trends Biochem. Sci. 20:1995;481-485.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 481-485
    • Welch, G.R.1
  • 5
    • 0012889356 scopus 로고
    • No turning back: The tension between reductionism and complexity facing biologists
    • Kell, D.B. and Welch, G.R. (1991) No turning back: the tension between reductionism and complexity facing biologists. The Times Higher Education Supplement No. 971 (August 9), 15.
    • (1991) The Times Higher Education Supplement , vol.971 , Issue.AUGUST 9 , pp. 15
    • Kell, D.B.1    Welch, G.R.2
  • 6
    • 84941404091 scopus 로고    scopus 로고
    • Untersuchungen über die Harnsstoffbildung in Tierkörper
    • Krebs H.A., Henseleit K. Untersuchungen über die Harnsstoffbildung in Tierkörper. Z. Physiol. Chem. 210:33-66;. [Translation by Holmes, F. L. (1991) Hans Krebs, Vol. 1, Oxford University Press].
    • Z. Physiol. Chem. , vol.210 , pp. 33-66
    • Krebs, H.A.1    Henseleit, K.2
  • 7
    • 84941404091 scopus 로고    scopus 로고
    • [Translation by Oxford University Press]
    • Krebs H.A., Henseleit K. Untersuchungen über die Harnsstoffbildung in Tierkörper. Z. Physiol. Chem. 210:33-66;. [Translation by Holmes, F. L. (1991) Hans Krebs, Vol. 1, Oxford University Press].
    • (1991) Hans Krebs , vol.1
    • Holmes, F.L.1
  • 8
    • 0037756877 scopus 로고
    • Surface structure in the integration of cell activity
    • Peters R.A. Surface structure in the integration of cell activity. Trans. Faraday Soc. 26:1930;797-807.
    • (1930) Trans. Faraday Soc. , vol.26 , pp. 797-807
    • Peters, R.A.1
  • 9
    • 3242714410 scopus 로고
    • Studies in organized enzyme systems
    • Series 52 Academic Press
    • Green, D.E. (1958) Studies in organized enzyme systems. The Harvey Lectures, Series 52, pp. 177-227, Academic Press.
    • (1958) The Harvey Lectures , pp. 177-227
    • Green, D.E.1
  • 12
    • 0343530977 scopus 로고
    • The Deveaux effect at oil-protoplasm interfaces
    • Kopac M.J. The Deveaux effect at oil-protoplasm interfaces. Biol. Bull. 75:1938;372-383.
    • (1938) Biol. Bull. , vol.75 , pp. 372-383
    • Kopac, M.J.1
  • 13
    • 0005830866 scopus 로고
    • Cytochemistry of centrifuged hyphae of Neurospora
    • Zalokar M. Cytochemistry of centrifuged hyphae of Neurospora. Exp. Cell Res. 19:1960;114-132.
    • (1960) Exp. Cell Res. , vol.19 , pp. 114-132
    • Zalokar, M.1
  • 14
    • 0014305510 scopus 로고
    • The molecular biology of Euglena gracilis. V. Enzyme localization
    • Kempner E.S., Miller J.H. The molecular biology of Euglena gracilis. V. Enzyme localization. Exp. Cell Res. 51:1968;150-156.
    • (1968) Exp. Cell Res. , vol.51 , pp. 150-156
    • Kempner, E.S.1    Miller, J.H.2
  • 15
    • 0041395893 scopus 로고
    • What is the cytosol?
    • Clegg J.S. What is the cytosol? Trends Biochem. Sci. 6:1983;436-437.
    • (1983) Trends Biochem. Sci. , vol.6 , pp. 436-437
    • Clegg, J.S.1
  • 16
    • 0021271614 scopus 로고
    • The cytomatrix: A short history of its study
    • Porter K.R. The cytomatrix: a short history of its study. J. Cell Biol. 99:1984;3s-12s.
    • (1984) J. Cell Biol. , vol.99
    • Porter, K.R.1
  • 17
    • 0029975931 scopus 로고    scopus 로고
    • The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants
    • Wang J.et al. The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants. J. Biol. Chem. 271:1996;6861-6865.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6861-6865
    • Wang, J.1
  • 18
    • 0029101859 scopus 로고
    • Fluorescent protein biosensors: Measurement of molecular dynamics in living cells
    • Giuliano K.A.et al. Fluorescent protein biosensors: measurement of molecular dynamics in living cells. Annu. Rev. Biophys. Biomol. Struct. 24:1995;405-434.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 405-434
    • Giuliano, K.A.1
  • 19
    • 0030462603 scopus 로고    scopus 로고
    • Role of cytoarchitecture in cytoplasmic transport
    • Luby-Phelps K., Weisiger R.A. Role of cytoarchitecture in cytoplasmic transport. Comp. Biochem. Physiol. 115B:1996;295-306.
    • (1996) Comp. Biochem. Physiol. , vol.115 , pp. 295-306
    • Luby-Phelps, K.1    Weisiger, R.A.2
  • 20
    • 0033991590 scopus 로고    scopus 로고
    • Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area
    • (in press)
    • Luby-Phelps K. Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area. Int. Rev. Cytol. 2000;. (in press).
    • (2000) Int. Rev. Cytol.
    • Luby-Phelps, K.1
  • 21
    • 0029841451 scopus 로고    scopus 로고
    • Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism
    • Knull H., Minton A.P. Structure within eukaryotic cytoplasm and its relationship to glycolytic metabolism. Cell Biochem. Function. 14:1996;237-248.
    • (1996) Cell Biochem. Function , vol.14 , pp. 237-248
    • Knull, H.1    Minton, A.P.2
  • 22
    • 0023677341 scopus 로고
    • Glycolysis in permeabilized L-929 cells
    • Clegg J.S., Jackson S.A. Glycolysis in permeabilized L-929 cells. Biochem. J. 255:1988;335-344.
    • (1988) Biochem. J. , vol.255 , pp. 335-344
    • Clegg, J.S.1    Jackson, S.A.2
  • 23
    • 0025247856 scopus 로고
    • Glucose metabolism and the channeling of glycolytic intermediates in permeabilized L-929 cells
    • Clegg J.S., Jackson S.A. Glucose metabolism and the channeling of glycolytic intermediates in permeabilized L-929 cells. Arch. Biochem. Biophys. 278:1990;452-460.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 452-460
    • Clegg, J.S.1    Jackson, S.A.2
  • 24
    • 0030768060 scopus 로고    scopus 로고
    • Flight muscle function in Drosophila requires colocalization of glycolytic enzymes
    • Wojtas K.et al. Flight muscle function in Drosophila requires colocalization of glycolytic enzymes. Mol. Biol. Cell. 8:1997;1665-1675.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1665-1675
    • Wojtas, K.1
  • 28
    • 0028304634 scopus 로고
    • Metabolic channeling versus free diffusion: Transition-time analysis
    • Welch G.R., Easterby J.S. Metabolic channeling versus free diffusion: transition-time analysis. Trends Biochem. Sci. 19:1994;193-197.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 193-197
    • Welch, G.R.1    Easterby, J.S.2
  • 29
    • 0004488109 scopus 로고
    • The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa
    • Yanofsky C., Rachmeler M. The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim. Biophys. Acta. 28:1958;640-641.
    • (1958) Biochim. Biophys. Acta , vol.28 , pp. 640-641
    • Yanofsky, C.1    Rachmeler, M.2
  • 30
    • 0024297340 scopus 로고
    • 3-Dimensional structure of the tryptophan synthase alpha-2-beta-2 multienzyme complex from Salmonella typhimurium
    • Hyde C.C.et al. 3-Dimensional structure of the tryptophan synthase alpha-2-beta-2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:1988;17857-17871.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1
  • 31
    • 48549111326 scopus 로고
    • Why are enzymes so big?
    • Srere P.A. Why are enzymes so big? Trends Biochem. Sci. 9:1984;387-390.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 387-390
    • Srere, P.A.1
  • 32
    • 0020135896 scopus 로고
    • Molecular evolution, intracellular organization, and the quinary structure of proteins
    • McConkey E.H. Molecular evolution, intracellular organization, and the quinary structure of proteins. Proc. Natl. Acad. Sci. U. S. A. 79:1982;3236-3240.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3236-3240
    • McConkey, E.H.1
  • 34
    • 0024319155 scopus 로고
    • Metabolic studies on citrate synthase mutants of yeast: A change in phenotype following transformation with an inactive enzyme
    • Kispal G.et al. Metabolic studies on citrate synthase mutants of yeast: a change in phenotype following transformation with an inactive enzyme. J. Biol. Chem. 264:1989;11204-11210.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11204-11210
    • Kispal, G.1
  • 35
    • 0014787708 scopus 로고
    • Physiological advantage of the mechanism of the tryptophan synthetase reaction
    • Manney T.R. Physiological advantage of the mechanism of the tryptophan synthetase reaction. J. Bacteriol. 102:1970;483-488.
    • (1970) J. Bacteriol. , vol.102 , pp. 483-488
    • Manney, T.R.1
  • 36
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi J.L.et al. Exploring the metabolic and genetic control of gene expression on a genomic scale. Science. 278:1997;680-686.
    • (1997) Science , vol.278 , pp. 680-686
    • Derisi, J.L.1
  • 38
    • 0032168794 scopus 로고    scopus 로고
    • Systematic functional analysis of the yeast genome
    • Oliver S.G.et al. Systematic functional analysis of the yeast genome. Trends Biotechnol. 16:1998;373-378.
    • (1998) Trends Biotechnol. , vol.16 , pp. 373-378
    • Oliver, S.G.1
  • 39
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien C.T.et al. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc. Nat. Acad. Sci. U. S. A. 88:1991;9578-9582.
    • (1991) Proc. Nat. Acad. Sci. U. S. A. , vol.88 , pp. 9578-9582
    • Chien, C.T.1
  • 40
    • 0033597939 scopus 로고    scopus 로고
    • Genetic selection of peptide inhibitors of biological pathways
    • Norman T.C.et al. Genetic selection of peptide inhibitors of biological pathways. Science. 285:1999;591-595.
    • (1999) Science , vol.285 , pp. 591-595
    • Norman, T.C.1
  • 41
    • 0002215847 scopus 로고
    • Protein organization in mitochondria
    • G.R. Welch. Academic Press
    • Srere P.A. Protein organization in mitochondria. Welch G.R. Organized Multienzyme Systems. 1985;1-61 Academic Press.
    • (1985) Organized Multienzyme Systems , pp. 1-61
    • Srere, P.A.1
  • 42
    • 0021381587 scopus 로고
    • Properties and metabolism of the aqueous cytoplasm and its boundaries
    • Clegg J.S. Properties and metabolism of the aqueous cytoplasm and its boundaries. Am. J. Physiol. 246:1984;R133-R151.
    • (1984) Am. J. Physiol. , vol.246
    • Clegg, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.