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Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.

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Molecular Biology of the Cell. 3rd edition.

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Chapter 5References

    General

    1. Branden, C.; Tooze, J. Introduction to Protein Structure. New York: Garland, 1991.
    2. Creighton, T.E. Proteins: Structures and Molecular Properties, 2nd ed. New York: W.H. Freeman, 1993.

    Cited

    1.
    Steitz, T.A.; Shoham, M.; Bennett, W.S., Jr. Structural dynamics of yeast hexokinase during catalysis. Philos. Trans. R. Soc. Lond. (Biol.) 1981;293:43–52. [PMC free article: PMC126065] [PubMed: 6115422]
    2.
    Monod, J.; Changeux, J.-P.; Jacob, F. Allosteric proteins and cellular control systems. J. Mol. Biol 1963;. 6:306–329. [PubMed: 13936070]
  1. Perutz, M. Cooperativity and Allosteric Regulation in Proteins. Cambridge, UK: Cambridge University Press, 1990.
  2. 3.
    Koshland, D.E., Jr. Control of enzyme activity and metabolic pathways. Trends Biochem. Sci. 1984;9:155–159.
  3. Umbarger, H.E. The origin of a useful conceptfeedback inhibition. Protein Sci. 1992;1:1392–1395. [PMC free article: PMC2142110] [PubMed: 1303757]
  4. 4.
    Cantor, C.R.; Schimmel, P.R. Biophysical Chemistry. Part III: The Behavior of Biological Macromolecules, Chaps. 15 and 17. New York: W.H. Freeman, 1980.
  5. Dickerson, R.E.; Geis, I. Hemoglobin: Structure, Function, Evolution and Pathology. Menlo Park, CA: Benjamin-Cummings, 1983.
  6. Monod, J.; Changeux, J.-P.; Jacob, F. Allosteric proteins and cellular control systems. J. Mol. Biol. 1963;6:306–329. [PubMed: 13936070]
  7. 5.
    Kantrowitz, E.R.; Lipscomb, W.N. Escherichia coli aspartate transcarbamylase: the relation between structure and function. Science. 1988;241:669–674. [PubMed: 3041592]
  8. Kantrowitz, E.R.; Lipscomb, W.N. Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition. Trends. Biochem. Sci 1990;. 15:53–59. [PubMed: 2186515]
  9. Schachman, H.K. Can a simple model account for the allosteric transition of aspartate transcarbamoylase? J. Biol. Chem 1988;. 263:18583–18586. [PubMed: 3058687]
  10. 6.
    Fischer, E.H.; Krebs, E.G. Conversion of phosphorylase beta to phosphorylase alpha in muscle extracts. J. Biol. Chem. 1955;216:121–132. [PubMed: 13252012]
  11. Johnson, L.N.; Barford, D. The effects of phosphorylation on the structure and function of proteins. Annu. Rev. Biophys. Biomol. Struct. 1993;22:199–232. [PubMed: 8347989]
  12. 7.
    Cohen, P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 1989;58:453–508. [PubMed: 2549856]
  13. Hanks, S.K.; Quinn, A.M.; Hunter, T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 1988;241:42–52. [PubMed: 3291115]
  14. Taylor, S.S.; Knighton, D.R.; Zheng, J.; Ten Eyck, L.F.; Sowadski, J.M. Structural framework for the protein kinase family. Annu. Rev. Cell Biol 1992;. 8:429–462. [PubMed: 1335745]
  15. 8.
    DeBondt, H.L.; Rosenblatt, J.; Jancarik, J. et al. Crystal structure of cyclin-dependent kinase 2. Nature. 1993;363:595–602. [PubMed: 8510751]
    9.
    Bourne, H.R.; Sanders, D.A.; McCormick, F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 1991;349:117–127. [PubMed: 1898771]
  16. Wittinghofer, A.; Pai, E.F. The structure of ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 1991;16:382–387. [PubMed: 1785141]
  17. 10.
    McCormick, F. ras GTPase activating protein: signal transmitter and signal terminator. Cell. 1989;56:5–8. [PubMed: 2535967]
    11.
    Berchtold, H.; Reshetnikova, L.; Reiser, C.O.A. et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 1993;365:126–132. [PubMed: 8371755]
  18. Kjeldgaard, M.; Nissen, P.; Thirup, S.; Nyborg, J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1993;1:35–50. [PubMed: 8069622]
  19. 12.
    Hill, T.L. Biochemical cycles and free energy transduction. Trends Biochem. Sci. 1977;2:204–207.
    13.
    Rayment, I.; Holden, H.M.; Whittaker, M. et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 1993;261:58–65. [PubMed: 8316858]
    14.
    Hokin, L.E. The molecular machine for driving the coupled transports of Na+ and K+ is an (Na+ + K+)-activated ATPase. Trends Biochem. Sci. 1976;1:233–237.
  20. Jencks, W.P. How does a calcium pump pump calcium? J. Biol. Chem. 1989;264:18855–18858. [PubMed: 2530226]
  21. 15.
    Alberts, B.; Miake-Lye, R. Unscrambling the puzzle of biological machines: the importance of the details. Cell. 1992;68:415–420. [PubMed: 1531448]
    16.
    Alberts, B.M. Protein machines mediate the basic genetic processes. Trends Genet 1985;. 1:26–30.
    17.
    Udgaonkar, J.B.; Baldwin, R.L. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 1988;335:694–699. [PubMed: 2845278]
  22. Kuwajima, K. The molten globular state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins. 1989;6:87–103. [PubMed: 2695928]
  23. 18.
    Agard, D.A. To fold or not to fold. Science. 1993;260:1903–1904. [PubMed: 8100365]
  24. Georgopoulos, C.; Welch, W.J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 1993;9:601–634. [PubMed: 8280473]
  25. Martin, J.; Langer, T.; Boteva, R. et al. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature. 1991;352:36–42. [PubMed: 1676490]
  26. 19.
    Baron, M.; Norman, D.G.; Campbell, I.D. Protein modules. Trends Biochem. Sci 1991;. 16:13–17. [PubMed: 2053133]
    20.
    Koch, C.A.; Anderson, D.; Moran, M.F.; Ellis, C.; Pawson, T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. 1991;252:668–674. [PubMed: 1708916]
    21.
    Hershko, A.; Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992;61:761–807. [PubMed: 1323239]
  27. Rechsteiner, M.; Hoffman, L.; Dubiel, W. The multicatalytic and 26S proteases. J. Biol. Chem 1993;. 268:6065–6068. [PubMed: 8454582]
  28. 22.
    Varshavsky, A. The N-end rule. Cell. 1992;69:725–735. [PubMed: 1317266]

By agreement with the publisher, this book is accessible by the search feature, but cannot be browsed.

Copyright © 1994, Bruce Alberts, Dennis Bray, Julian Lewis, Martin Raff, Keith Roberts, and James D Watson.
Bookshelf ID: NBK28292

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