Publications

Publications

Journal Article (15)

  1. 1.
    Popp, S.; Packschies, L.; Radzwill, N.; Vogel, K. P.; Steinhoff, H.; Reinstein, J.: Structural dynamics of the DnaK-peptide complex. Journal of Molecular Biology 347 (5), pp. 1039 - 1052 (2005)
  2. 2.
    Richter, K.; Muschler, P.; Hainzl, O.; Reinstein, J.; Buchner, J.: Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. The Journal of Biological Chemistry 278 (12), pp. 10328 - 10333 (2003)
  3. 3.
    Groemping, Y.; Reinstein, J.: Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. Journal of Molecular Biology (London) 314 (1), pp. 167 - 178 (2001)
  4. 4.
    Schlichting, I.; Reinstein, J.: pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog. Nature Structural and Molecular Biology 6 (8), pp. 721 - 723 (1999)
  5. 5.
    Gruen, M.; Becker, C.; Beste, A.; Reinstein, J.; Scheidig, A. J.; Goody, R. S.: 2′Halo-ATP and -GTP analogues: Rational phasing tools for protein crystallography. Protein Science 8 (11), pp. 2524 - 2528 (1999)
  6. 6.
    Lavie, A.; Reinstein, J.; Goody, R. S.; Schlichting, I.; Konrad, M.: Reply to "Improving AZT efficacy". Nature Medicine 4, p. 132 - 132 (1998)
  7. 7.
    Schlichting, I.; Reinstein, J.: Structure of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry 36, pp. 9290 - 9296 (1997)
  8. 8.
    Schlichting, I.; Reinstein, J.: Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry 36 (31), pp. 9290 - 9296 (1997)
  9. 9.
    Müller, C. W.; Schlauderer, G. J.; Reinstein, J.; Schulz, G. E.: Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding. Structure 4 (2), pp. 147 - 156 (1996)
  10. 10.
    Vogel, P. D.; Neuhofen, S.; Theyssen, H.; Reinstein, J.; Trommer, W. E.: Investigating nucleotide-binding to the heat-shock protein dnak using esr-spectroscopy. Biophysical Journal 70, pp. 433 - 321 (1996)
  11. 11.
    McCarty, J. S.; Buchberger, A.; Reinstein, J.; Bukau, B.: The role of ATP in the functional cycle of the DnaK chaperone system. Journal of Molecular Biology (London) 249 (1), pp. 126 - 137 (1995)
  12. 12.
    Divita, G.; Mueller, B.; Immendörfer, U.; Gautel, M.; Rittinger, K.; Restle, T.; Goody, R. S.: Kinetics of interaction of HIV reverse transcriptase with primer/template. Biochemistry 32 (31), pp. 7966 - 7971 (1993)
  13. 13.
    Divita, G.; Restle, T.; Goody, R. S.: Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence. FEBS Letters 324 (2), pp. 153 - 158 (1993)
  14. 14.
    Vetter, I. R.; Reinstein, J.; Konrad, M.; Goody, R. S.; Rösch, P.: NMR studies of the nucleotide binding-sites of adenylate kinase. Biological Chemistry Hoppe-Seyler 372 (9), p. 772 - 772 (1991)
  15. 15.
    Reinstein, J.; Gilles, A.; Rose, T.; Wittinghofer, A.; Saint−Girons, I.; Barzu, O.; Surewicz, W. K.; Mantsch, H. H.: Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. The Journal of Biological Chemistry 264 (14), pp. 8107 - 8112 (1989)

Book Chapter (2)

  1. 16.
    Schlee, S.; Reinstein, J.: Characterization of ATPase cycles of molecular chaperones by fluorescence and transient kinetic methods. In: Protein Folding Handbook, pp. 105 - 161 (Eds. Buchner, J.; Kiefhaber, T.). Wiley-VCH, Weinheim (2005)
  2. 17.
    Buchberger, A.; Reinstein, J.; Bukau, B.: The DnaK Chaperone system. In: Molecular Chaperones and Folding Catalysts: Regulation, Cellular Functions and Mechanisms, pp. 573 - 635 (Ed. Publishers, H. A.). Harwood Academic Publishers, Amsterdam (1999)
 
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