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Publications—2000


The publications on this site are being made available to the academic community for
use in teaching and research. All copyrights remain intact.

Peer-Reviewed Journal Articles (Research)

  1. Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. Tony A. Klink, Kenneth J. Woycechowsky, Kimberly M. Taylor, and Ronald T. Raines (2000). European Journal of Biochemistry 267, 566–572. [PubMed] [PDF]
  2. Origin of the "inactivation" of ribonuclease A at low salt concentration. Chiwook Park and Ronald T. Raines (2000). FEBS Letters 468, 199–202. [PubMed] [PDF]
  3. A ribonuclease A variant with low catalytic activity but high cytotoxicity. Lynn E. Bretscher, Richele L. Abel, and Ronald T. Raines (2000). Journal of Biological Chemistry 275, 9893-9896. [PubMed] [PDF]
  4. Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans. Lisa Friedman, Joshua J. Higgin, Gary Moulder, Robert Barstead, Ronald T. Raines, and Judith Kimble (2000). Proceedings of the National Academy of Sciences, U.S.A. 97, 4736–4741. [PubMed] [PDF]
  5. Sulfur shuffle: Modulating enzymatic activity by thiol–disulfide interchange. June M. Messmore, Steven K. Holmgren, Juneko E. Grilley, and Ronald T. Raines (2000). Bioconjugate Chemistry 11, 408–413. [PubMed] [PDF]
  6. Conformational stability is a determinant of ribonuclease A cytotoxicity. Tony A. Klink and Ronald T. Raines (2000). Journal of Biological Chemistry 275, 17463–17467. [PubMed] [PDF]
  7. Staudinger ligation: A peptide from a thioester and azide. Bradley L. Nilsson, Laura L. Kiessling, and Ronald T. Raines (2000). Organic Letters 2, 1939–1941. [PubMed] [PDF] [Supporting Information]
  8. A synapomorphic disulfide bond is critical for the conformational stability and cytotoxicity of an amphibian ribonuclease. Peter A. Leland, Kristine E. Staniszewski, Byung-Moon Kim, and Ronald T. Raines (2000). FEBS Letters 477, 203–207. [PubMed] [PDF]
  9. Genetic selection for dissociative inhibitors of designated protein–protein interactions. Sang-Hyun Park and Ronald T. Raines (2000). Nature Biotechnology 18, 847–851. [PubMed] [PDF]
  10. Decavanadate inhibits catalysis by ribonuclease A. June M. Messmore and Ronald T. Raines (2000). Archives of Biochemistry and Biophysics 381, 25–30. [PubMed] [PDF]
  11. Effect of bovine seminal ribonuclease and its various forms on bovine oocyte maturation. Tomás Slavík, Josef Matousek, Josef Fulka, and Ronald T. Raines (2000). Journal of Experimental Zoology 287, 394–399. [PubMed] [PDF]
  12. Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A. Margherita Ruoppolo, Floriana Vinci, Tony A. Klink, Ronald T. Raines, and Gennaro Marino (2000). Biochemistry 39, 12033–12042. [PubMed] [PDF]
  13. Pentavalent organo-vanadates as transition state analogues for phosphoryl transfer reactions. June M. Messmore and Ronald T. Raines (2000). Journal of the American Chemical Society 122, 9911–9916. [PubMed] [PDF]
  14. A highly active immobilized ribonuclease. Rozamond Y. Sweeney, Bradley R. Kelemen, Kenneth J. Woycechowsky, and Ronald T. Raines (2000). Analytical Biochemistry 286, 312–314. [PubMed] [PDF]
  15. Image of CoverCOVER ARTICLE: Dimer formation by a "monomeric" protein. Chiwook Park and Ronald T. Raines (2000). Protein Science 9, 2026–2033. [PubMed] [PDF]
  16. Excavating an active site: The nucleobase specificity of ribonuclease A. Bradley R. Kelemen, L. Wayne Schultz, Rozamond Y. Sweeney, and Ronald T. Raines (2000). Biochemistry 39, 14,487–14,494. [PubMed] [PDF]

Peer-Reviewed Journal Articles (Reviews)

  1. Native disulfide bond formation in proteins. Kenneth J. Woycechowsky and Ronald T. Raines (2000). Current Opinion in Chemical Biology 4, 533–539. [PubMed] [PDF]

Invited Journal Articles

  1. The S-Tag fusion system for protein purification. Ronald T. Raines, Mark McCormick, Thomas R. Van Oosbree, and Robert C. Mierendorf (2000). Methods in Enzymology 326, 362–376. [PubMed] [PDF]
  2. Green fluorescent protein chimeras to probe protein–protein interactions. Sang-Hyun Park and Ronald T. Raines (2000). Methods in Enzymology 328, 251–261. [PubMed] [PDF]

Conference Proceedings

  1. The stereoelectronic basis of collagen stability. Ronald T. Raines, Lynn E. Bretscher, Steven K. Holmgren, and Kimberly M. Taylor (2000). In Peptides for the New Millennium: Proceedings of the 16th American Peptide Symposium (Gregg B. Fields, James P. Tam, and Geroge Barany, Eds.), pp. 344–346, Kluwer Academic, Dordrecht, The Netherlands. [PDF]
  2. Contribution of mainchain–mainchain hydrogen bonds to the conformational stability of triple-helical collagen. Mark A. Danielson and Ronald T. Raines (2000). In Peptides for the New Millennium: Proceedings of the 16th American Peptide Symposium (Gregg B. Fields, James P. Tam, and Geroge Barany, Eds.), pp. 347–348, Kluwer Academic, Dordrecht, The Netherlands. [PDF]
  3. Effect of fluoro-substituted proline residues on the conformational stability of triple-helical collagen mimics. Lynn E. Bretscher, Kimberly M. Taylor, and Ronald T. Raines (2000). In Peptides for the New Millennium: Proceedings of the 16th American Peptide Symposium (Gregg B. Fields, James P. Tam, and Geroge Barany, Eds.), pp. 355–356, Kluwer Academic, Dordrecht, The Netherlands. [PDF]
  4. Modulating the conformational stability of triple-helical collagen by chemical modification. Cara L. Jenkins, Kimberly M. Taylor, and Ronald T. Raines (2000). In Peptides for the New Millennium: Proceedings of the Sixteenth American Peptide Symposium (Gregg B. Fields, James P. Tam, and Geroge Barany, Eds.), pp. 357–358, Kluwer Academic, Dordrecht, The Netherlands. [PDF]