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Biochemistry|October 17, 1989
Shielding of tryptophan residues of avidin by the binding of biotinG P Kurzban, G Gitlin, E A Bayer, et al.The Journal of Biological Chemistry|March 15, 1991
Expression of cloned bovine adrenal rhodaneseD M Miller, R Delgado, J M Chirgwin, et al.Journal of Periodontology|July 1, 1992
Immunohistological localization of cell adhesion proteins and integrins in the periodontiumB Steffensen, A H Duong, S B Milam, et al.The Journal of Biological Chemistry|May 5, 1995
The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNAW Kudlicki, O W Odom, G Kramer, et al.Analytical Biochemistry|December 1, 1984
Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinkingP M Horowitz, J C Lee, G A Williams, et al.The Journal of Biological Chemistry|October 17, 1998
Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expressionR J Trevino, T Tsalkova, G Kramer, et al.Molecular Microbiology|September 1, 1995
Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophagesS Dhandayuthapani, L E Via, C A Thomas, et al.Biopolymers|November 1, 1989
Secondary structure of a core protein from pig skin proteodermatan sulfate: CD and Fourier transform IR spectroscopic studies in solutionV Renugopalakrishnan, S P Damle, P M Horowitz, et al.The Journal of Biological Chemistry|February 21, 1997
Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)B T Brazil, J L Cleland, R S McDowell, et al.The Journal of Biological Chemistry|May 13, 1999
NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditionsR J Trevino, F Gliubich, R Berni, et al.Pageof 15