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Biochemistry|November 7, 1995
Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosomeW Kudlicki, J Chirgwin, G Kramer, et al.
Folding & Design|January 1, 1997
Ribosomes and ribosomal RNA as chaperones for folding of proteinsW Kudlicki, A Coffman, G Kramer, et al.
The Journal of Biological Chemistry|February 25, 1984
Purification to homogeneity and partial characterization of a 56,000-dalton protein phosphatase from rabbit reticulocytesE Wollny, K Watkins, G Kramer, et al.
The Journal of Biological Chemistry|January 10, 1980
Partial purification and characterization of reticulocyte phosphatase with activity for phosphorylated peptide initiation factor 2N Grankowski, D Lehmusvirta, G Kramer, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 1, 1985
The 90-kDa component of reticulocyte heme-regulated eIF-2 alpha (initiation factor 2 alpha-subunit) kinase is derived from the beta subunit of spectrinW Kudlicki, S Fullilove, G Kramer, et al.
The Journal of Biological Chemistry|December 6, 1996
Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomesW Kudlicki, O W Odom, G Kramer, et al.
The Journal of Biological Chemistry|June 17, 1994
Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNAW Kudlicki, O W Odom, G Kramer, et al.
Molecular Biology Reports|December 1, 1975
A simple method for the purification of reticulocyte globin messenger ribonucleic acidD Konecki, J M Cimadevilla, G Kramer, et al.
Journal of Molecular Biology|December 2, 1994
Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescenceW Kudlicki, O W Odom, G Kramer, et al.
The Journal of Biological Chemistry|September 25, 1986
The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinaseR E Wettenhall, W Kudlicki, G Kramer, et al.
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