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Annual Review of Biochemistry|June 8, 2001
Folding of newly translated proteins in vivo: the role of molecular chaperonesJ FrydmanTrends in Biochemical Sciences|March 1, 1997
Chaperones get in touch: the Hip-Hop connectionJ Frydman, J HöhfeldScience (New York, N.Y.)|June 7, 1996
Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanismsJ Frydman, F U HartlCurrent Opinion in Structural Biology|February 19, 2000
Protein folding in vivo: the importance of molecular chaperonesD E Feldman, J FrydmanProceedings of the National Academy of Sciences of the United States of America|June 1, 1992
An ATP-stabilized inhibitor of the proteasome is a component of the 1500-kDa ubiquitin conjugate-degrading complexJ Driscoll, J Frydman, A L GoldbergThe EMBO Journal|January 7, 1999
In vivo newly translated polypeptides are sequestered in a protected folding environmentV Thulasiraman, C F Yang, J FrydmanJournal of Structural Biology|October 3, 2001
Review: cellular substrates of the eukaryotic chaperonin TRiC/CCTA Y Dunn, M W Melville, J FrydmanBiochimica Et Biophysica Acta|February 15, 1991
An analysis of the topography of molecular forms 1 and 3 of rat liver biliverdin reductase using polyclonal antibodiesJ Frydman, M L Tomaro, R B FrydmanFEBS Letters|April 9, 1990
The in vivo and in vitro oxidation of molecular form 1 of biliverdin reductase to molecular form 3 by diamideM L Tomaro, J Frydman, R B FrydmanArchives of Biochemistry and Biophysics|May 1, 1991
Heme oxygenase induction by CoCl2, Co-protoporphyrin IX, phenylhydrazine, and diamide: evidence for oxidative stress involvementM L Tomaro, J Frydman, R B FrydmanPageof 3