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The Journal of Biological Chemistry|December 29, 1998
A new heat shock protein that binds nucleic acidsP Korber, T Zander, D Herschlag, et al.Cell|December 15, 1995
Why is DsbA such an oxidizing disulfide catalyst?U Grauschopf, J R Winther, P Korber, et al.The EMBO Journal|February 17, 2000
Structure of Hsp15 reveals a novel RNA-binding motifB L Staker, P Korber, J C Bardwell, et al.The EMBO Journal|February 17, 2000
Hsp15: a ribosome-associated heat shock proteinP Korber, J M Stahl, K H Nierhaus, et al.Protein Science : a Publication of the Protein Society|June 1, 1997
The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide bindingL W Guddat, J C Bardwell, T Zander, et al.Protein Science : a Publication of the Protein Society|September 23, 1997
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stabilityL W Guddat, J C Bardwell, R Glockshuber, et al.Molecular Microbiology|October 1, 1994
Building bridges: disulphide bond formation in the cellJ C BardwellProceedings of the National Academy of Sciences of the United States of America|August 15, 1991
Implications of ribozyme kinetics for targeting the cleavage of specific RNA molecules in vivo: more isn't always betterD HerschlagBiochemistry|February 11, 1992
Evidence for processivity and two-step binding of the RNA substrate from studies of J1/2 mutants of the Tetrahymena ribozymeD HerschlagRNA (New York, N.Y.)|February 19, 1999
Specificity from steric restrictions in the guanosine binding pocket of a group I ribozymeR Russell, D HerschlagPageof 17