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Structure (London, England : 1993)|July 10, 1998
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilizationL W Guddat, J C Bardwell, J L Martin
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|February 20, 1999
Chaperone activity with a redox switchU Jakob, W Muse, M Eser, et al.
The Journal of Biological Chemistry|May 2, 2000
DsbG, a protein disulfide isomerase with chaperone activityF Shao, M W Bader, U Jakob, 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.
Proceedings of the National Academy of Sciences of the United States of America|September 27, 2000
Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coliH Kadokura, M Bader, H Tian, et al.
The Journal of Biological Chemistry|June 16, 2000
Disulfide bonds are generated by quinone reductionM W Bader, T Xie, C A Yu, 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.
Cell|July 31, 1999
Oxidative protein folding is driven by the electron transport systemM Bader, W Muse, D P Ballou, et al.
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