NMR Solution Structure and Dynamics of the Peptidyl-prolyl cis–trans Isomerase Domain of the Trigger Factor from Mycoplasma genitalium Compared to FK506-binding Protein
- 10 May 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 318 (4) , 1097-1115
- https://doi.org/10.1016/s0022-2836(02)00112-2
Abstract
No abstract availableKeywords
This publication has 66 references indexed in Scilit:
- NMR solution structure of h Par14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator h Pin1 but indicates a different functionality of the protein 1 1Edited by A. FershtJournal of Molecular Biology, 2000
- Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalystsCellular and Molecular Life Sciences, 1999
- Protein folding in the cytosol: chaperonin-dependent and -independent mechanismsTrends in Biochemical Sciences, 1998
- The Amino-terminal 118 Amino Acids of Escherichia coli Trigger Factor Constitute a Domain That Is Necessary and Sufficient for Binding to RibosomesJournal of Biological Chemistry, 1997
- Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein foldingThe EMBO Journal, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.Proceedings of the National Academy of Sciences, 1996
- ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particleCell, 1988
- Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.Proceedings of the National Academy of Sciences, 1987
- Barrier to internal rotation of amides. I. FormamideThe Journal of Physical Chemistry, 1970