Similarities and differences between human cyclophilin A and other β-barrel structures: Structural refinement at 1.63 Å resolution
- 20 November 1992
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 228 (2) , 539-550
- https://doi.org/10.1016/0022-2836(92)90841-7
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Catalysis stepsNature, 1992
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexesCell, 1991
- Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsACell, 1991
- Conformational and geometrical properties of idealized β-barrels in proteinsJournal of Molecular Biology, 1990
- Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 Å resolutionJournal of Molecular Biology, 1990
- Kinetic β‐deuterium isotope effects suggest a covalent mechanism for the protein folding enzyme peptidylprolyl cis/trans‐isomeraseFEBS Letters, 1989
- One fold among manyNature, 1987
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982
- Orthogonal packing of .beta.-pleated sheets in proteinsBiochemistry, 1982
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolutionJournal of Molecular Biology, 1975