The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping
- 31 January 2000
- Vol. 8 (1) , 89-100
- https://doi.org/10.1016/s0969-2126(00)00084-8
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein foldingPublished by Elsevier ,2004
- Stability and folding of the cell cycle regulatory protein, p13suc1Journal of Molecular Biology, 1998
- Crystal Structure and Mutational Analysis of the Human CDK2 Kinase Complex with Cell Cycle–Regulatory Protein CksHs1Cell, 1996
- Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.Proceedings of the National Academy of Sciences, 1995
- Crystal Structure of the Human Cell Cycle Protein CksHs1: Single Domain Fold with Similarity to Kinase N-lobe DomainJournal of Molecular Biology, 1995
- Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences, 1994
- Human CksHs2 Atomic Structure: a Role for Its Hexameric Assembly in Cell Cycle ControlScience, 1993
- Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysisBiochemistry, 1993
- Sucl+ encodes a predicted 13-kilodalton protein that is essential for cell viability and is directly involved in the division cycle of Schizosaccharomyces pombe.Molecular and Cellular Biology, 1987
- The fission yeast cell cycle control gene cdc2: isolation of a sequence suc1 that suppresses cdc2 mutant functionMolecular Genetics and Genomics, 1986