An Essential Phosphorylation-site Domain of Human cdc25C Interacts with Both 14-3-3 and Cyclins
Open Access
- 1 September 2000
- journal article
- Published by Elsevier
- Vol. 275 (37) , 28849-28857
- https://doi.org/10.1074/jbc.m002942200
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- Crystal structure of the catalytic subunit of Cdc25B required for G 2 /M phase transition of the cell cycle 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1999
- Characterization of the interactions between human cdc25c, cdks, cyclins and cdk-cyclin complexesJournal of Molecular Biology, 1999
- A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphataseCurrent Biology, 1999
- Conformations of Primary Amphipathic Carrier Peptides in Membrane Mimicking EnvironmentsBiochemistry, 1997
- Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of PhosphoserineCell, 1996
- Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathwaysNature, 1995
- Functional analysis of the P box, a domain in cyclin B required for the activation of Cdc25Cell, 1993
- Clean TOCSY for proton spin system identification in macromoleculesJournal of the American Chemical Society, 1988
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980