Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae
- 5 November 1999
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 293 (4) , 753-761
- https://doi.org/10.1006/jmbi.1999.3215
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.Nature Structural & Molecular Biology, 1999
- Structure of CheA, a Signal-Transducing Histidine KinaseCell, 1999
- Antibacterial agents that inhibit two-component signal transduction systemsProceedings of the National Academy of Sciences, 1998
- Signal transduction via the histidyl‐aspartyl phosphorelayGenes to Cells, 1997
- Eukaryotes have “two-component” signal tranducersResearch in Microbiology, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- An Osmosensing Signal Transduction Pathway in YeastScience, 1993
- ALSCRIPT: a tool to format multiple sequence alignmentsProtein Engineering, Design and Selection, 1993
- PBS2, a yeast gene encoding a putative protein kinase, interacts with the RAS2 pathway and affects osmotic sensitivity of Saccharomyces cerevisiaeJournal of General Microbiology, 1992
- Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelayCell, 1991