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Structure of CheA, a Signal-Transducing Histidine Kinase
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Kinetic Analysis of YPD1-Dependent Phosphotransfer Reactions in the Yeast Osmoregulatory Phosphorelay System †
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Response to Hyperosmotic Stress
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Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1 1 1Edited by I. A. Wilson
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[20] Processing of X-ray diffraction data collected in oscillation mode
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Signal Transduction via the Multi-Step Phosphorelay: Not Necessarily a Road Less Traveled
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Yeast HOG1 MAP Kinase Cascade Is Regulated by a Multistep Phosphorelay Mechanism in the SLN1–YPD1–SSK1 “Two-Component” Osmosensor
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Structure of CheA, a Signal-Transducing Histidine Kinase
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Interaction Dynamics Determine Signaling and Output Pathway Responses
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Full-Length Structure of a Sensor Histidine Kinase Pinpoints Coaxial Coiled Coils as Signal Transducers and Modulators
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Ssk1p Response Regulator Binding Surface on Histidine- Containing Phosphotransfer Protein Ypd1p
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Saccharomyces cerevisiae Histidine Phosphotransferase Ypd1p Shuttles between the Nucleus and Cytoplasm for SLN1 -Dependent Phosphorylation of Ssk1p and Skn7p
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Differential Stabilities of Phosphorylated Response Regulator Domains Reflect Functional Roles of the Yeast Osmoregulatory SLN1 and SSK1 Proteins
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Biological Insights from Structures of Two-Component Proteins
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Conformational coupling in the chemotaxis response regulator CheY
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text
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January 2001 |