Characterization of CHARK, an unusual cytokinin receptor of rice
The signal transduction of the plant hormone cytokinin is mediated by a His-to-Asp phosphorelay. The canonical cytokinin receptor consists of an extra cytoplasmic hormone binding domain named cyclase/histidine kinase associated sensory extracellular ...
Mhyeddeen Halawa+3 more
doaj +1 more source
Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex. [PDF]
The binding of nitric oxide (NO) to the heme cofactor of heme-nitric oxide/oxygen binding (H-NOX) proteins can lead to the dissociation of the heme-ligating histidine residue and yield a five-coordinate nitrosyl complex, an important step for NO ...
Britt, R David+5 more
core +1 more source
Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations [PDF]
To enable the processing of chemical gradients, chemotactic bacteria possess large arrays of transmembrane chemoreceptors, the histidine kinase CheA, and the adaptor protein CheW, organized as coupled core-signaling units (CSU). Despite decades of study,
Cassidy, Keith+8 more
core +1 more source
Substrates modulate charge-reorganization allosteric effects in protein-protein association [PDF]
Protein function may be modulated by an event occurring far away from the functional site, a phenomenon termed allostery. While classically allostery involves conformational changes, we recently observed that charge redistribution within an antibody can also lead to an allosteric effect, modulating the kinetics of binding to target antigen.
arxiv
Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
SYAUP-CN-26 (1S, 2R-((3-bromophenethyl)amino)-N-(4-chloro-2-trifluoromethylphenyl) cyclohexane-1-sulfonamide) is a novel sulfonamide compound with excellent activity against Botrytis cinerea.
Kai Wang+6 more
doaj +1 more source
Probing the nucleotide-binding activity of a redox sensor: two-component regulatory control in chloroplasts [PDF]
Two-component signal transduction systems mediate adaptation to environmental changes in bacteria, plants, fungi, and protists. Each two-component system consists of a sensor histidine kinase and a response regu- lator. Chloroplast sensor kinase (CSK) is
Allen, JF+3 more
core +1 more source
Diversity and Evolution of Sensor Histidine Kinases in Eukaryotes [PDF]
Histidine kinases (HKs) are primary sensor proteins that act in cell signaling pathways generically referred to as "two-component systems" (TCSs). TCSs are among the most widely distributed transduction systems used by both prokaryotic and eukaryotic organisms to detect and respond to a broad range of environmental cues.
Kabbara, Samar+10 more
openaire +4 more sources
Prediction of kinase inhibitor response using activity profiling, in-vitro screening, and elastic net regression [PDF]
Many kinase inhibitors have been approved as cancer therapies. Recently, libraries of kinase inhibitors have been extensively profiled, thus providing a map of the strength of action of each compound on a large number of its targets. These profiled libraries define drug-kinase networks that can predict the effectiveness of new untested drugs and ...
arxiv +1 more source
Regulation of signal duration and the statistical dynamics of kinase activation by scaffold proteins [PDF]
Scaffolding proteins that direct the assembly of multiple kinases into a spatially localized signaling complex are often essential for the maintenance of an appropriate biological response. Although scaffolds are widely believed to have dramatic effects on the dynamics of signal propagation, the mechanisms that underlie these consequences are not well ...
arxiv +1 more source
The PAS domain-containing histidine kinase RpfS is a second sensor for the diffusible signal factor of Xanthomonas campestris [PDF]
Summary: A cell-cell signalling system mediated by the fatty acid signal DSF controls the virulence of Xanthomonas campestris pv. campestris (Xcc) to plants. The synthesis and recognition of the DSF signal depends upon different Rpf proteins.
Allan, John H.+5 more
core +2 more sources