Results 321 to 330 of about 135,820 (362)

Mammalian protein histidine kinases

The International Journal of Biochemistry & Cell Biology, 2003
The existence of protein kinases, known as histidine kinases, which phosphorylate their substrates on histidine residues has been well documented in bacteria and also in lower eukaryotes such as yeast and plants. Their biological roles in cellular signalling pathways within these organisms have also been well characterised.
Paul V. Attwood, Paul G. Besant, Eiling Tan   +2 more
openaire   +3 more sources

Nucleoside diphosphate kinase as protein histidine kinase

Naunyn-Schmiedeberg's Archives of Pharmacology, 2014
Like phosphorylation of serine, threonine, and tyrosine residues in many organisms, reversible histidine phosphorylation is a well-known regulatory signal in prokaryotes and lower eukaryotes. In vertebrates, phosphohistidine has been mainly described as a phosphorylated intermediate in enzymatic reactions, and it was believed that regulatory histidine ...
Paul V. Attwood, Thomas Wieland
openaire   +3 more sources

Histidine Kinase Inhibitors

2015
Dicarboximides and phenylpyrroles have been mainly used to control diseases caused by fungal strains that belong to the genera Botrytis, Sclerotinia, Monilinia, and Alternaria. Both types of fungicides overactivate Hog-like mitogen-activated protein kinases in the osmotic signal transduction pathway and result in cell death.
Shinpei Banno, Fumiyasu Fukumori, Makoto Fujimura, Akihiko Ichiishi   +3 more
openaire   +2 more sources

The Histidine Protein Kinase Superfamily

1999
Signal transduction in microorganisms and plants is often mediated by His-Asp phosphorelay systems. Two conserved families of proteins are centrally involved: histidine protein kinases and phospho-aspartyl response regulators. The kinases generally function in association with sensory elements that regulate their activities in response to environmental
Thorsten W. Grebe, Jeffry B. Stock
openaire   +3 more sources

Histidine kinases and response regulators in networks

Current Opinion in Microbiology, 2012
Two-component systems, composed of a histidine kinase (HK) and a response regulator (RR), are the major signal transduction devices in bacteria. Originally it was thought that these two components function as linear, phosphorylation-driven stimulus-response system.
Luitpold Fried, Ralf Heermann, Stefan Behr, Kirsten Jung   +3 more
openaire   +2 more sources

Histidine kinases: diversity of domain organization

Molecular Microbiology, 1999
Histidine kinases play a major role in signal transduction in prokaryotes for the cellular adaptation to environmental conditions and stresses. Recent progress in the three‐dimensional structure determination of two representative members of histidine kinases, EnvZ (class I) and CheA (class II), has revealed common structural features, as well as a ...
Masayori Inouye, Ling Qin, Rinku Dutta
openaire   +3 more sources

Bacterial histidine kinase as signal sensor and transducer [PDF]

The International Journal of Biochemistry & Cell Biology, 2006
Adaptation to an environmental stress is essential for cell survival in all organisms, from E. coli to human. To respond to changes in their surroundings, bacteria utilize two-component systems (TCSs), also known as histidyl-aspartyl phosphorelay (HAP) systems that consist of a histidine kinase (HK) sensor and a cognate response regulator (RR).
Ahmad Khorchid, Mitsuhiko Ikura
openaire   +2 more sources

Nucleotide binding by the histidine kinase CheA.

Nature structural biology, 2001
To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+).
Cindy M. Quezada, Alexandrine M. Bilwes, Brian R. Crane, Brian R. Crane, Laura R. Croal, Melvin I. Simon   +5 more
openaire   +4 more sources

Histidine kinases from bacteria to humans

Biochemical Society Transactions, 2013
It is more than 50 years since protein histidine phosphorylation was first discovered in 1962 by Boyer and co-workers; however, histidine kinases are still much less well recognized than the serine/threonine and tyrosine kinases. The best-known histidine kinases are the two-component signalling kinases that occur in bacteria, fungi and plants.
openaire   +2 more sources

Histidine Kinase Regulation by a Cyclophilin-like Inhibitor

Journal of Molecular Biology, 2008
The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a ...
Jacques, DA, Langley, DB, Jeffries, CM, Cunningham, KA, Burkholder, WF, Guss, JM, Trewhella, J   +6 more
openaire   +4 more sources