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  • Bacterial Proteins/*metabolism  (1)
  • Chemistry  (1)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 1
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    A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-03-15
    Description: Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macho, Alberto P -- Schwessinger, Benjamin -- Ntoukakis, Vardis -- Brutus, Alexandre -- Segonzac, Cecile -- Roy, Sonali -- Kadota, Yasuhiro -- Oh, Man-Ho -- Sklenar, Jan -- Derbyshire, Paul -- Lozano-Duran, Rosa -- Malinovsky, Frederikke Gro -- Monaghan, Jacqueline -- Menke, Frank L -- Huber, Steven C -- He, Sheng Yang -- Zipfel, Cyril -- BB/G024944/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- R01AI060761/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2014 Mar 28;343(6178):1509-12. doi: 10.1126/science.1248849. Epub 2014 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24625928" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*immunology/*microbiology ; Arabidopsis Proteins/agonists/*metabolism ; Bacterial Proteins/*metabolism ; Peptide Elongation Factor Tu/*metabolism ; Peptides/metabolism/pharmacology ; Phosphorylation ; Protein Tyrosine Phosphatases/*metabolism ; Pseudomonas syringae/enzymology/*pathogenicity ; Receptors, Pattern Recognition/agonists/*metabolism ; Tyrosine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A potent nonpeptide cholecystokinin antagonist selective for peripheral tissues isolated from Aspergillus alliaceus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-11
    Description: A new, competitive, nonpeptide cholecystokinin (CCK) antagonist, asperlicin, was isolated from the fungus Aspergillus alliaceus. The compound has 300 to 400 times the affinity for pancreatic, ileal, and gallbladder CCK receptors than proglumide, a standard agent of this class. Moreover, asperlicin is highly selective for peripheral CCK receptors relative to brain CCK and gastrin receptors. Since asperlicin also exhibits long-lasting CCK antagonist activity in vivo, it should provide a valuable tool for investigating the physiological and pharmacological actions of CCK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, R S -- Lotti, V J -- Monaghan, R L -- Birnbaum, J -- Stapley, E O -- Goetz, M A -- Albers-Schonberg, G -- Patchett, A A -- Liesch, J M -- Hensens, O D -- New York, N.Y. -- Science. 1985 Oct 11;230(4722):177-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994227" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspergillus/*metabolism ; Benzodiazepinones/*isolation & purification/pharmacology ; Chemical Phenomena ; Chemistry ; Cholecystokinin/*antagonists & inhibitors/pharmacology/physiology ; Dose-Response Relationship, Drug ; Gallbladder/drug effects ; Guinea Pigs ; Ileum/drug effects ; Pancreas/drug effects ; Rats ; Receptors, Cell Surface/drug effects ; Receptors, Cholecystokinin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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