Suppression of host cinnamyl alcohol dehydrogenase and phenylalanine ammonia lyase increases oat epidermal cell susceptibility to powdery mildew penetration

This publication has 34 references indexed in Scilit:

• Sulphinamoylacetates as sulphine precursors. Mechanism of basic hydrolysis and scheme of irreversible inactivation of cinnamoyl alcohol dehydrogenase, an enzyme of the lignification process
  Journal of the Chemical Society, Perkin Transactions 2, 1988
• Distribution of hydrolytic enzymes at barley powdery mildew encounter sites: implications for resistance associated with papilla formation in a compatible system
  Physiological Plant Pathology, 1985
• Effect of adult plant resistance on primary penetration of oats by Erysiphe graminis f. sp. avenae
  Physiological Plant Pathology, 1984
• A Convenient and Facile Synthesis of β-Aminosulfinyl-and β-Aminosulfonylalkanoic Esters from Metallated Esters andN-Sulfinylamines
  Synthesis, 1982
• Autofluorescence in oats infected by powdery mildew
  Transactions of the British Mycological Society, 1981
• Localized accumulation of fluorescent and u.v.-absorbing compounds at penetration sites in barley leaves infected with Erysiphe graminis hordei
  Physiological Plant Pathology, 1978
• α-aminooxy-β-phenylpropionic acid — a potent inhibitor of L-phenylalanine ammonia-lyase in vitro and in vivo
  Plant Science Letters, 1977
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Aggregation of Host Cytoplasm and the Formation of Papillae and Haustoria in Powdery Mildew of Barley
  Phytopathology®, 1975
• Phenylalanine Ammonia-lyase, Tyrosine Ammonia-lyase, and Lignin in Wheat Inoculated with Erysiphe graminis f. sp. tritici
  Phytopathology®, 1975