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phenylalanine ammonia lyase/hipersensitivitas
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[Phenylalanine ammonia-lyase activity and tobacco mosaic virus hypersensitivity of Nicotiana tabacum var. xanthine].
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Molecular cloning and functional analysis of pea cDNA E86 encoding homologous protein to hypersensitivity-related hsr203J.
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Clone E86 was isolated as cDNA for elicitor-inducible gene from pea epicotyls by differential screening. The deduced amino acid sequence of E86 showed high homology to hypersensitivity-related protein hsr203J in tobacco and also showed significant homologies to the Ser-active hydrolases, such as
Phenylalanine ammonia-lyase levels in protoplasts isolated from hypersensitive tobacco pre-infected with tobacco mosaic virus.
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Leaves of tobacco varieties carrying the N gene for hypersensitiviy react to tobacco mosaic virus (TMV) infection by forming necrotic lesions and by localizing the virus in the vicinity of these lesions. These changes are accompanied in the host by an increased metabolic activity, in particular by
Differential effects of phenylalanine ammonia lyase, cinnamyl alcohol dehydrogenase, and energetic metabolism inhibition on resistance of appropriate host and nonhost cereal-rust interactions.
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ABSTRACT Effects of phenylpropanoid and energetic metabolism inhibition on resistance were studied during appropriate host and nonhost cereal-rust interactions. In the appropriate barley-Puccinia hordei interaction, phenylalanine ammonia lyase (PAL) and cinnamyl alcohol dehydrogenase (CAD)
Plant disease and the regulation of enzymes involved in lignification : Effects of osmotic pressure on phenylpropanoid enzymes and on the hypersensitive response of tobacco to tobacco mosaic virus.
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Tobacco varieties carrying the N gene from Nicotiana glutinosa respond to infection by Tobacco Mosaic Virus (TMV) by forming necrotic local lesions (hypersensitive reaction), thereby localizing the infection. In this study, infected mesophyll leaf tissue of N. tabacum Samsun NN was treated with the
Induction, titration, and maintenance dosing regimen in a phase 2 study of pegvaliase for control of blood phenylalanine in adults with phenylketonuria.
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BACKGROUND
Phenylketonuria (PKU) is caused by a deficiency in phenylalanine hydroxylase enzyme activity that leads to phenylalanine (Phe) accumulation in the blood and brain. Elevated blood Phe levels are associated with complications in adults, including neurological, psychiatric, and cognitive
The strawberry fruit Fra a allergen functions in flavonoid biosynthesis.
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The strawberry Fra a 1 allergen is a homolog of the major birch pollen allergen Bet v 1. It is synthesized by red ripe fruits of Fragaria x ananassa while white fruits of a mutant genotype, which is known to be tolerated by individuals affected by allergy, are devoid of it. Proteomic analyses have
Pegvaliase for the treatment of phenylketonuria: Results of a long-term phase 3 clinical trial program (PRISM).
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BACKGROUND
Phenylketonuria (PKU) is caused by phenylalanine hydroxylase (PAH) deficiency that results in phenylalanine (Phe) accumulation. Pegvaliase, PEGylated recombinant Anabaena variabilis phenylalanine ammonia lyase (PAL), converts Phe to trans-cinnamic acid and ammonia, and is a potential
Pegvaliase for the treatment of phenylketonuria: Results of the phase 2 dose-finding studies with long-term follow-up
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Background: Phenylketonuria (PKU) is characterized by a deficiency in phenylalanine hydroxylase (PAH) that may lead to elevated blood phenylalanine (Phe) and significant neurocognitive and neuropsychological comorbidities. Pegvaliase
Production and applications of rosmarinic acid and structurally related compounds.
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Rosmarinic acid (α-o-caffeoyl-3,4-dihydroxyphenyllactic acid; RA) is a naturally occurring hydroxylated compound commonly found in species of the subfamily Nepetoideae of the Lamiaceae and Boraginaceae, such as Rosmarinus officinalis, Salvia officinalis, and Perilla frutescens. RA is biosynthesized
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