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papillon-lefevre disease/رشاد الصخر

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مقالاتالتجارب السريريةبراءات الاختراع
الصفحة 1 من عند 122 النتائج

Growing Slowly 1 locus encodes a PLS-type PPR protein required for RNA editing and plant development in Arabidopsis.

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Most pentatricopeptide repeat (PPR) proteins are involved in organelle post-transcriptional processes, including RNA editing. The PPR proteins include the PLS subfamily, containing characteristic triplets of P, L, and S motifs; however, their editing mechanisms and roles in developmental processes

Structure of a PLS-class pentatricopeptide repeat protein provides insights into mechanism of RNA recognition.

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Pentatricopeptide repeat (PPR) proteins are sequence-specific RNA-binding proteins that form a pervasive family of proteins conserved in yeast, plants, and humans. The plant PPR proteins are grouped mainly into the P and PLS classes. Here, we report the crystal structure of a PLS-class PPR protein

Comparative genomic analysis of the PAL genes in five Rosaceae species and functional identification of Chinese white pear.

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Phenylalanine ammonia lyase (PAL) plays an important role in the biosynthesis of secondary metabolites regulating plant growth response. To date, the evolutionary history of the PAL family in Rosaceae plants remains unclear. In this study, we identified 16 PAL homologous genes in five

Differential expression of four Arabidopsis PAL genes; PAL1 and PAL2 have functional specialization in abiotic environmental-triggered flavonoid synthesis.

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Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) catalyzes the first step in the phenylpropanoid pathway, and is considered an important regulation point between primary and secondary metabolism. In the present work we analyzed expression of the PAL genes in leaves of Arabidopsis thaliana rosette-stage

Molecular interactions of the phytotoxins destruxin B and sirodesmin PL with crucifers and cereals: metabolism and elicitation of plant defenses.

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Destruxin B and sirodesmin PL are phytotoxins produced by the phytopathogenic fungi Alternaria brassicae (Berk.) Sacc. and Leptosphaeria maculans (asexual stage Phoma lingam), respectively. The molecular interaction of destruxin B and sirodesmin PL with cruciferous and cereal species was

Functional analysis of the Arabidopsis PAL gene family in plant growth, development, and response to environmental stress.

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Phenylalanine ammonia-lyase (PAL) catalyzes the first step of the phenylpropanoid pathway, which produces precursors to a variety of important secondary metabolites. Arabidopsis (Arabidopsis thaliana) contains four PAL genes (PAL1-PAL4), but there has been no genetic analysis to assess the

Glucosinolate and phenylpropanoid biosynthesis are linked by proteasome-dependent degradation of PAL.

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Plants produce several hundreds of thousands of secondary metabolites that are important for adaptation to various environmental conditions. Although different groups of secondary metabolites are synthesized through unique biosynthetic pathways, plants must orchestrate their production

Comprehensive Prediction of Target RNA Editing Sites for PLS-Class PPR Proteins in Arabidopsis thaliana.

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Hundreds of RNA editing events, that is conversion of cytidines (Cs) to uridines (Us), have been observed in the mitochondrial and plastid transcriptome in vascular plants. Defects of C-to-U RNA editing affect a wide variety of physiological processes. These editing sites are recognized by

The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.

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In Arabidopsis thaliana, four genes have been annotated as provisionally encoding PAL. In this study, recombinant native AtPAL1, 2, and 4 were demonstrated to be catalytically competent for l-phenylalanine deamination, whereas AtPAL3, obtained as a N-terminal His-tagged protein, was of very low

QUIRKY interacts with STRUBBELIG and PAL OF QUIRKY to regulate cell growth anisotropy during Arabidopsis gynoecium development.

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Organ morphogenesis largely relies on cell division and elongation, which need to be both coordinated between cells and orchestrated with cytoskeleton dynamics. However, components that bridge the biological signals and the effectors that define cell shape remain poorly described. We have addressed

Interaction of PLS and PIN and hormonal crosstalk in Arabidopsis root development.

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Understanding how hormones and genes interact to coordinate plant growth is a major challenge in developmental biology. The activities of auxin, ethylene, and cytokinin depend on cellular context and exhibit either synergistic or antagonistic interactions. Here we use experimentation and network

Structural Analysis of the Arabidopsis AL2-PAL and PRC1 Complex Provides Mechanistic Insight into Active-to-Repressive Chromatin State Switch.

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Polycomb group proteins play essential roles in transcriptional gene repression during both animal and plant development. Polycomb repression complex 1 (PRC1) is one of the key functional modules in polycomb group silencing. It acts as both a reader of H3K27me3 (histone H3 lysine 27 trimethylation)
Phenylalanine ammonia lyase (PAL) from Arabidopsis thaliana (AtPAL2) is in general a very good catalyst for the amination of fluoro- and chloro-cinnamic acid derivatives yielding halogenated (S)-phenylalanine derivatives with ≥85% conversion and excellent ee values >99%. We have studied the

Mining the Arabidopsis and rice genomes for cyclophilin protein families.

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Cyclophilins, which possess peptidyl-prolyl isomerase activity, are cellular targets of immunosuppressant drugs and involved in a wide variety of functions. While the Arabidopsis thaliana genome contains the largest number of cyclophilins, the number of plant cyclophilins available in databases is

Down-regulation of Kelch domain-containing F-box protein in Arabidopsis enhances the production of (poly)phenols and tolerance to ultraviolet radiation.

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Phenylpropanoid biosynthesis in plants engenders myriad phenolics with diverse biological functions. Phenylalanine ammonia-lyase (PAL) is the first committed enzyme in the pathway, directing primary metabolic flux into a phenylpropanoid branch. Previously, we demonstrated that the Arabidopsis
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