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1.
Polymers (Basel) ; 16(9)2024 Apr 27.
Article in English | MEDLINE | ID: mdl-38732694

ABSTRACT

This study investigates the mechanical properties of coconut sawdust powder combined with polypropylene (PP). The effect of compatibility content, wood powder (WP) content, and injection molding parameters on the properties of coconut wood powder composite (WPC) is evaluated. The results could be used to figure out the optimal mechanical properties such as tensile strength, elongation, elastic modulus, and flexural strength by selecting suitable parameters and composition. The bonding between the WP particles and the PP matrix is good, and the WP is uniformly distributed across the composite matrix, as indicated in the scanning electron microscopy (SEM) results. Interestingly, with the presence of the compatibilizer oleamide, increasing the WP content from 20 wt.% to 40 wt.% did not result in WP accumulation in the composite matrix. Notably, at 20 wt.% WP, the elongation is the highest (at 7.40 wt.%), while at 30 wt.% WP, the elastic modulus reaches the highest value. The maximum ultimate tensile strength (UTS) value is obtained at 35 wt.% WP. Higher WP mostly results in greater flexural strength and shore D hardness. At 40 wt.% WP, the WPC achieves its peak shore D hardness of 77.6. The Taguchi results suggest that WP content is the most critical factor in the UTS value of coconut WPCs. The filling pressure ranks second, followed by the packing pressure. Finally, unlike the other characteristics, the melt temperature has a minimal impact on the UTS value.

2.
Plant Cell Physiol ; 62(11): 1662-1675, 2021 Dec 10.
Article in English | MEDLINE | ID: mdl-34329461

ABSTRACT

Plants employ two different types of immune receptors, cell surface pattern recognition receptors (PRRs) and intracellular nucleotide-binding and leucine-rich repeat-containing proteins (NLRs), to cope with pathogen invasion. Both immune receptors often share similar downstream components and responses but it remains unknown whether a PRR and an NLR assemble into the same protein complex or two distinct receptor complexes. We have previously found that the small GTPase OsRac1 plays key roles in the signaling of OsCERK1, a PRR for fungal chitin, and of Pit, an NLR for rice blast fungus, and associates directly and indirectly with both of these immune receptors. In this study, using biochemical and bioimaging approaches, we revealed that OsRac1 formed two distinct receptor complexes with OsCERK1 and with Pit. Supporting this result, OsCERK1 and Pit utilized different transport systems for anchorage to the plasma membrane (PM). Activation of OsCERK1 and Pit led to OsRac1 activation and, concomitantly, OsRac1 shifted from a small to a large protein complex fraction. We also found that the chaperone Hsp90 contributed to the proper transport of Pit to the PM and the immune induction of Pit. These findings illuminate how the PRR OsCERK1 and the NLR Pit orchestrate rice immunity through the small GTPase OsRac1.


Subject(s)
GTP Phosphohydrolases/genetics , NLR Proteins/genetics , Oryza/genetics , Plant Immunity/genetics , Plant Proteins/genetics , Receptors, Pattern Recognition/genetics , GTP Phosphohydrolases/metabolism , NLR Proteins/metabolism , Oryza/metabolism , Plant Proteins/metabolism , Receptors, Pattern Recognition/metabolism
3.
Plant Cell Physiol ; 54(12): 2058-70, 2013 Dec.
Article in English | MEDLINE | ID: mdl-24158358

ABSTRACT

OsRac1 is a member of the plant small GTPase Rac/Rop family and plays a key role in rice immunity. The constitutively active (CA) G19V mutation of OsRac1 was previously shown to induce reactive oxygen species production, phytoalexin synthesis and defense gene activation, leading to resistance to rice blast infection. To study further the effect of the G19V mutation in disease resistance, we introduced a single base substitution by gene targeting and removed the selectable marker using Cre-loxP site-specific recombination. The CA-OsRac1 gene generated by gene targeting was termed CA-gOsRac1. The G19V mutation was transferred from a targeting vector to the OsRac1 locus and stably transmitted to the next generation. In the leaf blade of homozygous CA-gOsRac1 plants, mutant transcript levels were much lower than in those of wild-type plants. In contrast, mutant transcripts in roots, leaf sheaths and panicles were more abundant than those in leaf blades. However, upon chitin treatment, the expression of defense-related genes PAL1 and PBZ1 in the cell culture was greater in the mutants compared with wild-type plants. Furthermore, induction of hypersensitive response (HR)-like cell death was observed in the leaf sheaths of mutant plants infected with a compatible race of rice blast fungus. In the CA-gOsRac1 plants, a number of genes previously shown to be induced by Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae (Xoo) infection were induced in the leaf sheath without pathogen infection. These results suggest that gene targeting will provide mutations useful for gene function studies and crop improvement.


Subject(s)
Oryza/metabolism , Plant Proteins/metabolism , Homologous Recombination/genetics , Homologous Recombination/physiology , Magnaporthe/pathogenicity , Oryza/immunology , Oryza/microbiology , Plant Immunity/genetics , Plant Immunity/physiology , Plant Proteins/genetics , Xanthomonas/pathogenicity
4.
Bioorg Med Chem Lett ; 15(8): 1973-7, 2005 Apr 15.
Article in English | MEDLINE | ID: mdl-15808450

ABSTRACT

A series of aminobenzimidazole-substituted pyrimidines were synthesized and evaluated for biochemical activity against CDK1. A high-speed parallel synthesis approach enabled the identification of a potent lead series having improved potency in the CDK1 assay (IC(50)<10nM). Cell cycle analysis showed that the compounds induced a G2/M block. Docking studies were carried out with a CDK1 homology model, and provide a rationale for the observed activities.


Subject(s)
Benzimidazoles/chemistry , Cyclin-Dependent Kinases/antagonists & inhibitors , Protein Kinase Inhibitors/chemistry , Pyrimidines/chemistry , Benzimidazoles/pharmacology , Humans , Protein Kinase Inhibitors/pharmacology , Pyrimidines/pharmacology
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