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Recently, extensive genetic and biochemical studies have shown that ubiquitin-mediated protein modification plays critical roles in plant immune responses [ 8, 11– 15].
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Although the mechanism is still elusive, studies have shown that sperm epigenetic modifications such as DNA demethylation, miRNA expression, and histone modification play critical roles in spermatogenesis; furthermore, they share similarity with the characteristics of embryonic stem cells.
The heritability of epigenetic modifications plays critical roles in maintaining cell-type-specific gene expression during cell divisions [ 1].
Post-translational modifications play critical role in the regulation of the β-catenin turnover by GSK3β [25].
Proteins that require FPP or GGPP posttranslational modifications play critical roles in transducing these signals [3], [18], [19], [20].
Emerging evidence suggests that posttranslational modifications play critical roles in regulating various protein functions.
Selection of the functional arm, the precision of miRNA processing and post-transcriptional modifications play critical roles in the refining and diversifying of mature miRNA sequence and eventual functional activity [ 16, 17].
Polyubiquitination is an essential posttranslational modification that plays critical roles in cellular signaling.
The presence of the PiAN induced onto the surface of the membrane via the plasma modification plays a critical role in improving the wettability and electrolyte retention, the interfacial adhesion between the electrodes and the separator, the cycle performance of the resulting lithium-ion polymer cell assembly.
Ubiquitin-mediated modification plays a critical role in regulating protein stability (Ciechanover and Schwartz, 1994).
Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes.
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