• Proceedings of the Korean Society of Life Science Conference
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• 2007.10a
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• pp.118.1-118.1
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• 2007

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• Proceedings of the PSK Conference
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• 2002.10a
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• pp.330.1-330.1
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• 2002

Arginine methylation is a common post-translation protein modification in eukaryotic cells. Protein-arginine N-methyltransferase transfer methyl groups from S-adenosyl-L-methionine to the guanidino group of arginine residues. However. The significant of this modification has been questionable. because it occurs rarely and is present at very low abundance. Recently, the discovery of two protein arginine methyltransferase, PRMT1 and CARM1, as cofactors required for responses to muclear Hormone receptors provided an indicationthat arginine methylationhave an important role in transcriptional regulation. (omitted)

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2005.09a
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• pp.331-336
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• 2005

Post translational modifications (PTMs) discovery is an important problem in proteomic. In the past, people discover PTMs by Tandem Mass Spectrometer based on ‘bottom-up’ strategy. However, such strategy suffers from the problem of failing to discover all PTMs. Recently, due to the improvement in proteomic technology, Taylor et al. proposed a database software to discover PTMs with ‘topdown’ strategy by FTMS, which avoids the disadvantages of ‘bottom-up’ approach. However, their proposed algorithm runs in exponential time, requires a database of proteins, and needs prior knowledge about PTM sites. In this paper, a new algorithm is proposed which can work without a protein database and can identify modifications in polynomial time. Besides, no prior knowledge about PTM sites is needed.

• Mass Spectrometry Letters
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• v.8 no.4
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• pp.69-78
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• 2017

Glycosylation, which is one of the most common post-translation modification (PTMs) of proteins, plays a variety of crucial roles in many cellular events and biotherapeutics. Recent advances have led to the development of various analytical methods employing a mass spectrometry for glycomic and glycoproteomic study. However, site-specific glycosylation analysis is still a relatively new area with high potential for technologies and method development. This review will cover current MS-based workflows and technologies for site-specific mapping of glycosylation ranging from glycopeptide preparation to MS analysis. Bioinformatic tools for comprehensive analysis of glycoprotein with high-throughput manner will be also included.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.5
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• pp.609-624
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• 2013

The objective of this study was to get a comprehensive understanding of how genes in chicken shell gland modulate eggshell strength at the early stage of active calcification. Four 32-week old of purebred Xianju hens with consistent high or low shell breakage strength were grouped into two pairs. Using Affymetrix Chicken Array, a whole-transcriptome analysis was performed on hen's shell gland at 9 h post oviposition. Gene ontology enrichment analysis for differentially expressed (DE) transcripts was performed using the web-based GOEAST, and the validation of DE-transcripts was tested by qRT-PCR. 1,195 DE-transcripts, corresponding to 941 unique genes were identified in hens with strong eggshell compared to weak shell hens. According to gene ontology annotations, there are 77 DE-transcripts encoding ion transporters and secreted extracellular matrix proteins, and at least 26 DE-transcripts related to carbohydrate metabolism or post-translation glycosylation modification; furthermore, there are 88 signaling DE-transcripts. GO term enrichment analysis suggests that some DE-transcripts mediate reproductive hormones or neurotransmitters to affect eggshell quality through a complex suite of biophysical processes. These results reveal some candidate genes involved with eggshell strength at the early stage of active calcification which may facilitate our understanding of regulating mechanisms of eggshell quality.

• Applied Biological Chemistry
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• v.32 no.3
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• pp.222-231
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• 1989

Three classes of proteinase inhibitors are known in soybean; the Kunitz trypsin inhibitor (SKTI), the Bowman-Birk proteinase inhibitor and its isoinhibitors. To study the molecular structure and expression characteristics of the SKTI, antibody was obtained by immunizing rabbit with the SKTI purified from soybean by preparative electrophoresis. Anti-SKTI antibody was not only specific for mature SKTI in soybean seed but also recognized the precursor which was synthesized in vitro. Translation in vitro was carried out in wheat germ extract with polyadenylated mRNA isolated from developing soybean seeds. One of the seed specific translation products, MW 24K, was identified to be the precursor for the SKTI by immunoprecipitation with anti-SKTI antibody. Mature SKTI of MW 20K, however, was not detected in the translates in vitro. These results suggest that the precursor polypeptide is synthesized from the mRNA and is cleaved to yield mature SKTI in soybean seed. The SKTI gene was expressed with the maturation of soybean seed in a tissue-specific and development stage-specific manner.

• BMB Reports
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• v.48 no.1
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• pp.25-29
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• 2015

Ubiquitination is a post translational modification which mostly links with proteasome dependent protein degradation. This process has been known to play pivotal roles in the number of biological events including apoptosis, cell signaling, transcription and translation. Although the process of ubiquitination has been studied extensively, the mechanism of polyubiquitination by multi protein E3 ubiquitin ligase, SCF complex remains elusive. In the present study, we identified UbcH5a as a novel stimulating factor for poly-ubiquitination catalyzed by $SCF^{hFBH1}$ using biochemical fractionations and MALDI-TOF. Moreover, we showed that recombinant UbcH5a and Cdc34 synergistically stimulate $SCF^{hFBH1}$ catalyzed polyubiquitination in vitro. These data may provide an important cue to understand the mechanism how the SCF complex efficiently polyubiquitinates target substrates.

• BMB Reports
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• v.53 no.11
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• pp.551-564
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• 2020

Proper development of the nervous system is critical for its function, and deficits in neural development have been implicated in many brain disorders. A precise and predictable developmental schedule requires highly coordinated gene expression programs that orchestrate the dynamics of the developing brain. Especially, recent discoveries have been showing that various mRNA chemical modifications can affect RNA metabolism including decay, transport, splicing, and translation in cell type- and tissue-specific manner, leading to the emergence of the field of epitranscriptomics. Moreover, accumulating evidences showed that certain types of RNA modifications are predominantly found in the developing brain and their dysregulation disrupts not only the developmental processes, but also neuronal activities, suggesting that epitranscriptomic mechanisms play critical post-transcriptional regulatory roles in development of the brain and etiology of brain disorders. Here, we review recent advances in our understanding of molecular regulation on transcriptome plasticity by RNA modifications in neurodevelopment and how alterations in these RNA regulatory programs lead to human brain disorders.

• Preventive Nutrition and Food Science
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• v.5 no.4
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• pp.184-188
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• 2000

HMG-CoA reductase is th rate-limiting enzyme of cholesterol biosynthesis. As intracellular levels of cholesterol should be regulated elaborately in response to external stimuli an internal needs, the expression of the HMG-CoA reductase gene is regulated intricately at several different levels from transcription to post-translational modification. In this study, we investigated the regulatory mechanism of HMG-CoA reductase gene expression at the post-transcriptional/pre-translational levels in a baby hamster kidney cell line, C100. when 25-hydroxycholesterol was added to cells cultured in medium containing 5% delipidized fetal bovine serum and 25$\mu$M lovastatin, the levels of HMG-CoA reductase mRNA decreased rapidly, which seemed to be due to the increased degradation of reductase mRNA. These suppressive effects of 25-hydroxycholesterol on MG-CoA reductase mRNA levels were blocked by a translation inhibitor, cycloheximide. Similarly, actinomycin D and 5,6-dichloro-1-$\beta$-D-ribofuranosylbenzimidazole, transcription inhibitors, blocked the 25-hydroxycholesterol-mediated degradation of HMG-CoA reductase mRNA. These results indicate that new protein/RNA synthesis is required for the degradation of HMG-CoA reductase mRNA. In addition, data from the transfection experiments shows that cis-acting determinants, regulating the stability of reductase mRNA, were scattered in the sequence corresponding to 1766-4313 based on the sequence of Syrian hamster HMG-CoA reductase cDNA. Our data suggests that sterol-mediated destabilization of reductase mRNA might be one of the important regulatory mechanism of HMG-CoA reductase gene expression.

• Korean Journal of Plant Tissue Culture
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• v.28 no.5
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• pp.283-287
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• 2001

Differential display based on PCR was employed to identify genes expressed during tuber-developing stage of potato (Solanum tuberosum L. cv. Irish Cobbler). An eukaryotic initiation factor 5A (eIF-5A) clone isolated from a cDNA library constructed with developing micro-tuber using a probe of PCR fragment. We isolated three positive clones and ore of them contained open reading frame. This clone revealed high sequence similarity to tomato eIF 5A cDNA. At the DNA level, there is 94.8% identity with the tomato eIF-5A4, whereas at the protein level there is a high identity with 97.5%. The potato eIF 5A clone is 716 bp in length and contains a single open reading frame from 57 to 539 bp, a 56 bp 5'-untranslated region and a 177 bp 3'-untranslated region. The deduced protein composed of 160 amino acid residues, with a predicted molecular mass of 17.4 kD and an estimated pl of 5.5. The sequence of 12 (STSKTGKHGHAK) amino acids among eIF-5A proteins is perfectly conserved from yeast to human. That sequence in potato eIF-5A protein is also conserved at position 46 to 57 amino acid. This region embeds the post-translational modification site of the lysine residue (at the seventh K) to hypusine that is crucial to eIF-5A activity. The northern blot analysis of eIF5A has shown abundant expression, mainly in flower organs (stamen, ovary, petal, sepal), fruit and stolen.