• 대한수학회지
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• 제54권1호
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• pp.35-57
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• 2017

In this paper, we study the natural star-operation defined by the set of associated primes of principal ideals of an integral domain, which is called the g-operation. We are mainly concerned with the ideal-theoretic properties of this star-operation. In particular, we investigate DG-domains (i.e., integral domains in which each ideal is a g-ideal), which form a proper subclass of the DW-domains. In order to provide some original examples, we examine the transfer of the DG-property to pullbacks. As an application of the g-operation, it is shown that w-divisorial Mori domains can be seen as a Gorenstein analogue of Krull domains.

• ETRI Journal
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• 제44권3호
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• pp.438-449
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• 2022

This study proposes a dependency grammar-based self-attention multilayered bidirectional long short-term memory (DG-M-Bi-LSTM) model for subject-predicate-object (SPO) tuple recognition from natural language (NL) sentences. To add recent knowledge to the knowledge base autonomously, it is essential to extract knowledge from numerous NL data. Therefore, this study proposes a high-accuracy SPO tuple recognition model that requires a small amount of learning data to extract knowledge from NL sentences. The accuracy of SPO tuple recognition using DG-M-Bi-LSTM is compared with that using NL-based self-attention multilayered bidirectional LSTM, DG-based bidirectional encoder representations from transformers (BERT), and NL-based BERT to evaluate its effectiveness. The DG-M-Bi-LSTM model achieves the best results in terms of recognition accuracy for extracting SPO tuples from NL sentences even if it has fewer deep neural network (DNN) parameters than BERT. In particular, its accuracy is better than that of BERT when the learning data are limited. Additionally, its pretrained DNN parameters can be applied to other domains because it learns the structural relations in NL sentences.

• Journal of Microbiology and Biotechnology
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• 제21권12호
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• pp.1299-1305
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• 2011

An important modification of thrombolytic agents is resistance to plasminogen activator inhibitor-1 (PAI-1). In previous studies, a new truncated PAI-1-resistant variant was developed based on deletion of the first three domains in t-PA and the substitution of KHRR 128-131 amino acids with AAAA in the truncated t-PA. The novel variant expressed in a static culture system of Chinese Hamster Ovary (CHO) DG44 cells exhibited a higher resistance to PAI-1 when compared with the full-length commercial drug; Actylase. In the present study, the truncated-mutant protein was expressed in CHO DG44 cells in 50 ml orbital shaking bioreactors. The final yield of the truncated-mutant in the culture was 752 IU/ml, representing a 63% increase compared with the static culture system. Therefore, these results suggest that using the combined features of a transient and stable expression system is feasible for the production of novel recombinant proteins in the quantities needed for preclinical studies.

• Journal of Microbiology and Biotechnology
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• 제24권11호
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• pp.1525-1535
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• 2014

The xynC gene, which encodes high molecular weight xylanase from Paenibacillus sp. DG-22, was cloned and expressed in Escherichia coli, and its nucleotide sequence was determined. The xynC gene comprised a 4,419bp open reading frame encoding 1,472 amino acid residues, including a 27 amino acid signal sequence. Sequence analysis indicated that XynC is a multidomain enzyme composed of two family 4_9 carbohydrate-binding modules (CBMs), a catalytic domain of family 10 glycosyl hydrolases, a family 9 CBM, and three S-layer homologous domains. Recombinant XynC was purified to homogeneity by heat treatment, followed by Avicel affinity chromatography. SDS-PAGE and zymogram analysis of the purified enzyme identified three active truncated xylanase species. Protein sequencing of these truncated proteins showed that all had identical N-terminal sequences. In the protein characterization, recombinant XynC exhibited optimal activity at pH 6.5 and $65^{\circ}C$ and remained stable at neutral to alkaline pH (pH 6.0-10.0). The xylanase activity of recombinant XynC was strongly inhibited by 1 mM $Cu^{2+}$ and $Hg^{2+}$, whereas it was noticeably enhanced by 10 mM dithiothreitol. The enzyme exhibited strong activity towards xylans, including beechwood xylan and arabinoxylan, whereas it showed no cellulase activity. The hydrolyzed product patterns of birchwood xylan and xylooligosaccharides by thin-layer chromatography confirmed XynC as an endoxylanase.

• 생명과학회지
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• 제27권12호
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• pp.1410-1414
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• 2017

대장균 트립토판 생성효소는 ${\alpha}_2{\beta}_2$ 복합체로 구성되며, 트립토판 생합성에서 최종 2 단계의 반응에 관여한다. 두 개의 소단위체는 분자 터널로 연결되어 있어, 기질 채널링이 일어난다. 활성 부위간 상호 조절하는 정교한 조절 기작에는 ${\alpha}$-루프 L6(${\alpha}L6$), ${\alpha}L2$, ${\alpha}L3$이 관여한다. 본 연구에서는 이 자리의 잔기치환체를 써서 소단위체에 특이적으로 결합하는 리간드의 영향을 조사하여 소단위체간 상호 조절기작에 따른 구조 변화를 살펴보았다. ${\alpha}TS$의 활성부위에 결합하는 D,L-${\alpha}$-glycerophosphate(GP)는 모든 잔기치환체를 야생형 수준으로 회복시켰다. ${\beta}TS$의 기질인 L-Ser는 다양한 효과를 나타낸다. 야생형과 NS104에서는 속도가 감소한 반면, GD51과 PH53에서는 거의 영향이 없었고, PT53와 DG56은 증가하였다. 이는 반응 중간 화학종의 분포의 변화와 연관될 가능성을 제시한다. GP와 L-Ser를 동시에 처리했을 때는 특이하게도 PH53는 가장 안정한 잔기치환체였다. 이는 Pro53가 소단위체간의 조절기작에서 중요한 역할을 하는 것을 시사한다.

• Journal of Microbiology and Biotechnology
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• 제9권5호
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• pp.582-588
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• 1999

A Brevibacterium lactofermentum gene coding for a glucose-specific permease of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was cloned, by complementing an Escherichia coli mutation affecting a ptsG gene with the B. lactofermentum genomic library, and completely sequenced. The gene was identified as a ptsG, which enables an E. coli transformant to transport non-metabolizable glucose analogue 2-deoxyglucose (2DG). The ptsG gene of B. lactofermentum consists of an open reading frame of 2,025 nucleotides encoding a polypeptide of 674 amino acid residues and a TAA stop codon. The 3' flanking region contains two stem-loop structures which may be involved in transcriptional termination. The deduced amino acid sequence of the B. lactofermentum enzyme $II^{GIe}$ specific to glucose ($EII^{GIe}$) has a high homology with the Corynebacterium glutamicum enzyme $II^{Man}$ specific to glucose and mannose ($EII^{Man}$), and the Brevibacterium ammoniagenes enzyme $II^{GIc}$ specific to glucose ($EII^{GIc}$). The 171-amino-acid C-terminal sequence of the $EII^{Glc}$ is also similar to the Escherichia coli enzyme $IIA^{GIc}$ specific to glucose ($IIA^{GIc}$). It is interesting that the arrangement of the structural domains, IIBCA, of the B. lactofermentum $EII^{GIc}$ protein is identical to that of EIIs specific to sucrose or $\beta$-glucoside. Several in vivo complementation studies indicated that the B. lactofermentum $EII^{Glc}$ protein could replace both $EII^{ Glc}$ and $EIIA^{Glc}$ in an E. coli ptsG mutant or crr mutant, respectively.