• Bulletin of the Korean Mathematical Society
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• v.59 no.2
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• pp.419-429
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• 2022

An integral domain R is an RTP domain (or has the radical trace property) (resp. an LTP domain) if I(R : I) is a radical ideal for each nonzero noninvertible ideal I (resp. I(R : I)R_P = PR_P for each minimal prime P of I(R : I)). Clearly each RTP domain is an LTP domain, but whether the two are equivalent is open except in certain special cases. In this paper, we study the descent of these notions from particular overrings of R to R itself.

• Molecules and Cells
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• v.43 no.12
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• pp.1023-1034
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• 2020

Complement fragment iC3b serves as a major opsonin for facilitating phagocytosis via its interaction with complement receptors CR3 and CR4, also known by their leukocyte integrin family names, αMβ2 and αXβ2, respectively. Although there is general agreement that iC3b binds to the αM and αX I-domains of the respective β2-integrins, much less is known regarding the regions of iC3b contributing to the αX I-domain binding. In this study, using recombinant αX I-domain, as well as recombinant fragments of iC3b as candidate binding partners, we have identified two distinct binding moieties of iC3b for the αX I-domain. They are the C3 convertase-generated N-terminal segment of the C3b α'-chain (α'NT) and the factor I cleavage-generated N-terminal segment in the CUBf region of α-chain. Additionally, we have found that the CUBf segment is a novel binding moiety of iC3b for the αM I-domain. The CUBf segment shows about a 2-fold higher binding activity than the α'NT for αX I-domain. We also have shown the involvement of crucial acidic residues on the iC3b side of the interface and basic residues on the I-domain side.

• Molecules and Cells
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• v.40 no.5
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• pp.355-362
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• 2017

The ${\beta}2$ integrins are cell surface transmembrane proteins regulating leukocyte functions, such as adhesion and migration. Two members of ${\beta}2$ integrin, ${\alpha}M{\beta}2$ and ${\alpha}X{\beta}2$, share the leukocyte distribution profile and integrin ${\alpha}X{\beta}2$ is involved in antigen presentation in dendritic cells and transendothelial migration of monocytes and macrophages to atherosclerotic lesions. ${\underline{R}}eceptor$ for ${\underline{a}}dvanced$ ${\underline{g}}lycation$ ${\underline{e}}nd$ ${\underline{p}}roducts$ (RAGE), a member of cell adhesion molecules, plays an important role in chronic inflammation and atherosclerosis. Although RAGE and ${\alpha}X{\beta}2$ play an important role in inflammatory response and the pathogenesis of atherosclerosis, the nature of their interaction and structure involved in the binding remain poorly defined. In this study, using I-domain as a ligand binding motif of ${\alpha}X{\beta}2$, we characterize the binding nature and the interacting moieties of ${\alpha}X$ I-domain and RAGE. Their binding requires divalent cations ($Mg^{2+}$ and $Mn^{2+}$) and shows an affinity on the sub-micro molar level: the dissociation constant of ${\alpha}X$ I-domains binding to RAGE being $0.49{\mu}M$. Furthermore, the ${\alpha}X$ I-domains recognize the V-domain, but not the C1 and C2-domains of RAGE. The acidic amino acid substitutions on the ligand binding site of ${\alpha}X$ I-domain significantly reduce the I-domain binding activity to soluble RAGE and the alanine substitutions of basic amino acids on the flat surface of the V-domain prevent the V-domain binding to ${\alpha}X$ I-domain. In conclusion, the main mechanism of ${\alpha}X$ I-domain binding to RAGE is a charge interaction, in which the acidic moieties of ${\alpha}X$ I-domains, including E244, and D249, recognize the basic residues on the RAGE V-domain encompassing K39, K43, K44, R104, and K107.

• Proceedings of the KSPS conference
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• 1996.02a
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• pp.41-46
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• 1996

Within the framework of prosodic phonology (or the theory of phonology-syntax connection), the rhythm unit is not regarded as a domain of phonological rules. But I argue in this paper that the rhythm unit functions as a domain of phonological rules in Korean. I discuss five phonological rules whose domain of application is the rhythm unit.

• Communications of the Korean Mathematical Society
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• v.39 no.1
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• pp.71-77
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• 2024

Let A be a commutative integral domain with identity element and S a multiplicatively closed subset of A. In this paper, we introduce the concept of S-valuation domains as follows. The ring A is said to be an S-valuation domain if for every two ideals I and J of A, there exists s ∈ S such that either sI ⊆ J or sJ ⊆ I. We investigate some basic properties of S-valuation domains. Many examples and counterexamples are provided.

• Journal of Life Science
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• v.17 no.9 s.89
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• pp.1303-1307
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• 2007

A tumor suppressor, merlin is a member of ERM family proteins. It consists of N-terminal FERM domain, ${\alpha}-helical$ region, and C-terminal domain. Alternative splicing of merlin's mRNA generates two isotypes of merlin. Isotype I, which has exon17 at the C-terminus instead of exon16 in isotype II, is known to have tumor suppressor activity. Like other ERM proteins, the C-terminal domain of merlin isotype I interacts to its FERM domain. That of isotype II, however, was reported not to bind FERM domain despite the large common part of C-terminal domain, which possibly binds FERM domain. Here, we show the binding of FERM domain to both C-terminal domains of merlin's two isotypes by isothermal titration calorimetry. These results support that merlin isotype II also can form a closed conformation or a multimer by intramolecular or intermolecular interactions using their FERM domain and C-terminal domain.

• Bulletin of the Korean Mathematical Society
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• v.61 no.3
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• pp.735-744
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• 2024

In this note, we shed new light on Krull domains from the point view of Gorenstein homological algebra. By using the so-called w-operation, we show that an integral domain R is Krull if and only if for any nonzero proper w-ideal I, the Gorenstein global dimension of the w-factor ring (R/I)_w is zero. Further, we obtain that an integral domain R is Dedekind if and only if for any nonzero proper ideal I, the Gorenstein global dimension of the factor ring R/I is zero.

• Journal of Microbiology and Biotechnology
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• v.25 no.2
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• pp.247-254
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• 2015

In this presentation, I describe the expression and purification of the recombinant liver X receptor β-ligand binding domain proteins in E. coli using a commercially available double cistronic vector, pACYCDuet-1, to express the receptor heterodimer in a single cell as the soluble form. I describe here the expression and characterization of a biologically active heterodimer composed of the liver X receptor β-ligand binding domain and retinoid X receptor α-ligand binding domain. Although many of these proteins were previously seen to be produced in E. coli as insoluble aggregates or "inclusion bodies", I show here that as a form of heterodimer they can be made in soluble forms that are biologically active. This suggests that co-expression of the liver X receptor β-ligand binding domain with its binding partner improves the solubility of the complex and probably assists in their correct folding, thereby functioning as a type of molecular chaperone.

• BMB Reports
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• v.51 no.7
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• pp.338-343
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• 2018

Transcription termination factor-1 (TTF-I) is an RNA polymerase 1-mediated transcription terminator and consisting of a C-terminal DNA-binding domain, central domain, and N-terminal regulatory domain. This protein binds to a so-called 'Sal box' composed of an 11-base pair motif. The interaction of TTF-I with the 'Sal box' is important for many cellular events, including efficient termination of RNA polymerase-1 activity involved in pre-rRNA synthesis and formation of a chromatin loop. To further understand the role of TTF-I in human immunodeficiency virus (HIV)-I virus production, we generated various TTF-I mutant forms. Through a series of studies of the over-expression of TTF-I and its derivatives along with co-transfection with either proviral DNA or HIV-I long terminal repeat (LTR)-driven reporter vectors, we determined that wild-type TTF-I downregulates HIV-I LTR activity and virus production, while the TTF-I Myb-like domain alone upregulated virus production, suggesting that wild-type TTF-I inhibits virus production and trans-activation of the LTR sequence; the Myb-like domain of TTF-I increased virus production and trans-activated LTR activity.

• MALSORI
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• no.19_20
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• pp.58-87
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• 1990

According to Government Phonology, at 1 phonological positions save the domain's head must be licensed in order to appear in the syllable structure. A non-nuclear head is licensed by the following nucleus, and the nuclei with phonetic content are licensed through government by the nuclear head of the domain at the level of the nuclear projection. Therefore, in the theory of Government Phonology it is claimed that words always end with a nucleus. With regard to the licensing of empty nuclei, Kaye(1990a) proposes the 'Empty Category Principle' and its sub-theory of 'Projection Government'. Government Phonology claims that a nucleus which dominates a vowel that regularly undergoes elision in certain contexts is underlyingly empty. This underlying empty nucleus is not manifested phonetically when it is properly governed by an unlicensed(i, e, a nucleus filled with a full vowel). It is when proper government fails to apply, that the empty nucleus is phonetically Interpreted. The purpose of this paper is to present a principled account of the process of $[i]{\Leftrightarrow}{\emptyset}$ alternation in Korean. Following Kaye's proposal, we assume that [i] of Korean is underlyingly empty. This position is pronounced as [i] if it is unlicensed, and is not phonetically realized if is licensed. Empty nuclei ape devided into two categories: domain-internal and domain-final. Firstly, we consider the question why Korean has little word ending with [i]. As for this, ECP states that domain-final empty nuclei are not pronounced if the language licenses domain-final empty nuclei. Whether a final empty nucleus may occur in the structure is parametric variation. This property is seen from the fact that words may appear to end in consonants in this language. Since Korean abounds with words ending in a consonant, it licenses domain-final empty nuclei. Therefore, it is quite natural that Korean has little word ending with [i]. Secondly, word-internal empty nuclei of Korean respect proper government and inter-onset government. That is, an empty nucleus in word-internal position will be pronounced with the vowel [i] if either proper government or inter-onset government fail to apply. Inter-onset government refers to the government established between two onsets across an empty nucleus. Thirdly, we consider words ending with [i], which seems to be exceptional to the final licensing. Host of them are. either mono-syllabic verbs(for instance, [s'i-] 'to write') or derived adjectives ending with [p'i] (for instance, [kip'i-] 'be happy'). As for the former, the 'inaccessibility for proper government' is applied because the empty nucleus appears in the first syllable. In latter case, domain-final empty nuclei are pronounced as [i] because of government-licensing. That is, final empty nucleus is pronounced to license the preceding onset dominating negatively charmed segments which empty nucleus of Korean cannot license.