• 대한자기공명의과학회:학술대회논문집
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• 대한자기공명의과학회.한국자기공명학회 2005년도 공동학술대회
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• pp.14-14
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• 2005

• 대한자기공명의과학회:학술대회논문집
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• 대한자기공명의과학회 1999년도 제4차 추계학술대회 초록집
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• pp.38-38
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• 1999

• 대한자기공명의과학회:학술대회논문집
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• 대한자기공명의과학회 1996년도 춘계학술대회 초록집
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• pp.14-15
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• 1996

• Investigative Magnetic Resonance Imaging
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• 제2권1호
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• pp.89-95
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• 1998

목적 : 인($^{31}P$) 자기공명분광법을 사용하여 사립체 근병(mitochondria myopathy) 환자의 대퇴부 근조직의 대사물질의 변화를 정상인과 비교조사하였다. 대상 및 방법 : 사립체 근병환자 10명과 정상인 10명을 대상으로 1.5T MRI/MRS 장비를 사용하여 인($^{31}P$) 자기공명분광법을 적용하였다. 오른쪽 대퇴부위의 근조직에 $4{\;}{\times}{\;}4{\;}{\times}4{\;}cm^{3}$ 의 관심부위 (volume of interest ; VOI)를 선정하여 image selected in vivo spectroscopy (ISIS)를 저용하였다. 인대사불질의 정\ulcorner분석은 Marquart algorithm을 사용하였다. 결과 : 사립체 근병환자의 특징은 정상인과 비교하여 Pe/PCr 대사비율이 상당히 증가하고 (P=0.003), ATP/PCr 대사비율은 상당히 감소하였다(p=0.004). 특히 ATP 중 ${\beta}-ATP/PCr$ 비율의 변화가 가장 심하게 나타났다. 환자군과 정상군의 pH 차이는 통계학적으로 큰 의의는 없었다. 결론 : 인($^{31}P$) 자기 공명분광법은 사립체 근병환자의 대퇴부 근조직의 ATP/PCr 과 Pi/PCr 대사비율을 토대로 유용한 임상 평가 자료를 제공하고, 따라서 근대사물질의 질병을 이해하는데 도움을 줄 것으로 사료된다.

• 한국자기공명학회논문지
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• 제11권1호
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• pp.30-41
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• 2007

The backbone molecular dynamics of the C-terminal part of the mouse Cdt1 protein (tCdt1, residues 420-557) was studied by high field NMR spectroscopy. The Secondary structure of this protein was suggested by analyzing of chemical shift of backbone atoms with programs TALOS and PECAN, together with NOE connectivities from 3D $^{15}N-HSQC-NOESY$ data. Measurement of dynamic parameters $T_1,\;T_2$ and NOE and limited proteolysis experiment provided information for domain organization of tCdt1(420-557). Analysis of the experimental data showed that the C-terminal part of the tCdt1 has well folded domain for residues 455-553. The residues 420-453 including ${\alpha}-helix$ (432-441) are flexible and probably belong to other functional domain in intact full length Cdt1 protein.

• 한국자기공명학회논문지
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• 제19권2호
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• pp.83-87
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• 2015

Syndesmos, which is co-localized with syndecan-4 cytoplasmic domain ($Syn4^{cyto}$) in focal contacts, interacts with various cell adhesion adaptor proteins including $Syn4^{cyto}$ to control cell signaling. Syndesmos consists of 211 amino acids and it exists as a dimer (44kDa) in solution. Recently, we have determined the structure of syndesmos by x-ray crystallography, however, dynamics related to syndecan binding still remain elusive. In this report, we performed NMR experiments to acquire biochemical and structural information of syndesmos. Based on a series of three-dimensional triple resonance experiments on a $^{13}C/^{15}N/^2H$ labeled protein, NMR spectra were obtained with well dispersed and homogeneous NMR data. We present the sequence specific backbone assignment of syndesmos and assigned NMR data with combination structural information can be directly used for the studies on interaction with $Syn4^{cyto}$ and other binding molecules.

• 한국자기공명학회논문지
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• 제24권3호
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• pp.86-90
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• 2020

Iron-sulfur (Fe-S) clusters are one of the most ancient yet essential cofactors mediating various essential biological processes. In prokaryotes, Fe-S clusters are generated via several distinctive biogenesis mechanisms, among which the ISC (Iron-Sulfur Cluster) mechanism plays a house-keeping role to satisfy cellular needs for Fe-S clusters. The Escherichia coli ISC mechanism is maintained by several essential protein factors, whose structural characterization has been of great interest to reveal mechanistic details of the Fe-S cluster biogenesis mechanisms. In particular, nuclear magnetic resonance (NMR) spectroscopic approaches have contributed much to elucidate dynamic features not only in the structural states of the protein components but also in the interaction between them. The present minireview discusses recent advances in elucidating structural features of IscU, the key player in the E. coli ISC mechanism. IscU accommodates exceptional structural flexibility for its versatile activities, for which NMR spectroscopy was particularly successful. We expect that understanding to the structural diversity of IscU provides critical insight to appreciate functional versatility of the Fe-S cluster biogenesis mechanism.

• 한국자기공명학회논문지
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• 제24권3호
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• pp.91-95
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• 2020

Transthyretin (TTR) is an abundant protein in blood plasma and cerebrospinal fluid (CSF), working as a homo-tetrameric complex to transport thyroxine (T₄) and a holo-retinol binding protein. TTR is well-known for its amyloidogenic property; several types of systemic amyloidosis diseases are caused by aggregation of either wild-type TTR or its variants, for which more than 100 mutations were reported to increase the amyloidogenicity of TTR. The rate-limiting step of TTR aggregation is the dissociation of a monomeric subunit from a tetrameric complex. A wide range of biochemical and biophysical techniques have been employed to elucidate the TTR aggregation processes, among which nuclear magnetic resonance (NMR) spectroscopy contributed much to characterize the structural and functional features of TTR during its aggregation processes. The present review focuses on discussing the recent advances of our understanding to the amyloidosis mechanism of TTR and to the structural features of its monomeric aggregation-prone state in solution. We expect that the present review provides novel insights to appreciate the molecular basis of TTR amyloidosis and to develop novel therapeutic strategies to treat diverse TTR-related diseases.

• 한국자기공명학회논문지
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• 제23권1호
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• pp.26-32
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• 2019

${\alpha}B$-crystallin (${\alpha}BC$) is a member of a small heat-shock protein (sHSP) superfamily and plays a predominant role in cellular protein homeostasis network by rescuing misfolded proteins from irreversible aggregation. ${\alpha}BC$ assembles into dynamic and polydisperse high molecular weight complexes containing 12 to 48 monomers; this variable stereochemistry of ${\alpha}BC$ has been linked to quaternary subunit exchange and its chaperone activity. The chaperone activity of ${\alpha}BC$ poses great potential as therapeutic agents for various neurodegenerative diseases. In this mini-review, we briefly outline the recent advancement in structural characterization of ${\alpha}BCs$ and its potential role to inhibit protein misfolding and aggregation in various human diseases. In particular, nuclear magnetic resonance (NMR) spectroscopy and its complimentary techniques have contributed much to elucidate highly-dynamic nature of ${\alpha}BCs$, among which notable advancements are discussed in detail. We highlight the importance of resolving the structural details of various ${\alpha}BC$ oligomers, their quaternary dynamics, and structural heterogeneity.

• 한국자기공명학회논문지
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• 제28권1호
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• pp.1-5
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• 2024

IscU, the iron-sulfur (Fe-S) cluster scaffold protein, is an essential protein for biogenesis of Fe-S clusters. Previous studies showed that IscU manifests a metamorphic structural feature; at least two structural states, namely the structured state (S-state) and the disordered state (D-state), interconverting in a physiological condition, was observed. Moreover, subsequent studies demonstrated that the metamorphic flexibility of IscU is important for its Fe-S cluster assembly activity as well as for an efficient interaction with various partner proteins. Although solution nuclear magnetic resonance (NMR) spectroscopy has been a useful tool to investigate this protein, the detailed molecular mechanism that sustains the structural heterogeneity of IscU is still unclear. To tackle this issue, we applied a high-pressure NMR (HP-NMR) technique to the IscU variant, IscU(I8K), which shows an increased population of the S-state. We found that the equilibrium between the S- and D-state was significantly perturbed by pressure application, and the specific regions of IscU exhibited more sensitivity to pressure than the other regions. Our results provide novel insights to appreciate the dynamic behaviors of IscU and the related versatile functionality.