칼슘과 아연으로 치환된 Y0.8 Pr0.₂ Ba₂ Cu₃ O7_δ 의 전기 및 자기적 성질에 관한 연구

김성재,전인,박영민,강재필,노태호,박현진,최숙자,송승기 명지대학교 자연과학연구소 1996 자연과학논문집 Vol.14 No.-

전이온도가 72K인 고온초전도체 Y?P?B?Cu?O?에서 초전도성을 감소시키는 Pr원소자리에 Ca과 Zn를 적당히 치환시켜 자기적 성질을 연구하였다. 초전도 전이온도(Tc)는 Ca이 치환된 시료의 경우 80~85k의 범위에서 측정되었으며, Zn가 치환된 경우에는 35~49K의 값을 보였다. 비저항의 온도 변화로부터 결정된 전기적 전이온도는 온도에 대한 자기모우먼트으 변화에서 구한 자기적 전이온도와 비슷한 값을 보였다. 자기이력곡선으로부터 Bean의 모델을 이용하여 Hcl(저임계자기장), Hc?(고임계자기장), 반자성정도, 임계전류밀도를 측정하였다. 이러한 성질들은 시료 내에 Ca의 치환량이 많아질수록 증가하였으며, Zn가 많아질수록 급격히 감소하였다. 특히 임계전류밀도는 x=0.0인 시료는 1.60x10?A/㎠이었으며 Ca이 치환된 시료는 1.30~1.98x10? A/㎠, Zn가 첨가된 시료는 3.5x10?~1.3x10?A/㎠의 값으로 계산되었다. 이것은 시료 내에서 Ca은 초전도성을 증가시키고, Zn는 초전도성을 감소시키는 것을 의미한다. We have studied magnetic properties as a appropriate substitute of Ca and Zn element for Prelement which reduces superconducting properties in the high-temperature superconductor Y?Pr?Ba?Cu?O? of transition temperature 72K. When Ca is put into, the critical temperature(Tc)showed the value of measurement at the range of 80~85K while for Zn the Tc had the range of 35~49K. The electric critical temperature determined by the temperature dependence of resistivity had a similar data to the magnetic field), Hc?(high critical magnetic field), diamagnetic ratio and critical current density have observed by Bean's model from the magnetic hysterisis curve. These properties were increased with adding Ca and abruptly decreased with adding Zn in the samples. Especially, the critical current density of x=0.0 sample was calculated at 1.60x10?A/㎠ and those of the other Ca-added samples at the range of 1.30~1.98xA/㎠and those of Zn-added samples at the range of 3.50x10?~1.30x10?A/㎠. These mean that Ca increases supercondecting properties in the sample and Zn element decreases them.

학생정신건강검진 시범운영사업에 따른 추진방안

김현정,김윤영,이혜숙,현미나,남동현,김상원,안동현 韓國學校保健學會 2009 韓國學校保健學會誌 Vol.22 No.1

Purpose: The purpose of the study was to·find the strategies of mental health screening in school. Based on the literature review, we discuss the importance of screening students in schools for mental health problems. Methods: Data from the 2008 Korean Mental Health Screening in Schools(2008-KMHSS) are used to estimate the outline of this screening. We administered the questionnaire for satisfaction of 2008-KMHSS for students(N=1,280), parents(N=2,672), school nurses(N=75), teachers(N=685), district personnels(N=6), and mental health center staffs(N=37). Also we interviewed a part of them by telephone and e-mail. And we reviewed the tools and methods for screening students for emotional/behavioral problems. Results: Mental health screening in schools is a very important, yet worrisome, agenda that is in its very early stages. From the 2008 Korean Mental Health Screening in Schools, 9,588 students(12.9%) needed more evaluation in the first stage. Of these, 6,910(72.1%) completed the second stage screening. In this sample, 1,975(28.6%) utilized the mental health services in school or community. 38.3% of students and 43.7% of their parents notified the2008-KMHSS. But only 12.1% of students and 10.9% of their parents dissatisfied with the screening. 9.9% of teachers and 22.7% of school nurses dissatisfied with the screening. Among them the school nurses were mostly dissatisfied, and they complained work burden from KMHSS. Mental health center staffs complained similar issues. The Children's Problem-behavior Screening Questionnaire(CPSQ) and Adolescents' Mental-health & Problem-behavior Screening Questionnaire(AMPQ) were compatible to screen students in schools for mental health problems in first stage. Conclusion: Mental health screening in schools needs careful planning and implementation. For successful mental health screening in schools, several elements need to be considered: careful planning, collaboration, staff training, and integrative mental health programs and services in community or schools.

Crystal structure of Tpa1 from <i>Saccharomyces cerevisiae</i> , a component of the messenger ribonucleoprotein complex

Kim, Hyoun Sook,Kim, Hye Lee,Kim, Kyoung Hoon,Kim, Do Jin,Lee, Sang Jae,Yoon, Ji Young,Yoon, Hye Jin,Lee, Hyang Yeon,Park, Seung Bum,Kim, Soon-Jong,Lee, Jae Young,Suh, Se Won Oxford University Press 2010 Nucleic acids research Vol.38 No.6

<P>Tpa1 (for termination and polyadenylation) from <I>Saccharomyces cerevisiae</I> is a component of a messenger ribonucleoprotein (mRNP) complex at the 3′ untranslated region of mRNAs. It comprises an N-terminal Fe(II)- and 2-oxoglutarate (2OG) dependent dioxygenase domain and a C-terminal domain. The N-terminal dioxygenase domain of a homologous Ofd1 protein from <I>Schizosaccharomyces pombe</I> was proposed to serve as an oxygen sensor that regulates the activity of the C-terminal degradation domain. Members of the Tpa1 family are also present in higher eukaryotes including humans. Here we report the crystal structure of <I>S. cerevisiae</I> Tpa1 as a representative member of the Tpa1 family. Structures have been determined as a binary complex with Fe(III) and as a ternary complex with Fe(III) and 2OG. The structures reveal that both domains of Tpa1 have the double-stranded β-helix fold and are similar to prolyl 4-hydroxylases. However, the binding of Fe(III) and 2OG is observed in the N-terminal domain only. We also show that Tpa1 binds to poly(rA), suggesting its direct interaction with mRNA in the mRNP complex. The structural and functional data reported in this study support a role of the Tpa1 family as a hydroxylase in the mRNP complex and as an oxygen sensor.</P>

Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex

Kim, Kyung Rok,Park, Sang Ho,Kim, Hyoun Sook,Rhee, Kyung Hee,Kim, Byung-Gyu,Kim, Dae Gyu,Park, Mi Seul,Kim, Hyun-Jung,Kim, Sunghoon,Han, Byung Woo Blackwell Publishing Ltd 2013 Proteins Vol.81 No.10

<P>Human cytosolic aspartyl-tRNA synthetase (DRS) catalyzes the attachment of the amino acid aspartic acid to its cognate tRNA and it is a component of the multi-tRNA synthetase complex (MSC) which has been known to be involved in unexpected signaling pathways. Here, we report the crystal structure of DRS at a resolution of 2.25 Å. DRS is a homodimer with a dimer interface of 3750.5 Å<SUP>2</SUP> which comprises 16.6% of the monomeric surface area. Our structure reveals the C-terminal end of the N-helix which is considered as a unique addition in DRS, and its conformation further supports the switching model of the N-helix for the transfer of tRNA<SUP>Asp</SUP> to elongation factor 1α. From our analyses of the crystal structure and post-translational modification of DRS, we suggest that the phosphorylation of Ser146 provokes the separation of DRS from the MSC and provides the binding site for an interaction partner with unforeseen functions.</P>

Structural basis for the inhibition of <i>Mycobacterium tuberculosis</i> <small>L</small> , <small>D</small> -transpeptidase by meropenem, a drug effective against extensively drug-resistant strains

Kim, Hyoun Sook,Kim, Jieun,Im, Ha Na,Yoon, Ji Young,An, Doo Ri,Yoon, Hye Jin,Kim, Jin Young,Min, Hye Kyeoung,Kim, Soon-Jong,Lee, Jae Young,Han, Byung Woo,Suh, Se Won International Union of Crystallography 2013 Acta crystallographica. Section D, Biological crys Vol.69 No.3

<▼1><P>The crystal structure of <I>M. tuberculosis</I><SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidase (Ldt<SUB>Mt2</SUB>; Rv2518c) has been determined in both ligand-free and meropenem-bound forms. The detailed view of the interactions between meropenem and Ldt<SUB>Mt2</SUB> will be useful in structure-guided discovery of new antituberculosis drugs.</P></▼1><▼2><P>Difficulty in the treatment of tuberculosis and growing drug resistance in <I>Mycobacterium tuberculosis</I> (<I>Mtb</I>) are a global health issue. Carbapenems inactivate <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidases; meropenem, when administered with clavulanate, showed <I>in vivo</I> activity against extensively drug-resistant <I>Mtb</I> strains. Ldt<SUB>Mt2</SUB> (Rv2518c), one of two functional <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidases in <I>Mtb</I>, is predominantly expressed over Ldt<SUB>Mt1</SUB> (Rv0116c). Here, the crystal structure of N-terminally truncated Ldt<SUB>Mt2</SUB> (residues Leu131–Ala408) is reported in both ligand-free and meropenem-bound forms. The structure of meropenem-inhibited Ldt<SUB>Mt2</SUB> provides a detailed structural view of the interactions between a carbapenem drug and <I>Mtb</I><SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidase. The structures revealed that the catalytic <SMALL>L</SMALL>,<SMALL>D</SMALL>-­transpeptidase domain of Ldt<SUB>Mt2</SUB> is preceded by a bacterial immunogloblin-like Big_5 domain and is followed by an extended C-terminal tail that interacts with both domains. Furthermore, it is shown using mass analyses that meropenem acts as a suicide inhibitor of Ldt<SUB>Mt2</SUB>. Upon acylation of the catalytic Cys354 by meropenem, the ‘active-site lid’ undergoes a large conformational change to partially cover the active site so that the bound meropenem is accessible to the bulk solvent <I>via</I> three narrow paths. This work will facilitate structure-guided discovery of <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidase inhibitors as novel antituberculosis drugs against drug-resistant <I>Mtb</I>.</P></▼2>

The Cell Shape-determining Csd6 Protein from <i>Helicobacter pylori</i> Constitutes a New Family of <small>L,D</small> -Carboxypeptidase

Kim, Hyoun Sook,Im, Ha Na,An, Doo Ri,Yoon, Ji Young,Jang, Jun Young,Mobashery, Shahriar,Hesek, Dusan,Lee, Mijoon,Yoo, Jakyung,Cui, Minghua,Choi, Sun,Kim, Cheolhee,Lee, Nam Ki,Kim, Soon-Jong,Kim, Jin Y American Society for Biochemistry and Molecular Bi 2015 The Journal of biological chemistry Vol.290 No.41

<▼1><P><B>Background:</B> Csd6 is one of the cell shape-determining proteins in <I>H. pylori</I>.</P><P><B>Results:</B> The active site of Csd6 is tailored to function as an <SMALL>L</SMALL>,<SMALL>D</SMALL>-carboxypeptidase in the peptidoglycan-trimming process.</P><P><B>Conclusion:</B> Csd6 constitutes a new family of <SMALL>L</SMALL>,<SMALL>D</SMALL>-carboxypeptidase.</P><P><B>Significance:</B> The substrate limitation of Csd6 is a strategy that <I>H. pylori</I> uses to regulate its helical cell shape and motility.</P></▼1><▼2><P><I>Helicobacter pylori</I> causes gastrointestinal diseases, including gastric cancer. Its high motility in the viscous gastric mucosa facilitates colonization of the human stomach and depends on the helical cell shape and the flagella. In <I>H. pylori</I>, Csd6 is one of the cell shape-determining proteins that play key roles in alteration of cross-linking or by trimming of peptidoglycan muropeptides. Csd6 is also involved in deglycosylation of the flagellar protein FlaA. To better understand its function, biochemical, biophysical, and structural characterizations were carried out. We show that Csd6 has a three-domain architecture and exists as a dimer in solution. The N-terminal domain plays a key role in dimerization. The middle catalytic domain resembles those of <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidases, but its pocket-shaped active site is uniquely defined by the four loops I to IV, among which loops I and III show the most distinct variations from the known <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidases. Mass analyses confirm that Csd6 functions only as an <SMALL>L</SMALL>,<SMALL>D</SMALL>-carboxypeptidase and not as an <SMALL>L</SMALL>,<SMALL>D</SMALL>-transpeptidase. The <SMALL>D</SMALL>-Ala-complexed structure suggests possible binding modes of both the substrate and product to the catalytic domain. The C-terminal nuclear transport factor 2-like domain possesses a deep pocket for possible binding of pseudaminic acid, and <I>in silico</I> docking supports its role in deglycosylation of flagellin. On the basis of these findings, it is proposed that <I>H. pylori</I> Csd6 and its homologs constitute a new family of <SMALL>L</SMALL>,<SMALL>D</SMALL>-carboxypeptidase. This work provides insights into the function of Csd6 in regulating the helical cell shape and motility of <I>H. pylori</I>.</P></▼2>

Structural basis for the substrate recognition of peptidoglycan pentapeptides by <i>Enterococcus faecalis</i> VanY_B

Kim, Hyoun Sook,Hahn, Hyunggu,Kim, Jieun,Jang, Dong Man,Lee, Ji Yeon,Back, Jang Mi,Im, Ha Na,Kim, Haelee,Han, Byung Woo,Suh, Se Won Elsevier 2018 INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Vol.119 No.-

<P><B>Abstract</B></P> <P>Vancomycin resistance in <I>Enterococci</I> and its transfer to methicillin-resistant <I>Staphylococcus aureus</I> are challenging problems in health care institutions worldwide. High-level vancomycin resistance is conferred by acquiring either transposable elements of the <I>VanA</I> or <I>VanB</I> type. <I>Enterococcus faecalis</I> VanY<SUB>B</SUB> in the <I>VanB</I>-type operon is a <SMALL>D</SMALL>,<SMALL>D</SMALL>-carboxypeptidase that recognizes the peptidyl-<SMALL>D</SMALL>-Ala<SUP>4</SUP>-<SMALL>D</SMALL>-Ala<SUP>5</SUP> extremity of peptidoglycan and hydrolyses the terminal <SMALL>D</SMALL>-Ala on the extracellular side of the cell wall, thereby increasing the level of glycopeptide antibiotics resistance. However, at the molecular level, it remains unclear how VanY<SUB>B</SUB> manipulates peptidoglycan peptides for vancomycin resistance. In this study, we have determined the crystal structures of <I>E. faecalis</I> VanY<SUB>B</SUB> in the <SMALL>D</SMALL>-Ala-<SMALL>D</SMALL>-Ala-bound, <SMALL>D</SMALL>-Ala-bound, and -unbound states. The interactions between VanY<SUB>B</SUB> and <SMALL>D</SMALL>-Ala-<SMALL>D</SMALL>-Ala observed in the crystal provide the molecular basis for the recognition of peptidoglycan substrates by VanY<SUB>B</SUB>. Moreover, comparisons with the related VanX and VanXY enzymes reveal distinct structural features of <I>E. faecalis</I> VanY<SUB>B</SUB> around the active-site cleft, thus shedding light on its unique substrate specificity. Our results could serve as the foundation for unravelling the molecular mechanism of vancomycin resistance and for developing novel antibiotics against the vancomycin-resistant <I>Enterococcus</I> species.</P>

Characterization of morphological characteristics of exotic weeds of the genus Veronica (Scrophulariaceae) for image recognition

Hyoun Sook Kim,Sang Jin Lee,Sang Myong Lee,Bazarragchaa Badamtsetseg,Joongku Lee 한국잡초학회 2018 한국잡초학회 별책(학술대회 초록집) Vol.38 No.2

Association of Guanosine Triphosphate Cyclohydrolase 1 Gene Polymorphisms with Fibromyalgia Syndrome in a Korean Population

KIM, SEONG-KYU,KIM, SEONG-HO,NAH, SEONG-SU,LEE, JI HYUN,HONG, SEUNG-JAE,KIM, HYUN-SOOK,LEE, HYE-SOON,KIM, HYOUN AH,JOUNG, CHUNG-IL,BAE, JISUK,CHOE, JUNG-YOON,LEE, SHIN-SEOK Journal of Rheumatology 2013 The Journal of rheumatology Vol.40 No.3

<P><B>Objective.</B></P><P>Guanosine triphosphate cyclohydrolase 1 (GCH1) is the rate-limiting enzyme in the synthesis of tetrahydrobiopterin, which is an essential cofactor in nitric oxide (NO) production. Polymorphisms in the <I>GCH1</I> gene have been implicated in protection against pain sensitivity. The aim of our study was to determine whether single-nucleotide polymorphisms (SNP) in the <I>GCH1</I> gene affect susceptibility and/or pain sensitivity in fibromyalgia syndrome (FM).</P><P><B>Methods.</B></P><P>A total of 409 patients with FM and 422 controls were enrolled. The alleles and genotypes at 4 positions [rs3783641(T>A), rs841(C>T), rs752688(C>T), and rs4411417(T>C)] in the <I>GCH1</I> gene were analyzed. The associations of the <I>GCH1</I> SNP with susceptibility and clinical measures in patients with FM were assessed.</P><P><B>Results.</B></P><P>The frequencies of alleles and genotypes of the 4 SNP did not differ between patients with FM and healthy controls. Among 13 constructed haplotypes, we further examined 4 (CCTT, TTCT, TTCA, and CCTA) with > 1% frequency in both FM and controls. No associations of <I>GCH1</I> polymorphisms with FM-related activity or severity indexes were found, although the number and total score of tender points in patients with FM differed among the 4 haplotypes (p = 0.03 and p = 0.01, respectively). The CCTA haplotype of <I>GCH1</I> was associated with significantly lower pain sensitivity and occurred less frequently than the CCTT haplotype in patients with FM (p = 0.04, OR 0.45, 95% CI 0.21–0.96).</P><P><B>Conclusion.</B></P><P>Our study provides evidence that certain <I>GCH1</I> haplotypes may be protective against susceptibility and pain sensitivity in FM. Our data suggest that NO is responsible for pain sensitivity in the pathogenesis of FM.</P>

Structural basis of octanoic acid recognition by lipoate-protein ligase B

Kim, Do Jin,Lee, Sang Jae,Kim, Hyoun Sook,Kim, Kyoung Hoon,Lee, Hyung Ho,Yoon, Hye Jin,Suh, Se Won Wiley Subscription Services, Inc., A Wiley Company 2008 Proteins Vol.70 No.4