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      KCI등재 SCOPUS SCIE

      A short guide to histone deacetylases including recent progress on class II enzymes

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      https://www.riss.kr/link?id=A106610699

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      다국어 초록 (Multilingual Abstract)

      The interaction between histones and DNA is important for eukaryotic gene expression. A loose interaction caused, for example, by the neutralization of a positive charge on the histone surface by acetylation, induces a less compact chromatin structure...

      The interaction between histones and DNA is important for eukaryotic gene expression. A loose interaction caused, for example, by the neutralization of a positive charge on the histone surface by acetylation, induces a less compact chromatin structure, resulting in feasible accessibility of RNA polymerase and increased gene expression. In contrast, the formation of a tight chromatin structure due to the deacetylation of histone lysine residues on the surface by histone deacetylases enforces the interaction between the histones and DNA, which minimizes the chance of RNA polymerases contacting DNA, resulting in decreased gene expression. Therefore, the balance of the acetylation of histones mediated by histone acetylases (HATs) and histone deacetylases (HDACs) is an issue of transcription that has long been studied in relation to posttranslational modification. In this review, current knowledge of HDACs is briefly described with an emphasis on recent progress in research on HDACs, especially on class IIa HDACs.

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      참고문헌 (Reference)

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      2 Buker, S. M., "Two different Argonaute complexes are required for siRNA generation and heterochromatin assembly in fission yeast" 14 : 200-207, 2007

      3 Rundlett, S. E., "Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4by RPD3" 392 : 831-835, 1998

      4 Kazantsev, A. G., "Therapeutic application of histone deacetylase inhibitors for central nervous system disorders" 7 : 854-868, 2008

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      6 Wen, Y. D., "The histone deacetylase-3 complex contains nuclear receptor corepressors" 97 : 7202-7207, 2000

      7 Guenther, M. G., "The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3" 21 : 6091-6101, 2001

      8 Brachmann, C. B., "The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability" 9 : 2888-2902, 1995

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      10 Wu, J., "TUP1 utilizes histone H3/H2Bspecific HDA1 deacetylase to repress gene activity in yeast" 7 : 117-126, 2001

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      18 Du, J., "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase" 334 : 806-809, 2011

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      23 Grozinger, C. M., "Regulation of histone deacetylase 4 and 5and transcriptional activity by 14-3-3-dependent cellular localization" 97 : 7835-7840, 2000

      24 Mathias, R. A., "Post-translational modifications regulate class IIa histone deacetylase(HDAC)function in health and disease" 14 : 456-470, 2015

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      26 Robyr, D., "Microarray deacetylation maps determine genome-wide functions for yeast histone deacetylases" 109 : 437-446, 2002

      27 Mihaylova, M. M., "Metabolic reprogramming by class I and II histone deacetylases" 24 : 48-57, 2013

      28 Kerckaert, J. P., "LAZ3, a novel zinc-finger encoding gene, is disrupted by recurring chromosome 3q27 translocations in human lymphomas" 5 : 66-70, 1993

      29 Kao, H. Y., "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRTmediated repression" 14 : 55-66, 2000

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      31 Hudson, G. M., "Insights into the recruitment of class IIa histone deacetylases(HDACs)to the SMRT/NCoR transcriptional repression complex" 290 : 18237-18244, 2015

      32 Fischle, W., "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo" 276 : 35826-35835, 2001

      33 Schuetz, A., "Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity" 283 : 11355-11363, 2008

      34 Xiong, B., "Hos1 is a lysine deacetylase for the Smc3 subunit of cohesin" 20 : 1660-1665, 2010

      35 Ayer, D. E., "Histone deacetylases : transcriptional repression with SINers and NuRDs" 9 : 193-198, 1999

      36 Eckschlager, T, "Histone deacetylase inhibitors as anticancer drugs" 18 : 2017

      37 Minucci, S., "Histone deacetylase inhibitors and the promise of epigenetic(and more)treatments for cancer" 6 : 38-51, 2006

      38 Koutsounas, I., "Histone deacetylase inhibitors and pancreatic cancer: are there any promising clinical trials?" 19 : 1173-1181, 2013

      39 Winkler, R., "Histone deacetylase 6(HDAC6)is an essential modifier of glucocorticoid-induced hepatic gluconeogenesis" 61 : 513-523, 2012

      40 Hai, Y., "Histone deacetylase 10 structure and molecular function as a polyamine deacetylase" 8 : 15368-, 2017

      41 Wu, J., "HDA2 and HDA3are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1" 98 : 4391-4396, 2001

      42 Rundlett, S. E., "HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription" 93 : 14503-14508, 1996

      43 Carmen, A. A., "HDA1 and HDA3 are components of a yeast histone deacetylase(HDA)complex" 271 : 15837-15844, 1996

      44 Vogelauer, M., "Global histone acetylation and deacetylation in yeast" 408 : 495-498, 2000

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      59 McKinsey, T. A., "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinasestimulated binding of 14-3-3 to histone deacetylase 5" 97 : 14400-14405, 2000

      60 Glozak, M. A., "Acetylation/deacetylation modulates the stability of DNA replication licensing factor Cdt1" 284 : 11446-11453, 2009

      61 Di Gennaro, E., "Acetylation of proteins as novel target for antitumor therapy : review article" 26 : 435-441, 2004

      62 Guo, C., "ATM regulates ionizing radiationinduced disruption of HDAC1 : PP1 : Rb complexes" 19 : 504-510, 2007

      63 Zhang, H., "A new functional domain of Bcl6 family that recruits histone deacetylases" 1540 : 188-200, 2001

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      65 Muslin, A. J., "14-3-3 proteins : regulation of subcellular localization by molecular interference" 12 : 703-709, 2000

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      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2009-09-21 학회명변경 한글명 : 대한생화학ㆍ분자생물학회 -> 생화학분자생물학회
      영문명 : Korean Society Of Medical Biochemistry And Molecular Biology -> Korean Society Of Biochemistry And Molecular Biology
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      2008-01-01 평가 SCI 등재 (등재유지) KCI등재
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      1998-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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