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      KCI등재후보

      Bioinformatics Analysis of Hsp20 Sequences in Proteobacteria

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      https://www.riss.kr/link?id=A104426698

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      다국어 초록 (Multilingual Abstract)

      Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are ...

      Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock
      proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell’s danger signaling cascade. Heat shock protein, Hsp20 is
      a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria.
      It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.

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      다국어 초록 (Multilingual Abstract)

      Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are ...

      Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell’s danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria.
      It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.

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      참고문헌 (Reference)

      1 Rembold, C, "cGMP-mediated phosphorylation of heat shock protein 20 mau cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery" 524 : 865-878, 2000

      2 Lee, K, "The hierarchical system of the ‘Alphaproteobacteria’; Xanthobacteraceae fam. nov. and Erythrobacteraceae fam. nov" 55 : 1907-1919, 2005

      3 Thompson, J, "The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools" (25) : 4876-4882, 1997

      4 Page, R, "TREEVIEW: An application to display phylogenetic trees on personal computers" 12 : 357-358, 1996

      5 Ludwig, W, "Overview: a phylogenetic backbone and taxonomic framework for prokaryotic systematics" Springer 49-66, 2001

      6 Dedysh, S, "NifH and NifD phylogenies: an evolutionary basis for understanding nitrogen fixation capabilities of methanotrophic bacteria" 150 : 1301-1313, 2004

      7 Mulder, N.J, "New developments in the InterPro database" 35 : D224-D228, 2007

      8 Trotter, E, "Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae" 277 : 44817-44825, 2002

      9 Schlesinger, M, "Minireview: Heat Shock Proteins" 265 : 12111-12114, 1990

      10 Suzuki, A, "MKBP, a novel member of the heat shock protein family, binds and activates the myotonic dystrophy protein kinase" 140 : 1113-1124, 1998

      1 Rembold, C, "cGMP-mediated phosphorylation of heat shock protein 20 mau cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery" 524 : 865-878, 2000

      2 Lee, K, "The hierarchical system of the ‘Alphaproteobacteria’; Xanthobacteraceae fam. nov. and Erythrobacteraceae fam. nov" 55 : 1907-1919, 2005

      3 Thompson, J, "The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools" (25) : 4876-4882, 1997

      4 Page, R, "TREEVIEW: An application to display phylogenetic trees on personal computers" 12 : 357-358, 1996

      5 Ludwig, W, "Overview: a phylogenetic backbone and taxonomic framework for prokaryotic systematics" Springer 49-66, 2001

      6 Dedysh, S, "NifH and NifD phylogenies: an evolutionary basis for understanding nitrogen fixation capabilities of methanotrophic bacteria" 150 : 1301-1313, 2004

      7 Mulder, N.J, "New developments in the InterPro database" 35 : D224-D228, 2007

      8 Trotter, E, "Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae" 277 : 44817-44825, 2002

      9 Schlesinger, M, "Minireview: Heat Shock Proteins" 265 : 12111-12114, 1990

      10 Suzuki, A, "MKBP, a novel member of the heat shock protein family, binds and activates the myotonic dystrophy protein kinase" 140 : 1113-1124, 1998

      11 Davies, E.L, "Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL" 145 : 183-189, 2006

      12 Meeks, M, "Heat shock protein 20-mediated force suppression in forskolin-relaxed swine carotid artery" 288 : C633-C639, 2005

      13 Rice, P, "Emboss: the European Molecular Open Software Suite" 16 : 276-277, 2000

      14 Rice, P, "Emboss: the European Molecular Open Software Suite" 16 : 276-277, 2000

      15 Oganesyan, N, "Effect of osmotic stress and recombinant protein overexpression and crystallization" 52 : 280-285, 2007

      16 Landes, C, "Dot-plot comparison by multivariate analysis (DOCMA): a tool for classifying protein sequences" 9 : 191-196, 1992

      17 Kim, K.K, "Crystal structure of a small heat-shock protein" 394 : 595-599, 1998

      18 Chandra, S, "Comparative insect mitochondrial genomes: Differences despite conserved genome synteny" 5 : 1308-1318, 2006

      19 Miroschnichenko, M, "Caminibacter profundus sp. Nov., a novel thermophile of Nautiliales ord. nov. within the class ‘Epsilonproteobacteria’, isolated from a deep-sea hydrothermal vent" 54 : 41-45, 2004

      20 Thompson, J, "CLUSTAL W: improving sensitivity of progressive multiple sequence alignments through sequence weighting, position specific gap penalties and weight matrix choice" 22 : 4673-4680, 1994

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2020 평가예정 신규평가 신청대상 (신규평가)
      2019-12-01 평가 등재후보 탈락 (계속평가)
      2018-12-01 평가 등재후보로 하락 (계속평가) KCI등재후보
      2015-01-01 평가 등재학술지 선정 (계속평가) KCI등재
      2013-01-01 평가 등재후보 1차 FAIL (등재후보1차) KCI등재후보
      2012-01-01 평가 등재후보학술지 유지 (기타) KCI등재후보
      2011-01-01 평가 등재후보 1차 FAIL (등재후보2차) KCI등재후보
      2010-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2009-01-01 평가 등재후보학술지 유지 (등재후보2차) KCI등재후보
      2008-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2006-01-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.11 0.11 0.13
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.11 0.09 0.353 0
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