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      Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbate = Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbate

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      https://www.riss.kr/link?id=A82503513

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      다국어 초록 (Multilingual Abstract)

      The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive. Here, under oxidative stress (100 μM hydrogen peroxide), antioxidant (100 μM ascorbate) or control conditions 169 proteins were identified by electospray ionisation fourier transform ion cyclotron resonance mass spectrometry. The majority of these proteins (70%) were found to contain SUMOylation consensus sequences. From the remaining proteins a small number (12%) were found to contain possible SUMO interacting motifs. The proteins identified included DNA and RNA binding proteins, structural proteins and proteasomal proteins. Several of the proteins identified under oxidative stress conditions had previously been identified as SUMOylated proteins, thus validating the method presented. [BMB reports 2010; 43(11): 720-725]
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      The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive...

      The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive. Here, under oxidative stress (100 μM hydrogen peroxide), antioxidant (100 μM ascorbate) or control conditions 169 proteins were identified by electospray ionisation fourier transform ion cyclotron resonance mass spectrometry. The majority of these proteins (70%) were found to contain SUMOylation consensus sequences. From the remaining proteins a small number (12%) were found to contain possible SUMO interacting motifs. The proteins identified included DNA and RNA binding proteins, structural proteins and proteasomal proteins. Several of the proteins identified under oxidative stress conditions had previously been identified as SUMOylated proteins, thus validating the method presented. [BMB reports 2010; 43(11): 720-725]

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      참고문헌 (Reference)

      1 Gutierrez, G. J., "Ubiquitin and SUMO systems in the regulation of mitotic checkpoints" 31 : 324-332, 2006

      2 Jakobs, A., "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation" 35 : e109-, 2007

      3 Jakobs, A., "Ubc9 fusion- directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation" 4 : 245-250, 2007

      4 Pollice, A., "The promiscuity of ARF interactions with the proteasome" 582 : 3257-3262, 2008

      5 Grant, M. M., "The presence of ascorbate induces expression of brain derived neurotrophic factor in SH-SY5Y neuroblastoma cells after peroxide insult, which is associated with increased survival" 5 : 534-540, 2005

      6 Ren, J., "Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0" 9 : 3409-3412, 2009

      7 Sekiyama, N., "Structure of the small ubiquitin- like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3" 283 : 35966-35975, 2008

      8 Bayer, P., "Structure determination of the small ubiquitin-related modifier SUMO-1" 280 : 275-286, 1998

      9 Hecker, C., "Specification of SUMO1- and SUMO2-interacting motifs" 281 : 16117-16127, 2006

      10 Song, J., "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation" 280 : 40122-40129, 2005

      1 Gutierrez, G. J., "Ubiquitin and SUMO systems in the regulation of mitotic checkpoints" 31 : 324-332, 2006

      2 Jakobs, A., "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation" 35 : e109-, 2007

      3 Jakobs, A., "Ubc9 fusion- directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation" 4 : 245-250, 2007

      4 Pollice, A., "The promiscuity of ARF interactions with the proteasome" 582 : 3257-3262, 2008

      5 Grant, M. M., "The presence of ascorbate induces expression of brain derived neurotrophic factor in SH-SY5Y neuroblastoma cells after peroxide insult, which is associated with increased survival" 5 : 534-540, 2005

      6 Ren, J., "Systematic study of protein sumoylation: development of a site-specific predictor of SUMOsp 2.0" 9 : 3409-3412, 2009

      7 Sekiyama, N., "Structure of the small ubiquitin- like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3" 283 : 35966-35975, 2008

      8 Bayer, P., "Structure determination of the small ubiquitin-related modifier SUMO-1" 280 : 275-286, 1998

      9 Hecker, C., "Specification of SUMO1- and SUMO2-interacting motifs" 281 : 16117-16127, 2006

      10 Song, J., "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation" 280 : 40122-40129, 2005

      11 Hay, R. T., "SUMO: a history of modification" 18 : 1-12, 2005

      12 Pfander, B., "SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase" 436 : 428-433, 2005

      13 Terashima, T., "SUMO-1 colocalized with mutant atrophin-1 with expanded polyglutamines accelerates intranuclear aggregation and cell death" 13 : 2359-2364, 2002

      14 Li, M., "SUMO wrestling with type 1 diabetes" 83 : 504-513, 2005

      15 Dorval, V., "SUMO on the road to neurodegeneration" 1773 : 694-706, 2007

      16 Bossis, G., "Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes" 21 : 349-357, 2006

      17 Johnson, E. S., "Protein modification by SUMO" 73 : 355-382, 2004

      18 Paulsen, C. E., "Orchestrating redox signaling networks through regulatory cysteine switches" 5 : 47-62, 2010

      19 He, Y., "Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B" 66 : 1239-1256, 2009

      20 Gharahdaghi, F., "Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity" 20 : 601-605, 1999

      21 Creese, A., "Liquid chromatography electron capture dissociation tandem mass spectrometry (LC-ECD-MS/MS) versus liquid chromatography collision-induced dissociation tandem mass spectrometry (LC-CID-MS/MS) for the identification of proteins" 18 : 891-897, 2007

      22 Wohlschlegel, J. A., "Global analysis of protein sumoylation in Saccharomyces cerevisiae" 279 : 45662-45668, 2004

      23 Saitoh, H., "Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3" 275 : 6252-6258, 2000

      24 Chow, S., "Drawing area-proportional Venn and Euler diagrams" 466-477, 2004

      25 Vertegaal, A. C., "Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics" 5 : 2298-2310, 2006

      26 Hannich, J. T., "Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae" 280 : 4102-4110, 2005

      27 Rosas-Acosta, G., "A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers" 4 : 56-72, 2005

      28 Rigaut, G., "A generic protein purification method for protein complex characterization and proteome exploration" 17 : 1030-1032, 1999

      29 Perry, J. J., "A SIMultaneous role for SUMO and ubiquitin" 33 : 201-208, 2008

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      학술지등록 한글명 : BMB reports
      외국어명 : BMB reports
      2024 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2021-01-01 평가 등재학술지 선정 (해외등재 학술지 평가) KCI등재
      2020-12-01 평가 등재후보로 하락 (해외등재 학술지 평가) KCI등재후보
      2013-07-17 학술지명변경 한글명 : BMB reports -> BMB Reports
      외국어명 : BMB reports -> BMB Reports
      KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-09-21 학회명변경 한글명 : 대한생화학ㆍ분자생물학회 -> 생화학분자생물학회
      영문명 : Korean Society Of Medical Biochemistry And Molecular Biology -> Korean Society Of Biochemistry And Molecular Biology
      KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2002-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      1999-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 2.76 0.5 1.94
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      1.45 1.12 0.646 0.12
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