메뉴 건너뛰기




Volumn 6, Issue 1, 2009, Pages 30-37

Of proteins and DNA - Proteomic role in the field of chromatin research

Author keywords

[No Author keywords available]

Indexed keywords

DNA; PROTEIN;

EID: 72949110782     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/b907925b     Document Type: Review
Times cited : (4)

References (46)
  • 1
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • R. D. Kornberg Chromatin structure: a repeating unit of histones and DNA Science 1974 184 868 871
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 2
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 resolution
    • K. Luger A. W. Mader R. K. Richmond D. F. Sargent T. J. Richmond Crystal structure of the nucleosome core particle at 2.8 resolution Nature 1997 389 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 34548544648 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, part II: ATP-dependent chromatin remodeling
    • DOI 10.1016/j.molmed.2007.07.004, PII S1471491407001475
    • G. G. Wang C. D. Allis P. Chi Chromatin remodeling and cancer, Part II: ATP-dependent chromatin remodeling Trends Mol. Med. 2007 13 373 380 (Pubitemid 47385382)
    • (2007) Trends in Molecular Medicine , vol.13 , Issue.9 , pp. 373-380
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 4
    • 34249795487 scopus 로고    scopus 로고
    • Histone variant nucleosomes: Structure, function and implication in disease
    • M. Boulard P. Bouvet T. K. Kundu S. Dimitrov Histone variant nucleosomes: structure, function and implication in disease Subcell. Biochem. 2007 41 71 89
    • (2007) Subcell. Biochem. , vol.41 , pp. 71-89
    • Boulard, M.1    Bouvet, P.2    Kundu, T.K.3    Dimitrov, S.4
  • 5
    • 44649186259 scopus 로고    scopus 로고
    • The histone H1 family: Specific members, specific functions
    • A. Izzo K. Kamieniarz R. Schneider The histone H1 family: specific members, specific functions Biol. Chem. 2008 389 333 343
    • (2008) Biol. Chem. , vol.389 , pp. 333-343
    • Izzo, A.1    Kamieniarz, K.2    Schneider, R.3
  • 6
    • 34548433964 scopus 로고    scopus 로고
    • Marking histone H3 variants: How, when and why?
    • A. Loyola G. Almouzni Marking histone H3 variants: how, when and why? Trends Biochem. Sci. 2007 32 425 433
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 425-433
    • Loyola, A.1    Almouzni, G.2
  • 7
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications lessons from professional pocket pickers
    • S. D. Taverna H. Li A. J. Ruthenburg C. D. Allis D. J. Patel How chromatin-binding modules interpret histone modifications lessons from professional pocket pickers Nat. Struct. Mol. Biol. 2007 14 1025 1040
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 8
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B. D. Strahl C. D. Allis The language of covalent histone modifications Nature 2000 403 41 45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 10
    • 33846809241 scopus 로고    scopus 로고
    • Characterization of histones and their post-translational modifications by mass spectrometry
    • B. A. Garcia J. Shabanowitz D. F. Hunt Characterization of histones and their post-translational modifications by mass spectrometry Curr. Opin. Chem. Biol. 2007 11 66 73
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 66-73
    • Garcia, B.A.1    Shabanowitz, J.2    Hunt, D.F.3
  • 11
    • 33645471026 scopus 로고    scopus 로고
    • Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry
    • D. Bonenfant M. Coulot H. Towbin P. Schindler J. van Oostrum Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry Mol. Cell Proteomics 2006 5 541 552
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 541-552
    • Bonenfant, D.1    Coulot, M.2    Towbin, H.3    Schindler, P.4    Van Oostrum, J.5
  • 12
    • 32344453899 scopus 로고    scopus 로고
    • Mass spectrometric characterization of human histone H3: A bird's eye view
    • C. E. Thomas N. L. Kelleher C. A. Mizzen Mass spectrometric characterization of human histone H3: a bird's eye view J. Proteome Res. 2006 5 240 247
    • (2006) J. Proteome Res. , vol.5 , pp. 240-247
    • Thomas, C.E.1    Kelleher, N.L.2    Mizzen, C.A.3
  • 13
    • 34948821302 scopus 로고    scopus 로고
    • Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail
    • L. Jiang J. N. Smith S. L. Anderson P. Ma C. A. Mizzen N. L. Kelleher Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail J. Biol. Chem. 2007 282 27923 27934
    • (2007) J. Biol. Chem. , vol.282 , pp. 27923-27934
    • Jiang, L.1    Smith, J.N.2    Anderson, S.L.3    Ma, P.4    Mizzen, C.A.5    Kelleher, N.L.6
  • 18
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 Complexes Mediate Nucleosome Assembly Pathways Dependent or Independent of DNA Synthesis
    • DOI 10.1016/S0092-8674(03)01064-X
    • H. Tagami D. Ray-Gallet G. Almouzni Y. Nakatani Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis Cell 2004 116 51 61 (Pubitemid 38156183)
    • (2004) Cell , vol.116 , Issue.1 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 19
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: A brief overview
    • H. Kitano Systems biology: a brief overview Science 2002 295 1662 1664
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 25
    • 53349156368 scopus 로고    scopus 로고
    • Biochemistry. Not comparable, but complementary
    • L. J. Jensen P. Bork Biochemistry. Not comparable, but complementary Science 2008 322 56 57
    • (2008) Science , vol.322 , pp. 56-57
    • Jensen, L.J.1    Bork, P.2
  • 28
    • 47249100637 scopus 로고    scopus 로고
    • A RECQ-RNA5 polymerase II association identified by targeted proteomic analysis of human chromatin
    • O. Aygun J. Svejstrup Y. Liu A RECQ-RNA5 polymerase II association identified by targeted proteomic analysis of human chromatin Proc. Natl. Acad. Sci. U. S. A. 2008 105 8580 8584
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8580-8584
    • Aygun, O.1    Svejstrup, J.2    Liu, Y.3
  • 30
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • J. S. Lai W. Herr Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations Proc. Natl. Acad. Sci. U. S. A. 1992 89 6958 6962
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6958-6962
    • Lai, J.S.1    Herr, W.2
  • 31
    • 61449095752 scopus 로고    scopus 로고
    • Reverse ChIP
    • N. Rusk Reverse ChIP Nat. Methods 2009 6 187
    • (2009) Nat. Methods , vol.6 , pp. 187
    • Rusk, N.1
  • 33
    • 33745623633 scopus 로고    scopus 로고
    • The dynamic alterations of H2AX complex during DNA repair detected by a proteomic approach reveal the critical roles of Ca(2+)/calmodulin in the ionizing radiation-induced cell cycle arrest
    • Y. C. Du S. Gu J. Zhou T. Wang H. Cai M. A. Macinnes E. M. Bradbury X. Chen The dynamic alterations of H2AX complex during DNA repair detected by a proteomic approach reveal the critical roles of Ca(2+)/calmodulin in the ionizing radiation-induced cell cycle arrest Mol. Cell. Proteomics 2006 5 1033 1044
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1033-1044
    • Du, Y.C.1    Gu, S.2    Zhou, J.3    Wang, T.4    Cai, H.5    MacInnes, M.A.6    Bradbury, E.M.7    Chen, X.8
  • 34
    • 34248999095 scopus 로고    scopus 로고
    • Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases
    • G. I. Chen A. C. Gingras Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases Methods 2007 42 298 305
    • (2007) Methods , vol.42 , pp. 298-305
    • Chen, G.I.1    Gingras, A.C.2
  • 36
    • 48749124117 scopus 로고    scopus 로고
    • ChIPping away at gene regulation
    • C. E. Massie I. G. Mills ChIPping away at gene regulation EMBO Rep. 2008 9 337 343
    • (2008) EMBO Rep. , vol.9 , pp. 337-343
    • Massie, C.E.1    Mills, I.G.2
  • 37
    • 25444491189 scopus 로고    scopus 로고
    • Easy detection of chromatin binding proteins by the histone association assay
    • R. M. Ricke A. K. Bielinsky Easy detection of chromatin binding proteins by the histone association assay Biol. Proced. Online 2005 7 60 69
    • (2005) Biol. Proced. Online , vol.7 , pp. 60-69
    • Ricke, R.M.1    Bielinsky, A.K.2
  • 38
    • 58149085861 scopus 로고    scopus 로고
    • Purification of proteins associated with specific genomic Loci
    • J. Déjardin R. E. Kingston Purification of proteins associated with specific genomic Loci Cell 2009 136 175 186
    • (2009) Cell , vol.136 , pp. 175-186
    • Déjardin, J.1    Kingston, R.E.2
  • 39
  • 41
    • 35649000073 scopus 로고    scopus 로고
    • Chromatin fine structure of the c-MYC insulator element/DNase I-hypersensitive site i is not preserved during mitosis
    • J. Komura H. Ikehata T. Ono Chromatin fine structure of the c-MYC insulator element/DNase I-hypersensitive site I is not preserved during mitosis Proc. Natl. Acad. Sci. U. S. A. 2007 104 15741 15746
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15741-15746
    • Komura, J.1    Ikehata, H.2    Ono, T.3
  • 42
    • 59949099230 scopus 로고    scopus 로고
    • A SILAC-based DNA protein interaction screen that identifies candidate binding proteins to functional DNA elements
    • G. Mittler F. Butter M. Mann A SILAC-based DNA protein interaction screen that identifies candidate binding proteins to functional DNA elements Genome Res. 2009 19 284 293
    • (2009) Genome Res. , vol.19 , pp. 284-293
    • Mittler, G.1    Butter, F.2    Mann, M.3
  • 43
    • 66149100528 scopus 로고    scopus 로고
    • A Novel Proteomics Approach for the Discovery of Chromatin-Associated Protein Networks
    • J. P. Lambert L. Mitchell A. Rudner K. Baetz D. Figeys A Novel Proteomics Approach for the Discovery of Chromatin-Associated Protein Networks Mol. Cell. Proteomics 2009 8 870 882
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 870-882
    • Lambert, J.P.1    Mitchell, L.2    Rudner, A.3    Baetz, K.4    Figeys, D.5
  • 46
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • G. Mizuguchi X. Shen J. Landry W. H. Wu S. Sen C. Wu ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex Science 2004 303 343 348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.