메뉴 건너뛰기




Volumn 10, Issue 10, 2011, Pages 4416-4427

PUB-MS: A mass spectrometry-based method to monitor protein-protein proximity in vivo

Author keywords

biotinylation; multiplexing; protein protein interactions; proximity; pulse chase; SILAC

Indexed keywords

BIOTIN; BIOTIN ACCEPTOR PEPTIDE; BIRA PROTEIN; ISOTOPE; LIGASE; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 80053927559     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200189p     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 39749192575 scopus 로고    scopus 로고
    • Self-organization in cell biology: A brief history
    • DOI 10.1038/nrm2357, PII NRM2357
    • Karsenti, E. Self-organization in cell biology: a brief history Nat. Rev. Mol. Cell. Biol. 2008, 9, 255-262 (Pubitemid 351301833)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 255-262
    • Karsenti, E.1
  • 2
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • DOI 10.1083/jcb.200108110
    • Misteli, T. The concept of self-organization in cellular architecture J. Cell Biol. 2001, 155, 181-185 (Pubitemid 34289292)
    • (2001) Journal of Cell Biology , vol.155 , Issue.2 , pp. 181-185
    • Misteli, T.1
  • 3
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • DOI 10.1006/meth.2001.1211
    • Day, R. N.; Periasamy, A.; Schaufele, F. Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus Methods 2001, 25, 4-18 (Pubitemid 32905284)
    • (2001) Methods , vol.25 , Issue.1 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 4
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • DOI 10.1016/S0962-8924(98)01434-2, PII S0962892498014342
    • Pollok, B. A.; Heim, R. Using GFP in FRET-based applications Trends Cell Biol. 1999, 9, 57-60 (Pubitemid 29151793)
    • (1999) Trends in Cell Biology , vol.9 , Issue.2 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 5
    • 0036696695 scopus 로고    scopus 로고
    • The use of resonance energy transfer in high-throughput screening: BRET versus FRET
    • Boute, N.; Jockers, R.; Issad, T. The use of resonance energy transfer in high-throughput screening: BRET versus FRET Trends Pharmacol. Sci. 2002, 23, 351-354
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 351-354
    • Boute, N.1    Jockers, R.2    Issad, T.3
  • 6
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
    • Pfleger, K. D.; Eidne, K. A. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET) Nat. Methods 2006, 3, 165-174
    • (2006) Nat. Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 8
    • 3242657478 scopus 로고    scopus 로고
    • Mapping biochemical networks with protein-fragment complementation assays
    • Remy, I; Michnick, S. W. Mapping biochemical networks with protein-fragment complementation assays Methods Mol. Biol. 2004, 261, 411-426
    • (2004) Methods Mol. Biol. , vol.261 , pp. 411-426
    • Remy, I.1    Michnick, S.W.2
  • 9
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • DOI 10.1038/340245a0
    • Fields, S.; Song, O. A novel genetic system to detect protein-protein interactions Nature 1989, 340, 245-246 (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 12
    • 0346728687 scopus 로고    scopus 로고
    • Use of protein biotinylation in vivo for chromatin immunoprecipitation
    • DOI 10.1016/j.ab.2003.10.015
    • Viens, A.; Mechold, U.; Lehrmann, H.; Harel-Bellan, A.; Ogryzko, V. Use of protein biotinylation in vivo for chromatin immunoprecipitation Anal. Biochem. 2004, 325, 68-76 (Pubitemid 38050268)
    • (2004) Analytical Biochemistry , vol.325 , Issue.1 , pp. 68-76
    • Viens, A.1    Mechold, U.2    Lehrmann, H.3    Harel-Bellan, A.4    Ogryzko, V.5
  • 13
    • 64749092881 scopus 로고    scopus 로고
    • Use of in vivo biotinylation to study protein-protein and protein-DNA interactions in mouse embryonic stem cells
    • Kim, J.; Cantor, A. B.; Orkin, S. H.; Wang, J. Use of in vivo biotinylation to study protein-protein and protein-DNA interactions in mouse embryonic stem cells Nat. Protoc. 2009, 4, 506-517
    • (2009) Nat. Protoc. , vol.4 , pp. 506-517
    • Kim, J.1    Cantor, A.B.2    Orkin, S.H.3    Wang, J.4
  • 15
    • 77951160864 scopus 로고    scopus 로고
    • A native chromatin purification system for epigenomic profiling in Caenorhabditis elegans
    • Ooi, S. L.; Henikoff, J. G.; Henikoff, S. A native chromatin purification system for epigenomic profiling in Caenorhabditis elegans Nucleic Acids Res. 2010, 38 (4) e26
    • (2010) Nucleic Acids Res. , vol.38 , Issue.4 , pp. 26
    • Ooi, S.L.1    Henikoff, J.G.2    Henikoff, S.3
  • 16
    • 33644860985 scopus 로고    scopus 로고
    • The use of biotin tagging in Saccharomyces cerevisiae improves the sensitivity of chromatin immunoprecipitation
    • van Werven, F. J.; Timmers, H. T. The use of biotin tagging in Saccharomyces cerevisiae improves the sensitivity of chromatin immunoprecipitation Nucleic Acids Res. 2006, 34, e33
    • (2006) Nucleic Acids Res. , vol.34 , pp. 33
    • Van Werven, F.J.1    Timmers, H.T.2
  • 17
    • 52949105379 scopus 로고    scopus 로고
    • Use of protein biotinylation in vivo for immunoelectron microscopic localization of a specific protein isoform
    • Viens, A.; Harper, F.; Pichard, E.; Comisso, M.; Pierron, G.; Ogryzko, V. Use of protein biotinylation in vivo for immunoelectron microscopic localization of a specific protein isoform J. Histochem. Cytochem. 2008, 56, 911-919
    • (2008) J. Histochem. Cytochem. , vol.56 , pp. 911-919
    • Viens, A.1    Harper, F.2    Pichard, E.3    Comisso, M.4    Pierron, G.5    Ogryzko, V.6
  • 18
    • 33745842279 scopus 로고    scopus 로고
    • Analysis of human histone H2AZ deposition in vivo argues against its direct role in epigenetic templating mechanisms
    • DOI 10.1128/MCB.00584-06
    • Viens, A.; Mechold, U.; Brouillard, F.; Gilbert, C.; Leclerc, P.; Ogryzko, V. Analysis of human histone H2AZ deposition in vivo argues against its direct role in epigenetic templating mechanisms Mol. Cell. Biol. 2006, 26, 5325-5335 (Pubitemid 44036202)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.14 , pp. 5325-5335
    • Viens, A.1    Mechold, U.2    Brouillard, F.3    Gilbert, C.4    Leclerc, P.5    Ogryzko, V.6
  • 19
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Vorm, O.; Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 1996, 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric Structure and ATPase Activity of the Human TIP48/TIP49 Complex
    • DOI 10.1016/j.jmb.2006.11.030, PII S0022283606015701
    • Puri, T.; Wendler, P.; Sigala, B.; Saibil, H.; Tsaneva, I. R. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex J. Mol. Biol. 2007, 366, 179-192 (Pubitemid 46123336)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 23
    • 0034026194 scopus 로고    scopus 로고
    • The HP1 protein family: Getting a grip on chromatin
    • DOI 10.1016/S0959-437X(00)00058-7
    • Eissenberg, J. C.; Elgin, S. C. The HP1 protein family: getting a grip on chromatin Curr. Opin. Genet. Dev. 2000, 10, 204-210 (Pubitemid 30182255)
    • (2000) Current Opinion in Genetics and Development , vol.10 , Issue.2 , pp. 204-210
    • Eissenberg, J.C.1    Elgin, S.C.2
  • 25
    • 0033838255 scopus 로고    scopus 로고
    • Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: Direct chromoshadow domain-KAP-1 corepressor interaction is essential
    • DOI 10.1128/MCB.20.17.6449-6465.2000
    • Lechner, M. S.; Begg, G. E.; Speicher, D. W.; Rauscher, F. J., 3rd Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain-KAP-1 corepressor interaction is essential Mol. Cell. Biol. 2000, 20, 6449-6465 (Pubitemid 30650232)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.17 , pp. 6449-6465
    • Lechner, M.S.1    Begg, G.E.2    Speicher, D.W.3    Rauscher III, F.J.4
  • 26
    • 0033013868 scopus 로고    scopus 로고
    • KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: A potential role for Kruppel-associated box- zinc finger proteins in heterochromatin-mediated gene silencing
    • Ryan, R. F.; Schultz, D. C.; Ayyanathan, K; Singh, P. B.; Friedman, J. R.; Fredericks, W. J.; Rauscher, F. J., 3rd KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing Mol. Cell. Biol. 1999, 19, 4366-4378 (Pubitemid 29242011)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4366-4378
    • Ryan, R.F.1    Schultz, D.C.2    Ayyanathan, K.3    Singh, P.B.4    Friedman, J.R.5    Fredericks, W.J.6    Rauscher III, F.J.7
  • 27
    • 0033582544 scopus 로고    scopus 로고
    • Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
    • Shibahara, K.; Stillman, B. Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin Cell 1999, 96, 575-585 (Pubitemid 29106844)
    • (1999) Cell , vol.96 , Issue.4 , pp. 575-585
    • Shibahara, K.-I.1    Stillman, B.2
  • 29
    • 33646589676 scopus 로고    scopus 로고
    • Chaperone-mediated assembly of centromeric chromatin in vitro
    • Furuyama, T.; Dalal, Y.; Henikoff, S. Chaperone-mediated assembly of centromeric chromatin in vitro Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 6172-6177
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6172-6177
    • Furuyama, T.1    Dalal, Y.2    Henikoff, S.3
  • 30
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • DOI 10.1083/jcb.152.2.375
    • Chadwick, B. P.; Willard, H. F. A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome J. Cell Biol. 2001, 152, 375-384 (Pubitemid 34285606)
    • (2001) Journal of Cell Biology , vol.152 , Issue.2 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 31
    • 0035394053 scopus 로고    scopus 로고
    • Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome
    • Chadwick, B. P.; Valley, C. M.; Willard, H. F. Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome Nucleic Acids Res. 2001, 29, 2699-2705 (Pubitemid 32685032)
    • (2001) Nucleic Acids Research , vol.29 , Issue.13 , pp. 2699-2705
    • Chadwick, B.P.1    Valley, C.M.2    Willard, H.F.3
  • 32
    • 0035336967 scopus 로고    scopus 로고
    • Histone H2A variants and the inactive X chromosome: Identification of a second macroH2A variant
    • Chadwick, B. P.; Willard, H. F. Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant Hum. Mol. Genet. 2001, 10, 1101-1113 (Pubitemid 32447788)
    • (2001) Human Molecular Genetics , vol.10 , Issue.10 , pp. 1101-1113
    • Chadwick, B.P.1    Willard, H.F.2
  • 34
    • 33845455112 scopus 로고    scopus 로고
    • The analysis of histone modifications
    • DOI 10.1016/j.bbapap.2006.08.009, PII S1570963906002834, Posttranslational Modifications in Proteomics
    • Villar-Garea, A.; Imhof, A. The analysis of histone modifications Biochim. Biophys. Acta 2006, 1764, 1932-1939 (Pubitemid 44895024)
    • (2006) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1764 , Issue.12 , pp. 1932-1939
    • Villar-Garea, A.1    Imhof, A.2
  • 35
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi, S. P.; Rist, B.; Gerber, S. A.; Turecek, F.; Gelb, M. H.; Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 1999, 17, 994-999 (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 36
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 37
    • 47749105733 scopus 로고    scopus 로고
    • Protein-protein interaction detection in vitro and in cells by proximity biotinylation
    • DOI 10.1021/ja801445p
    • Fernandez-Suarez, M.; Chen, T. S.; Ting, A. Y. Protein-protein interaction detection in vitro and in cells by proximity biotinylation J. Am. Chem. Soc. 2008, 130, 9251-9253 (Pubitemid 352031133)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.29 , pp. 9251-9253
    • Fernandez-Suarez, M.1    Chen, T.S.2    Ting, A.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.