메뉴 건너뛰기




Volumn 94, Issue , 2013, Pages 89-109

Mass spectrometry-based identification of proteins interacting with nucleic acids

Author keywords

DNA affinity capture; Mass spectrometry; Protein DNA interactions; Protein RNA interactions; RNA affinity capture; Transcription factors

Indexed keywords

BIOTIN; DNA BINDING PROTEIN; DNA DEPENDENT PROTEIN KINASE; DNA FRAGMENT; FORMALDEHYDE; MITOCHONDRIAL DNA; NUCLEIC ACID; OLIGONUCLEOTIDE; PEPTIDE NUCLEIC ACID; PLASMID DNA; PROTEIN HYDROLYSATE; RESTRICTION ENDONUCLEASE; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; SINGLE STRANDED DNA; SMALL NUCLEAR RIBONUCLEOPROTEIN; STREPTAVIDIN; TELOMERASE REVERSE TRANSCRIPTASE;

EID: 84885051211     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.09.011     Document Type: Review
Times cited : (31)

References (122)
  • 1
    • 68949213578 scopus 로고    scopus 로고
    • Insights from genomic profiling of transcription factors
    • Farnham P. Insights from genomic profiling of transcription factors. Nat Rev Genet 2009, 10:605-616.
    • (2009) Nat Rev Genet , vol.10 , pp. 605-616
    • Farnham, P.1
  • 2
    • 33747881750 scopus 로고    scopus 로고
    • The general transcription machinery and general cofactors
    • Thomas M.C., Chiang C.-M. The general transcription machinery and general cofactors. Crit Rev Biochem Mol Biol 2006, 41:105-178.
    • (2006) Crit Rev Biochem Mol Biol , vol.41 , pp. 105-178
    • Thomas, M.C.1    Chiang, C.-M.2
  • 4
    • 79955668025 scopus 로고    scopus 로고
    • Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation
    • Kato S., Yokoyama A., Fujiki R. Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation. Trends Biochem Sci 2011, 36:272-281.
    • (2011) Trends Biochem Sci , vol.36 , pp. 272-281
    • Kato, S.1    Yokoyama, A.2    Fujiki, R.3
  • 6
    • 82955239833 scopus 로고    scopus 로고
    • Identifying novel transcriptional components controlling energy metabolism
    • Gupta R.K., Rosen E.D., Spiegelman B.M. Identifying novel transcriptional components controlling energy metabolism. Cell Metab 2011, 14:739-745.
    • (2011) Cell Metab , vol.14 , pp. 739-745
    • Gupta, R.K.1    Rosen, E.D.2    Spiegelman, B.M.3
  • 7
    • 84883830383 scopus 로고    scopus 로고
    • Identification of transcription factor-DNA interactions in vivo
    • Odom D.T. Identification of transcription factor-DNA interactions in vivo. Subcell Biochem 2011, 52:175-191.
    • (2011) Subcell Biochem , vol.52 , pp. 175-191
    • Odom, D.T.1
  • 8
    • 77953348282 scopus 로고    scopus 로고
    • Q&A: ChIP-seq technologies and the study of gene regulation
    • Liu E.T., Pott S., Huss M. Q&A: ChIP-seq technologies and the study of gene regulation. BMC Biol 2010, 8:56.
    • (2010) BMC Biol , vol.8 , pp. 56
    • Liu, E.T.1    Pott, S.2    Huss, M.3
  • 9
    • 70349312354 scopus 로고    scopus 로고
    • ChIP-seq: advantages and challenges of a maturing technology
    • Park P.J. ChIP-seq: advantages and challenges of a maturing technology. Nat Rev Genet 2009, 10:669-680.
    • (2009) Nat Rev Genet , vol.10 , pp. 669-680
    • Park, P.J.1
  • 10
    • 84872588984 scopus 로고    scopus 로고
    • Methods for analysis of transcription factor DNA-binding specificity in vitro
    • Springer Netherlands, Dordrecht, T.R. Hughes (Ed.)
    • Jolma A., Taipale J. Methods for analysis of transcription factor DNA-binding specificity in vitro. A handbook of transcription factors 2011, vol. 52:155-173. Springer Netherlands, Dordrecht. T.R. Hughes (Ed.).
    • (2011) A handbook of transcription factors , vol.52 , pp. 155-173
    • Jolma, A.1    Taipale, J.2
  • 11
    • 34247492103 scopus 로고    scopus 로고
    • Footprinting: a method for determining the sequence selectivity, affinity and kinetics of DNA-binding ligands
    • Hampshire A.J., Rusling D.A., Broughton-Head V.J., Fox K.R. Footprinting: a method for determining the sequence selectivity, affinity and kinetics of DNA-binding ligands. Methods 2007, 42:128-140.
    • (2007) Methods , vol.42 , pp. 128-140
    • Hampshire, A.J.1    Rusling, D.A.2    Broughton-Head, V.J.3    Fox, K.R.4
  • 12
    • 43149123786 scopus 로고    scopus 로고
    • Quantitative DNase footprint titration: a tool for analyzing the energetics of protein-DNA interactions
    • Connaghan-Jones K.D., Moody A.D., Bain D.L. Quantitative DNase footprint titration: a tool for analyzing the energetics of protein-DNA interactions. Nat Protoc 2008, 3:900-914.
    • (2008) Nat Protoc , vol.3 , pp. 900-914
    • Connaghan-Jones, K.D.1    Moody, A.D.2    Bain, D.L.3
  • 13
    • 34548169696 scopus 로고    scopus 로고
    • Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions
    • Hellman L.M., Fried M.G. Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions. Nat Protoc 2007, 2:1849-1861.
    • (2007) Nat Protoc , vol.2 , pp. 1849-1861
    • Hellman, L.M.1    Fried, M.G.2
  • 14
    • 84861974460 scopus 로고    scopus 로고
    • In silico discovery of DNA regulatory sites and modules
    • Humana Press, S. Krawetz (Ed.)
    • Benos P.V. In silico discovery of DNA regulatory sites and modules. Bioinformatics for Systems Biology 2009, 353-366. Humana Press. S. Krawetz (Ed.).
    • (2009) Bioinformatics for Systems Biology , pp. 353-366
    • Benos, P.V.1
  • 15
    • 77955487479 scopus 로고    scopus 로고
    • The role of transcription factor binding sites in promoters and their in silico detection
    • Humana Press, Totowa, NJ, S. Krawetz (Ed.)
    • Werner T. The role of transcription factor binding sites in promoters and their in silico detection. Bioinformatics for systems biology 2009, 339-352. Humana Press, Totowa, NJ. S. Krawetz (Ed.).
    • (2009) Bioinformatics for systems biology , pp. 339-352
    • Werner, T.1
  • 16
    • 33644876958 scopus 로고    scopus 로고
    • TRANSFAC(R) and its module TRANSCompel(R): transcriptional gene regulation in eukaryotes
    • Matys V. TRANSFAC(R) and its module TRANSCompel(R): transcriptional gene regulation in eukaryotes. Nucleic Acids Res 2006, 34:D108-D110.
    • (2006) Nucleic Acids Res , vol.34
    • Matys, V.1
  • 17
    • 75549083247 scopus 로고    scopus 로고
    • JASPAR 2010: the greatly expanded open-access database of transcription factor binding profiles
    • Database issue
    • Portales-Casamar E., Thongjuea S., Kwon A.T., Arenillas D., Zhao X., Valen E., et al. JASPAR 2010: the greatly expanded open-access database of transcription factor binding profiles. Nucleic Acids Res 2010, (Database issue):D105-D110.
    • (2010) Nucleic Acids Res
    • Portales-Casamar, E.1    Thongjuea, S.2    Kwon, A.T.3    Arenillas, D.4    Zhao, X.5    Valen, E.6
  • 18
    • 78951488810 scopus 로고    scopus 로고
    • Functional dissection of IME1 transcription using quantitative promoter-reporter screening
    • Kahana S., Pnueli L., Kainth P., Sassi H.E., Andrews B., Kassir Y. Functional dissection of IME1 transcription using quantitative promoter-reporter screening. Genetics 2010, 186:829-841.
    • (2010) Genetics , vol.186 , pp. 829-841
    • Kahana, S.1    Pnueli, L.2    Kainth, P.3    Sassi, H.E.4    Andrews, B.5    Kassir, Y.6
  • 19
    • 80055099276 scopus 로고    scopus 로고
    • Genomic analysis reveals a novel nuclear factor-κB (NF-κB)-binding site in Alu-repetitive elements
    • Antonaki A., Demetriades C., Polyzos A., Banos A., Vatsellas G., Lavigne M.D., et al. Genomic analysis reveals a novel nuclear factor-κB (NF-κB)-binding site in Alu-repetitive elements. J Biol Chem 2011, 286:38768-38782.
    • (2011) J Biol Chem , vol.286 , pp. 38768-38782
    • Antonaki, A.1    Demetriades, C.2    Polyzos, A.3    Banos, A.4    Vatsellas, G.5    Lavigne, M.D.6
  • 20
    • 70350340058 scopus 로고    scopus 로고
    • Profiling the human protein-DNA interactome reveals MAPK1 as a transcriptional repressor of interferon signalling
    • Hu S., Xie Z., Onishi A., Yu X., Jiang L., Lin J., et al. Profiling the human protein-DNA interactome reveals MAPK1 as a transcriptional repressor of interferon signalling. Cell 2009, 139:610-622.
    • (2009) Cell , vol.139 , pp. 610-622
    • Hu, S.1    Xie, Z.2    Onishi, A.3    Yu, X.4    Jiang, L.5    Lin, J.6
  • 21
    • 0000731879 scopus 로고
    • Affinity purification of sequence-specific DNA binding proteins
    • Kadonaga J.T., Tjian R. Affinity purification of sequence-specific DNA binding proteins. Proc Natl Acad Sci U S A 1986, 83:5889-5893.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 5889-5893
    • Kadonaga, J.T.1    Tjian, R.2
  • 22
    • 0035937826 scopus 로고    scopus 로고
    • A role for poly(ADP-ribose) polymerase in the transcriptional regulation of the melanoma growth stimulatory activity (CXCL1) gene expression
    • Nirodi C., NagDas S., Gygi S.P., Olson G., Aebersold R., Richmond A. A role for poly(ADP-ribose) polymerase in the transcriptional regulation of the melanoma growth stimulatory activity (CXCL1) gene expression. J Biol Chem 2001, 276:9366-9374.
    • (2001) J Biol Chem , vol.276 , pp. 9366-9374
    • Nirodi, C.1    NagDas, S.2    Gygi, S.P.3    Olson, G.4    Aebersold, R.5    Richmond, A.6
  • 23
    • 43849096419 scopus 로고    scopus 로고
    • Proteomic analysis of nuclear factors binding to an intronic enhancer in the myelin proteolipid protein gene
    • Dobretsova A., Johnson J.W., Jones R.C., Edmondson R.D., Wight P.A. Proteomic analysis of nuclear factors binding to an intronic enhancer in the myelin proteolipid protein gene. J Neurochem 2008, 105:1979-1995.
    • (2008) J Neurochem , vol.105 , pp. 1979-1995
    • Dobretsova, A.1    Johnson, J.W.2    Jones, R.C.3    Edmondson, R.D.4    Wight, P.A.5
  • 25
    • 59949099230 scopus 로고    scopus 로고
    • A SILAC-based DNA protein interaction screen that identifies candidate binding proteins to functional DNA elements
    • Mittler G., Butter F., Mann M. 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
  • 26
    • 0030746109 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies
    • Yaneva M., Kowalewski T., Lieber M.R. Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies. EMBO J 1997, 16:5098-5112.
    • (1997) EMBO J , vol.16 , pp. 5098-5112
    • Yaneva, M.1    Kowalewski, T.2    Lieber, M.R.3
  • 27
    • 50849088977 scopus 로고    scopus 로고
    • Purification and identification of positive regulators binding to a novel element in the c-Jun promoter
    • Jiang D., Zhou Y., Moxley R.A., Jarrett H.W. Purification and identification of positive regulators binding to a novel element in the c-Jun promoter. Biochemistry 2008, 47:9318-9334.
    • (2008) Biochemistry , vol.47 , pp. 9318-9334
    • Jiang, D.1    Zhou, Y.2    Moxley, R.A.3    Jarrett, H.W.4
  • 28
    • 76749135860 scopus 로고    scopus 로고
    • Purification and identification of a transcription factor, USF-2, binding to E-box element in the promoter of human telomerase reverse transcriptase (hTERT)
    • Jiang S., Galindo M.R., Jarrett H.W. Purification and identification of a transcription factor, USF-2, binding to E-box element in the promoter of human telomerase reverse transcriptase (hTERT). Proteomics 2010, 10:203-211.
    • (2010) Proteomics , vol.10 , pp. 203-211
    • Jiang, S.1    Galindo, M.R.2    Jarrett, H.W.3
  • 29
    • 78650950392 scopus 로고    scopus 로고
    • Identification of the homeobox protein Prx1 (MHox, Prrx-1) as a regulator of osterix expression and mediator of tumor necrosis factor α action in osteoblast differentiation
    • Lu X., Beck G.R., Gilbert L.C., Camalier C.E., Bateman N.W., Hood B.L., et al. Identification of the homeobox protein Prx1 (MHox, Prrx-1) as a regulator of osterix expression and mediator of tumor necrosis factor α action in osteoblast differentiation. J Bone Miner Res 2011, 26:209-219.
    • (2011) J Bone Miner Res , vol.26 , pp. 209-219
    • Lu, X.1    Beck, G.R.2    Gilbert, L.C.3    Camalier, C.E.4    Bateman, N.W.5    Hood, B.L.6
  • 30
    • 77956988666 scopus 로고
    • [11] DNA-cellulose chromatography
    • Academic Press, K.M. Lawrence Grossman (Ed.)
    • Alberts B., Herrick G. [11] DNA-cellulose chromatography. Methods in Enzymology 1971, vol. 21:198-217. Academic Press. K.M. Lawrence Grossman (Ed.).
    • (1971) Methods in Enzymology , vol.21 , pp. 198-217
    • Alberts, B.1    Herrick, G.2
  • 31
    • 0022650157 scopus 로고
    • Purification of nuclear factor I by DNA recognition site affinity chromatography
    • Rosenfeld P.J., Kelly T.J. Purification of nuclear factor I by DNA recognition site affinity chromatography. J Biol Chem 1986, 261:1398-1408.
    • (1986) J Biol Chem , vol.261 , pp. 1398-1408
    • Rosenfeld, P.J.1    Kelly, T.J.2
  • 32
    • 47949099787 scopus 로고    scopus 로고
    • Modern tools for identification of nucleic acid-binding proteins
    • Hégarat N., François J.-C., Praseuth D. Modern tools for identification of nucleic acid-binding proteins. Biochimie 2008, 90:1265-1272.
    • (2008) Biochimie , vol.90 , pp. 1265-1272
    • Hégarat, N.1    François, J.-C.2    Praseuth, D.3
  • 33
    • 27644528492 scopus 로고    scopus 로고
    • Mass spectrometric screening of transcriptional regulators using DNA affinity capture assay
    • Park S.-S., Ko B.J., Kim B.-G. Mass spectrometric screening of transcriptional regulators using DNA affinity capture assay. Anal Biochem 2005, 344:152-154.
    • (2005) Anal Biochem , vol.344 , pp. 152-154
    • Park, S.-S.1    Ko, B.J.2    Kim, B.-G.3
  • 34
    • 0344305798 scopus 로고    scopus 로고
    • Affinity capture of specific DNA-binding proteins for mass spectrometric identification
    • Yaneva M., Tempst P. Affinity capture of specific DNA-binding proteins for mass spectrometric identification. Anal Chem 2003, 75:6437-6448.
    • (2003) Anal Chem , vol.75 , pp. 6437-6448
    • Yaneva, M.1    Tempst, P.2
  • 35
    • 33749054454 scopus 로고    scopus 로고
    • Isolation and mass spectrometry of specific DNA binding proteins
    • Yaneva M., Tempst P. Isolation and mass spectrometry of specific DNA binding proteins. Methods Mol Biol 2006, 338:291-303.
    • (2006) Methods Mol Biol , vol.338 , pp. 291-303
    • Yaneva, M.1    Tempst, P.2
  • 37
    • 48949115074 scopus 로고    scopus 로고
    • Trapping of transcription factors with symmetrical DNA using thiol-disulfide exchange chemistry
    • Panda M., Jiang D., Jarrett H.W. Trapping of transcription factors with symmetrical DNA using thiol-disulfide exchange chemistry. J Chromatogr A 2008, 1202:75-82.
    • (2008) J Chromatogr A , vol.1202 , pp. 75-82
    • Panda, M.1    Jiang, D.2    Jarrett, H.W.3
  • 39
    • 83755172769 scopus 로고    scopus 로고
    • Role of sequence encoded κB DNA geometry in gene regulation by Dorsal
    • Mrinal N., Tomar A., Nagaraju J. Role of sequence encoded κB DNA geometry in gene regulation by Dorsal. Nucleic Acids Res 2011, 39:9574-9591.
    • (2011) Nucleic Acids Res , vol.39 , pp. 9574-9591
    • Mrinal, N.1    Tomar, A.2    Nagaraju, J.3
  • 40
    • 84858189033 scopus 로고    scopus 로고
    • Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA
    • Babayeva N.D., Baranovskaya O.I., Tahirov T.H. Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA. PLoS One 2012, 7:e33698.
    • (2012) PLoS One , vol.7
    • Babayeva, N.D.1    Baranovskaya, O.I.2    Tahirov, T.H.3
  • 41
    • 0004419978 scopus 로고    scopus 로고
    • A gene encoding a novel RFX-associated transactivator is mutated in the majority of MHC class II deficiency patients
    • Masternak K., Barras E., Zufferey M., Conrad B., Corthals G., Aebersold R., et al. A gene encoding a novel RFX-associated transactivator is mutated in the majority of MHC class II deficiency patients. Nat Genet 1998, 20:273-277.
    • (1998) Nat Genet , vol.20 , pp. 273-277
    • Masternak, K.1    Barras, E.2    Zufferey, M.3    Conrad, B.4    Corthals, G.5    Aebersold, R.6
  • 42
    • 0035863877 scopus 로고    scopus 로고
    • DNA-bound transcription factor complexes analysed by mass-spectrometry: binding of novel proteins to the human c-fos SRE and related sequences
    • Drewett V., Molina H., Millar A., Muller S., von Hesler F., Shaw P.E. DNA-bound transcription factor complexes analysed by mass-spectrometry: binding of novel proteins to the human c-fos SRE and related sequences. Nucleic Acids Res 2001, 29:479-487.
    • (2001) Nucleic Acids Res , vol.29 , pp. 479-487
    • Drewett, V.1    Molina, H.2    Millar, A.3    Muller, S.4    von Hesler, F.5    Shaw, P.E.6
  • 44
    • 53549115641 scopus 로고    scopus 로고
    • Quantitative proteomic identification of MAZ as a transcriptional regulator of muscle-specific genes in skeletal and cardiac myocytes
    • Himeda C.L., Ranish J.A., Hauschka S.D. Quantitative proteomic identification of MAZ as a transcriptional regulator of muscle-specific genes in skeletal and cardiac myocytes. Mol Cell Biol 2008, 28:6521-6535.
    • (2008) Mol Cell Biol , vol.28 , pp. 6521-6535
    • Himeda, C.L.1    Ranish, J.A.2    Hauschka, S.D.3
  • 46
    • 21744439811 scopus 로고    scopus 로고
    • YB-1 represses AP1-dependent gene transactivation and interacts with an AP-1 DNA sequence
    • Samuel S., Twizere J.-C., Bernstein L.R. YB-1 represses AP1-dependent gene transactivation and interacts with an AP-1 DNA sequence. Biochem J 2005, 388:921-928.
    • (2005) Biochem J , vol.388 , pp. 921-928
    • Samuel, S.1    Twizere, J.-C.2    Bernstein, L.R.3
  • 48
    • 84870625990 scopus 로고    scopus 로고
    • Unbiased proteomic analysis of proteins interacting with the HIV-1 5'LTR sequence: role of the transcription factor Meis
    • (Epub 2012 Aug 16)
    • Tacheny A., Michel S., Dieu M., Payen L., Arnould T., Renard P. Unbiased proteomic analysis of proteins interacting with the HIV-1 5'LTR sequence: role of the transcription factor Meis. Nucleic Acids Res 2012, 40(21):e168. (Epub 2012 Aug 16). 10.1093/nar/gks733.
    • (2012) Nucleic Acids Res , vol.40 , Issue.21
    • Tacheny, A.1    Michel, S.2    Dieu, M.3    Payen, L.4    Arnould, T.5    Renard, P.6
  • 49
    • 0024319092 scopus 로고
    • Magnetic DNA affinity purification of yeast transcription factor tau-a new purification principle for the ultrarapid isolation of near homogeneous factor
    • Gabrielsen O.S., Hornes E., Korsnes L., Ruet A., Oyen T.B. Magnetic DNA affinity purification of yeast transcription factor tau-a new purification principle for the ultrarapid isolation of near homogeneous factor. Nucleic Acids Res 1989, 17:6253-6267.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6253-6267
    • Gabrielsen, O.S.1    Hornes, E.2    Korsnes, L.3    Ruet, A.4    Oyen, T.B.5
  • 50
    • 0037047250 scopus 로고    scopus 로고
    • Oligonucleotide trapping method for purification of transcription factors
    • Gadgil H., Jarrett H.W. Oligonucleotide trapping method for purification of transcription factors. J Chromatogr A 2002, 966:99-110.
    • (2002) J Chromatogr A , vol.966 , pp. 99-110
    • Gadgil, H.1    Jarrett, H.W.2
  • 51
    • 33750012915 scopus 로고    scopus 로고
    • Promoter trapping of c-jun promoter-binding transcription factors
    • Jiang D., Moxley R.A., Jarrett H.W. Promoter trapping of c-jun promoter-binding transcription factors. J Chromatogr A 2006, 1133:83-94.
    • (2006) J Chromatogr A , vol.1133 , pp. 83-94
    • Jiang, D.1    Moxley, R.A.2    Jarrett, H.W.3
  • 52
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg O.G., Winter R.B., von Hippel P.H. Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 1981, 20:6929-6948.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    von Hippel, P.H.3
  • 53
    • 84868324280 scopus 로고    scopus 로고
    • Unbiased discovery of interactions at a control locus driving expression of the cancer-specific therapeutic and diagnostic target, mesothelin
    • Ren Y.R., Chaerkady R., Hu S., Wan J., Qian J., Zhu H., et al. Unbiased discovery of interactions at a control locus driving expression of the cancer-specific therapeutic and diagnostic target, mesothelin. J Proteome Res 2012, 11(11):5301-5310.
    • (2012) J Proteome Res , vol.11 , Issue.11 , pp. 5301-5310
    • Ren, Y.R.1    Chaerkady, R.2    Hu, S.3    Wan, J.4    Qian, J.5    Zhu, H.6
  • 54
    • 0033582269 scopus 로고    scopus 로고
    • Tissue-specific and developmental stage-specific DNA binding by a mammalian SWI/SNF complex associated with human fetal-to-adult globin gene switching
    • O'Neill D., Yang J., Erdjument-Bromage H., Bornschlegel K., Tempst P., Bank A. Tissue-specific and developmental stage-specific DNA binding by a mammalian SWI/SNF complex associated with human fetal-to-adult globin gene switching. Proc Natl Acad Sci U S A 1999, 96:349-354.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 349-354
    • O'Neill, D.1    Yang, J.2    Erdjument-Bromage, H.3    Bornschlegel, K.4    Tempst, P.5    Bank, A.6
  • 55
    • 77957773762 scopus 로고    scopus 로고
    • A multiprotein complex necessary for both transcription and DNA replication at the β-globin locus
    • Karmakar S., Mahajan M.C., Schulz V., Boyapaty G., Weissman S.M. A multiprotein complex necessary for both transcription and DNA replication at the β-globin locus. EMBO J 2010, 29:3260-3271.
    • (2010) EMBO J , vol.29 , pp. 3260-3271
    • Karmakar, S.1    Mahajan, M.C.2    Schulz, V.3    Boyapaty, G.4    Weissman, S.M.5
  • 56
    • 33747191722 scopus 로고    scopus 로고
    • Probing early growth response 1 interacting proteins at the active promoter in osteoblast cells using oligoprecipitation and mass spectrometry
    • Meng Z., Camalier C.E., Lucas D.A., Veenstra T.D., Beck G.R., Conrads T.P. Probing early growth response 1 interacting proteins at the active promoter in osteoblast cells using oligoprecipitation and mass spectrometry. J Proteome Res 2006, 5:1931-1939.
    • (2006) J Proteome Res , vol.5 , pp. 1931-1939
    • Meng, Z.1    Camalier, C.E.2    Lucas, D.A.3    Veenstra, T.D.4    Beck, G.R.5    Conrads, T.P.6
  • 57
    • 1342282907 scopus 로고    scopus 로고
    • Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer
    • Himeda C.L., Ranish J.A., Angello J.C., Maire P., Aebersold R., Hauschka S.D. Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer. Mol Cell Biol 2004, 24:2132-2143.
    • (2004) Mol Cell Biol , vol.24 , pp. 2132-2143
    • Himeda, C.L.1    Ranish, J.A.2    Angello, J.C.3    Maire, P.4    Aebersold, R.5    Hauschka, S.D.6
  • 58
    • 0035894409 scopus 로고    scopus 로고
    • A new analytical scale DNA affinity binding assay for analyses of specific protein-DNA interactions
    • Kumar N.V., Bernstein L.R. A new analytical scale DNA affinity binding assay for analyses of specific protein-DNA interactions. Anal Biochem 2001, 299:203-210.
    • (2001) Anal Biochem , vol.299 , pp. 203-210
    • Kumar, N.V.1    Bernstein, L.R.2
  • 59
    • 34548607098 scopus 로고    scopus 로고
    • YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site
    • Samuel S., Beifuss K.K., Bernstein L.R. YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site. Biochim Biophys Acta 2007, 1769:525-531.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 525-531
    • Samuel, S.1    Beifuss, K.K.2    Bernstein, L.R.3
  • 60
    • 56449088387 scopus 로고    scopus 로고
    • Members of the NuRD chromatin remodeling complex interact with AUF1 in developing cortical neurons
    • Lee C., Gyorgy A., Maric D., Sadri N., Schneider R.J., Barker J.L., et al. Members of the NuRD chromatin remodeling complex interact with AUF1 in developing cortical neurons. Cereb Cortex 2008, 18:2909-2919.
    • (2008) Cereb Cortex , vol.18 , pp. 2909-2919
    • Lee, C.1    Gyorgy, A.2    Maric, D.3    Sadri, N.4    Schneider, R.J.5    Barker, J.L.6
  • 61
    • 76649092342 scopus 로고    scopus 로고
    • Quantitative nanoproteomics for protein complexes (QNanoPX) related to estrogen transcriptional action
    • Cheng P.-C., Chang H.-K., Chen S.-H. Quantitative nanoproteomics for protein complexes (QNanoPX) related to estrogen transcriptional action. Mol Cell Proteomics 2010, 9:209-224.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 209-224
    • Cheng, P.-C.1    Chang, H.-K.2    Chen, S.-H.3
  • 62
    • 84861182619 scopus 로고    scopus 로고
    • S-Glutathionylation signaling in cell biology: progress and prospects
    • Pastore A., Piemonte F. S-Glutathionylation signaling in cell biology: progress and prospects. Eur J Pharm Sci 2012, 46:279-292.
    • (2012) Eur J Pharm Sci , vol.46 , pp. 279-292
    • Pastore, A.1    Piemonte, F.2
  • 64
    • 0037677203 scopus 로고    scopus 로고
    • PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4
    • Arora T., Liu B., He H., Kim J., Murphy T.L., Murphy K.M., et al. PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4. J Biol Chem 2003, 278:21327-21330.
    • (2003) J Biol Chem , vol.278 , pp. 21327-21330
    • Arora, T.1    Liu, B.2    He, H.3    Kim, J.4    Murphy, T.L.5    Murphy, K.M.6
  • 66
    • 68349127402 scopus 로고    scopus 로고
    • Mass spectrometric screening of transcriptional regulators involved in antibiotic biosynthesis in streptomyces coelicolor A3(2)
    • Park S.-S., Yang Y.-H., Song E., Kim E.-J., Kim W.S., Sohng J.K., et al. Mass spectrometric screening of transcriptional regulators involved in antibiotic biosynthesis in streptomyces coelicolor A3(2). J Ind Microbiol Biotechnol 2009, 36:1073-1083.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 1073-1083
    • Park, S.-S.1    Yang, Y.-H.2    Song, E.3    Kim, E.-J.4    Kim, W.S.5    Sohng, J.K.6
  • 67
    • 0344034180 scopus 로고    scopus 로고
    • Solution study of the NF-κB p50-DNA complex by UV laser protein-DNA cross-linking¶
    • Angelov D., Charra M., Müller C.W., Cadet J., Dimitrov S. Solution study of the NF-κB p50-DNA complex by UV laser protein-DNA cross-linking¶. Photochem Photobiol 2003, 77:592-596.
    • (2003) Photochem Photobiol , vol.77 , pp. 592-596
    • Angelov, D.1    Charra, M.2    Müller, C.W.3    Cadet, J.4    Dimitrov, S.5
  • 68
    • 0037108987 scopus 로고    scopus 로고
    • Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation
    • Hirsch J.D., Eslamizar L., Filanoski B.J., Malekzadeh N., Haugland R.P., Beechem J.M., et al. Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation. Anal Biochem 2002, 308:343-357.
    • (2002) Anal Biochem , vol.308 , pp. 343-357
    • Hirsch, J.D.1    Eslamizar, L.2    Filanoski, B.J.3    Malekzadeh, N.4    Haugland, R.P.5    Beechem, J.M.6
  • 69
    • 58149085861 scopus 로고    scopus 로고
    • Purification of proteins associated with specific genomic Loci
    • Déjardin J., Kingston R.E. 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
  • 70
    • 70349780947 scopus 로고    scopus 로고
    • Biochemical isolation of mtDNA nucleoids from animal cells
    • Bogenhagen D.F. Biochemical isolation of mtDNA nucleoids from animal cells. Methods Mol Biol 2009, 554:3-14.
    • (2009) Methods Mol Biol , vol.554 , pp. 3-14
    • Bogenhagen, D.F.1
  • 71
    • 63249132195 scopus 로고    scopus 로고
    • DNA sampling: a method for probing protein binding at specific loci on bacterial chromosomes
    • Butala M., Busby S.J.W., Lee D.J. DNA sampling: a method for probing protein binding at specific loci on bacterial chromosomes. Nucleic Acids Res 2009, 37:e37.
    • (2009) Nucleic Acids Res , vol.37
    • Butala, M.1    Busby, S.J.W.2    Lee, D.J.3
  • 72
    • 84864308607 scopus 로고
    • Mitochondrial DNA, nucleoid structure
    • Bogenhagen D.F. Mitochondrial DNA, nucleoid structure. Biochim Biophys Acta 1819, 2012:914-920.
    • (1819) Biochim Biophys Acta , vol.2012 , pp. 914-920
    • Bogenhagen, D.F.1
  • 73
    • 80054776386 scopus 로고    scopus 로고
    • Sequence-specific capture of protein-DNA complexes for mass spectrometric protein identification
    • Wu C.-H., Chen S., Shortreed M.R., Kreitinger G.M., Yuan Y., Frey B.L., et al. Sequence-specific capture of protein-DNA complexes for mass spectrometric protein identification. PLoS One 2011, 6:e26217.
    • (2011) PLoS One , vol.6
    • Wu, C.-H.1    Chen, S.2    Shortreed, M.R.3    Kreitinger, G.M.4    Yuan, Y.5    Frey, B.L.6
  • 74
    • 73949130070 scopus 로고    scopus 로고
    • Dissecting the expression dynamics of RNA-binding proteins in posttranscriptional regulatory networks
    • Mittal N., Roy N., Babu M.M., Janga S.C. Dissecting the expression dynamics of RNA-binding proteins in posttranscriptional regulatory networks. Proc Natl Acad Sci U S A 2009, 106:20300-20305.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20300-20305
    • Mittal, N.1    Roy, N.2    Babu, M.M.3    Janga, S.C.4
  • 75
    • 60949088035 scopus 로고    scopus 로고
    • Mapping of RNA-protein interactions
    • Gopinath S.C.B. Mapping of RNA-protein interactions. Anal Chim Acta 2009, 636:117-128.
    • (2009) Anal Chim Acta , vol.636 , pp. 117-128
    • Gopinath, S.C.B.1
  • 76
    • 77950295790 scopus 로고    scopus 로고
    • Minireview: global regulation and dynamics of ribonucleic acid
    • Keene J.D. Minireview: global regulation and dynamics of ribonucleic acid. Endocrinology 2010, 151:1391-1397.
    • (2010) Endocrinology , vol.151 , pp. 1391-1397
    • Keene, J.D.1
  • 77
    • 54949148332 scopus 로고    scopus 로고
    • Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system
    • Hogan D.J., Riordan D.P., Gerber A.P., Herschlag D., Brown P.O. Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system. PLoS Biol 2008, 6:e255.
    • (2008) PLoS Biol , vol.6
    • Hogan, D.J.1    Riordan, D.P.2    Gerber, A.P.3    Herschlag, D.4    Brown, P.O.5
  • 78
    • 77950920903 scopus 로고    scopus 로고
    • Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP
    • Hafner M., Landthaler M., Burger L., Khorshid M., Hausser J., Berninger P., et al. Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 2010, 141:129-141.
    • (2010) Cell , vol.141 , pp. 129-141
    • Hafner, M.1    Landthaler, M.2    Burger, L.3    Khorshid, M.4    Hausser, J.5    Berninger, P.6
  • 79
    • 0032726856 scopus 로고    scopus 로고
    • Optimized RNA gel-shift and UV cross-linking assays for characterization of cytoplasmic RNA-protein interactions
    • [1042]
    • Thomson A.M., Rogers J.T., Walker C.E., Staton J.M., Leedman P.J. Optimized RNA gel-shift and UV cross-linking assays for characterization of cytoplasmic RNA-protein interactions. Biotechniques 1999, 27:1032-1039. [1042].
    • (1999) Biotechniques , vol.27 , pp. 1032-1039
    • Thomson, A.M.1    Rogers, J.T.2    Walker, C.E.3    Staton, J.M.4    Leedman, P.J.5
  • 80
    • 84555195894 scopus 로고    scopus 로고
    • Evaluating posttranscriptional regulation of cytokine genes
    • Rattenbacher B., Bohjanen P.R. Evaluating posttranscriptional regulation of cytokine genes. Methods Mol Biol 2012, 820:71-89.
    • (2012) Methods Mol Biol , vol.820 , pp. 71-89
    • Rattenbacher, B.1    Bohjanen, P.R.2
  • 82
    • 81255210913 scopus 로고    scopus 로고
    • Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3' UTR structures
    • Ward A.M., Bidet K., Yinglin A., Ler S.G., Hogue K., Blackstock W., et al. Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3' UTR structures. RNA Biol 2011, 8:1173-1186.
    • (2011) RNA Biol , vol.8 , pp. 1173-1186
    • Ward, A.M.1    Bidet, K.2    Yinglin, A.3    Ler, S.G.4    Hogue, K.5    Blackstock, W.6
  • 83
    • 84876735323 scopus 로고    scopus 로고
    • Protein interactions with piALU RNA indicates putative participation of retroRNA in the cell cycle, DNA repair and chromatin assembly
    • Blackwell B.J., Lopez M.F., Wang J., Krastins B., Sarracino D., Tollervey J.R., et al. Protein interactions with piALU RNA indicates putative participation of retroRNA in the cell cycle, DNA repair and chromatin assembly. Mob Genet Elem 2012, 2:26-35.
    • (2012) Mob Genet Elem , vol.2 , pp. 26-35
    • Blackwell, B.J.1    Lopez, M.F.2    Wang, J.3    Krastins, B.4    Sarracino, D.5    Tollervey, J.R.6
  • 84
    • 38349140689 scopus 로고    scopus 로고
    • The regulatory element in the 3'-untranslated region of human papillomavirus 16 inhibits expression by binding CUG-binding protein 1
    • Goraczniak R., Gunderson S.I. The regulatory element in the 3'-untranslated region of human papillomavirus 16 inhibits expression by binding CUG-binding protein 1. J Biol Chem 2008, 283:2286-2296.
    • (2008) J Biol Chem , vol.283 , pp. 2286-2296
    • Goraczniak, R.1    Gunderson, S.I.2
  • 85
    • 33646777450 scopus 로고    scopus 로고
    • Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes
    • Bose S.K., Sengupta T.K., Bandyopadhyay S., Spicer E.K. Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes. Biochem J 2006, 396:99-107.
    • (2006) Biochem J , vol.396 , pp. 99-107
    • Bose, S.K.1    Sengupta, T.K.2    Bandyopadhyay, S.3    Spicer, E.K.4
  • 86
    • 33745592162 scopus 로고    scopus 로고
    • Identification of cellular factors associated with the 3'-nontranslated region of the hepatitis C virus genome
    • Harris D., Zhang Z., Chaubey B., Pandey V.N. Identification of cellular factors associated with the 3'-nontranslated region of the hepatitis C virus genome. Mol Cell Proteomics 2006, 5:1006-1018.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1006-1018
    • Harris, D.1    Zhang, Z.2    Chaubey, B.3    Pandey, V.N.4
  • 87
    • 79955379829 scopus 로고    scopus 로고
    • RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site
    • Kar A., Fushimi K., Zhou X., Ray P., Shi C., Chen X., et al. RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice site. Mol Cell Biol 2011, 31:1812-1821.
    • (2011) Mol Cell Biol , vol.31 , pp. 1812-1821
    • Kar, A.1    Fushimi, K.2    Zhou, X.3    Ray, P.4    Shi, C.5    Chen, X.6
  • 90
    • 0031829287 scopus 로고    scopus 로고
    • A sequence-specific RNA-binding protein complements apobec-1 To edit apolipoprotein B mRNA
    • Mehta A., Driscoll D.M. A sequence-specific RNA-binding protein complements apobec-1 To edit apolipoprotein B mRNA. Mol Cell Biol 1998, 18:4426-4432.
    • (1998) Mol Cell Biol , vol.18 , pp. 4426-4432
    • Mehta, A.1    Driscoll, D.M.2
  • 91
    • 31144443606 scopus 로고    scopus 로고
    • The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex
    • Patel G.P., Ma S., Bag J. The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex. Nucleic Acids Res 2005, 33:7074-7089.
    • (2005) Nucleic Acids Res , vol.33 , pp. 7074-7089
    • Patel, G.P.1    Ma, S.2    Bag, J.3
  • 92
    • 81755176093 scopus 로고    scopus 로고
    • HnRNP A1 and hnRNP F modulate the alternative splicing of exon 11 of the insulin receptor gene
    • Talukdar I., Sen S., Urbano R., Thompson J., Yates J.R., Webster N.J.G. hnRNP A1 and hnRNP F modulate the alternative splicing of exon 11 of the insulin receptor gene. PLoS One 2011, 6:e27869.
    • (2011) PLoS One , vol.6
    • Talukdar, I.1    Sen, S.2    Urbano, R.3    Thompson, J.4    Yates, J.R.5    Webster, N.J.G.6
  • 93
    • 84871740038 scopus 로고    scopus 로고
    • HnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition
    • Peddigari S., Li P.W.-L., Rabe J.L., Martin S.L. hnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition. Nucleic Acids Res 2013, 41:575-585.
    • (2013) Nucleic Acids Res , vol.41 , pp. 575-585
    • Peddigari, S.1    Li, P.W.-L.2    Rabe, J.L.3    Martin, S.L.4
  • 94
    • 67649774581 scopus 로고    scopus 로고
    • Unbiased RNA-protein interaction screen by quantitative proteomics
    • Butter F., Scheibe M., Mörl M., Mann M. Unbiased RNA-protein interaction screen by quantitative proteomics. Proc Natl Acad Sci U S A 2009, 106:10626-10631.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 10626-10631
    • Butter, F.1    Scheibe, M.2    Mörl, M.3    Mann, M.4
  • 96
    • 84934441756 scopus 로고    scopus 로고
    • RNA affinity tags for the rapid purification and investigation of RNAs and RNA-protein complexes
    • Walker S.C., Scott F.H., Srisawat C., Engelke D.R. RNA affinity tags for the rapid purification and investigation of RNAs and RNA-protein complexes. Methods Mol Biol 2008, 488:23-40.
    • (2008) Methods Mol Biol , vol.488 , pp. 23-40
    • Walker, S.C.1    Scott, F.H.2    Srisawat, C.3    Engelke, D.R.4
  • 98
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson D.S., Szostak J.W. In vitro selection of functional nucleic acids. Annu Rev Biochem 1999, 68:611-647.
    • (1999) Annu Rev Biochem , vol.68 , pp. 611-647
    • Wilson, D.S.1    Szostak, J.W.2
  • 99
    • 34548778175 scopus 로고    scopus 로고
    • The U1 snRNA hairpin II as a RNA affinity tag for selecting snoRNP complexes
    • Piekna-Przybylska D., Liu B., Fournier M.J. The U1 snRNA hairpin II as a RNA affinity tag for selecting snoRNP complexes. Methods Enzymol 2007, 425:317-353.
    • (2007) Methods Enzymol , vol.425 , pp. 317-353
    • Piekna-Przybylska, D.1    Liu, B.2    Fournier, M.J.3
  • 100
    • 38949107432 scopus 로고    scopus 로고
    • Tethering of proteins to RNAs by bacteriophage proteins
    • Keryer-Bibens C., Barreau C., Osborne H.B. Tethering of proteins to RNAs by bacteriophage proteins. Biol Cell 2008, 100:125-138.
    • (2008) Biol Cell , vol.100 , pp. 125-138
    • Keryer-Bibens, C.1    Barreau, C.2    Osborne, H.B.3
  • 101
    • 0035001466 scopus 로고    scopus 로고
    • Streptavidin aptamers: affinity tags for the study of RNAs and ribonucleoproteins
    • Srisawat C., Engelke D.R. Streptavidin aptamers: affinity tags for the study of RNAs and ribonucleoproteins. RNA 2001, 7:632-641.
    • (2001) RNA , vol.7 , pp. 632-641
    • Srisawat, C.1    Engelke, D.R.2
  • 102
    • 0024385955 scopus 로고
    • Antisense probing of the human U4/U6 snRNP with biotinylated 2'-OMe RNA oligonucleotides
    • Blencowe B.J., Sproat B.S., Ryder U., Barabino S., Lamond A.I. Antisense probing of the human U4/U6 snRNP with biotinylated 2'-OMe RNA oligonucleotides. Cell 1989, 59:531-539.
    • (1989) Cell , vol.59 , pp. 531-539
    • Blencowe, B.J.1    Sproat, B.S.2    Ryder, U.3    Barabino, S.4    Lamond, A.I.5
  • 103
    • 0029763191 scopus 로고    scopus 로고
    • Purification of telomerase from Euplotes aediculatus: requirement of a primer 3' overhang
    • Lingner J., Cech T.R. Purification of telomerase from Euplotes aediculatus: requirement of a primer 3' overhang. Proc Natl Acad Sci U S A 1996, 93:10712-10717.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10712-10717
    • Lingner, J.1    Cech, T.R.2
  • 104
    • 77953640328 scopus 로고    scopus 로고
    • Identification of novel ribonucleo-protein complexes from the brain-specific snoRNA MBII-52
    • Soeno Y., Taya Y., Stasyk T., Huber L.A., Aoba T., Hüttenhofer A. Identification of novel ribonucleo-protein complexes from the brain-specific snoRNA MBII-52. RNA 2010, 16:1293-1300.
    • (2010) RNA , vol.16 , pp. 1293-1300
    • Soeno, Y.1    Taya, Y.2    Stasyk, T.3    Huber, L.A.4    Aoba, T.5    Hüttenhofer, A.6
  • 105
    • 79953321612 scopus 로고    scopus 로고
    • Quantitative profiling of in vivo-assembled RNA-protein complexes using a novel integrated proteomic approach
    • [M110.007385]
    • Tsai B.P., Wang X., Huang L., Waterman M.L. Quantitative profiling of in vivo-assembled RNA-protein complexes using a novel integrated proteomic approach. Mol Cell Proteomics 2011, 10. [M110.007385].
    • (2011) Mol Cell Proteomics , vol.10
    • Tsai, B.P.1    Wang, X.2    Huang, L.3    Waterman, M.L.4
  • 106
    • 79952202326 scopus 로고    scopus 로고
    • PAIR technology: exon-specific RNA-binding protein isolation in live cells
    • Bell T.J., Eiríksdóttir E., Langel U., Eberwine J. PAIR technology: exon-specific RNA-binding protein isolation in live cells. Methods Mol Biol 2011, 683:473-486.
    • (2011) Methods Mol Biol , vol.683 , pp. 473-486
    • Bell, T.J.1    Eiríksdóttir, E.2    Langel, U.3    Eberwine, J.4
  • 107
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates J.R., Ruse C.I., Nakorchevsky A. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 2009, 11:49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 108
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB
    • Ranish J.A., Yudkovsky N., Hahn S. Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB. Genes Dev 1999, 13:49-63.
    • (1999) Genes Dev , vol.13 , pp. 49-63
    • Ranish, J.A.1    Yudkovsky, N.2    Hahn, S.3
  • 109
    • 84865595374 scopus 로고    scopus 로고
    • The expanding field of SILAC
    • Ong S.-E. The expanding field of SILAC. Anal Bioanal Chem 2012, 404:967-976.
    • (2012) Anal Bioanal Chem , vol.404 , pp. 967-976
    • Ong, S.-E.1
  • 110
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 2006, 7:952-958.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 112
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
    • Bantscheff M., Lemeer S., Savitski M.M., Kuster B. Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal Bioanal Chem 2012, 404:939-965.
    • (2012) Anal Bioanal Chem , vol.404 , pp. 939-965
    • Bantscheff, M.1    Lemeer, S.2    Savitski, M.M.3    Kuster, B.4
  • 114
    • 39049195201 scopus 로고    scopus 로고
    • Quantitative proteomics by stable isotope labeling and mass spectrometry
    • Humana Press, R. Matthiesen (Ed.)
    • Pan S., Aebersold R. Quantitative proteomics by stable isotope labeling and mass spectrometry. Mass spectrometry data analysis in proteomics 2007, 209-218. Humana Press. R. Matthiesen (Ed.).
    • (2007) Mass spectrometry data analysis in proteomics , pp. 209-218
    • Pan, S.1    Aebersold, R.2
  • 115
    • 77954354238 scopus 로고    scopus 로고
    • KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sites
    • Himeda C.L., Ranish J.A., Pearson R.C.M., Crossley M., Hauschka S.D. KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sites. Mol Cell Biol 2010, 30:3430-3443.
    • (2010) Mol Cell Biol , vol.30 , pp. 3430-3443
    • Himeda, C.L.1    Ranish, J.A.2    Pearson, R.C.M.3    Crossley, M.4    Hauschka, S.D.5
  • 116
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu J.-L., Huang S.-Y., Chow N.-H., Chen S.-H. Stable-isotope dimethyl labeling for quantitative proteomics. Anal Chem 2003, 75:6843-6852.
    • (2003) Anal Chem , vol.75 , pp. 6843-6852
    • Hsu, J.-L.1    Huang, S.-Y.2    Chow, N.-H.3    Chen, S.-H.4
  • 117
    • 77950369832 scopus 로고    scopus 로고
    • A domesticated transposon mediates the effects of a single-nucleotide polymorphism responsible for enhanced muscle growth
    • Butter F., Kappei D., Buchholz F., Vermeulen M., Mann M. A domesticated transposon mediates the effects of a single-nucleotide polymorphism responsible for enhanced muscle growth. EMBO Rep 2010, 11:305-311.
    • (2010) EMBO Rep , vol.11 , pp. 305-311
    • Butter, F.1    Kappei, D.2    Buchholz, F.3    Vermeulen, M.4    Mann, M.5
  • 118
    • 79551474552 scopus 로고    scopus 로고
    • Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome
    • Ly L., Wasinger V.C. Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome. Proteomics 2011, 11:513-534.
    • (2011) Proteomics , vol.11 , pp. 513-534
    • Ly, L.1    Wasinger, V.C.2
  • 119
    • 74549226503 scopus 로고    scopus 로고
    • HMGB proteins: interactions with DNA and chromatin
    • Stros M. HMGB proteins: interactions with DNA and chromatin. Biochim Biophys Acta 2010, 1799:101-113.
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 101-113
    • Stros, M.1
  • 120
    • 0742306815 scopus 로고    scopus 로고
    • Computational prediction of transcription-factor binding site locations
    • Bulyk M.L. Computational prediction of transcription-factor binding site locations. Genome Biol 2003, 5:201.
    • (2003) Genome Biol , vol.5 , pp. 201
    • Bulyk, M.L.1
  • 121
    • 77249087077 scopus 로고    scopus 로고
    • DNA-centered approaches to characterize regulatory protein-DNA interaction complexes
    • Simicevic J., Deplancke B. DNA-centered approaches to characterize regulatory protein-DNA interaction complexes. Mol Biosyst 2010, 6:462-468.
    • (2010) Mol Biosyst , vol.6 , pp. 462-468
    • Simicevic, J.1    Deplancke, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.