메뉴 건너뛰기




Volumn 449, Issue C, 2008, Pages 317-342

Chapter 15 Co-Immunoprecipitation Techniques for Assessing RNA-Protein Interactions In Vivo

Author keywords

[No Author keywords available]

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; RNA; RNA POLYMERASE;

EID: 59649092360     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)02415-4     Document Type: Chapter
Times cited : (29)

References (61)
  • 1
    • 3343003673 scopus 로고    scopus 로고
    • Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes
    • Abruzzi K.C., Lacadie S., and Rosbash M. Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes. EMBO J 23 (2004) 2620-2631
    • (2004) EMBO J , vol.23 , pp. 2620-2631
    • Abruzzi, K.C.1    Lacadie, S.2    Rosbash, M.3
  • 2
    • 33344478052 scopus 로고    scopus 로고
    • Regulation of yeast NRD1 expression by premature transcription termination
    • Arigo J.T., Carroll K.L., Ames J.M., and Corden J.L. Regulation of yeast NRD1 expression by premature transcription termination. Mol. Cell 21 (2006) 641-651
    • (2006) Mol. Cell , vol.21 , pp. 641-651
    • Arigo, J.T.1    Carroll, K.L.2    Ames, J.M.3    Corden, J.L.4
  • 3
    • 15944429355 scopus 로고    scopus 로고
    • DNA-protein crosslinks: Their induction, repair, and biological consequences
    • Barker S., Weinfeld M., and Murray D. DNA-protein crosslinks: Their induction, repair, and biological consequences. Mutat. Res. 589 (2005) 111-135
    • (2005) Mutat. Res. , vol.589 , pp. 111-135
    • Barker, S.1    Weinfeld, M.2    Murray, D.3
  • 4
    • 31144448042 scopus 로고    scopus 로고
    • AU-rich elements and associated factors: Are there unifying principles
    • Barreau C., Paillard L., and Osborne H.B. AU-rich elements and associated factors: Are there unifying principles. Nucleic Acids Res. 33 (2005) 7138-7150
    • (2005) Nucleic Acids Res. , vol.33 , pp. 7138-7150
    • Barreau, C.1    Paillard, L.2    Osborne, H.B.3
  • 6
    • 0037133254 scopus 로고    scopus 로고
    • Transcription: Surprising role for an elusive small nuclear RNA
    • Blencowe B.J. Transcription: Surprising role for an elusive small nuclear RNA. Curr. Biol. 12 (2002) R147-R149
    • (2002) Curr. Biol. , vol.12
    • Blencowe, B.J.1
  • 8
    • 0036121097 scopus 로고    scopus 로고
    • Open reading frame 50 protein of Kaposi's sarcoma-associated herpesvirus directly activates the viral PAN and K12 genes by binding to related response elements
    • Chang P.J., Shedd D., Gradoville L., Cho M.S., Chen L.W., Chang J., and Miller G. Open reading frame 50 protein of Kaposi's sarcoma-associated herpesvirus directly activates the viral PAN and K12 genes by binding to related response elements. J. Virol. 76 (2002) 3168-3178
    • (2002) J. Virol. , vol.76 , pp. 3168-3178
    • Chang, P.J.1    Shedd, D.2    Gradoville, L.3    Cho, M.S.4    Chen, L.W.5    Chang, J.6    Miller, G.7
  • 9
    • 0021689433 scopus 로고
    • Monoclonal antibody characterization of the C proteins of heterogeneous nuclear ribonucleoprotein complexes in vertebrate cells
    • Choi Y.D., and Dreyfuss G. Monoclonal antibody characterization of the C proteins of heterogeneous nuclear ribonucleoprotein complexes in vertebrate cells. J. Cell Biol. 99 (1984) 1997-2204
    • (1984) J. Cell Biol. , vol.99 , pp. 1997-2204
    • Choi, Y.D.1    Dreyfuss, G.2
  • 10
    • 0036352777 scopus 로고    scopus 로고
    • Tethered function assays using 3′ untranslated regions
    • Coller J., and Wickens M. Tethered function assays using 3′ untranslated regions. Methods 26 (2002) 142-150
    • (2002) Methods , vol.26 , pp. 142-150
    • Coller, J.1    Wickens, M.2
  • 11
    • 33845662140 scopus 로고    scopus 로고
    • Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element
    • Conrad N.K., Mili S., Marshall E.L., Shu M.D., and Steitz J.A. Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element. Mol. Cell 24 (2006) 943-953
    • (2006) Mol. Cell , vol.24 , pp. 943-953
    • Conrad, N.K.1    Mili, S.2    Marshall, E.L.3    Shu, M.D.4    Steitz, J.A.5
  • 12
    • 34547510230 scopus 로고    scopus 로고
    • Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail
    • Conrad N.K., Shu M.D., Uyhazi K.E., and Steitz J.A. Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail. Proc. Natl. Acad. Sci. USA 104 (2007) 10412-10417
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10412-10417
    • Conrad, N.K.1    Shu, M.D.2    Uyhazi, K.E.3    Steitz, J.A.4
  • 13
    • 20044369601 scopus 로고    scopus 로고
    • A Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts
    • Conrad N.K., and Steitz J.A. A Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts. EMBO J 24 (2005) 1831-1841
    • (2005) EMBO J , vol.24 , pp. 1831-1841
    • Conrad, N.K.1    Steitz, J.A.2
  • 14
    • 2942594809 scopus 로고    scopus 로고
    • The Herpesvirus saimiri small nuclear RNAs recruit AU-rich element-binding proteins but do not alter host AU-rich element-containing mRNA levels in virally transformed T cells
    • Cook H.L., Mischo H.E., and Steitz J.A. The Herpesvirus saimiri small nuclear RNAs recruit AU-rich element-binding proteins but do not alter host AU-rich element-containing mRNA levels in virally transformed T cells. Mol. Cell. Biol. 24 (2004) 4522-4533
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4522-4533
    • Cook, H.L.1    Mischo, H.E.2    Steitz, J.A.3
  • 15
    • 3142546235 scopus 로고    scopus 로고
    • The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation
    • Dean J.L., Sully G., Clark A.R., and Saklatvala J. The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. Cell Signal 16 (2004) 1113-1121
    • (2004) Cell Signal , vol.16 , pp. 1113-1121
    • Dean, J.L.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 17
    • 0030803671 scopus 로고    scopus 로고
    • AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation
    • Fan X.C., Myer V.E., and Steitz J.A. AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation. Genes Dev. 11 (1997) 2557-2568
    • (1997) Genes Dev. , vol.11 , pp. 2557-2568
    • Fan, X.C.1    Myer, V.E.2    Steitz, J.A.3
  • 18
    • 37849019535 scopus 로고    scopus 로고
    • The 3′ untranslated region of Sindbis virus represses the deadenylation of viral transcripts in mosquito and mammalian cells
    • Garneau N.L., Sokoloski K.J., Opyrchal M., Neff C.P., Wilusz C.J., and Wilusz J. The 3′ untranslated region of Sindbis virus represses the deadenylation of viral transcripts in mosquito and mammalian cells. J. Virol. 82 (2007) 880-892
    • (2007) J. Virol. , vol.82 , pp. 880-892
    • Garneau, N.L.1    Sokoloski, K.J.2    Opyrchal, M.3    Neff, C.P.4    Wilusz, C.J.5    Wilusz, J.6
  • 19
    • 0027992089 scopus 로고
    • The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins
    • Gorlach M., Burd C.G., and Dreyfuss G. The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. J. Biol. Chem. 269 (1994) 23074-23078
    • (1994) J. Biol. Chem. , vol.269 , pp. 23074-23078
    • Gorlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 20
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow E., and Lane D. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 21
    • 34249053165 scopus 로고    scopus 로고
    • RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation
    • Hogg J.R., and Collins K. RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation. RNA 13 (2007) 868-880
    • (2007) RNA , vol.13 , pp. 868-880
    • Hogg, J.R.1    Collins, K.2
  • 22
    • 33645824089 scopus 로고    scopus 로고
    • Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails
    • Hosoda N., Lejeune F., and Maquat L.E. Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails. Mol. Cell. Biol. 26 (2006) 3085-3097
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3085-3097
    • Hosoda, N.1    Lejeune, F.2    Maquat, L.E.3
  • 23
    • 0018040673 scopus 로고
    • Studies on histone organization in the nucleosome using formaldehyde as a reversible cross-linking agent
    • Jackson V. Studies on histone organization in the nucleosome using formaldehyde as a reversible cross-linking agent. Cell 15 (1978) 945-954
    • (1978) Cell , vol.15 , pp. 945-954
    • Jackson, V.1
  • 25
    • 34548780330 scopus 로고    scopus 로고
    • Biochemical purification of box H/ACA RNPs involved in pseudouridylation
    • Karijolich J., Stephenson D., and Yu Y.T. Biochemical purification of box H/ACA RNPs involved in pseudouridylation. Methods Enzymol. 425 (2007) 241-262
    • (2007) Methods Enzymol. , vol.425 , pp. 241-262
    • Karijolich, J.1    Stephenson, D.2    Yu, Y.T.3
  • 26
    • 0030426455 scopus 로고    scopus 로고
    • RNA recognition by autoantigens and autoantibodies
    • Keene J.D. RNA recognition by autoantigens and autoantibodies. Mol. Biol. Rep. 23 (1996) 173-181
    • (1996) Mol. Biol. Rep. , vol.23 , pp. 173-181
    • Keene, J.D.1
  • 27
    • 33845275018 scopus 로고    scopus 로고
    • RIP-Chip: The isolation and identification of mRNAs, microRNAs and protein components of ribonucleoprotein complexes from cell extracts
    • Keene J.D., Komisarow J.M., and Friedersdorf M.B. RIP-Chip: The isolation and identification of mRNAs, microRNAs and protein components of ribonucleoprotein complexes from cell extracts. Nat. Protoc. 1 (2006) 302-307
    • (2006) Nat. Protoc. , vol.1 , pp. 302-307
    • Keene, J.D.1    Komisarow, J.M.2    Friedersdorf, M.B.3
  • 28
    • 33845265038 scopus 로고    scopus 로고
    • Dynamic association and localization of human H/ACA RNP proteins
    • Kittur N., Darzacq X., Roy S., Singer R.H., and Meier U.T. Dynamic association and localization of human H/ACA RNP proteins. RNA 12 (2006) 2057-2062
    • (2006) RNA , vol.12 , pp. 2057-2062
    • Kittur, N.1    Darzacq, X.2    Roy, S.3    Singer, R.H.4    Meier, U.T.5
  • 29
    • 0033153348 scopus 로고    scopus 로고
    • hnRNP complexes: Composition, structure, and function
    • Krecic A.M., and Swanson M.S. hnRNP complexes: Composition, structure, and function. Curr. Opin. Cell Biol. 11 (1999) 363-371
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 363-371
    • Krecic, A.M.1    Swanson, M.S.2
  • 30
    • 0035878119 scopus 로고    scopus 로고
    • Messenger RNAs are recruited for nuclear export during transcription
    • Lei E.P., Krebber H., and Silver P.A. Messenger RNAs are recruited for nuclear export during transcription. Genes Dev. 15 (2001) 1771-1782
    • (2001) Genes Dev. , vol.15 , pp. 1771-1782
    • Lei, E.P.1    Krebber, H.2    Silver, P.A.3
  • 31
    • 0019459464 scopus 로고
    • Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus
    • Lerner M.R., Boyle J.A., Hardin J.A., and Steitz J.A. Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus. Science 211 (1981) 400-402
    • (1981) Science , vol.211 , pp. 400-402
    • Lerner, M.R.1    Boyle, J.A.2    Hardin, J.A.3    Steitz, J.A.4
  • 32
    • 0000341684 scopus 로고
    • Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus
    • Lerner M.R., and Steitz J.A. Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus. Proc. Natl. Acad. Sci. USA 76 (1979) 5495-5499
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5495-5499
    • Lerner, M.R.1    Steitz, J.A.2
  • 33
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • Listerman I., Sapra A.K., and Neugebauer K.M. Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat. Struct. Mol. Biol. 13 (2006) 815-822
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 34
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen J., Shu M.D., and Steitz J.A. Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell 103 (2000) 1121-1131
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 35
    • 0019515261 scopus 로고
    • Nuclear ribonucleoprotein particles probed in living cells
    • Mayrand S., and Pederson T. Nuclear ribonucleoprotein particles probed in living cells. Proc. Natl. Acad. Sci. USA 78 (1981) 2208-2212
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2208-2212
    • Mayrand, S.1    Pederson, T.2
  • 36
    • 0030979415 scopus 로고    scopus 로고
    • Photocross-linking of nucleic acids to associated proteins
    • Meisenheimer K.M., and Koch T.H. Photocross-linking of nucleic acids to associated proteins. Crit. Rev. Biochem. Mol. Biol. 32 (1997) 101-140
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 101-140
    • Meisenheimer, K.M.1    Koch, T.H.2
  • 37
    • 0034791334 scopus 로고    scopus 로고
    • Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: Candidate intermediates in formation and export of mRNA
    • Mili S., Shu H.J., Zhao Y., and Pinol-Roma S. Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: Candidate intermediates in formation and export of mRNA. Mol. Cell. Biol. 21 (2001) 7307-7319
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7307-7319
    • Mili, S.1    Shu, H.J.2    Zhao, Y.3    Pinol-Roma, S.4
  • 38
    • 7044272280 scopus 로고    scopus 로고
    • Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses
    • Mili S., and Steitz J.A. Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. RNA 10 (2004) 1692-1694
    • (2004) RNA , vol.10 , pp. 1692-1694
    • Mili, S.1    Steitz, J.A.2
  • 39
    • 0030933006 scopus 로고    scopus 로고
    • Identification of HuR as a protein implicated in AUUUA-mediated mRNA decay
    • Myer V.E., Fan X.C., and Steitz J.A. Identification of HuR as a protein implicated in AUUUA-mediated mRNA decay. EMBO J 16 (1997) 2130-2139
    • (1997) EMBO J , vol.16 , pp. 2130-2139
    • Myer, V.E.1    Fan, X.C.2    Steitz, J.A.3
  • 40
    • 0029797247 scopus 로고    scopus 로고
    • The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals
    • Nakielny S., and Dreyfuss G. The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals. J. Cell Biol. 134 (1996) 1365-1373
    • (1996) J. Cell Biol. , vol.134 , pp. 1365-1373
    • Nakielny, S.1    Dreyfuss, G.2
  • 41
    • 0036354884 scopus 로고    scopus 로고
    • Reversible cross-linking combined with immunoprecipitation to study RNA-protein interactions in vivo
    • Niranjanakumari S., Lasda E., Brazas R., and Garcia-Blanco M.A. Reversible cross-linking combined with immunoprecipitation to study RNA-protein interactions in vivo. Methods 26 (2002) 182-190
    • (2002) Methods , vol.26 , pp. 182-190
    • Niranjanakumari, S.1    Lasda, E.2    Brazas, R.3    Garcia-Blanco, M.A.4
  • 42
    • 0027139910 scopus 로고
    • Mapping Polycomb-repressed domains in the bithorax complex using in vivo formaldehyde cross-linked chromatin
    • Orlando V., and Paro R. Mapping Polycomb-repressed domains in the bithorax complex using in vivo formaldehyde cross-linked chromatin. Cell 75 (1993) 1187-1198
    • (1993) Cell , vol.75 , pp. 1187-1198
    • Orlando, V.1    Paro, R.2
  • 43
    • 0031080378 scopus 로고    scopus 로고
    • Analysis of chromatin structure by in vivo formaldehyde cross-linking
    • Orlando V., Strutt H., and Paro R. Analysis of chromatin structure by in vivo formaldehyde cross-linking. Methods 11 (1997) 205-214
    • (1997) Methods , vol.11 , pp. 205-214
    • Orlando, V.1    Strutt, H.2    Paro, R.3
  • 44
    • 6344228386 scopus 로고    scopus 로고
    • Biotinylated tags for recovery and characterization of ribonucleoprotein complexes
    • 604, 606
    • Penalva L.O., and Keene J.D. Biotinylated tags for recovery and characterization of ribonucleoprotein complexes. Biotechniques 37 (2004) 608-610 604, 606
    • (2004) Biotechniques , vol.37 , pp. 608-610
    • Penalva, L.O.1    Keene, J.D.2
  • 45
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng S.S., Chen C.Y., Xu N., and Shyu A.B. RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J 17 (1998) 3461-3470
    • (1998) EMBO J , vol.17 , pp. 3461-3470
    • Peng, S.S.1    Chen, C.Y.2    Xu, N.3    Shyu, A.B.4
  • 46
    • 0028057811 scopus 로고
    • RNA annealing activities in HeLa nuclei
    • Portman D.S., and Dreyfuss G. RNA annealing activities in HeLa nuclei. EMBO J 13 (1994) 213-221
    • (1994) EMBO J , vol.13 , pp. 213-221
    • Portman, D.S.1    Dreyfuss, G.2
  • 47
    • 0032824051 scopus 로고    scopus 로고
    • Identification of RNA-protein contacts within functional ribonucleoprotein complexes by RNA site-specific labeling and UV crosslinking
    • Reed R., and Chiara M.D. Identification of RNA-protein contacts within functional ribonucleoprotein complexes by RNA site-specific labeling and UV crosslinking. Methods 18 (1999) 3-12
    • (1999) Methods , vol.18 , pp. 3-12
    • Reed, R.1    Chiara, M.D.2
  • 48
    • 0001473216 scopus 로고
    • Formaldehyde-mediated DNA-protein crosslinking: A probe for in vivo chromatin structures
    • Solomon M.J., and Varshavsky A. Formaldehyde-mediated DNA-protein crosslinking: A probe for in vivo chromatin structures. Proc. Natl. Acad. Sci. USA 82 (1985) 6470-6474
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6470-6474
    • Solomon, M.J.1    Varshavsky, A.2
  • 49
    • 0036241373 scopus 로고    scopus 로고
    • Characterization of interactions between RTA and the promoter of polyadenylated nuclear RNA in Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8
    • Song M.J., Li X., Brown H.J., and Sun R. Characterization of interactions between RTA and the promoter of polyadenylated nuclear RNA in Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8. J. Virol. 76 (2002) 5000-5013
    • (2002) J. Virol. , vol.76 , pp. 5000-5013
    • Song, M.J.1    Li, X.2    Brown, H.J.3    Sun, R.4
  • 50
    • 0036353344 scopus 로고    scopus 로고
    • RNA affinity tags for purification of RNAs and ribonucleoprotein complexes
    • Srisawat C., and Engelke D.R. RNA affinity tags for purification of RNAs and ribonucleoprotein complexes. Methods 26 (2002) 156-161
    • (2002) Methods , vol.26 , pp. 156-161
    • Srisawat, C.1    Engelke, D.R.2
  • 51
    • 0029966233 scopus 로고    scopus 로고
    • Polyadenylated nuclear RNA encoded by Kaposi sarcoma-associated herpesvirus
    • Sun R., Lin S.F., Gradoville L., and Miller G. Polyadenylated nuclear RNA encoded by Kaposi sarcoma-associated herpesvirus. Proc. Natl. Acad. Sci. USA 93 (1996) 11883-11888
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11883-11888
    • Sun, R.1    Lin, S.F.2    Gradoville, L.3    Miller, G.4
  • 52
    • 33745622860 scopus 로고    scopus 로고
    • Genomic localization of RNA binding proteins reveals links between pre-mRNA processing and transcription
    • Swinburne I.A., Meyer C.A., Liu X.S., Silver P.A., and Brodsky A.S. Genomic localization of RNA binding proteins reveals links between pre-mRNA processing and transcription. Genome Res. 16 (2006) 912-921
    • (2006) Genome Res. , vol.16 , pp. 912-921
    • Swinburne, I.A.1    Meyer, C.A.2    Liu, X.S.3    Silver, P.A.4    Brodsky, A.S.5
  • 53
    • 0036351379 scopus 로고    scopus 로고
    • Ribonomics: Identifying mRNA subsets in mRNP complexes using antibodies to RNA-binding proteins and genomic arrays
    • Tenenbaum S.A., Lager P.J., Carson C.C., and Keene J.D. Ribonomics: Identifying mRNA subsets in mRNP complexes using antibodies to RNA-binding proteins and genomic arrays. Methods 26 (2002) 191-198
    • (2002) Methods , vol.26 , pp. 191-198
    • Tenenbaum, S.A.1    Lager, P.J.2    Carson, C.C.3    Keene, J.D.4
  • 54
    • 0019332761 scopus 로고
    • The identification by affinity chromatography of the rat liver ribosomal proteins that bind to elongator and initiator transfer ribonucleic acids
    • Ulbrich N., Wool I.G., Ackerman E., and Sigler P.B. The identification by affinity chromatography of the rat liver ribosomal proteins that bind to elongator and initiator transfer ribonucleic acids. J. Biol. Chem. 255 (1980) 7010-7019
    • (1980) J. Biol. Chem. , vol.255 , pp. 7010-7019
    • Ulbrich, N.1    Wool, I.G.2    Ackerman, E.3    Sigler, P.B.4
  • 55
    • 27944508215 scopus 로고    scopus 로고
    • CLIP: a method for identifying protein-RNA interaction sites in living cells
    • Ule J., Jensen K., Mele A., and Darnell R.B. CLIP: a method for identifying protein-RNA interaction sites in living cells. Methods 37 (2005) 376-386
    • (2005) Methods , vol.37 , pp. 376-386
    • Ule, J.1    Jensen, K.2    Mele, A.3    Darnell, R.B.4
  • 56
    • 33947262696 scopus 로고    scopus 로고
    • AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2
    • Vasudevan S., and Steitz J.A. AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2. Cell 128 (2007) 1105-1118
    • (2007) Cell , vol.128 , pp. 1105-1118
    • Vasudevan, S.1    Steitz, J.A.2
  • 57
    • 0019086007 scopus 로고
    • Cross-linking of mRNA to proteins by irradiation of intact cells with ultraviolet light
    • Wagenmakers A.J., Reinders R.J., and van Venrooij W.J. Cross-linking of mRNA to proteins by irradiation of intact cells with ultraviolet light. Eur. J. Biochem. 112 (1980) 323-330
    • (1980) Eur. J. Biochem. , vol.112 , pp. 323-330
    • Wagenmakers, A.J.1    Reinders, R.J.2    van Venrooij, W.J.3
  • 58
    • 0026323541 scopus 로고
    • Identification of amino acid residues at interface of protein-nucleic acid complexes by photochemical cross-linking
    • Williams K.R., and Konigsberg W.H. Identification of amino acid residues at interface of protein-nucleic acid complexes by photochemical cross-linking. Methods Enzymol. 208 (1991) 516-539
    • (1991) Methods Enzymol. , vol.208 , pp. 516-539
    • Williams, K.R.1    Konigsberg, W.H.2
  • 59
    • 0032823604 scopus 로고    scopus 로고
    • Identification and characterization of proteins binding A + U-rich elements
    • Wilson G.M., and Brewer G. Identification and characterization of proteins binding A + U-rich elements. Methods 17 (1999) 74-83
    • (1999) Methods , vol.17 , pp. 74-83
    • Wilson, G.M.1    Brewer, G.2
  • 61
    • 0029957833 scopus 로고    scopus 로고
    • Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma
    • Zhong W., Wang H., Herndier B., and Ganem D. Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma. Proc. Natl. Acad. Sci. USA 93 (1996) 6641-6646
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6641-6646
    • Zhong, W.1    Wang, H.2    Herndier, B.3    Ganem, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.