메뉴 건너뛰기




Volumn 21, Issue 11, 2013, Pages 2014-2024

Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROID KRUPPEL LIKE FACTOR; ETOPOSIDE; MULTIPROTEIN COMPLEX; PROTEIN P53; RABEX5 PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN 1A; TRANSCRIPTION FACTOR GAL4; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84887404373     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.08.027     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 45549098595 scopus 로고    scopus 로고
    • Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo
    • C.T. Archer, A. Delahodde, F. Gonzalez, S.A. Johnston, and T. Kodadek Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo J. Biol. Chem. 283 2008 12614 12623
    • (2008) J. Biol. Chem. , vol.283 , pp. 12614-12623
    • Archer, C.T.1    Delahodde, A.2    Gonzalez, F.3    Johnston, S.A.4    Kodadek, T.5
  • 2
    • 65549140251 scopus 로고    scopus 로고
    • A phosphorylation cascade controls the degradation of active SREBP1
    • M.T. Bengoechea-Alonso, and J. Ericsson A phosphorylation cascade controls the degradation of active SREBP1 J. Biol. Chem. 284 2009 5885 5895
    • (2009) J. Biol. Chem. , vol.284 , pp. 5885-5895
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 3
    • 79251596169 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation
    • K.P. Bhat, and S.F. Greer Proteolytic and non-proteolytic roles of ubiquitin and the ubiquitin proteasome system in transcriptional regulation Biochim. Biophys. Acta 1809 2011 150 155
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 150-155
    • Bhat, K.P.1    Greer, S.F.2
  • 5
    • 0029906977 scopus 로고    scopus 로고
    • Erythroid Krüppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions
    • X.Y. Chen, and J.J. Bieker Erythroid Krüppel-like factor (EKLF) contains a multifunctional transcriptional activation domain important for inter- and intramolecular interactions EMBO J. 15 1996 5888 5896
    • (1996) EMBO J. , vol.15 , pp. 5888-5896
    • Chen, X.Y.1    Bieker, J.J.2
  • 6
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 8
    • 19644388865 scopus 로고    scopus 로고
    • NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites
    • P. Di Lello, B.D. Nguyen, T.N. Jones, K. Potempa, M.S. Kobor, P. Legault, and J.G. Omichinski NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites Biochemistry 44 2005 7678 7686
    • (2005) Biochemistry , vol.44 , pp. 7678-7686
    • Di Lello, P.1    Nguyen, B.D.2    Jones, T.N.3    Potempa, K.4    Kobor, M.S.5    Legault, P.6    Omichinski, J.G.7
  • 10
  • 11
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • S. Elsasser, and D. Finley Delivery of ubiquitinated substrates to protein-unfolding machines Nat. Cell Biol. 7 2005 742 749
    • (2005) Nat. Cell Biol. , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 12
    • 0028174097 scopus 로고
    • Analyses of beta-thalassemia mutant DNA interactions with erythroid Krüppel-like factor (EKLF), an erythroid cell-specific transcription factor
    • W.C. Feng, C.M. Southwood, and J.J. Bieker Analyses of beta-thalassemia mutant DNA interactions with erythroid Krüppel-like factor (EKLF), an erythroid cell-specific transcription factor J. Biol. Chem. 269 1994 1493 1500
    • (1994) J. Biol. Chem. , vol.269 , pp. 1493-1500
    • Feng, W.C.1    Southwood, C.M.2    Bieker, J.J.3
  • 13
    • 69449101615 scopus 로고    scopus 로고
    • Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein
    • J.C. Ferreon, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein Proc. Natl. Acad. Sci. USA 106 2009 13260 13265
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13260-13265
    • Ferreon, J.C.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 14
    • 84861869979 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes in transcription
    • F. Geng, S. Wenzel, and W.P. Tansey Ubiquitin and proteasomes in transcription Annu. Rev. Biochem. 81 2012 177 201
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 177-201
    • Geng, F.1    Wenzel, S.2    Tansey, W.P.3
  • 15
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • S. Grzesiek, and A. Bax Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR J. Am. Chem. Soc. 114 1992 6291 6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 16
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • K. Haglund, and I. Dikic Ubiquitylation and cell signaling EMBO J. 24 2005 3353 3359
    • (2005) EMBO J. , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 17
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Y. Haupt, R. Maya, A. Kazaz, and M. Oren Mdm2 promotes the rapid degradation of p53 Nature 387 1997 296 299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 18
    • 0034296394 scopus 로고    scopus 로고
    • Basic Medical Research Award the ubiquitin system
    • A. Hershko, A. Ciechanover, and A. Varshavsky Basic Medical Research Award. The ubiquitin system Nat. Med. 6 2000 1073 1081
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 19
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • M. Hochstrasser Evolution and function of ubiquitin-like protein-conjugation systems Nat. Cell Biol. 2 2000 E153 E157
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 22
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • J.H. Hurley, S. Lee, and G. Prag Ubiquitin-binding domains Biochem. J. 399 2006 361 372
    • (2006) Biochem. J. , vol.399 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 23
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • F. Ikeda, and I. Dikic Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series EMBO Rep. 9 2008 536 542
    • (2008) EMBO Rep. , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 24
    • 0026225733 scopus 로고
    • Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution
    • M. Ikura, L.E. Kay, and A. Bax Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution J. Biomol. NMR 1 1991 299 304
    • (1991) J. Biomol. NMR , vol.1 , pp. 299-304
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 25
    • 34447505016 scopus 로고
    • Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation
    • L.E. Kay, G.Y. Xu, and T. Yamazaki Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation J. Magn. Reson. A 109 1994 129 133
    • (1994) J. Magn. Reson. A , vol.109 , pp. 129-133
    • Kay, L.E.1    Xu, G.Y.2    Yamazaki, T.3
  • 26
    • 77449127817 scopus 로고    scopus 로고
    • No Splicing, no dicing: Non-proteolytic roles of the ubiquitin-proteasome system in transcription
    • T. Kodadek No Splicing, no dicing: non-proteolytic roles of the ubiquitin-proteasome system in transcription J. Biol. Chem. 285 2010 2221 2226
    • (2010) J. Biol. Chem. , vol.285 , pp. 2221-2226
    • Kodadek, T.1
  • 27
    • 33750023437 scopus 로고    scopus 로고
    • Keeping transcriptional activators under control
    • T. Kodadek, D. Sikder, and K. Nalley Keeping transcriptional activators under control Cell 127 2006 261 264
    • (2006) Cell , vol.127 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 51 55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
  • 30
    • 49449118629 scopus 로고    scopus 로고
    • NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: Structural similarities between VP16 and p53
    • C. Langlois, C. Mas, P. Di Lello, L.M. Jenkins, P. Legault, and J.G. Omichinski NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53 J. Am. Chem. Soc. 130 2008 10596 10604
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10596-10604
    • Langlois, C.1    Mas, C.2    Di Lello, P.3    Jenkins, L.M.4    Legault, P.5    Omichinski, J.G.6
  • 31
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 34
    • 0026619586 scopus 로고
    • Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments
    • T.M. Logan, E.T. Olejniczak, R.X. Xu, and S.W. Fesik Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments FEBS Lett. 314 1992 413 418
    • (1992) FEBS Lett. , vol.314 , pp. 413-418
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 35
    • 53549094933 scopus 로고    scopus 로고
    • Ubiquitin binding and conjugation regulate the recruitment of Rabex-5 to early endosomes
    • R. Mattera, and J.S. Bonifacino Ubiquitin binding and conjugation regulate the recruitment of Rabex-5 to early endosomes EMBO J. 27 2008 2484 2494
    • (2008) EMBO J. , vol.27 , pp. 2484-2494
    • Mattera, R.1    Bonifacino, J.S.2
  • 36
    • 84855945551 scopus 로고    scopus 로고
    • P53 degradation activity, expression, and subcellular localization of E6 proteins from 29 human papillomavirus genotypes
    • T. Mesplède, D. Gagnon, F. Bergeron-Labrecque, I. Azar, H. Sénéchal, F. Coutlée, and J. Archambault p53 degradation activity, expression, and subcellular localization of E6 proteins from 29 human papillomavirus genotypes J. Virol. 86 2012 94 107
    • (2012) J. Virol. , vol.86 , pp. 94-107
    • Mesplède, T.1    Gagnon, D.2    Bergeron-Labrecque, F.3    Azar, I.4    Sénéchal, H.5    Coutlée, F.6    Archambault, J.7
  • 37
    • 0027211845 scopus 로고
    • A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Krüppel family of nuclear proteins
    • I.J. Miller, and J.J. Bieker A novel, erythroid cell-specific murine transcription factor that binds to the CACCC element and is related to the Krüppel family of nuclear proteins Mol. Cell. Biol. 13 1993 2776 2786
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2776-2786
    • Miller, I.J.1    Bieker, J.J.2
  • 38
    • 20444399163 scopus 로고    scopus 로고
    • The regulation of proteasome degradation by multi-ubiquitin chain binding proteins
    • J. Miller, and C. Gordon The regulation of proteasome degradation by multi-ubiquitin chain binding proteins FEBS Lett. 579 2005 3224 3230
    • (2005) FEBS Lett. , vol.579 , pp. 3224-3230
    • Miller, J.1    Gordon, C.2
  • 39
    • 0033571527 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo
    • E. Molinari, M. Gilman, and S. Natesan Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo EMBO J. 18 1999 6439 6447
    • (1999) EMBO J. , vol.18 , pp. 6439-6447
    • Molinari, E.1    Gilman, M.2    Natesan, S.3
  • 40
    • 17644386183 scopus 로고    scopus 로고
    • The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing
    • M. Muratani, C. Kung, K.M. Shokat, and W.P. Tansey The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing Cell 120 2005 887 899
    • (2005) Cell , vol.120 , pp. 887-899
    • Muratani, M.1    Kung, C.2    Shokat, K.M.3    Tansey, W.P.4
  • 42
    • 0028990264 scopus 로고
    • Lethal beta-thalassaemia in mice lacking the erythroid CACCC-transcription factor EKLF
    • A.C. Perkins, A.H. Sharpe, and S.H. Orkin Lethal beta-thalassaemia in mice lacking the erythroid CACCC-transcription factor EKLF Nature 375 1995 318 322
    • (1995) Nature , vol.375 , pp. 318-322
    • Perkins, A.C.1    Sharpe, A.H.2    Orkin, S.H.3
  • 43
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C.M. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 44
    • 33748751591 scopus 로고    scopus 로고
    • Phosphorylation and ubiquitination of the transcription factor sterol regulatory element-binding protein-1 in response to DNA binding
    • T. Punga, M.T. Bengoechea-Alonso, and J. Ericsson Phosphorylation and ubiquitination of the transcription factor sterol regulatory element-binding protein-1 in response to DNA binding J. Biol. Chem. 281 2006 25278 25286
    • (2006) J. Biol. Chem. , vol.281 , pp. 25278-25286
    • Punga, T.1    Bengoechea-Alonso, M.T.2    Ericsson, J.3
  • 45
    • 33646010066 scopus 로고    scopus 로고
    • EKLF/KLF1 is ubiquitinated in vivo and its stability is regulated by activation domain sequences through the 26S proteasome
    • K.J. Quadrini, and J.J. Bieker EKLF/KLF1 is ubiquitinated in vivo and its stability is regulated by activation domain sequences through the 26S proteasome FEBS Lett. 580 2006 2285 2293
    • (2006) FEBS Lett. , vol.580 , pp. 2285-2293
    • Quadrini, K.J.1    Bieker, J.J.2
  • 46
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • S.E. Salghetti, M. Muratani, H. Wijnen, B. Futcher, and W.P. Tansey Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis Proc. Natl. Acad. Sci. USA 97 2000 3118 3123
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 47
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • S.E. Salghetti, A.A. Caudy, J.G. Chenoweth, and W.P. Tansey Regulation of transcriptional activation domain function by ubiquitin Science 293 2001 1651 1653
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 49
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • S.C. Shih, D.J. Katzmann, J.D. Schnell, M. Sutanto, S.D. Emr, and L. Hicke Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis Nat. Cell Biol. 4 2002 389 393
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 50
    • 0344270908 scopus 로고    scopus 로고
    • Transcription-dependent degradation controls the stability of the SREBP family of transcription factors
    • A. Sundqvist, and J. Ericsson Transcription-dependent degradation controls the stability of the SREBP family of transcription factors Proc. Natl. Acad. Sci. USA 100 2003 13833 13838
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13833-13838
    • Sundqvist, A.1    Ericsson, J.2
  • 51
    • 23844530704 scopus 로고    scopus 로고
    • Control of lipid metabolism by phosphorylation-dependent degradation of the SREBP family of transcription factors by SCF(Fbw7)
    • A. Sundqvist, M.T. Bengoechea-Alonso, X. Ye, V. Lukiyanchuk, J. Jin, J.W. Harper, and J. Ericsson Control of lipid metabolism by phosphorylation- dependent degradation of the SREBP family of transcription factors by SCF(Fbw7) Cell Metab. 1 2005 379 391
    • (2005) Cell Metab. , vol.1 , pp. 379-391
    • Sundqvist, A.1    Bengoechea-Alonso, M.T.2    Ye, X.3    Lukiyanchuk, V.4    Jin, J.5    Harper, J.W.6    Ericsson, J.7
  • 52
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • K.A. Swanson, R.S. Kang, S.D. Stamenova, L. Hicke, and I. Radhakrishnan Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation EMBO J. 22 2003 4597 4606
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 53
    • 84858147489 scopus 로고    scopus 로고
    • Ubiquitin and SUMO in DNA repair at a glance
    • H.D. Ulrich Ubiquitin and SUMO in DNA repair at a glance J. Cell Sci. 125 2012 249 254
    • (2012) J. Cell Sci. , vol.125 , pp. 249-254
    • Ulrich, H.D.1
  • 56
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • A.M. Weissman Themes and variations on ubiquitylation Nat. Rev. Mol. Cell Biol. 2 2001 169 178
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 57
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: Hot spots and varied specificity
    • J.M. Winget, and T. Mayor The diversity of ubiquitin recognition: hot spots and varied specificity Mol. Cell 38 2010 627 635
    • (2010) Mol. Cell , vol.38 , pp. 627-635
    • Winget, J.M.1    Mayor, T.2
  • 58
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • M. Wittekind, and L. Mueller HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins J. Magn. Reson. B. 101 1993 201 205
    • (1993) J. Magn. Reson. B. , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 59
    • 65449119145 scopus 로고    scopus 로고
    • Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains
    • J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains EMBO J. 28 2009 948 958
    • (2009) EMBO J. , vol.28 , pp. 948-958
    • Wojciak, J.M.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 60
    • 84860848476 scopus 로고    scopus 로고
    • Functional interactions between erythroid Krüppel-like factor (EKLF/KLF1) and protein phosphatase PPM1B/PP2Cβ
    • Y.Y. Yien, and J.J. Bieker Functional interactions between erythroid Krüppel-like factor (EKLF/KLF1) and protein phosphatase PPM1B/PP2Cβ J. Biol. Chem. 287 2012 15193 15204
    • (2012) J. Biol. Chem. , vol.287 , pp. 15193-15204
    • Yien, Y.Y.1    Bieker, J.J.2
  • 61
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage lambda N-peptide/boxB RNA
    • C. Zwahlen, P. Legault, S.J.F. Vincent, J. Greenblatt, R. Konrat, and L.E. Kay Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage lambda N-peptide/boxB RNA J. Am. Chem. Soc. 119 1997 6711 6721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.