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Volumn 401, Issue 1, 2010, Pages 97-114

Solution Structure of Histone Chaperone ANP32B: Interaction with Core Histones H3-H4 through Its Acidic Concave Domain

Author keywords

ANP32; Histone; ITC; LRR domain; NMR

Indexed keywords

ACIDIC NUCLEAR PHOSPHOPROTEIN 32 B; CHAPERONE; HISTONE H3; HISTONE H4; NUCLEAR PROTEIN; PHOSPHOPROTEIN; UNCLASSIFIED DRUG;

EID: 77954758377     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.005     Document Type: Article
Times cited : (35)

References (84)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 angstrom resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg R.D., Lorch Y.L. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 1999, 98:285-294.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.L.2
  • 3
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • Loyola A., Almouzni G. Histone chaperones, a supporting role in the limelight. Biochim. Biophys. Acta 2004, 1677:3-11.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 5
    • 44449104927 scopus 로고    scopus 로고
    • Clothing up DNA for all seasons: histone chaperones and nucleosome assembly pathways
    • Rocha W., Verreault A. Clothing up DNA for all seasons: histone chaperones and nucleosome assembly pathways. FEBS Lett. 2008, 582:1938-1949.
    • (2008) FEBS Lett. , vol.582 , pp. 1938-1949
    • Rocha, W.1    Verreault, A.2
  • 6
    • 44949119317 scopus 로고    scopus 로고
    • Histone chaperones in nucleosome eviction and histone exchange
    • Park Y.J., Luger K. Histone chaperones in nucleosome eviction and histone exchange. Curr. Opin. Struct. Biol. 2008, 18:282-289.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 282-289
    • Park, Y.J.1    Luger, K.2
  • 9
    • 0035799281 scopus 로고    scopus 로고
    • Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
    • Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D. Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr. Biol. 2001, 11:463-473.
    • (2001) Curr. Biol. , vol.11 , pp. 463-473
    • Sharp, J.A.1    Fouts, E.T.2    Krawitz, D.C.3    Kaufman, P.D.4
  • 11
    • 33749505109 scopus 로고    scopus 로고
    • Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly
    • Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A., Dunbrack R., et al. Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Nat. Struct. Mol. Biol. 2006, 13:921-929.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 921-929
    • Tang, Y.1    Poustovoitov, M.V.2    Zhao, K.3    Garfinkel, M.4    Canutescu, A.5    Dunbrack, R.6
  • 12
    • 46649121282 scopus 로고    scopus 로고
    • Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus
    • Malay A.D., Umehara T., Matsubara-Malay K., Padmanabhan B., Yokoyama S. Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus. J. Biol. Chem. 2008, 283:14022-14031.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14022-14031
    • Malay, A.D.1    Umehara, T.2    Matsubara-Malay, K.3    Padmanabhan, B.4    Yokoyama, S.5
  • 13
    • 2942550662 scopus 로고    scopus 로고
    • Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PH05 and PH08 genes
    • Adkins M.W., Howar S.R., Tyler J.K. Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PH05 and PH08 genes. Mol. Cell 2004, 14:657-666.
    • (2004) Mol. Cell , vol.14 , pp. 657-666
    • Adkins, M.W.1    Howar, S.R.2    Tyler, J.K.3
  • 14
    • 38549161648 scopus 로고    scopus 로고
    • Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5
    • Munemasa Y., Suzuki T., Aizawa K., Miyamoto S., Imai Y., Matsumura T., et al. Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5. Mol. Cell. Biol. 2008, 28:1171-1181.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1171-1181
    • Munemasa, Y.1    Suzuki, T.2    Aizawa, K.3    Miyamoto, S.4    Imai, Y.5    Matsumura, T.6
  • 15
    • 0028369492 scopus 로고
    • Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII
    • Vaesen M., Barnikolwatanabe S., Gotz H., Awni L.A., Cole T., Zimmermann B., et al. Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII. Biol. Chem. Hoppe-Seyler 1994, 375:113-126.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 113-126
    • Vaesen, M.1    Barnikolwatanabe, S.2    Gotz, H.3    Awni, L.A.4    Cole, T.5    Zimmermann, B.6
  • 18
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • Seo S.B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell 2001, 104:119-130.
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 19
    • 0037134538 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
    • Seo S.B., Macfarlan T., McNamara P., Hong R., Mukai Y., Heo S., Chakravarti D. Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. J. Biol. Chem. 2002, 277:14005-14010.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14005-14010
    • Seo, S.B.1    Macfarlan, T.2    McNamara, P.3    Hong, R.4    Mukai, Y.5    Heo, S.6    Chakravarti, D.7
  • 20
    • 17844367134 scopus 로고    scopus 로고
    • The Anp32 family of proteins containing leucine-rich repeats
    • Matilla A., Radrizzani M. The Anp32 family of proteins containing leucine-rich repeats. Cerebellum 2005, 4:7-18.
    • (2005) Cerebellum , vol.4 , pp. 7-18
    • Matilla, A.1    Radrizzani, M.2
  • 21
    • 34250802262 scopus 로고    scopus 로고
    • The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins
    • Huyton T., Wolberger C. The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins. Protein Sci. 2007, 16:1308-1315.
    • (2007) Protein Sci. , vol.16 , pp. 1308-1315
    • Huyton, T.1    Wolberger, C.2
  • 22
    • 42649087416 scopus 로고    scopus 로고
    • Structural bases for recognition of Anp32/LANP proteins
    • de Chiara C., Menon R.P., Pastore A. Structural bases for recognition of Anp32/LANP proteins. FEBS J. 2008, 275:2548-2560.
    • (2008) FEBS J. , vol.275 , pp. 2548-2560
    • de Chiara, C.1    Menon, R.P.2    Pastore, A.3
  • 24
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • Natsume R., Eitoku M., Akai Y., Sano N., Horikoshi M., Senda T. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Nature 2007, 446:338-341.
    • (2007) Nature , vol.446 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 25
    • 0034761101 scopus 로고    scopus 로고
    • The crystal structure of nucleoplasmin core: implications for histone binding and nucleosome assembly
    • Dutta S., Akey I.V., Dingwall C., Hartman K.L., Laue T., Nolte R.T., et al. The crystal structure of nucleoplasmin core: implications for histone binding and nucleosome assembly. Mol. Cell 2001, 8:841-853.
    • (2001) Mol. Cell , vol.8 , pp. 841-853
    • Dutta, S.1    Akey, I.V.2    Dingwall, C.3    Hartman, K.L.4    Laue, T.5    Nolte, R.T.6
  • 26
    • 0037313853 scopus 로고    scopus 로고
    • The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
    • Namboodiri V.M.H., Dutta S., Akey I.V., Head J.F., Akey C.W. The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure 2003, 11:175-186.
    • (2003) Structure , vol.11 , pp. 175-186
    • Namboodiri, V.M.H.1    Dutta, S.2    Akey, I.V.3    Head, J.F.4    Akey, C.W.5
  • 27
    • 31944450097 scopus 로고    scopus 로고
    • The structure of nucleosome assembly protein 1
    • Park Y.J., Luger K. The structure of nucleosome assembly protein 1. Proc. Natl Acad. Sci. USA 2006, 103:1248-1253.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1248-1253
    • Park, Y.J.1    Luger, K.2
  • 28
    • 34248351582 scopus 로고    scopus 로고
    • Relationship between the structure of SET/TAF-I beta/INHAT and its histone chaperone activity
    • Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., et al. Relationship between the structure of SET/TAF-I beta/INHAT and its histone chaperone activity. Proc. Natl Acad. Sci. USA 2007, 104:4285-4290.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 4285-4290
    • Muto, S.1    Senda, M.2    Akai, Y.3    Sato, L.4    Suzuki, T.5    Nagai, R.6
  • 30
    • 44149123117 scopus 로고    scopus 로고
    • Structural basis of histone H4 recognition by p55
    • Song J.J., Garlick J.D., Kingston R.E. Structural basis of histone H4 recognition by p55. Genes Dev. 2008, 22:1313-1318.
    • (2008) Genes Dev. , vol.22 , pp. 1313-1318
    • Song, J.J.1    Garlick, J.D.2    Kingston, R.E.3
  • 31
    • 46049093174 scopus 로고    scopus 로고
    • Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46
    • Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J., Pratap J.V., et al. Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46. Structure 2008, 16:1077-1085.
    • (2008) Structure , vol.16 , pp. 1077-1085
    • Murzina, N.V.1    Pei, X.Y.2    Zhang, W.3    Sparkes, M.4    Vicente-Garcia, J.5    Pratap, J.V.6
  • 33
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 2004, 116:51-61.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 34
    • 0025816844 scopus 로고
    • Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro
    • Ishimi Y., Kikuchi A. Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J. Biol. Chem. 1991, 266:7025-7029.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7025-7029
    • Ishimi, Y.1    Kikuchi, A.2
  • 35
    • 0242497812 scopus 로고    scopus 로고
    • Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails
    • McBryant S.J., Park Y.J., Abernathy S.M., Laybourn P.J., Nyborg J.K., Luger K. Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails. J. Biol. Chem. 2003, 278:44574-44583.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44574-44583
    • McBryant, S.J.1    Park, Y.J.2    Abernathy, S.M.3    Laybourn, P.J.4    Nyborg, J.K.5    Luger, K.6
  • 36
    • 0032545296 scopus 로고    scopus 로고
    • Template activating factor-I remodels the chromatin structure and stimulates transcription from the chromatin template
    • Okuwaki M., Nagata K. Template activating factor-I remodels the chromatin structure and stimulates transcription from the chromatin template. J. Biol. Chem. 1998, 273:34511-34518.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34511-34518
    • Okuwaki, M.1    Nagata, K.2
  • 37
    • 34250309212 scopus 로고    scopus 로고
    • Vps75, a new yeast member of the NAP histone chaperone family
    • Selth L., Svejstrup J.Q. Vps75, a new yeast member of the NAP histone chaperone family. J. Biol. Chem. 2007, 282:12358-12362.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12358-12362
    • Selth, L.1    Svejstrup, J.Q.2
  • 38
    • 0022006731 scopus 로고
    • Co-existence of two different types of soluble histone complexes in nuclei of Xenopus laevis oocytes
    • Kleinschmidt J.A., Fortkamp E., Krohne G., Zentgraf H., Franke W.W. Co-existence of two different types of soluble histone complexes in nuclei of Xenopus laevis oocytes. J. Biol. Chem. 1985, 260:1166-1176.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1166-1176
    • Kleinschmidt, J.A.1    Fortkamp, E.2    Krohne, G.3    Zentgraf, H.4    Franke, W.W.5
  • 39
    • 0023663912 scopus 로고
    • Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts
    • Dilworth S.M., Black S.J., Laskey R.A. Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts. Cell 1987, 51:1009-1018.
    • (1987) Cell , vol.51 , pp. 1009-1018
    • Dilworth, S.M.1    Black, S.J.2    Laskey, R.A.3
  • 40
    • 0018959726 scopus 로고
    • Assembly of nucleosomes: the reaction involving X. laevis nucleoplasmin
    • Earnshaw W.C., Honda B.M., Laskey R.A., Thomas J.O. Assembly of nucleosomes: the reaction involving X. laevis nucleoplasmin. Cell 1980, 21:373-383.
    • (1980) Cell , vol.21 , pp. 373-383
    • Earnshaw, W.C.1    Honda, B.M.2    Laskey, R.A.3    Thomas, J.O.4
  • 41
    • 0036163533 scopus 로고    scopus 로고
    • Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro
    • Umehara T., Chimura T., Ichikawa N., Horikoshi M. Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro. Genes Cells 2002, 7:59-73.
    • (2002) Genes Cells , vol.7 , pp. 59-73
    • Umehara, T.1    Chimura, T.2    Ichikawa, N.3    Horikoshi, M.4
  • 42
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J.F., Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 1989, 179:131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 43
    • 37549033509 scopus 로고    scopus 로고
    • Isothermal titration calorimetry at very low c
    • Tellinghuisen J. Isothermal titration calorimetry at very low c. Anal. Biochem. 2008, 373:395-397.
    • (2008) Anal. Biochem. , vol.373 , pp. 395-397
    • Tellinghuisen, J.1
  • 44
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: can low affinity systems be studied by isothermal titration calorimetry
    • Turnbull W.B., Daranas A.H. On the value of c: can low affinity systems be studied by isothermal titration calorimetry. J. Am. Chem. Soc. 2003, 125:14859-14866.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 45
    • 34247385124 scopus 로고    scopus 로고
    • The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3
    • Casares S., Eiso A.B., Eshuis H., Lopez-Mayorga O., van Nuland N.A.J., Conejero-Lara F. The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3. BMC Struct.Biol. 2007, 7:22.
    • (2007) BMC Struct.Biol. , vol.7 , pp. 22
    • Casares, S.1    Eiso, A.B.2    Eshuis, H.3    Lopez-Mayorga, O.4    van Nuland, N.A.J.5    Conejero-Lara, F.6
  • 46
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset P., Hus J.C., Blackledge M., Marion D. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR 2000, 16:23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 47
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 2004, 278:353-378.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 48
    • 0242355012 scopus 로고    scopus 로고
    • Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment
    • Jee J., Güntert P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment. J. Struct. Funct. Genomics 2003, 4:179-189.
    • (2003) J. Struct. Funct. Genomics , vol.4 , pp. 179-189
    • Jee, J.1    Güntert, P.2
  • 50
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures
    • Clore G.M., Garrett D.S. R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures. J. Am. Chem. Soc. 1999, 121:9008-9012.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 51
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 1995, 20:478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 52
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 2001, 11:725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 53
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B ′-U2A' protein complex bound to a fragment of U2 small nuclear RNA
    • Price S.R., Evans P.R., Nagai K. Crystal structure of the spliceosomal U2B ′-U2A' protein complex bound to a fragment of U2 small nuclear RNA. Nature 1998, 394:645-650.
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evans, P.R.2    Nagai, K.3
  • 54
    • 0344527798 scopus 로고    scopus 로고
    • Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains
    • Radhakrishnan I., Pérez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., Wright P.E. Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains. J. Mol. Biol. 1999, 287:859-865.
    • (1999) J. Mol. Biol. , vol.287 , pp. 859-865
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 55
    • 0026319199 scopus 로고
    • Protein folding and association-insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association-insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991, 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 56
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 57
    • 30344473323 scopus 로고    scopus 로고
    • Involvement of template-activating factor I/SET in transcription of adenovirus early genes as a positive-acting factor
    • Haruki H., Okuwaki M., Miyagishi M., Taira K., Nagata K. Involvement of template-activating factor I/SET in transcription of adenovirus early genes as a positive-acting factor. J. Virol. 2006, 80:794-801.
    • (2006) J. Virol. , vol.80 , pp. 794-801
    • Haruki, H.1    Okuwaki, M.2    Miyagishi, M.3    Taira, K.4    Nagata, K.5
  • 61
    • 70349471574 scopus 로고    scopus 로고
    • Bacterial cell-free system for highly efficient protein synthesis
    • Wiley-VCH, Weinheim, Germany, A.S. Spirin, J.R. Swartz (Eds.)
    • Kigawa T., Matsuda T., Yabuki T., Yokoyama S. Bacterial cell-free system for highly efficient protein synthesis. Cell-Free Protein Synthesis 2007, Wiley-VCH, Weinheim, Germany. A.S. Spirin, J.R. Swartz (Eds.).
    • (2007) Cell-Free Protein Synthesis
    • Kigawa, T.1    Matsuda, T.2    Yabuki, T.3    Yokoyama, S.4
  • 62
    • 33751101136 scopus 로고    scopus 로고
    • Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3
    • Tochio N., Koshiba S., Kobayashi N., Inoue M., Yabuki T., Aoki M., et al. Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3. Protein Sci. 2006, 15:2534-2543.
    • (2006) Protein Sci. , vol.15 , pp. 2534-2543
    • Tochio, N.1    Koshiba, S.2    Kobayashi, N.3    Inoue, M.4    Yabuki, T.5    Aoki, M.6
  • 63
    • 33644840499 scopus 로고    scopus 로고
    • Solution structure of the SWIRM domain of human histone demethylase LSD1
    • Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M., et al. Solution structure of the SWIRM domain of human histone demethylase LSD1. Structure 2006, 14:457-468.
    • (2006) Structure , vol.14 , pp. 457-468
    • Tochio, N.1    Umehara, T.2    Koshiba, S.3    Inoue, M.4    Yabuki, T.5    Aoki, M.6
  • 64
    • 0018435056 scopus 로고
    • New procedure for purifying histone pairs H2AH2B and H-3H-4 from chromatin using hydroxylapatite
    • Simon R.H., Felsenfeld G. New procedure for purifying histone pairs H2AH2B and H-3H-4 from chromatin using hydroxylapatite. Nucleic Acids Res. 1979, 6:689-696.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 689-696
    • Simon, R.H.1    Felsenfeld, G.2
  • 66
    • 0034100123 scopus 로고    scopus 로고
    • A human homologue of yeast anti-silencing factor has histone chaperone activity
    • Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M. A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells 2000, 5:221-233.
    • (2000) Genes Cells , vol.5 , pp. 221-233
    • Munakata, T.1    Adachi, N.2    Yokoyama, N.3    Kuzuhara, T.4    Horikoshi, M.5
  • 68
    • 34547923673 scopus 로고    scopus 로고
    • KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
    • Kobayashi N., Iwahara J., Koshiba S., Tomizawa T., Tochio N., Güntert P., et al. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. J. Biomol. NMR 2007, 39:31-52.
    • (2007) J. Biomol. NMR , vol.39 , pp. 31-52
    • Kobayashi, N.1    Iwahara, J.2    Koshiba, S.3    Tomizawa, T.4    Tochio, N.5    Güntert, P.6
  • 69
    • 34249765651 scopus 로고
    • NMR View-a computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NMR View-a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 71
    • 1842426942 scopus 로고    scopus 로고
    • Direct demonstration of structural similarity between native and denatured eglin C
    • Ohnishi S., Lee A.L., Edgell M.H., Shortle D. Direct demonstration of structural similarity between native and denatured eglin C. Biochemistry 2004, 43:4064-4070.
    • (2004) Biochemistry , vol.43 , pp. 4064-4070
    • Ohnishi, S.1    Lee, A.L.2    Edgell, M.H.3    Shortle, D.4
  • 72
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Rückert M., Otting G. Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments. J. Am. Chem. Soc. 2000, 122:7793-7797.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Rückert, M.1    Otting, G.2
  • 73
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M., Delaglio F., Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 1998, 131:373-378.
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 74
    • 42149130389 scopus 로고    scopus 로고
    • NMR: prediction of molecular alignment from structure using the PALES software
    • Zweckstetter M. NMR: prediction of molecular alignment from structure using the PALES software. Nat. Protoc. 2008, 3:679-690.
    • (2008) Nat. Protoc. , vol.3 , pp. 679-690
    • Zweckstetter, M.1
  • 75
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 1999, 13:289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 76
    • 69849094976 scopus 로고    scopus 로고
    • Structural basis for the sequence-specific RNA-recognition mechanism of human CUG-BP1 RRM3
    • Tsuda K., Kuwasako K., Takahashi M., Someya T., Inoue M., Terada T., et al. Structural basis for the sequence-specific RNA-recognition mechanism of human CUG-BP1 RRM3. Nucleic Acids Res. 2009, 37:5151-5166.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5151-5166
    • Tsuda, K.1    Kuwasako, K.2    Takahashi, M.3    Someya, T.4    Inoue, M.5    Terada, T.6
  • 77
  • 78
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996, 14:29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 79
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization
    • Grzesiek S., Anglister J., Bax A. Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization. J. Magn. Reson., Ser. B 1993, 101:114-119.
    • (1993) J. Magn. Reson., Ser. B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 80
    • 0000612671 scopus 로고    scopus 로고
    • PLUSH TACSY: homonuclear planar TACSY with two-band selective shaped pulses applied to C-alpha,C' transfer and C-beta,C-aromatic correlations
    • Carlomagno T., Maurer M., Sattler M., Schwendinger M.G., Glaser S.J., Griesinger C. PLUSH TACSY: homonuclear planar TACSY with two-band selective shaped pulses applied to C-alpha,C' transfer and C-beta,C-aromatic correlations. J. Biomol. NMR 1996, 8:161-170.
    • (1996) J. Biomol. NMR , vol.8 , pp. 161-170
    • Carlomagno, T.1    Maurer, M.2    Sattler, M.3    Schwendinger, M.G.4    Glaser, S.J.5    Griesinger, C.6
  • 81
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K., Riek R., Wider G., Wüthrich K. Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl Acad. Sci. USA 1997, 94:12366-12371.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 82
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins
    • Salzmann M., Pervushin K., Wider G., Senn H., Wüthrich K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl Acad. Sci. USA 1998, 95:13585-13590.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wüthrich, K.5
  • 83
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
    • Salzmann M., Wider G., Pervushin K., Senn H., Wüthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J. Am. Chem. Soc. 1999, 121:844-848.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wüthrich, K.5
  • 84
    • 0033599567 scopus 로고    scopus 로고
    • TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein
    • Yang D.W., Kay L.E. TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein. J. Am. Chem. Soc. 1999, 121:2571-2575.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2571-2575
    • Yang, D.W.1    Kay, L.E.2


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