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Volumn 390, Issue 2, 2009, Pages 231-244

The Box H/ACA snoRNP Assembly Factor Shq1p is a Chaperone Protein Homologous to Hsp90 Cochaperones that Binds to the Cbf5p Enzyme

Author keywords

chaperone; CS domain; H ACA snoRNP biogenesis; Shq1

Indexed keywords

CASEIN KINASE I; CHAPERONE; DYSKERIN; HEAT SHOCK PROTEIN 90; NUCLEAR PROTEIN; PSEUDOURIDINE; RNA; SMALL NUCLEOLAR RIBONUCLEOPROTEIN; TELOMERASE;

EID: 67349095697     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.076     Document Type: Article
Times cited : (19)

References (67)
  • 1
    • 19444374397 scopus 로고    scopus 로고
    • The many facets of H/ACA ribonucleoproteins
    • Meier U.T. The many facets of H/ACA ribonucleoproteins. Chromosoma 114 (2005) 1-14
    • (2005) Chromosoma , vol.114 , pp. 1-14
    • Meier, U.T.1
  • 3
    • 0030771087 scopus 로고    scopus 로고
    • Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA
    • Ni J., Tien A.L., and Fournier M.J. Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA. Cell 89 (1997) 565-573
    • (1997) Cell , vol.89 , pp. 565-573
    • Ni, J.1    Tien, A.L.2    Fournier, M.J.3
  • 4
    • 0030711050 scopus 로고    scopus 로고
    • Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs
    • Ganot P., Bortolin M.L., and Kiss T. Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs. Cell 89 (1997) 799-809
    • (1997) Cell , vol.89 , pp. 799-809
    • Ganot, P.1    Bortolin, M.L.2    Kiss, T.3
  • 5
    • 0037013831 scopus 로고    scopus 로고
    • Cajal body-specific small nuclear RNAs: a novel class of 2′-O-methylation and pseudouridylation guide RNAs
    • Darzacq X., Jady B.E., Verheggen C., Kiss A.M., Bertrand E., and Kiss T. Cajal body-specific small nuclear RNAs: a novel class of 2′-O-methylation and pseudouridylation guide RNAs. EMBO J. 21 (2002) 2746-2756
    • (2002) EMBO J. , vol.21 , pp. 2746-2756
    • Darzacq, X.1    Jady, B.E.2    Verheggen, C.3    Kiss, A.M.4    Bertrand, E.5    Kiss, T.6
  • 6
    • 0042967786 scopus 로고    scopus 로고
    • A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs
    • Richard P., Darzacq X., Bertrand E., Jady B.E., Verheggen C., and Kiss T. A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs. EMBO J. 22 (2003) 4283-4293
    • (2003) EMBO J. , vol.22 , pp. 4283-4293
    • Richard, P.1    Darzacq, X.2    Bertrand, E.3    Jady, B.E.4    Verheggen, C.5    Kiss, T.6
  • 7
    • 0842347403 scopus 로고    scopus 로고
    • U17/snR30 is a ubiquitous snoRNA with two conserved sequence motifs essential for 18S rRNA production
    • Atzorn V., Fragapane P., and Kiss T. U17/snR30 is a ubiquitous snoRNA with two conserved sequence motifs essential for 18S rRNA production. Mol. Cell. Biol. 24 (2004) 1769-1778
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1769-1778
    • Atzorn, V.1    Fragapane, P.2    Kiss, T.3
  • 8
    • 0030738552 scopus 로고    scopus 로고
    • U14 small nucleolar RNA makes multiple contacts with the pre-ribosomal RNA
    • Morrissey J.P., and Tollervey D. U14 small nucleolar RNA makes multiple contacts with the pre-ribosomal RNA. Chromosoma 105 (1997) 515-522
    • (1997) Chromosoma , vol.105 , pp. 515-522
    • Morrissey, J.P.1    Tollervey, D.2
  • 9
    • 17944388104 scopus 로고    scopus 로고
    • Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal
    • Jady B.E., Bertrand E., and Kiss T. Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal. J. Cell Biol. 164 (2004) 647-652
    • (2004) J. Cell Biol. , vol.164 , pp. 647-652
    • Jady, B.E.1    Bertrand, E.2    Kiss, T.3
  • 10
    • 0035253526 scopus 로고    scopus 로고
    • Stable expression in yeast of the mature form of human telomerase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p
    • Dez C., Henras A., Faucon B., Lafontaine D., Caizergues-Ferrer M., and Henry Y. Stable expression in yeast of the mature form of human telomerase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p. Nucleic Acids Res. 29 (2001) 598-603
    • (2001) Nucleic Acids Res. , vol.29 , pp. 598-603
    • Dez, C.1    Henras, A.2    Faucon, B.3    Lafontaine, D.4    Caizergues-Ferrer, M.5    Henry, Y.6
  • 11
    • 0032961170 scopus 로고    scopus 로고
    • A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3′ end
    • Mitchell J.R., Cheng J., and Collins K. A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3′ end. Mol. Cell. Biol. 19 (1999) 567-576
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 567-576
    • Mitchell, J.R.1    Cheng, J.2    Collins, K.3
  • 12
    • 0035670851 scopus 로고    scopus 로고
    • The snoRNA domain of vertebrate telomerase RNA functions to localize the RNA within the nucleus
    • Lukowiak A.A., Narayanan A., Li Z.H., Terns R.M., and Terns M.P. The snoRNA domain of vertebrate telomerase RNA functions to localize the RNA within the nucleus. RNA 7 (2001) 1833-1844
    • (2001) RNA , vol.7 , pp. 1833-1844
    • Lukowiak, A.A.1    Narayanan, A.2    Li, Z.H.3    Terns, R.M.4    Terns, M.P.5
  • 13
    • 39149123489 scopus 로고    scopus 로고
    • Unveiling substrate RNA binding to H/ACA RNPs: one side fits all
    • Li H. Unveiling substrate RNA binding to H/ACA RNPs: one side fits all. Curr. Opin. Struct. Biol. 18 (2008) 78-85
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 78-85
    • Li, H.1
  • 14
    • 33847187076 scopus 로고    scopus 로고
    • Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs
    • Matera A.G., Terns R.M., and Terns M.P. Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs. Nat. Rev. Mol. Cell Biol. 8 (2007) 209-220
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 209-220
    • Matera, A.G.1    Terns, R.M.2    Terns, M.P.3
  • 15
    • 33646076438 scopus 로고    scopus 로고
    • Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells
    • Darzacq X., Kittur N., Roy S., Shav-Tal Y., Singer R.H., and Meier U.T. Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells. J. Cell Biol. 173 (2006) 207-218
    • (2006) J. Cell Biol. , vol.173 , pp. 207-218
    • Darzacq, X.1    Kittur, N.2    Roy, S.3    Shav-Tal, Y.4    Singer, R.H.5    Meier, U.T.6
  • 16
    • 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
  • 17
    • 20744440616 scopus 로고    scopus 로고
    • The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae
    • Ballarino M., Morlando M., Pagano F., Fatica A., and Bozzoni I. The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 25 (2005) 5396-5403
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5396-5403
    • Ballarino, M.1    Morlando, M.2    Pagano, F.3    Fatica, A.4    Bozzoni, I.5
  • 18
    • 16244366466 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly
    • Yang P.K., Hoareau C., Froment C., Monsarrat B., Henry Y., and Chanfreau G. Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly. Mol. Cell. Biol. 25 (2005) 3295-3304
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3295-3304
    • Yang, P.K.1    Hoareau, C.2    Froment, C.3    Monsarrat, B.4    Henry, Y.5    Chanfreau, G.6
  • 20
    • 0035943003 scopus 로고    scopus 로고
    • The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1
    • Pellizzoni L., Baccon J., Charroux B., and Dreyfuss G. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol. 11 (2001) 1079-1088
    • (2001) Curr. Biol. , vol.11 , pp. 1079-1088
    • Pellizzoni, L.1    Baccon, J.2    Charroux, B.3    Dreyfuss, G.4
  • 22
    • 0037159511 scopus 로고    scopus 로고
    • The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis
    • Yang P.K., Rotondo G., Porras T., Legrain P., and Chanfreau G. The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis. J. Biol. Chem. 277 (2002) 45235-45242
    • (2002) J. Biol. Chem. , vol.277 , pp. 45235-45242
    • Yang, P.K.1    Rotondo, G.2    Porras, T.3    Legrain, P.4    Chanfreau, G.5
  • 23
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 (2002) 180-183
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6
  • 24
    • 59449098081 scopus 로고    scopus 로고
    • Structure and functional studies of the CS domain of the essential H/ACA RNP assembly protein Shq1
    • Singh M., Gonzales F.A., Cascio D., Heckmann N., Chanfreau G., and Feigon J. Structure and functional studies of the CS domain of the essential H/ACA RNP assembly protein Shq1. J. Biol. Chem. 284 (2008) 1906-1916
    • (2008) J. Biol. Chem. , vol.284 , pp. 1906-1916
    • Singh, M.1    Gonzales, F.A.2    Cascio, D.3    Heckmann, N.4    Chanfreau, G.5    Feigon, J.6
  • 25
    • 36549003965 scopus 로고    scopus 로고
    • InterPro and InterProScan: tools for protein sequence classification and comparison
    • Mulder N., and Apweiler R. InterPro and InterProScan: tools for protein sequence classification and comparison. Methods Mol. Biol. 396 (2007) 59-70
    • (2007) Methods Mol. Biol. , vol.396 , pp. 59-70
    • Mulder, N.1    Apweiler, R.2
  • 26
    • 66449111635 scopus 로고    scopus 로고
    • SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs
    • Epub ahead of print
    • Grozdanov P.N., Roy S., Kittur N., and Meier U.T. SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs. RNA (2009) Epub ahead of print
    • (2009) RNA
    • Grozdanov, P.N.1    Roy, S.2    Kittur, N.3    Meier, U.T.4
  • 27
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm L., Kaariainen S., Rosenstrom P., and Schenkel A. Searching protein structure databases with DaliLite v.3. Bioinformatics 24 (2008) 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 28
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alpha-crystallin domain fold in a chaperone assembly
    • Stamler R., Kappe G., Boelens W., and Slingsby C. Wrapping the alpha-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353 (2005) 68-79
    • (2005) J. Mol. Biol. , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 29
    • 0031897370 scopus 로고    scopus 로고
    • Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52
    • Buchner J., Weikl T., Bugl H., Pirkl F., and Bose S. Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52. Methods Enzymol. 290 (1998) 418-429
    • (1998) Methods Enzymol. , vol.290 , pp. 418-429
    • Buchner, J.1    Weikl, T.2    Bugl, H.3    Pirkl, F.4    Bose, S.5
  • 30
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • Takahashi A., Casais C., Ichimura K., and Shirasu K. HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc. Natl. Acad. Sci. USA 100 (2003) 11777-11782
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 31
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 (2006) 1013-1017
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5    Piper, P.W.6
  • 32
    • 57049133465 scopus 로고    scopus 로고
    • Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants
    • Kadota Y., Amigues B., Ducassou L., Madaoui H., Ochsenbein F., Guerois R., and Shirasu K. Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants. EMBO Rep. 9 (2008) 1209-1215
    • (2008) EMBO Rep. , vol.9 , pp. 1209-1215
    • Kadota, Y.1    Amigues, B.2    Ducassou, L.3    Madaoui, H.4    Ochsenbein, F.5    Guerois, R.6    Shirasu, K.7
  • 33
    • 54349122449 scopus 로고    scopus 로고
    • Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes
    • Zhang M., Boter M., Li K., Kadota Y., Panaretou B., Prodromou C., et al. Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes. EMBO J. 27 (2008) 2789-2798
    • (2008) EMBO J. , vol.27 , pp. 2789-2798
    • Zhang, M.1    Boter, M.2    Li, K.3    Kadota, Y.4    Panaretou, B.5    Prodromou, C.6
  • 34
    • 1942436961 scopus 로고    scopus 로고
    • Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain
    • Lee Y.T., Jacob J., Michowski W., Nowotny M., Kuznicki J., and Chazin W.J. Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. J. Biol. Chem. 279 (2004) 16511-16517
    • (2004) J. Biol. Chem. , vol.279 , pp. 16511-16517
    • Lee, Y.T.1    Jacob, J.2    Michowski, W.3    Nowotny, M.4    Kuznicki, J.5    Chazin, W.J.6
  • 36
    • 4744356146 scopus 로고    scopus 로고
    • The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly
    • Lingelbach L.B., and Kaplan K.B. The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly. Mol. Cell. Biol. 24 (2004) 8938-8950
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8938-8950
    • Lingelbach, L.B.1    Kaplan, K.B.2
  • 37
    • 33845959149 scopus 로고    scopus 로고
    • Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p
    • Catlett M.G., and Kaplan K.B. Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J. Biol. Chem. 281 (2006) 33739-33748
    • (2006) J. Biol. Chem. , vol.281 , pp. 33739-33748
    • Catlett, M.G.1    Kaplan, K.B.2
  • 38
    • 34547555987 scopus 로고    scopus 로고
    • KinasePhos 2.0: a web server for identifying protein kinase-specific phosphorylation sites based on sequences and coupling patterns
    • Wong Y.H., Lee T.Y., Liang H.K., Huang C.M., Wang T.Y., Yang Y.H., et al. KinasePhos 2.0: a web server for identifying protein kinase-specific phosphorylation sites based on sequences and coupling patterns. Nucleic Acids Res. 35 (2007) W588-W594
    • (2007) Nucleic Acids Res. , vol.35
    • Wong, Y.H.1    Lee, T.Y.2    Liang, H.K.3    Huang, C.M.4    Wang, T.Y.5    Yang, Y.H.6
  • 39
    • 26444473237 scopus 로고    scopus 로고
    • The role of the casein kinase 1 (CK1) family in different signaling pathways linked to cancer development
    • Knippschild U., Wolff S., Giamas G., Brockschmidt C., Wittau M., Wurl P.U., et al. The role of the casein kinase 1 (CK1) family in different signaling pathways linked to cancer development. Onkologie 28 (2005) 508-514
    • (2005) Onkologie , vol.28 , pp. 508-514
    • Knippschild, U.1    Wolff, S.2    Giamas, G.3    Brockschmidt, C.4    Wittau, M.5    Wurl, P.U.6
  • 40
    • 35448947338 scopus 로고    scopus 로고
    • Chemical dissection of the APC repeat 3 multistep phosphorylation by the concerted action of protein kinases CK1 and GSK3
    • Ferrarese A., Marin O., Bustos V.H., Venerando A., Antonelli M., Allende J.E., and Pinna L.A. Chemical dissection of the APC repeat 3 multistep phosphorylation by the concerted action of protein kinases CK1 and GSK3. Biochemistry 46 (2007) 11902-11910
    • (2007) Biochemistry , vol.46 , pp. 11902-11910
    • Ferrarese, A.1    Marin, O.2    Bustos, V.H.3    Venerando, A.4    Antonelli, M.5    Allende, J.E.6    Pinna, L.A.7
  • 41
    • 0035162071 scopus 로고    scopus 로고
    • Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3′-end formation
    • Gross S., and Moore C.L. Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3′-end formation. Mol. Cell. Biol. 21 (2001) 8045-8055
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8045-8055
    • Gross, S.1    Moore, C.L.2
  • 42
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: participation in multiple cellular processes in eukaryotes
    • Knippschild U., Gocht A., Wolff S., Huber N., Lohler J., and Stoter M. The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell. Signalling 17 (2005) 675-689
    • (2005) Cell. Signalling , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Lohler, J.5    Stoter, M.6
  • 43
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
    • Muchowski P.J., and Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin. Proc. Natl. Acad. Sci. USA 95 (1998) 1004-1009
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 44
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose S., Weikl T., Bugl H., and Buchner J. Chaperone function of Hsp90-associated proteins. Science 274 (1996) 1715-1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 45
    • 0034725641 scopus 로고    scopus 로고
    • Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone
    • Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A., and Toft D.O. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 (2000) 23045-23052
    • (2000) J. Biol. Chem. , vol.275 , pp. 23045-23052
    • Weaver, A.J.1    Sullivan, W.P.2    Felts, S.J.3    Owen, B.A.4    Toft, D.O.5
  • 46
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao R., Davey M., Hsu Y.C., Kaplanek P., Tong A., Parsons A.B., et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120 (2005) 715-727
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3    Kaplanek, P.4    Tong, A.5    Parsons, A.B.6
  • 48
    • 39049143941 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
    • Zhao R., Kakihara Y., Gribun A., Huen J., Yang G., Khanna M., et al. Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180 (2008) 563-578
    • (2008) J. Cell Biol. , vol.180 , pp. 563-578
    • Zhao, R.1    Kakihara, Y.2    Gribun, A.3    Huen, J.4    Yang, G.5    Khanna, M.6
  • 49
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440 (2006) 637-643
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5    Ignatchenko, A.6
  • 50
    • 33749247285 scopus 로고    scopus 로고
    • Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA
    • Normand C., Capeyrou R., Quevillon-Cheruel S., Mougin A., Henry Y., and Caizergues-Ferrer M. Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA. RNA 12 (2006) 1868-1882
    • (2006) RNA , vol.12 , pp. 1868-1882
    • Normand, C.1    Capeyrou, R.2    Quevillon-Cheruel, S.3    Mougin, A.4    Henry, Y.5    Caizergues-Ferrer, M.6
  • 54
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori S., Abeygunawardana C., Johnson M.O., and Vanzijl P.C.M. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. Ser. B 108 (1995) 94-98
    • (1995) J. Magn. Reson. Ser. B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Vanzijl, P.C.M.4
  • 56
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S., and Ad B. 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    Ad, B.2
  • 57
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram D.R., and Kay L.E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. Ser. B 103 (1994) 203-216
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 59
    • 85083125988 scopus 로고    scopus 로고
    • Goddard T. D. & Kneller, D. G. SPARKY 3. University of California, San Francisco.
    • Goddard T. D. & Kneller, D. G. SPARKY 3. University of California, San Francisco.
  • 60
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J. Biomol. NMR 24 (2002) 171-189
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 61
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 62
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319 (2002) 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 63
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. 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
  • 65
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. 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
  • 66
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm L., and Sander C. Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res. 25 (1997) 231-234
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 67
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-5, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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