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Volumn 2, Issue 2, 2008, Pages 147-149

1H, 13C and 15N resonance assignment of the ubiquitin-like domain from Dsk2p

Author keywords

Dsk2p; Proteasome; Ubiquitin like domain; UBL

Indexed keywords

CARBON; CELL CYCLE PROTEIN; DSK2 PROTEIN, S CEREVISIAE; NITROGEN; PROTON; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN;

EID: 68849100753     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-008-9107-7     Document Type: Article
Times cited : (3)

References (22)
  • 1
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMRspectral analysis
    • doi:10.1007/BF00417486
    • Bartels C, Xia T, Guntert P et al (1995) The program XEASY for computer-supported NMRspectral analysis. J BiomolNMR 5:1-10. doi:10.1007/BF00417486
    • (1995) J Biomol NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Guntert, P.3
  • 2
    • 0030015075 scopus 로고    scopus 로고
    • Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
    • DOI 10.1083/jcb.133.6.1331
    • Biggins S, Ivanovska I, Rose MD (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133:1331-1346. doi:10.1083/jcb.133.6.1331 (Pubitemid 26192333)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1331-1346
    • Biggins, S.1    Ivanovska, I.2    Rose, M.D.3
  • 3
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free R, and complete cross-validation for dipolar coupling refinement of nmr structures
    • DOI 10.1021/ja991789k
    • Clore GM, Garrett DS (1999) R-factor, Free R, and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures. J Am Chem Soc 121:9008-9012. doi:10.1021/ja991789k (Pubitemid 29477367)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.39 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 7
    • 34248180045 scopus 로고    scopus 로고
    • A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome
    • DOI 10.1091/mbc.E06-10-0965
    • Ghaboosi N, Deshaies RJ (2007) A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome. Mol Biol Cell 18:1953-1963. doi:10.1091/mbc.E06-10-0965 (Pubitemid 46717574)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1953-1963
    • Ghaboosi, N.1    Deshaies, R.J.2
  • 8
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • DOI 10.1023/A:1025467918856
    • Hall JB, Fushman D (2003) Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. J Biomol NMR 27:261-275. doi:10.1023/A:1025467918856 (Pubitemid 37185125)
    • (2003) Journal of Biomolecular NMR , vol.27 , Issue.3 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2
  • 9
    • 33751581527 scopus 로고    scopus 로고
    • Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway
    • DOI 10.1038/sj.emboj.7601418, PII 7601418
    • Ishii T, Funakoshi M, Kobayashi H (2006) Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J 25:5492-5503. doi:10.1038/sj.emboj. 7601418 (Pubitemid 44847190)
    • (2006) EMBO Journal , vol.25 , Issue.23 , pp. 5492-5503
    • Ishii, T.1    Funakoshi, M.2    Kobayashi, H.3
  • 12
    • 33644859939 scopus 로고    scopus 로고
    • Structures of the Dsk2 UBL and UBA domains and their complex
    • doi:10.1107/S0907444905037777
    • Lowe ED, Hasan N, Trempe JF et al (2006) Structures of the Dsk2 UBL and UBA domains and their complex. Acta Crystallogr D Biol Crystallogr 62:177-188. doi:10.1107/S0907444905037777
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 177-188
    • Lowe, E.D.1    Hasan, N.2    Trempe, J.F.3
  • 13
    • 17044420416 scopus 로고    scopus 로고
    • Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition
    • doi:10.1016/j.str.2005. 01.011
    • Ohno A, Jee J, Fujiwara K et al (2005) Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition. Struct 13:521-532. doi:10.1016/j.str.2005. 01.011
    • (2005) Struct , vol.13 , pp. 521-532
    • Ohno, A.1    Jee, J.2    Fujiwara, K.3
  • 14
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • DOI 10.1038/nsmb962, PII NSMB962
    • Raasi S, Varadan R, Fushman D et al (2005) Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nat Struct Mol Biol 12:708-714. doi:10.1038/nsmb962 (Pubitemid 43086277)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.8 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 15
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • doi:10.1021/ja001068h
    • Ruckert M, Otting G (2000) Alignment of Biological Macromolecules in Novel Nonionic Liquid Crystalline Media for NMR Experiments. J Am Chem Soc 122:7793-7797. doi:10.1021/ja001068h
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 16
    • 1342304089 scopus 로고    scopus 로고
    • 63-linked Di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • DOI 10.1074/jbc.M309184200
    • Varadan R, Assfalg M, Haririnia A et al (2004) Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J Biol Chem 279:7055-7063. doi:10.1074/jbc.M309184200 (Pubitemid 38248851)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 17
    • 20444391345 scopus 로고    scopus 로고
    • Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain
    • DOI 10.1016/j.molcel.2005.05.013, PII S1097276505013195
    • Varadan R, Assfalg M, Raasi S et al (2005) Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain. Mol Cell 18:687-698. doi:10.1016/j.molcel.2005. 05.013 (Pubitemid 40804804)
    • (2005) Molecular Cell , vol.18 , Issue.6 , pp. 687-698
    • Varadan, R.1    Assfalg, M.2    Raasi, S.3    Pickart, C.4    Fushman, D.5
  • 18
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • DOI 10.1016/j.cell.2004.06.014, PII S0092867404005835
    • Verma R, Oania R, Graumann J et al (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitinproteasome system. Cell 118:99-110. doi:10.1016/j.cell.2004. 06.014 (Pubitemid 38902817)
    • (2004) Cell , vol.118 , Issue.1 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 20
    • 0028393784 scopus 로고
    • 13C chemical-shift data
    • doi:10.1007/BF00175245
    • 13C chemical-shift data. J Biomol NMR 4:171-180. doi:10.1007/ BF00175245
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 21
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • doi:10.1021/bi00121a010
    • Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651. doi:10.1021/bi00121a010
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 22
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: Nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • doi:10.1016/j.jmb.2007.12.029
    • Zhang D, Raasi S, Fushman D (2008) Affinity makes the difference: Nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J Mol Biol 377:162-180. doi:10.1016/j.jmb. 2007.12.029
    • (2008) J Mol Biol , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.