메뉴 건너뛰기




Volumn 13, Issue 5, 2012, Pages 462-468

A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex

Author keywords

HOIL 1L; HOIP; linear ubiquitin chain assembly complex; NF kB activation; UBA UBL interaction

Indexed keywords

PROTEIN HOIL 1L; PROTEIN HOIP; REGULATOR PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84860478940     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2012.24     Document Type: Article
Times cited : (50)

References (25)
  • 1
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: A new regulator of NF-kB activation
    • Iwai K, Tokunaga F (2009) Linear polyubiquitination: a new regulator of NF-kB activation. EMBO Rep 10: 706-713
    • (2009) EMBO Rep , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 2
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-kB activation
    • Tokunaga F et al (2009) Involvement of linear polyubiquitylation of NEMO in NF-kB activation. Nat Cell Biol 11: 123-132
    • (2009) Nat Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1
  • 4
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach B et al (2011) Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471: 591-596
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 5
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-kB activity and apoptosis
    • Ikeda F et al (2011) SHARPIN forms a linear ubiquitin ligase complex regulating NF-kB activity and apoptosis. Nature 471: 637-641
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 7
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains-from structures to functions
    • Dikic I, Wakatsuki S, Walters KJ (2009) Ubiquitin-binding domains-from structures to functions. Nat Rev Mol Cell Biol 10: 659-671
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 8
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper JW, Schulman BA (2006) Structural complexity in ubiquitin recognition. Cell 124: 1133-1136
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 9
    • 84873189921 scopus 로고    scopus 로고
    • Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex
    • [Epub ahead of print] doi:10.1007/s12104-011-9350-1
    • Uekusa Y et al (2011) Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex. Biomol NMR Assign [Epub ahead of print] doi:10.1007/s12104-011-9350-1
    • (2011) Biomol NMR Assign
    • Uekusa, Y.1
  • 11
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: Nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • 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
    • (2008) J Mol Biol , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein C, Blanc E, Roversi P, Bricogne G (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364: 215-230 (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 17
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams JP, Leslie AG (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr D Biol Crystallogr 52: 30-42
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallog 26: 283-291
    • (1993) J Appl Crystallog , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78: 1606-1619 (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 23
    • 0004040543 scopus 로고
    • San Francisco: University of California
    • Goddard T, Kneller D (1993) SPARKY 3. San Francisco: University of California
    • (1993) SPARKY 3
    • Goddard, T.1    Kneller, D.2
  • 25
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen YH, Yang JT, Martinez HM (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11: 4120-4131
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.