메뉴 건너뛰기




Volumn 23, Issue 5, 2014, Pages 662-667

Solution structure of lysine-free (K0) ubiquitin

Author keywords

CS Rosetta; K0 Ub; NMR; Ubiquitin

Indexed keywords

LYSINE; LYSINE FREE UBIQUITIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84901026702     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2450     Document Type: Article
Times cited : (6)

References (33)
  • 2
    • 84877313192 scopus 로고    scopus 로고
    • Assembly, analysis and architecture of atypical ubiquitin chains
    • Hospenthal MK, Freund SM, Komander D (2013) Assembly, analysis and architecture of atypical ubiquitin chains. Nat Struct Mol Biol 20:555-565.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 555-565
    • Hospenthal, M.K.1    Freund, S.M.2    Komander, D.3
  • 3
    • 58149280817 scopus 로고    scopus 로고
    • Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate
    • Ikeda H, Kerppola TK (2008) Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate. Mol Biol Cell 19:4588-4601.
    • (2008) Mol Biol Cell , vol.19 , pp. 4588-4601
    • Ikeda, H.1    Kerppola, T.K.2
  • 4
    • 84868671432 scopus 로고    scopus 로고
    • Comprehensive study of protein ubiquitylation sites by conjugation of engineered lysine-less ubiquitin
    • Oshikawa K, Matsumoto M, Nakayama KI (2012) Comprehensive study of protein ubiquitylation sites by conjugation of engineered lysine-less ubiquitin. Seikagaku 84:479-487.
    • (2012) Seikagaku , vol.84 , pp. 479-487
    • Oshikawa, K.1    Matsumoto, M.2    Nakayama, K.I.3
  • 5
    • 84856637551 scopus 로고    scopus 로고
    • Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin
    • Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI (2012) Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin. J Proteome Res 11:796-807.
    • (2012) J Proteome Res , vol.11 , pp. 796-807
    • Oshikawa, K.1    Matsumoto, M.2    Oyamada, K.3    Nakayama, K.I.4
  • 6
    • 79953221150 scopus 로고    scopus 로고
    • The role of monoubiquitination in endocytic degradation of human ether-A-go-go-related gene (hERG) channels under low K1 conditions
    • Sun T, Guo J, Shallow H, Yang T, Xu J, Li W, Hanson C, Wu JG, Li X, Massaeli H, Zhang S (2011) The role of monoubiquitination in endocytic degradation of human ether-A-go-go-related gene (hERG) channels under low K1 conditions. J Biol Chem 286:6751-6759.
    • (2011) J Biol Chem , vol.286 , pp. 6751-6759
    • Sun, T.1    Guo, J.2    Shallow, H.3    Yang, T.4    Xu, J.5    Li, W.6    Hanson, C.7    Wu, J.G.8    Li, X.9    Massaeli, H.10    Zhang, S.11
  • 8
    • 33847056330 scopus 로고    scopus 로고
    • Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH
    • Eddins MJ, Waradan R, Fushman D, Pickart CM, Wolberger C (2007) Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH. J Mol Biol 367:204-211.
    • (2007) J Mol Biol , vol.367 , pp. 204-211
    • Eddins, M.J.1    Waradan, R.2    Fushman, D.3    Pickart, C.M.4    Wolberger, C.5
  • 10
    • 0032744041 scopus 로고    scopus 로고
    • Effect of hydrophobic core packing on sidechain dynamics
    • Johnson EC, Handel TM (1999) Effect of hydrophobic core packing on sidechain dynamics. J Biomol NMR 15:135-143.
    • (1999) J Biomol NMR , vol.15 , pp. 135-143
    • Johnson, E.C.1    Handel, T.M.2
  • 11
    • 0033566738 scopus 로고    scopus 로고
    • Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin
    • Johnson EC, Lazar GA, Desjarlais JR, Handel TM (1999) Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin. Structure 7:967-976.
    • (1999) Structure , vol.7 , pp. 967-976
    • Johnson, E.C.1    Lazar, G.A.2    Desjarlais, J.R.3    Handel, T.M.4
  • 12
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar GA, Desjarlais JR, Handel TM (1997) De novo design of the hydrophobic core of ubiquitin. Protein Sci 6:1167-1178.
    • (1997) Protein Sci , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 13
    • 0033458847 scopus 로고    scopus 로고
    • Rotamer strain as a determinant of protein structural specificity
    • Lazar GA, Johnson EC, Desjarlais JR, Handel TM (1999) Rotamer strain as a determinant of protein structural specificity. Protein Sci 8:2598-2610.
    • (1999) Protein Sci , vol.8 , pp. 2598-2610
    • Lazar, G.A.1    Johnson, E.C.2    Desjarlais, J.R.3    Handel, T.M.4
  • 14
    • 37349046664 scopus 로고    scopus 로고
    • Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins
    • Haririnai A, Verma R, Purohit N, Twarog MZ, Deshaies RJ, Bolon D, Fushman D (2008) Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins. J Mol Biol 375: 979-996.
    • (2008) J Mol Biol , vol.375 , pp. 979-996
    • Haririnai, A.1    Verma, R.2    Purohit, N.3    Twarog, M.Z.4    Deshaies, R.J.5    Bolon, D.6    Fushman, D.7
  • 16
    • 84866998027 scopus 로고    scopus 로고
    • Structural and biochemical studies of the open state of Lys48-linked diubiquitin
    • Lai MY, Zhang D, Laronde-Leblanc N, Fushman D (2012) Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochim Biophys Acta 1823:2046-2056.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 2046-2056
    • Lai, M.Y.1    Zhang, D.2    Laronde-Leblanc, N.3    Fushman, D.4
  • 17
    • 84879834151 scopus 로고    scopus 로고
    • Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains
    • Castaneda CA, Kashyap TR, Nakasone MA, Krueger S, Fushman D (2013) Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains. Structure 21:1168-1181.
    • (2013) Structure , vol.21 , pp. 1168-1181
    • Castaneda, C.A.1    Kashyap, T.R.2    Nakasone, M.A.3    Krueger, S.4    Fushman, D.5
  • 18
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G, Marquardt JL, Ottiger M, Bax A (1998) Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J Am Chem Soc 120:6836-6837.
    • (1998) J Am Chem Soc , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 19
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194: 531-544.
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 20
    • 79851490872 scopus 로고    scopus 로고
    • Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H-15N NMR spectroscopy
    • Esadze A, Li DW, Wang T, Bruschweiler R, Iwahara J (2011) Dynamics of lysine side-chain amino groups in a protein studied by heteronuclear 1H-15N NMR spectroscopy. J Am Chem Soc 133:909-919.
    • (2011) J Am Chem Soc , vol.133 , pp. 909-919
    • Esadze, A.1    Li, D.W.2    Wang, T.3    Bruschweiler, R.4    Iwahara, J.5
  • 21
    • 23144437542 scopus 로고    scopus 로고
    • Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements
    • Eghbalnia HR, Wang L, Bahrami A, Assadi A, Markley JL (2005) Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements. J Biomol NMR 32:71-81.
    • (2005) J Biomol NMR , vol.32 , pp. 71-81
    • Eghbalnia, H.R.1    Wang, L.2    Bahrami, A.3    Assadi, A.4    Markley, J.L.5
  • 22
    • 68349093958 scopus 로고    scopus 로고
    • TALOS plus : A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS plus : A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 24
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter M, Bax A (2000) Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 122:3791-3792.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 28
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Mag Res Sp 34: 93-158.
    • (1999) Prog Nucl Mag Res Sp , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 31
    • 0033057676 scopus 로고    scopus 로고
    • A doubletseparated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings
    • Cordier F, Dingley AJ, Grzesiek S (1999) A doubletseparated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings. J Biomol NMR 13:175-180.
    • (1999) J Biomol NMR , vol.13 , pp. 175-180
    • Cordier, F.1    Dingley, A.J.2    Grzesiek, S.3
  • 32
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • 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.
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.