메뉴 건너뛰기




Volumn 54, Issue , 2010, Pages 1-16

Activation of ubiquitin and ubiquitin-like proteins

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

EID: 84934876880     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-6676-6_1     Document Type: Article
Times cited : (24)

References (61)
  • 1
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H., Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: pp. 373-428
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 2
    • 0033106369 scopus 로고    scopus 로고
    • Gettin’ down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke, L. (1999) Gettin’ down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol 9: pp. 107-112
    • (1999) Trends Cell Biol , vol.9 , pp. 107-112
    • Hicke, L.1
  • 3
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signaling in the NF-κB Pathway
    • Chen, Z.J. (2005) Ubiquitin signaling in the NF-κB Pathway. Nat Cell Biol 7: pp. 758-765
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 4
    • 0032702598 scopus 로고    scopus 로고
    • Role of covalent modifications of histones in regulating gene expression
    • Spencer, V.A., Davie, J.R. (1999) Role of covalent modifications of histones in regulating gene expression. Gene 240: pp. 1-12
    • (1999) Gene , vol.240 , pp. 1-12
    • Spencer, V.A.1    Davie, J.R.2
  • 5
    • 34547838920 scopus 로고    scopus 로고
    • Biological meaning of ubiquitination and DNA fragmentation in human spermatozoa
    • Muratori, M., Marchiani, S., Criscuoli, L. (2007) Biological meaning of ubiquitination and DNA fragmentation in human spermatozoa. Soc Reprod Fertil Suppl 63: pp. 153-158
    • (2007) Soc Reprod Fertil Suppl , vol.63 , pp. 153-158
    • Muratori, M.1    Marchiani, S.2    Criscuoli, L.3
  • 6
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher, O., Felberbaum, R., Hochstrasser, M. (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: pp. 159-180
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 7
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. (2009) Origin and function of ubiquitin-like proteins. Nature 458: pp. 422-429
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 8
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • Ciechanover, A., Ben-Saadon, R. (2003) N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol 14: pp. 103-106
    • (2003) Trends Cell Biol , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 9
    • 34547957271 scopus 로고    scopus 로고
    • A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p
    • Williams, C., Den, B.M., Sprenger, R.R. (2007) A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. J Biol Chem 282: pp. 22534-22543
    • (2007) J Biol Chem , vol.282 , pp. 22534-22543
    • Williams, C.1    Den, B.M.2    Sprenger, R.R.3
  • 10
    • 68549119002 scopus 로고    scopus 로고
    • Role of the RING-CH domain of viral ligase mK3 in ubiquitination of nonlysine and lysine MHC I residues
    • Herr, R.A., Harris, J., Fang, S. (2009) Role of the RING-CH domain of viral ligase mK3 in ubiquitination of nonlysine and lysine MHC I residues. Traffic 10: pp. 1301-1317
    • (2009) Traffic , vol.10 , pp. 1301-1317
    • Herr, R.A.1    Harris, J.2    Fang, S.3
  • 11
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez, J.G., Moras, D. (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22: pp. 211-216
    • (1997) Trends Biochem Sci , vol.22 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 12
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A.L., Siepmann, T.J. (1997) Pathways of ubiquitin conjugation. FASEB J 11: pp. 1257-1268
    • (1997) FASEB J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 13
    • 0021102445 scopus 로고
    • Ubiquitin adenylate: Structure and role in ubiquitin activation
    • Haas, A.L., Warms, J.V., Rose, I.A. (1983) Ubiquitin adenylate: Structure and role in ubiquitin activation. Biochemistry 22: pp. 4388-4394
    • (1983) Biochemistry , vol.22 , pp. 4388-4394
    • Haas, A.L.1    Warms, J.V.2    Rose, I.A.3
  • 14
    • 0028308828 scopus 로고
    • Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme
    • Burch, T.J., Haas, A.L. (1994) Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme. Biochemistry 33: pp. 7300-7308
    • (1994) Biochemistry , vol.33 , pp. 7300-7308
    • Burch, T.J.1    Haas, A.L.2
  • 15
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas, A.L., Warms, J.V., Hershko, A. (1982) Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J Biol Chem 257: pp. 2543-2548
    • (1982) J Biol Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3
  • 16
    • 0020479562 scopus 로고
    • The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis
    • Haas, A.L., Rose, I.A. (1982) The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J Biol Chem 257: pp. 10329-10337
    • (1982) J Biol Chem , vol.257 , pp. 10329-10337
    • Haas, A.L.1    Rose, I.A.2
  • 17
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • Haas, A.L., Bright, P.M. (1988) The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes. J Biol Chem 263: pp. 13258-13267
    • (1988) J Biol Chem , vol.263 , pp. 13258-13267
    • Haas, A.L.1    Bright, P.M.2
  • 18
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • Pickart, C.M., Rose, I.A. (1985) Functional heterogeneity of ubiquitin carrier proteins. J Biol Chem 260: pp. 1573-1581
    • (1985) J Biol Chem , vol.260 , pp. 1573-1581
    • Pickart, C.M.1    Rose, I.A.2
  • 19
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake, M.W., Wuebbens, M.M., Rajagopalan, K.V. (2001) Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414: pp. 325-329
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 20
    • 19444371837 scopus 로고    scopus 로고
    • Structural analysis of Escherichia Coli ThiF
    • Duda, D.M., Walden, H., Sfondouris, J. (2005) Structural analysis of Escherichia Coli ThiF. J Mol Biol 349: pp. 774-786
    • (2005) J Mol Biol , vol.349 , pp. 774-786
    • Duda, D.M.1    Walden, H.2    Sfondouris, J.3
  • 21
    • 33747219426 scopus 로고    scopus 로고
    • The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like ß-grasp domains
    • Iyer, L.M., Burroughs, A.M., Aravind, L. (2006) The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like ß-grasp domains. Genome Biol 7: pp. R60
    • (2006) Genome Biol , vol.7
    • Iyer, L.M.1    Burroughs, A.M.2    Aravind, L.3
  • 22
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • Rudolph, M.J., Wuebbens, M.M., Rajagopalan, K.V. (2001) Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol 8: pp. 42-46
    • (2001) Nat Struct Biol , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 23
    • 67650450156 scopus 로고    scopus 로고
    • How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic
    • Regni, C.A., Roush, R.F., Miller, D.J. (2009) How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic. EMBO J 28: pp. 1953-1964
    • (2009) EMBO J , vol.28 , pp. 1953-1964
    • Regni, C.A.1    Roush, R.F.2    Miller, D.J.3
  • 24
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman, B.A., Harper, J.W. (2009) Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 10: pp. 319-331
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 25
    • 0038526241 scopus 로고    scopus 로고
    • Protein interactions within the N-end rule ubiquitin ligation pathway
    • Siepmann, T.J., Bohnsack, R.N., Tokgöz, Z. (2003) Protein interactions within the N-end rule ubiquitin ligation pathway. J Biol Chem 278: pp. 9448-9457
    • (2003) J Biol Chem , vol.278 , pp. 9448-9457
    • Siepmann, T.J.1    Bohnsack, R.N.2    Tokgöz, Z.3
  • 26
    • 0037697382 scopus 로고    scopus 로고
    • Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer
    • Bohnsack, R.N., Haas, A.L. (2003) Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer. J Biol Chem 278: pp. 26823-26830
    • (2003) J Biol Chem , vol.278 , pp. 26823-26830
    • Bohnsack, R.N.1    Haas, A.L.2
  • 27
    • 84889624219 scopus 로고    scopus 로고
    • ISG15-dependent regulation
    • Mayer, R.J., Ciechanover, A., Rechsteiner, M. eds., Wiley-VCH Verlag, Weinheim, German
    • Haas, A.L. ISG15-dependent regulation. In: Mayer, R.J., Ciechanover, A., Rechsteiner, M. eds. (2006) Protein Degradation. Wiley-VCH Verlag, Weinheim, Germany, pp. 103-131
    • (2006) Protein Degradation , pp. 103-131
    • Haas, A.L.1
  • 28
    • 0013601039 scopus 로고
    • Immunochemical probes of ubiquitin pool dynamics
    • Rechsteiner, M. eds, Plenum Press, New Yor
    • Haas, A.L. Immunochemical probes of ubiquitin pool dynamics. In: Rechsteiner, M. eds. (1988) Ubiquitin. Plenum Press, New York, pp. 173-206
    • (1988) Ubiquitin , pp. 173-206
    • Haas, A.L.1
  • 29
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NED 8
    • Walden, H., Podgorski, M.S., Schulman, B.A. (2003) Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NED 8. Nature 422: pp. 330-334
    • (2003) Nature , vol.422 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 30
    • 0347416977 scopus 로고    scopus 로고
    • The structure of the APPBP1-UBA3-NED 8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1
    • Walden, H., Podgorski, M.S., Huang, D.T. (2003) The structure of the APPBP1-UBA3-NED 8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol Cell 12: pp. 1427-1437
    • (2003) Mol Cell , vol.12 , pp. 1427-1437
    • Walden, H.1    Podgorski, M.S.2    Huang, D.T.3
  • 31
    • 33846548206 scopus 로고    scopus 로고
    • Basis for a ubiquitin-like protein thioester switch toggling E1-E 2 affinity
    • Huang, D.T., Hunt, H.W., Zhuang, M. (2007) Basis for a ubiquitin-like protein thioester switch toggling E1-E 2 affinity. Nature 445: pp. 394-398
    • (2007) Nature , vol.445 , pp. 394-398
    • Huang, D.T.1    Hunt, H.W.2    Zhuang, M.3
  • 32
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    • Lois, L.M., Lima, C.D. (2005) Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J 24: pp. 439-451
    • (2005) EMBO J , vol.24 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 33
    • 47549111312 scopus 로고    scopus 로고
    • Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes
    • Lee, I., Schindelin, H. (2008) Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell 134: pp. 268-278
    • (2008) Cell , vol.134 , pp. 268-278
    • Lee, I.1    Schindelin, H.2
  • 34
    • 0027165193 scopus 로고
    • Cloning of a cDNA which encodes a novel ubiquitin-like protein
    • Kumar, S., Yoshida, Y., Noda, M. (1993) Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem Biophys Res Commun 195: pp. 393-399
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 393-399
    • Kumar, S.1    Yoshida, Y.2    Noda, M.3
  • 35
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NED 8 and interactions with ubiquitin pathway enzymes
    • Whitby, F.G., Xia, G., Pickart, C.M. (1998) Crystal structure of the human ubiquitin-like protein NED 8 and interactions with ubiquitin pathway enzymes. J Biol Chem 273: pp. 34983-34991
    • (1998) J Biol Chem , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3
  • 36
    • 30144434909 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ThiS-T hiF complex, a key component of the sulfur transfer system in thiamin biosynthesis
    • Lehmann, C., Begley, T.P., Ealick, S.E. (2006) Structure of the Escherichia coli ThiS-T hiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45: pp. 11-19
    • (2006) Biochemistry , vol.45 , pp. 11-19
    • Lehmann, C.1    Begley, T.P.2    Ealick, S.E.3
  • 37
    • 0032568948 scopus 로고    scopus 로고
    • Thiamin biosynthesis in Escherichia coli. Identification of This thiocarboxylate as the immediate sulfur donor in the thiazole formation
    • Taylor, S.V., Kelleher, N.L., Kinsland, C. (1998) Thiamin biosynthesis in Escherichia coli. Identification of This thiocarboxylate as the immediate sulfur donor in the thiazole formation. J Biol Chem 273: pp. 16555-16560
    • (1998) J Biol Chem , vol.273 , pp. 16555-16560
    • Taylor, S.V.1    Kelleher, N.L.2    Kinsland, C.3
  • 38
    • 0028577266 scopus 로고
    • Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs
    • Handley-Gearhart, P.M., Stephen, A.G., Trausch-Azar, J.S. (1994) Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs. J Biol Chem 269: pp. 33171-33178
    • (1994) J Biol Chem , vol.269 , pp. 33171-33178
    • Handley-Gearhart, P.M.1    Stephen, A.G.2    Trausch-Azar, J.S.3
  • 39
    • 0029022079 scopus 로고
    • An essential yeast gene encoding a homolog of ubiquitin-activating enzyme
    • Dohmen, R.J., Stappen, R., McGrath, J.P. (1995) An essential yeast gene encoding a homolog of ubiquitin-activating enzyme. J Biol Chem 270: pp. 18099-18109
    • (1995) J Biol Chem , vol.270 , pp. 18099-18109
    • Dohmen, R.J.1    Stappen, R.2    McGrath, J.P.3
  • 40
    • 33744948323 scopus 로고    scopus 로고
    • Pleiotropic effects of ATPMg2+ binding in the catalytic cycle of ubiquitin activating enzyme
    • Tokgöz, Z., Bohnsack, R.N., Haas, A.L. (2006) Pleiotropic effects of ATPMg2+ binding in the catalytic cycle of ubiquitin activating enzyme. J Biol Chem 281: pp. 14729-14737
    • (2006) J Biol Chem , vol.281 , pp. 14729-14737
    • Tokgöz, Z.1    Bohnsack, R.N.2    Haas, A.L.3
  • 41
    • 0141448966 scopus 로고    scopus 로고
    • Thermodynamic and extrathermodynamic requirements of enzyme catalysis
    • Wolfenden, R. (2003) Thermodynamic and extrathermodynamic requirements of enzyme catalysis. Biophys Chem 105: pp. 559-572
    • (2003) Biophys Chem , vol.105 , pp. 559-572
    • Wolfenden, R.1
  • 42
    • 0028235968 scopus 로고
    • Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1)
    • Pickart, C.M., Kasperek, E.M., Beal, R. (1994) Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1). J Biol Chem 269: pp. 7115-7123
    • (1994) J Biol Chem , vol.269 , pp. 7115-7123
    • Pickart, C.M.1    Kasperek, E.M.2    Beal, R.3
  • 43
    • 0026492497 scopus 로고
    • Ganglioside binding proteins of calf brain with ubiquitin-like N-terminals
    • Zdebska, E., Antoniewicz, J., Nilsson, B. (1992) Ganglioside binding proteins of calf brain with ubiquitin-like N-terminals. Eur J Biochem 210: pp. 483-489
    • (1992) Eur J Biochem , vol.210 , pp. 483-489
    • Zdebska, E.1    Antoniewicz, J.2    Nilsson, B.3
  • 44
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal, R., Deveraux, Q., Xia, G. (1996) Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci U.S.A 93: pp. 861-866
    • (1996) Proc Natl Acad Sci U.S.A , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3
  • 45
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar, S., Bugg, C.E., Cook, W.J. (1987) Structure of ubiquitin refined at 1.8 Å resolution. J Mol Biol 194: pp. 531-544
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 46
    • 0021810622 scopus 로고
    • The inactivation of ubiquitin accounts for the inability to demonstrate ATP, ubiquitin-dependent proteolysis in liver extracts
    • Haas, A.L., Murphy, K.E., Bright, P.M. (1985) The inactivation of ubiquitin accounts for the inability to demonstrate ATP, ubiquitin-dependent proteolysis in liver extracts. J Biol Chem 260: pp. 4694-4703
    • (1985) J Biol Chem , vol.260 , pp. 4694-4703
    • Haas, A.L.1    Murphy, K.E.2    Bright, P.M.3
  • 47
    • 0023886211 scopus 로고
    • Ubiquitin carboxyl-terminal peptides. Substrates for ubiquitin activating enzyme
    • Jonnalagadda, S., Ecker, D.J., Sternberg, E.J. (1988) Ubiquitin carboxyl-terminal peptides. Substrates for ubiquitin activating enzyme. J Biol Chem 263: pp. 5016-5019
    • (1988) J Biol Chem , vol.263 , pp. 5016-5019
    • Jonnalagadda, S.1    Ecker, D.J.2    Sternberg, E.J.3
  • 48
    • 0023656339 scopus 로고
    • Gene synthesis, expression, structures and functional activities of site-specific mutants of ubiquitin
    • Ecker, D.J., Butt, T.R., Marsh, J. (1987) Gene synthesis, expression, structures and functional activities of site-specific mutants of ubiquitin. J Biol Chem 262: pp. 14213-14221
    • (1987) J Biol Chem , vol.262 , pp. 14213-14221
    • Ecker, D.J.1    Butt, T.R.2    Marsh, J.3
  • 49
    • 50149089376 scopus 로고    scopus 로고
    • Structural dissection of a gating mechanism preventing misactivation of ubiquitin by NED 8’s E1
    • Souphron, J., Waddell, M.B., Paydar, A. (2008) Structural dissection of a gating mechanism preventing misactivation of ubiquitin by NED 8’s E1. Biochemistry 47: pp. 8961-8969
    • (2008) Biochemistry , vol.47 , pp. 8961-8969
    • Souphron, J.1    Waddell, M.B.2    Paydar, A.3
  • 50
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook, W.J., Jeffrey, L.C., Kasperek, E. (1994) Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J Mol Biol 236: pp. 601-609
    • (1994) J Mol Biol , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3
  • 51
    • 0038820381 scopus 로고    scopus 로고
    • Solution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding
    • Kang, R.S., Daniels, C.M., Francis, S.A. (2003) Solution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding. Cell 113: pp. 621-630
    • (2003) Cell , vol.113 , pp. 621-630
    • Kang, R.S.1    Daniels, C.M.2    Francis, S.A.3
  • 52
    • 14044278879 scopus 로고    scopus 로고
    • Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins
    • Prag, G., Lee, S., Mattera, R. (2005) Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins. Proc Natl Acad Sci USA 102: pp. 2334-2339
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2334-2339
    • Prag, G.1    Lee, S.2    Mattera, R.3
  • 53
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson, K.A., Kang, R.S., Stamenova, S.D. (2003) Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J 22: pp. 4597-4606
    • (2003) EMBO J , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3
  • 54
    • 61649103747 scopus 로고    scopus 로고
    • Structural Basis for Recognition of Diubiquitins by NEMO
    • Lo, Y.C., Lin, S.C., Rospigliosi, C.C. (2009) Structural Basis for Recognition of Diubiquitins by NEMO. Mol Cell 33: pp. 605-615
    • (2009) Mol Cell , vol.33 , pp. 605-615
    • Lo, Y.C.1    Lin, S.C.2    Rospigliosi, C.C.3
  • 55
    • 33644792262 scopus 로고    scopus 로고
    • Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5
    • Lee, S., Tsai, Y.C., Mattera, R. (2006) Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5. Nat Struct Mol Biol 13: pp. 264-271
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 264-271
    • Lee, S.1    Tsai, Y.C.2    Mattera, R.3
  • 56
    • 0032504021 scopus 로고    scopus 로고
    • Structure determination of the small ubiquitin-related modifier SUMO-1
    • Bayer, P., Arndt, A., Metzger, S. (1998) Structure determination of the small ubiquitin-related modifier SUMO-1. J Mol Biol 280: pp. 275-286
    • (1998) J Mol Biol , vol.280 , pp. 275-286
    • Bayer, P.1    Arndt, A.2    Metzger, S.3
  • 57
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield, P.M., Vierstra, R.D. (1992) Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis. J Biol Chem 267: pp. 14799-14803
    • (1992) J Biol Chem , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 58
    • 13244249669 scopus 로고    scopus 로고
    • Structural basis for recruitment of Ubc12 by an E2 binding domain in NED 8’s E1
    • Huang, D.T., Paydar, A., Zhuang, M. (2005) Structural basis for recruitment of Ubc12 by an E2 binding domain in NED 8’s E1. Mol Cell 17: pp. 341-350
    • (2005) Mol Cell , vol.17 , pp. 341-350
    • Huang, D.T.1    Paydar, A.2    Zhuang, M.3
  • 59
    • 53049083773 scopus 로고    scopus 로고
    • The basis for selective E1-E 2 interactions in the ISG15 conjugation system
    • Durfee, L.A., Kelley, M.L., Huibregtse, J.M. (2008) The basis for selective E1-E 2 interactions in the ISG15 conjugation system. J Biol Chem 283: pp. 23895-23902
    • (2008) J Biol Chem , vol.283 , pp. 23895-23902
    • Durfee, L.A.1    Kelley, M.L.2    Huibregtse, J.M.3
  • 60
    • 34447337222 scopus 로고    scopus 로고
    • The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications
    • Wang, J., Hu, W., Cai, S. (2007) The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications. Mol Cell 27: pp. 228-237
    • (2007) Mol Cell , vol.27 , pp. 228-237
    • Wang, J.1    Hu, W.2    Cai, S.3
  • 61
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NED 8-activating enzyme as a new approach to treat cancer
    • Soucy, T.A., Smith, P.G., Milhollen, M.A. (2009) An inhibitor of NED 8-activating enzyme as a new approach to treat cancer. Nature 458: pp. 732-736
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.