메뉴 건너뛰기




Volumn 12, Issue 9, 2007, Pages 3419-3430

Structural and electrostatic properties of ubiquitination and related pathways

Author keywords

Electrostatic potential; High throughput modelling; Review; Structure based design; Ubiquitin; Ubiquitin conjugating enzyme; Ubiquitin like protein

Indexed keywords

UBIQUITIN;

EID: 34347240365     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/2323     Document Type: Article
Times cited : (9)

References (73)
  • 1
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • DOI 10.1038/nrm1700
    • R. L. Welchman, C. Gordon and R. J. Mayer: Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6, 599-609 (2005) (Pubitemid 41081264)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.8 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 2
    • 33748742143 scopus 로고    scopus 로고
    • MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation
    • DOI 10.1074/jbc.M602283200
    • B. P. Downes, S. A. Saracco, S. S. Lee, D. N. Crowell and R. D. Vierstra: MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. J Biol Chem 281, 27145-57 (2006) (Pubitemid 44401744)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 27145-27157
    • Downes, B.P.1    Saracco, S.A.2    Sang, S.L.3    Crowell, D.N.4    Vierstra, R.D.5
  • 4
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • DOI 10.1126/science.1127085
    • D. Mukhopadhyay and H. Riezman: Proteasomeindependent functions of ubiquitin in endocytosis and signaling. Science 315, 201-5 (2007) (Pubitemid 46166358)
    • (2007) Science , vol.315 , Issue.5809 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 5
    • 0036674441 scopus 로고    scopus 로고
    • Structural attributes in the conjugation of ubiquitin, SUMO and RUB to protein substrates
    • S. Goettsch and P. Bayer: Structural attributes in the conjugation of ubiquitin, SUMO and RUB to protein substrates. Front Biosci 7, a148-62 (2002)
    • (2002) Front Biosci , vol.7
    • Goettsch, S.1    Bayer, P.2
  • 6
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • M. Koegl, T. Hoppe, S. Schlenker, H. D. Ulrich, T. U. Mayer and S. Jentsch: A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-44 (1999) (Pubitemid 29122806)
    • (1999) Cell , vol.96 , Issue.5 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 7
    • 33746664765 scopus 로고    scopus 로고
    • Can sequence determine function?
    • J. A. Gerlt and P. C. Babbitt: Can sequence determine function? Genome Biol 1, REVIEWS0005 (2000)
    • (2000) Genome Biol , vol.1
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 8
    • 33746622998 scopus 로고    scopus 로고
    • Protein-protein interactions more conserved within species than across species
    • S. Mika and B. Rost: Protein-protein interactions more conserved within species than across species. PLoS Comput Biol 2, e79 (2006)
    • PLoS Comput Biol , vol.2 , Issue.2006
    • Mika, S.1    Rost, B.2
  • 9
    • 0034651549 scopus 로고    scopus 로고
    • Structural alignment of ferredoxin and flavodoxin based on electrostatic potentials: Implications for their interactions with photosystem I and ferredoxin-NADP reductase
    • DOI 10.1002/(SICI)1097-0134(20000215)38:3<301::AID-PROT6>3.0.CO;2-Y
    • G. M. Ullmann, M. Hauswald, A. Jensen and E. W. Knapp: Structural alignment of ferredoxin and flavodoxin based on electrostatic potentials: implications for their interactions with photosystem I and ferredoxin-NADP reductase. Proteins 38, 301-9 (2000) (Pubitemid 30084339)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.3 , pp. 301-309
    • Ullmann, G.M.1    Hauswald, M.2    Jensen, A.3    Knapp, E.-W.4
  • 10
    • 0031414717 scopus 로고    scopus 로고
    • 6 may be isofunctional with tyrosine 83 in plastocyanin
    • DOI 10.1021/bi971241v
    • G. M. Ullmann, M. Hauswald, A. Jensen, N. M. Kostic and E. W. Knapp: Comparison of the physiologically equivalent proteins cytochrome c6 and plastocyanin on the basis of their electrostatic potentials. Tryptophan 63 in cytochrome c6 may be isofunctional with tyrosine 83 in plastocyanin. Biochemistry 36, 16187-96 (1997) (Pubitemid 28065033)
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16187-16196
    • Matthias Ullmann, G.1    Hauswald, M.2    Jensen, A.3    Kostic, N.M.4    Knapp, E.-W.5
  • 11
    • 0344837306 scopus 로고    scopus 로고
    • Conservation of electrostatic properties within enzyme families and superfamilies
    • DOI 10.1021/bi026918f
    • D. R. Livesay, P. Jambeck, A. Rojnuckarin and S. Subramaniam: Conservation of electrostatic properties within enzyme families and superfamilies. Biochemistry 42, 3464-73 (2003) (Pubitemid 36368640)
    • (2003) Biochemistry , vol.42 , Issue.12 , pp. 3464-3473
    • Livesay, D.R.1    Jambeck, P.2    Rojnuckarin, A.3    Subramaniam, S.4
  • 12
    • 4444314569 scopus 로고    scopus 로고
    • Determinants of functionality in the ubiquitin conjugating enzyme family
    • DOI 10.1016/j.str.2004.06.017, PII S0969212604002515
    • P. J. Winn, T. L. Religa, J. N. D. Battey, A. Banerjee and R. C. Wade: Determinants of functionality in the ubiquitin conjugating enzyme family. Structure 12, 1563-74 (2004) (Pubitemid 39200510)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1563-1574
    • Winn, P.J.1    Religa, T.L.2    Battey, J.N.D.3    Banerjee, A.4    Wade, R.C.5
  • 13
    • 0030772385 scopus 로고    scopus 로고
    • Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system
    • DOI 10.1074/jbc.272.34.21381
    • H. Tong, G. Hateboer, A. Perrakis, R. Bernards and T. K. Sixma: Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitinconjugating system. J Biol Chem 272, 21381-7 (1997) (Pubitemid 27374007)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.34 , pp. 21381-21387
    • Tong, H.1    Hateboer, G.2    Perrakis, A.3    Bernards, R.4    Sixma, T.K.5
  • 14
    • 0032168745 scopus 로고    scopus 로고
    • Structure of ubiquitin-conjugating enzyme 9 displays significant differences with other ubiquitin-conjugating enzymes which may reflect its specificity for sumo rather than ubiquitin
    • DOI 10.1107/S0907444998002480
    • M. F. Giraud, J. M. Desterro and J. H. Naismith: Structure of ubiquitin-conjugating enzyme 9 displays significant differences with other ubiquitin-conjugating enzymes which may reflect its specificity for sumo rather than ubiquitin. Acta Crystallogr D Biol Crystallogr 54, 891-8 (1998) (Pubitemid 28443601)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.5 , pp. 891-898
    • Giraud, M.-F.1    Desterro, J.M.P.2    Naismith, J.H.3
  • 15
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1997.0987
    • A. J. McCoy, V. C. Epa and P. M. Colman: Electrostatic complementarity at protein/protein interfaces. J Mol Biol 268, 570-84 (1997) (Pubitemid 27208075)
    • (1997) Journal of Molecular Biology , vol.268 , Issue.2 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 16
    • 0031820915 scopus 로고    scopus 로고
    • Electrotactins: A class of adhesion proteins with conserved electrostatic and structural motifs
    • S. A. Botti, C. E. Felder, J. L. Sussman and I. Silman: Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs. Protein Eng 11, 415-20 (1998) (Pubitemid 28347249)
    • (1998) Protein Engineering , vol.11 , Issue.6 , pp. 415-420
    • Botti, S.A.1    Felder, C.E.2    Sussman, J.L.3    Silman, I.4
  • 17
    • 0037472358 scopus 로고    scopus 로고
    • Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site
    • DOI 10.1016/S0304-3940(02)01298-3
    • G. Johnson and S. W. Moore: Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Neurosci Lett 337, 37-40 (2003) (Pubitemid 36078305)
    • (2003) Neuroscience Letters , vol.337 , Issue.1 , pp. 37-40
    • Johnson, G.1    Moore, S.W.2
  • 20
    • 0030891436 scopus 로고    scopus 로고
    • Simulation of the diffusional association of barnase and barstar
    • R. R. Gabdoulline and R. C. Wade: Simulation of the diffusional association of barnase and barstar. Biophys J 72, 1917-29 (1997) (Pubitemid 27184422)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 1917-1929
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 21
    • 0033168847 scopus 로고    scopus 로고
    • MolSurfer: Two-dimensional maps for navigating three-dimensional structures of proteins
    • DOI 10.1016/S0968-0004(99)01412-7, PII S0968000499014127
    • R. R. Gabdoulline, R. C. Wade and D. Walther: MolSurfer: two-dimensional maps for navigating threedimensional structures of proteins. Trends Biochem Sci 24, 285-7 (1999) (Pubitemid 29301694)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.7 , pp. 285-287
    • Gabdoulline, R.R.1    Wade, R.C.2    Walther, D.3
  • 22
    • 0035204346 scopus 로고    scopus 로고
    • Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome F
    • F. De Rienzo, R. R. Gabdoulline, M. C. Menziani, P. G. De Benedetti and R. C. Wade: Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f. Biophys J 81, 3090-104 (2001) (Pubitemid 33111461)
    • (2001) Biophysical Journal , vol.81 , Issue.6 , pp. 3090-3104
    • De Rienzo, F.1    Gabdoulline, R.R.2    Cristina Menziani, M.3    De Benedetti, P.G.4    Wade, R.C.5
  • 25
    • 3042683893 scopus 로고    scopus 로고
    • EF-site and PDBjViewer: Database and viewer for protein functional sites
    • DOI 10.1093/bioinformatics/bth073
    • K. Kinoshita and H. Nakamura: eF-site and PDBjViewer: database and viewer for protein functional sites. Bioinformatics 20, 1329-30 (2004) (Pubitemid 38807590)
    • (2004) Bioinformatics , vol.20 , Issue.8 , pp. 1329-1330
    • Kinoshita, K.1    Nakamura, H.2
  • 27
    • 37349014019 scopus 로고    scopus 로고
    • Application of new multiresolution methods for the comparison of biomolecular electrostatic properties in the absence of global structural similarity
    • DOI 10.1137/050647670
    • X. Zhang, C. L. Bajaj, B. Kwon, T. J. Dolinsky, J. E. Nielsen and N. A. Baker: Application of New Multiresolution Methods for the Comparison of Biomolecular Electrostatic Properties in the Absence of Global Structural Similarity. Multiscale Model Sim 5, 1196-1213 (2006) (Pubitemid 350285619)
    • (2006) Multiscale Modeling and Simulation , vol.5 , Issue.4 , pp. 1196-1213
    • Zhang, X.1    Bajaj, C.L.2    Kwon, B.3    Dolinsky, T.J.4    Nielsen, J.E.5    Baker, N.A.6
  • 28
    • 0036873086 scopus 로고    scopus 로고
    • The Poisson-Boltzmann equation for biomolecular electrostatics: A tool for structural biology
    • DOI 10.1002/jmr.577
    • F. Fogolari, A. Brigo and H. Molinari: The Poisson-Boltzmann equation for biomolecular electrostatics: a tool for structural biology. J Mol Recognit 15, 377-92 (2002) (Pubitemid 36101029)
    • (2002) Journal of Molecular Recognition , vol.15 , Issue.6 , pp. 377-392
    • Fogolari, F.1    Brigo, A.2    Molinari, H.3
  • 30
    • 0032726693 scopus 로고    scopus 로고
    • Classification of protein sequences by homology modeling and quantitative analysis of electrostatic similarity
    • DOI 10.1002/(SICI)1097-0134(19991115)37:3<379::AID-PROT6>3.0.CO;2-K
    • N. Blomberg, R. R. Gabdoulline, M. Nilges and R. C. Wade: Classification of protein sequences by homology modeling and quantitative analysis of electrostatic similarity. Proteins 37, 379-87 (1999) (Pubitemid 29519728)
    • (1999) Proteins: Structure, Function and Genetics , vol.37 , Issue.3 , pp. 379-387
    • Blomberg, N.1    Gabdoulline, R.R.2    Nilges, M.3    Wade, R.C.4
  • 31
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes
    • DOI 10.1074/jbc.273.52.34983
    • F. G. Whitby, G. Xia, C. M. Pickart and C. P. Hill: Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J Biol Chem 273, 34983-91 (1998) (Pubitemid 29028197)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.52 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 32
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou and M. Nei: The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4, 406-25 (1987)
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 35
    • 12944271968 scopus 로고    scopus 로고
    • FAST: A novel protein structure alignment algorithm
    • DOI 10.1002/prot.20331
    • J. Zhu and Z. Weng: FAST: a novel protein structure alignment algorithm. Proteins 58, 618-27 (2005) (Pubitemid 40176034)
    • (2005) Proteins: Structure, Function and Genetics , vol.58 , Issue.3 , pp. 618-627
    • Zhu, J.1    Weng, Z.2
  • 36
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • J. M. Desterro, M. S. Rodriguez and R. T. Hay: SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 2, 233-9 (1998) (Pubitemid 128373648)
    • (1998) Molecular Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 37
    • 0033546283 scopus 로고    scopus 로고
    • The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1)
    • Q. Liu, C. Jin, X. Liao, Z. Shen, D. J. Chen and Y. Chen: The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). J Biol Chem 274, 16979-87 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 16979-16987
    • Liu, Q.1    Jin, C.2    Liao, X.3    Shen, Z.4    Chen, D.J.5    Chen, Y.6
  • 38
    • 0041972581 scopus 로고    scopus 로고
    • Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation
    • DOI 10.1021/bi0345283
    • M. H. Tatham, S. Kim, B. Yu, E. Jaffray, J. Song, J. Zheng, M. S. Rodriguez, R. T. Hay and Y. Chen: Role of an N-terminal site of Ubc9 in SUMO-1,-2, and-3 binding and conjugation. Biochemistry 42, 9959-69 (2003) (Pubitemid 37012872)
    • (2003) Biochemistry , vol.42 , Issue.33 , pp. 9959-9969
    • Tatham, M.H.1    Kim, S.2    Yu, B.3    Jaffray, E.4    Song, J.5    Zheng, J.6    Rodriguez, M.S.7    Hay, R.T.8    Chen, Y.9
  • 39
  • 40
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    • DOI 10.1038/sj.emboj.7600552
    • L. M. Lois and C. D. Lima: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. Embo J 24, 439-51 (2005) (Pubitemid 40343247)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 41
    • 13244249669 scopus 로고    scopus 로고
    • Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1
    • DOI 10.1016/j.molcel.2004.12.020, PII S1097276505010026
    • D. T. Huang, A. Paydar, M. Zhuang, M. B. Waddell, J. M. Holton and B. A. Schulman: Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1. Mol Cell 17, 341-50 (2005) (Pubitemid 40193306)
    • (2005) Molecular Cell , vol.17 , Issue.3 , pp. 341-350
    • Huang, D.T.1    Paydar, A.2    Zhuang, M.3    Waddell, M.B.4    Holton, J.M.5    Schulman, B.A.6
  • 42
    • 0033516511 scopus 로고    scopus 로고
    • Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution
    • DOI 10.1006/jmbi.1999.2859
    • T. Miura, W. Klaus, B. Gsell, C. Miyamoto and H. Senn: Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution. J Mol Biol 290, 213-28 (1999) (Pubitemid 29308586)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.1 , pp. 213-228
    • Miura, T.1    Klaus, W.2    Gsell, B.3    Miyamoto, C.4    Senn, H.5
  • 43
    • 0034788322 scopus 로고    scopus 로고
    • Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail
    • DOI 10.1016/S0969-2126(01)00657-8, PII S0969212601006578
    • K. S. Hamilton, M. J. Ellison, K. R. Barber, R. S. Williams, J. T. Huzil, S. McKenna, C. Ptak, M. Glover and G. S. Shaw: Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structure (Camb) 9, 897-904 (2001) (Pubitemid 32972156)
    • (2001) Structure , vol.9 , Issue.10 , pp. 897-904
    • Hamilton, K.S.1    Ellison, M.J.2    Barber, K.R.3    Williams, R.S.4    Huzil, J.T.5    McKenna, S.6    Ptak, C.7    Glover, M.8    Shaw, G.S.9
  • 44
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • DOI 10.1016/j.molcel.2006.02.008, PII S1097276506000906
    • P. S. Brzovic, A. Lissounov, D. E. Christensen, D. W. Hoyt and R. E. Klevit: A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol Cell 21, 873-80 (2006) (Pubitemid 43376136)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 45
    • 8744284437 scopus 로고    scopus 로고
    • Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly
    • DOI 10.1074/jbc.M409576200
    • N. Merkley and G. S. Shaw: Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly. J Biol Chem 279, 47139-47 (2004) (Pubitemid 39523129)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 47139-47147
    • Merkley, N.1    Shaw, G.S.2
  • 46
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8
    • DOI 10.1038/nature01456
    • H. Walden, M. S. Podgorski and B. A. Schulman: Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8. Nature 422, 330-4 (2003) (Pubitemid 36378362)
    • (2003) Nature , vol.422 , Issue.6929 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 47
    • 0026722530 scopus 로고
    • The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins
    • K. R. Loeb and A. L. Haas: The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins. J Biol Chem 267, 7806-13 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 7806-7813
    • Loeb, K.R.1    Haas, A.L.2
  • 49
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • DOI 10.1093/emboj/20.3.362
    • W. Yuan and R. M. Krug: Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. Embo J 20, 362-71 (2001) (Pubitemid 32126972)
    • (2001) EMBO Journal , vol.20 , Issue.3 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 50
    • 0023876086 scopus 로고
    • A 15-kDa interferoninduced protein is derived by COOH-terminal processing of a 17-kDa precursor
    • E. Knight, Jr., D. Fahey, B. Cordova, M. Hillman, R. Kutny, N. Reich and D. Blomstrom: A 15-kDa interferoninduced protein is derived by COOH-terminal processing of a 17-kDa precursor. J Biol Chem 263, 4520-2 (1988)
    • (1988) J Biol Chem , vol.263 , pp. 4520-4522
    • Knight Jr., E.1    Fahey, D.2    Cordova, B.3    Hillman, M.4    Kutny, R.5    Reich, N.6    Blomstrom, D.7
  • 51
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1 SUMO-2 co-complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • L. Shen, C. Dong, H. Liu, J. H. Naismith and R. T. Hay: The structure of SENP1 SUMO-2 co-complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J (2006)
    • (2006) Biochem J
    • Shen, L.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 52
    • 14844299866 scopus 로고    scopus 로고
    • Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
    • DOI 10.1042/BJ20041210
    • Z. Xu and S. W. Au: Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Biochem J 386, 325-30 (2005) (Pubitemid 40343790)
    • (2005) Biochemical Journal , vol.386 , Issue.2 , pp. 325-330
    • Xu, Z.1    Au, S.W.N.2
  • 54
    • 0030924351 scopus 로고    scopus 로고
    • A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis
    • F. Osaka, H. Seino, T. Seno and F. Yamao: A ubiquitinconjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis. Mol Cell Biol 17, 3388-97 (1997) (Pubitemid 27215054)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.6 , pp. 3388-3397
    • Osaka, F.1    Seino, H.2    Seno, T.3    Yamao, F.4
  • 55
    • 0032877357 scopus 로고    scopus 로고
    • Molecular cloning of cDNA encoding a cyclin-selective ubiquitin carrier protein (E2-C) from Carassius auratus (goldfish) and expression analysis of the cloned gene
    • DOI 10.1016/S0014-5793(99)01189-8, PII S0014579399011898
    • M. Tokumoto, Y. Nagahama and T. Tokumoto: Molecular cloning of cDNA encoding a cyclin-selective ubiquitin carrier protein (E2-C) from Carassius auratus (goldfish) and expression analysis of the cloned gene. FEBS Lett 458, 375-7 (1999) (Pubitemid 29433838)
    • (1999) FEBS Letters , vol.458 , Issue.3 , pp. 375-377
    • Tokumoto, M.1    Nagahama, Y.2    Tokumoto, T.3
  • 56
    • 0030113930 scopus 로고    scopus 로고
    • Identification of a novel ubiquitin-conjugating enzyme involved in mitotic cyclin degradation
    • H. Yu, R. W. King, J. M. Peters and M. W. Kirschner: Identification of a novel ubiquitin-conjugating enzyme involved in mitotic cyclin degradation. Curr Biol 6, 455-66 (1996) (Pubitemid 126656293)
    • (1996) Current Biology , vol.6 , Issue.4 , pp. 455-466
    • Yu, H.1    King, R.W.2    Peters, J.-M.3    Kirschner, M.W.4
  • 57
    • 0029807944 scopus 로고    scopus 로고
    • How proteolysis drives the cell cycle
    • DOI 10.1126/science.274.5293.1652
    • R. W. King, R. J. Deshaies, J. M. Peters and M. W. Kirschner: How proteolysis drives the cell cycle. Science 274, 1652-9 (1996) (Pubitemid 26414887)
    • (1996) Science , vol.274 , Issue.5293 , pp. 1652-1659
    • King, R.W.1    Deshaies, R.J.2    Peters, J.-M.3    Kirschner, M.W.4
  • 58
    • 0032526671 scopus 로고    scopus 로고
    • Functional analysis of the Saccharomyces cerevisiae UBC11 gene
    • DOI 10.1002/(SICI)1097-0061(19980615)14:8<747::AID-YEA271>3.0.CO;2- T
    • F. M. Townsley and J. V. Ruderman: Functional analysis of the Saccharomyces cerevisiae UBC11 gene. Yeast 14, 747-57 (1998) (Pubitemid 28277571)
    • (1998) Yeast , vol.14 , Issue.8 , pp. 747-757
    • Townsley, F.M.1    Ruderman, J.V.2
  • 59
    • 0029585565 scopus 로고
    • Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2
    • DOI 10.1016/0014-5793(95)01323-7
    • P. Kaiser, S. Mandl, M. Schweiger and R. Schneider: Characterization of functionally independent domains in the human ubiquitin conjugating enzyme UbcH2. FEBS Lett 377, 193-6 (1995) (Pubitemid 26015070)
    • (1995) FEBS Letters , vol.377 , Issue.2 , pp. 193-196
    • Kaiser, P.1    Mandl, S.2    Schweiger, M.3    Schneider, R.4
  • 61
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • DOI 10.1038/329131a0
    • S. Jentsch, J. P. McGrath and A. Varshavsky: The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-4 (1987) (Pubitemid 17125247)
    • (1987) Nature , vol.329 , Issue.6135 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 62
  • 63
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • K. Robzyk, J. Recht and M. A. Osley: Rad6-dependent ubiquitination of histone H2B in yeast. Science 287, 501-4 (2000)
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 64
    • 0025874685 scopus 로고
    • Cloning and characterization of a Saccharomyces cerevisiae gene encoding a new member of the ubiquitin-conjugating protein family
    • S. Qin, B. Nakajima, M. Nomura and S. M. Arfin: Cloning and characterization of a Saccharomyces cerevisiae gene encoding a new member of the ubiquitinconjugating protein family. J Biol Chem 266, 15549-54 (1991) (Pubitemid 21907684)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.23 , pp. 15549-15554
    • Qin, S.1    Nakajima, B.2    Nomura, M.3    Arfin, S.M.4
  • 65
    • 0024117989 scopus 로고
    • The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity
    • P. Sung, S. Prakash and L. Prakash: The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes Dev 2, 1476-85 (1988)
    • (1988) Genes Dev , vol.2 , pp. 1476-1485
    • Sung, P.1    Prakash, S.2    Prakash, L.3
  • 67
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: Identification of two active site residues
    • DOI 10.1021/bi960099f
    • C. N. Larsen, J. S. Price and K. D. Wilkinson: Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry 35, 6735-44 (1996) (Pubitemid 26172432)
    • (1996) Biochemistry , vol.35 , Issue.21 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 68
    • 0033841688 scopus 로고    scopus 로고
    • Blue copper proteins: A comparative analysis of their molecular interaction properties
    • F. De Rienzo, R. R. Gabdoulline, M. C. Menziani and R. C. Wade: Blue copper proteins: a comparative analysis of their molecular interaction properties. Protein Sci 9, 1439-54 (2000) (Pubitemid 30659183)
    • (2000) Protein Science , vol.9 , Issue.8 , pp. 1439-1454
    • De Rienzo, F.1    Gabdoulline, R.R.2    Menziani, M.C.3    Wade, R.C.4
  • 69
    • 85083131322 scopus 로고    scopus 로고
    • Comparative cross-species analysis of biochemical pathways using protein interaction fields
    • M. Stein, R. R. Gabdoulline and R. C. Wade: Comparative cross-species analysis of biochemical pathways using protein interaction fields. Personal communication (2007)
    • (2007) Personal Communication
    • Stein, M.1    Gabdoulline, R.R.2    Wade, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.