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Volumn 8, Issue 16, 2003, Pages 746-754

Drug discovery in the ubiquitin regulatory pathway

Author keywords

Cancer biology; Drug Discovery; Drug discovery; Genetics; HECT; Inflammation; Ligase; Molecular Medicine; Oncology; Pharmaceutical Science; RING; Small molecule; Structural Biology; Ubiquitin protease; Ubiqutin; Ubl; Virology

Indexed keywords

BORTEZOMIB; CARRIER PROTEIN; ISOPROTEIN; PROTEASOME INHIBITOR; PROTEINASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 0042934147     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(03)02780-6     Document Type: Review
Times cited : (61)

References (81)
  • 1
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 2
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8
    • Walden H., et al. Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8. Nature. 422:2003;330-334.
    • (2003) Nature , vol.422 , pp. 330-334
    • Walden, H.1
  • 3
    • 0034881624 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13
    • Moraes T.F., et al. Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Nat. Struct. Biol. 8:2001;669-673.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 669-673
    • Moraes, T.F.1
  • 4
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark A.P., et al. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell. 105:2001;711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1
  • 5
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2:2001;169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 6
    • 0033846567 scopus 로고    scopus 로고
    • Divergent N-terminal sequences target an inducible testis deubiquitinating enzyme to distinct subcellular structures
    • Lin H., et al. Divergent N-terminal sequences target an inducible testis deubiquitinating enzyme to distinct subcellular structures. Mol. Cell. Biol. 20:2000;6568-6578.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6568-6578
    • Lin, H.1
  • 7
    • 0037131242 scopus 로고    scopus 로고
    • Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1
    • Cope G.A., et al. Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science. 298:2002;608-611.
    • (2002) Science , vol.298 , pp. 608-611
    • Cope, G.A.1
  • 8
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell. 103:2000;351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 9
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 96:1999;645-653.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 10
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., et al. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15:1995;1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1
  • 11
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann D.J., et al. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3:2002;893-905.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1
  • 12
    • 0037342894 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 markedly enhances sensitivity of multiple myeloma tumor cells to chemotherapeutic agents
    • Ma M.H., et al. The proteasome inhibitor PS-341 markedly enhances sensitivity of multiple myeloma tumor cells to chemotherapeutic agents. Clin. Cancer Res. 9:2003;1136-1144.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 1136-1144
    • Ma, M.H.1
  • 13
    • 0031772952 scopus 로고    scopus 로고
    • SCF and APC: The Yin and Yang of cell cycle regulated proteolysis
    • Peters J.M. SCF and APC: the Yin and Yang of cell cycle regulated proteolysis. Curr. Opin. Cell Biol. 10:1998;759-768.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 759-768
    • Peters, J.M.1
  • 14
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters J.M. The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell. 9:2002;931-943.
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 15
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., et al. Mdm2 promotes the rapid degradation of p53. Nature. 387:1997;296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1
  • 16
    • 0031780665 scopus 로고    scopus 로고
    • Ubiquitin, E6-AP, and their role in p53 inactivation
    • Scheffner M. Ubiquitin, E6-AP, and their role in p53 inactivation. Pharmacol. Ther. 78:1998;129-139.
    • (1998) Pharmacol. Ther. , vol.78 , pp. 129-139
    • Scheffner, M.1
  • 17
    • 0035942224 scopus 로고    scopus 로고
    • Skp2 is oncogenic and overexpressed in human cancers
    • Gstaiger M., et al. Skp2 is oncogenic and overexpressed in human cancers. Proc. Natl. Acad. Sci. U. S. A. 98:2001;5043-5048.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5043-5048
    • Gstaiger, M.1
  • 18
    • 0036733716 scopus 로고    scopus 로고
    • Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer
    • Signoretti S., et al. Oncogenic role of the ubiquitin ligase subunit Skp2 in human breast cancer. J. Clin. Invest. 110:2002;633-641.
    • (2002) J. Clin. Invest. , vol.110 , pp. 633-641
    • Signoretti, S.1
  • 19
    • 0036645405 scopus 로고    scopus 로고
    • Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: Modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis
    • Masuda T.A., et al. Clinical and biological significance of S-phase kinase-associated protein 2 (Skp2) gene expression in gastric carcinoma: modulation of malignant phenotype by Skp2 overexpression, possibly via p27 proteolysis. Cancer Res. 62:2002;3819-3825.
    • (2002) Cancer Res. , vol.62 , pp. 3819-3825
    • Masuda, T.A.1
  • 20
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C., et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature. 412:2001;346-351.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1
  • 21
    • 0038128204 scopus 로고    scopus 로고
    • High-throughput immunoblotting: Ubiquitin-like protein ISG15 modifies key regulators of signal transduction
    • in press
    • Malakhov, M.P. et al. High-throughput immunoblotting: ubiquitin-like protein ISG15 modifies key regulators of signal transduction. J. Biol. Chem. (in press).
    • J. Biol. Chem.
    • Malakhov, M.P.1
  • 22
    • 0037443090 scopus 로고    scopus 로고
    • Protein ISGylation modulates the JAK-STAT signaling pathway
    • Malakhova O.A., et al. Protein ISGylation modulates the JAK-STAT signaling pathway. Genes Dev. 17:2003;455-460.
    • (2003) Genes Dev. , vol.17 , pp. 455-460
    • Malakhova, O.A.1
  • 23
    • 0037155882 scopus 로고    scopus 로고
    • UBP43 (USP18) specifically removes ISG15 from conjugated proteins
    • Malakhov M.P., et al. UBP43 (USP18) specifically removes ISG15 from conjugated proteins. J. Biol. Chem. 277:2002;9976-9981.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9976-9981
    • Malakhov, M.P.1
  • 24
    • 0037177798 scopus 로고    scopus 로고
    • Lipopolysaccharide activates the expression of ISG15-specific protease UBP43 via interferon regulatory factor 3
    • Malakhova O., et al. Lipopolysaccharide activates the expression of ISG15-specific protease UBP43 via interferon regulatory factor 3. J. Biol. Chem. 277:2002;14703-14711.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14703-14711
    • Malakhova, O.1
  • 25
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes M.D., et al. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. U. S. A. 98:2001;14440-14445.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14440-14445
    • Gomes, M.D.1
  • 26
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 294:2001;1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1
  • 27
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton R.Y., et al. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell. 7:1996;2029-2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1
  • 28
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays N.W., et al. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 3:2001;24-29.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1
  • 29
    • 0033615648 scopus 로고    scopus 로고
    • A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes
    • Gardner R.G., Hampton R.Y. A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes. J. Biol. Chem. 274:1999;31671-31678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31671-31678
    • Gardner, R.G.1    Hampton, R.Y.2
  • 30
    • 0033561039 scopus 로고    scopus 로고
    • TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling
    • Lomaga M.A., et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev. 13:1999;1015-1024.
    • (1999) Genes Dev. , vol.13 , pp. 1015-1024
    • Lomaga, M.A.1
  • 31
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: Viruses make the connection
    • Coscoy L., Ganem D. PHD domains and E3 ubiquitin ligases: viruses make the connection. Trends Cell Biol. 13:2003;7-12.
    • (2003) Trends Cell Biol. , vol.13 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 32
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus J.E., et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell. 107:2001;55-65.
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1
  • 33
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O., et al. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat. Struct. Biol. 9:2002;812-817.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 812-817
    • Pornillos, O.1
  • 34
    • 0037240325 scopus 로고    scopus 로고
    • Rare genetic mutations shed light on the pathogenesis of Parkinson disease
    • Dawson T.M., Dawson V.L. Rare genetic mutations shed light on the pathogenesis of Parkinson disease. J. Clin. Invest. 111:2003;145-151.
    • (2003) J. Clin. Invest. , vol.111 , pp. 145-151
    • Dawson, T.M.1    Dawson, V.L.2
  • 35
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 392:1998;605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 36
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of α-synuclein by parkin from human brain: Implications for Parkinson's disease
    • Shimura H., et al. Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease. Science. 293:2001;263-269.
    • (2001) Science , vol.293 , pp. 263-269
    • Shimura, H.1
  • 37
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by pael-R in Drosophila
    • Yang Y., et al. Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by pael-R in Drosophila. Neuron. 37:2003;911-924.
    • (2003) Neuron , vol.37 , pp. 911-924
    • Yang, Y.1
  • 38
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • Leroy E., et al. The ubiquitin pathway in Parkinson's disease. Nature. 395:1998;451-452.
    • (1998) Nature , vol.395 , pp. 451-452
    • Leroy, E.1
  • 39
    • 0033544368 scopus 로고    scopus 로고
    • Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson's disease
    • Maraganore D.M., et al. Case-control study of the ubiquitin carboxy-terminal hydrolase L1 gene in Parkinson's disease. Neurology. 53:1999;1858-1860.
    • (1999) Neurology , vol.53 , pp. 1858-1860
    • Maraganore, D.M.1
  • 40
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect α-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., et al. The UCH-L1 gene encodes two opposing enzymatic activities that affect α-synuclein degradation and Parkinson's disease susceptibility. Cell. 111:2002;209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1
  • 41
    • 0036791512 scopus 로고    scopus 로고
    • Latest developments in crystallography and structure-based design of protein kinase inhibitors as drug candidates
    • Williams D.H., Mitchell T. Latest developments in crystallography and structure-based design of protein kinase inhibitors as drug candidates. Curr. Opin. Pharmacol. 2:2002;567-573.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 567-573
    • Williams, D.H.1    Mitchell, T.2
  • 42
    • 0025050664 scopus 로고
    • A specific inhibitor of the ubiquitin activating enzyme: Synthesis and characterization of adenosyl-phospho-ubiquitinol, a nonhydrolyzable ubiquitin adenylate analogue
    • Wilkinson K.D., et al. A specific inhibitor of the ubiquitin activating enzyme: synthesis and characterization of adenosyl-phospho-ubiquitinol, a nonhydrolyzable ubiquitin adenylate analogue. Biochemistry. 29:1990;7373-7380.
    • (1990) Biochemistry , vol.29 , pp. 7373-7380
    • Wilkinson, K.D.1
  • 43
    • 0036773256 scopus 로고    scopus 로고
    • Panepophenanthrin, from a mushroom strain, a novel inhibitor of the ubiquitin-activating enzyme
    • Sekizawa R., et al. Panepophenanthrin, from a mushroom strain, a novel inhibitor of the ubiquitin-activating enzyme. J. Nat. Prod. 65:2002;1491-1493.
    • (2002) J. Nat. Prod. , vol.65 , pp. 1491-1493
    • Sekizawa, R.1
  • 44
    • 0032513037 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 Å resolution
    • Worthylake D.K., et al. Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 Å resolution. J. Biol. Chem. 273:1998;6271-6276.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6271-6276
    • Worthylake, D.K.1
  • 45
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang L., et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science. 286:1999;1321-1326.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1
  • 46
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N., et al. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell. 102:2000;533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1
  • 47
    • 0034788322 scopus 로고    scopus 로고
    • Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail
    • Hamilton K.S., et al. Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structure (Camb). 9:2001;897-904.
    • (2001) Structure (Camb) , vol.9 , pp. 897-904
    • Hamilton, K.S.1
  • 48
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor V., et al. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell. 108:2002;345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1
  • 49
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase
    • Verdecia M.A., et al. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol. Cell. 11:2003;249-259.
    • (2003) Mol. Cell , vol.11 , pp. 249-259
    • Verdecia, M.A.1
  • 50
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng N., et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature. 416:2002;703-709.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 51
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
    • Schindler T., et al. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science. 289:2000;1938-1942.
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1
  • 52
    • 0037195103 scopus 로고    scopus 로고
    • Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain
    • Du F., et al. Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain. Proc. Natl. Acad. Sci. U. S. A. 99:2002;14110-14115.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14110-14115
    • Du, F.1
  • 53
    • 0035254951 scopus 로고    scopus 로고
    • Efficient electrostatic solvation model for protein-fragment docking
    • Majeux N., et al. Efficient electrostatic solvation model for protein-fragment docking. Proteins. 42:2001;256-268.
    • (2001) Proteins , vol.42 , pp. 256-268
    • Majeux, N.1
  • 54
    • 0035977612 scopus 로고    scopus 로고
    • Isolation and structure elucidation of Chlorofusin, a novel p53-MDM2 antagonist from a Fusarium sp
    • Duncan S.J., et al. Isolation and structure elucidation of Chlorofusin, a novel p53-MDM2 antagonist from a Fusarium sp. J. Am. Chem. Soc. 123:2001;554-560.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 554-560
    • Duncan, S.J.1
  • 55
    • 0035895350 scopus 로고    scopus 로고
    • Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53
    • Stoll R., et al. Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53. Biochemistry. 40:2001;336-344.
    • (2001) Biochemistry , vol.40 , pp. 336-344
    • Stoll, R.1
  • 56
    • 0037044103 scopus 로고    scopus 로고
    • The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure
    • Zhao J., et al. The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure. Cancer Lett. 183:2002;69-77.
    • (2002) Cancer Lett. , vol.183 , pp. 69-77
    • Zhao, J.1
  • 57
    • 0026728171 scopus 로고
    • Inhibition of ubiquitin-protein ligase (E3) by mono- and bifunctional phenylarsenoxides. Evidence for essential vicinal thiols and a proximal nucleophile
    • Berleth E.S., et al. Inhibition of ubiquitin-protein ligase (E3) by mono- and bifunctional phenylarsenoxides. Evidence for essential vicinal thiols and a proximal nucleophile. J. Biol. Chem. 267:1992;16403-16411.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16403-16411
    • Berleth, E.S.1
  • 58
    • 0037189502 scopus 로고    scopus 로고
    • A small molecule ubiquitination inhibitor blocks NF-κB-dependent cytokine expression in cells and rats
    • Swinney D.C., et al. A small molecule ubiquitination inhibitor blocks NF-κB-dependent cytokine expression in cells and rats. J. Biol. Chem. 277:2002;23573-23581.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23573-23581
    • Swinney, D.C.1
  • 59
    • 18744406282 scopus 로고    scopus 로고
    • Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors
    • Lai Z., et al. Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors. Proc. Natl. Acad. Sci. U. S. A. 99:2002;14734-14739.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14734-14739
    • Lai, Z.1
  • 60
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie P.H., et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science. 274:1996;948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1
  • 61
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston S.C., et al. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18:1999;3877-3887.
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1
  • 62
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova E., Lima C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell. 5:2000;865-876.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 63
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M., et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell. 111:2002;1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1
  • 64
    • 0036260967 scopus 로고    scopus 로고
    • Thio-dependent enzymes and their inhibitors: Review
    • Leung-Tong R., et al. Thio-dependent enzymes and their inhibitors: review. Curr. Med. Chem. 9:2002;979-1002.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 979-1002
    • Leung-Tong, R.1
  • 65
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky A., et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9:2002;1149-1159.
    • (2002) Chem. Biol. , vol.9 , pp. 1149-1159
    • Borodovsky, A.1
  • 66
    • 0035839603 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway
    • Mullally J.E., et al. Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway. J. Biol. Chem. 276:2001;30366-30373.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30366-30373
    • Mullally, J.E.1
  • 67
    • 0036070772 scopus 로고    scopus 로고
    • Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death
    • Mullally J.E., Fitzpatrick F.A. Pharmacophore model for novel inhibitors of ubiquitin isopeptidases that induce p53-independent cell death. Mol. Pharmacol. 62:2002;351-358.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 351-358
    • Mullally, J.E.1    Fitzpatrick, F.A.2
  • 68
    • 0037422599 scopus 로고    scopus 로고
    • Positive and negative regulation of APP amyloidogenesis by sumoylation
    • Li Y., et al. Positive and negative regulation of APP amyloidogenesis by sumoylation. Proc. Natl. Acad. Sci. U. S. A. 100:2003;259-264.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 259-264
    • Li, Y.1
  • 69
    • 0034712842 scopus 로고    scopus 로고
    • A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination
    • Podust V.N., et al. A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4579-4584.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4579-4584
    • Podust, V.N.1
  • 70
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • Leng R.P., et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell. 112:2003;779-791.
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1
  • 71
    • 0035970096 scopus 로고    scopus 로고
    • Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
    • Zhang Y., et al. Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. Proc. Natl. Acad. Sci. U. S. A. 98:2001;974-979.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 974-979
    • Zhang, Y.1
  • 72
    • 0037148527 scopus 로고    scopus 로고
    • The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition
    • Kang D., et al. The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition. J. Cell Biol. 156:2002;249-259.
    • (2002) J. Cell Biol. , vol.156 , pp. 249-259
    • Kang, D.1
  • 73
    • 0037142070 scopus 로고    scopus 로고
    • Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth
    • Urano T., et al. Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. Nature. 417:2002;871-875.
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1
  • 74
    • 0033020726 scopus 로고    scopus 로고
    • A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division
    • Cai S.Y., et al. A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2828-2833.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2828-2833
    • Cai, S.Y.1
  • 75
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: Endogenous caspase inhibitors with multiple biological activities
    • Yang Y.L., Li X.M. The IAP family: endogenous caspase inhibitors with multiple biological activities. Cell Res. 10:2000;169-177.
    • (2000) Cell Res. , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 76
    • 0036900545 scopus 로고    scopus 로고
    • New tricks for ubiquitin and friends
    • Wilkinson C.R. New tricks for ubiquitin and friends. Trends Cell Biol. 12:2002;545-546.
    • (2002) Trends Cell Biol. , vol.12 , pp. 545-546
    • Wilkinson, C.R.1
  • 77
    • 0036891851 scopus 로고    scopus 로고
    • Lymphocyte-specific murine deubiquitinating enzymes induced by cytokines
    • Baek K.H. Lymphocyte-specific murine deubiquitinating enzymes induced by cytokines. Am. J. Hematol. 71:2002;340-345.
    • (2002) Am. J. Hematol. , vol.71 , pp. 340-345
    • Baek, K.H.1
  • 78
    • 0033393957 scopus 로고    scopus 로고
    • TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src
    • Wong B.R., et al. TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol. Cell. 4:1999;1041-1049.
    • (1999) Mol. Cell , vol.4 , pp. 1041-1049
    • Wong, B.R.1
  • 79
    • 6544270833 scopus 로고    scopus 로고
    • Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice
    • Naito A., et al. Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice. Genes Cells. 4:1999;353-362.
    • (1999) Genes Cells , vol.4 , pp. 353-362
    • Naito, A.1
  • 80
    • 0035667189 scopus 로고    scopus 로고
    • Resistance is futile: Assimilation of cellular machinery by HIV-1
    • Perez O.D., Nolan G.P. Resistance is futile: assimilation of cellular machinery by HIV-1. Immunity. 15:2001;687-690.
    • (2001) Immunity , vol.15 , pp. 687-690
    • Perez, O.D.1    Nolan, G.P.2
  • 81
    • 0034708641 scopus 로고    scopus 로고
    • The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons
    • Chen Y., et al. The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons. J. Biol. Chem. 275:2000;8929-8935.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8929-8935
    • Chen, Y.1


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