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Volumn 7, Issue 1, 2012, Pages

Largazole and its derivatives selectively inhibit ubiquitin activating enzyme (E1)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 1B; KETONE DERIVATIVE; LARGAZOLE DERIVATIVE; TELOMERIC REPEAT BINDING FACTOR 1; UBIQUITIN; UBIQUITIN ACTIVATING ENZYME 1; UNCLASSIFIED DRUG; ADENINE; DEPSIPEPTIDE; GREEN FLUORESCENT PROTEIN; LARGAZOLE; THIAZOLE DERIVATIVE; UBE1 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 84862965075     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029208     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 0020022916 scopus 로고
    • Mechanisms of intracellular protein breakdown
    • Hershko A, Ciechanover A, (1982) Mechanisms of intracellular protein breakdown. Annu Rev Biochem 51: 335-364.
    • (1982) Annu Rev Biochem , vol.51 , pp. 335-364
    • Hershko, A.1    Ciechanover, A.2
  • 2
    • 0018772190 scopus 로고
    • Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP
    • Hershko A, Ciechanover A, Rose IA, (1979) Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP. Proc Natl Acad Sci U S A 76: 3107-3110.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 3107-3110
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 3
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas AL, Warms JV, Hershko A, Rose IA, (1982) Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J Biol Chem 257: 2543-2548.
    • (1982) J Biol Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 4
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis
    • Hershko A, Ciechanover A, Heller H, Haas AL, Rose IA, (1980) Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci U S A 77: 1783-1786.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 5
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • Hershko A, Heller H, (1985) Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates. Biochem Biophys Res Commun 128: 1079-1086.
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 1079-1086
    • Hershko, A.1    Heller, H.2
  • 6
    • 41149150219 scopus 로고    scopus 로고
    • The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy
    • Chu IM, Hengst L, Slingerland JM, (2008) The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy. Nat Rev Cancer 8: 253-267.
    • (2008) Nat Rev Cancer , vol.8 , pp. 253-267
    • Chu, I.M.1    Hengst, L.2    Slingerland, J.M.3
  • 7
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M, Tam SW, Theodoras AM, Beer-Romero P, Del Sal G, et al. (1995) Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 269: 682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Beer-Romero, P.4    Del Sal, G.5
  • 8
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: cell-cycle control and cancer
    • Nakayama KI, Nakayama K, (2006) Ubiquitin ligases: cell-cycle control and cancer. Nat Rev Cancer 6: 369-381.
    • (2006) Nat Rev Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 9
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski MD, Deshaies RJ, (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6: 9-20.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 10
    • 2442623052 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligase and its control by NEDD8-conjugating system
    • Chiba T, Tanaka K, (2004) Cullin-based ubiquitin ligase and its control by NEDD8-conjugating system. Curr Protein Pept Sci 5: 177-184.
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 177-184
    • Chiba, T.1    Tanaka, K.2
  • 11
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: building an expressway to protein destruction
    • Pan ZQ, Kentsis A, Dias DC, Yamoah K, Wu K, (2004) Nedd8 on cullin: building an expressway to protein destruction. Oncogene 23: 1985-1997.
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 12
    • 0034712842 scopus 로고    scopus 로고
    • A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination
    • Podust VN, Brownell JE, Gladysheva TB, Luo RS, Wang C, et al. (2000) A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination. Proc Natl Acad Sci U S A 97: 4579-4584.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4579-4584
    • Podust, V.N.1    Brownell, J.E.2    Gladysheva, T.B.3    Luo, R.S.4    Wang, C.5
  • 13
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • Nalepa G, Rolfe M, Harper JW, (2006) Drug discovery in the ubiquitin-proteasome system. Nat Rev Drug Discov 5: 596-613.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 14
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D, Dikic I, (2009) Targeting the ubiquitin system in cancer therapy. Nature 458: 438-444.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 15
    • 13744260574 scopus 로고    scopus 로고
    • Missing the target: ubiquitin ligase drugs stall
    • Garber K, (2005) Missing the target: ubiquitin ligase drugs stall. J Natl Cancer Inst 97: 166-167.
    • (2005) J Natl Cancer Inst , vol.97 , pp. 166-167
    • Garber, K.1
  • 16
    • 0028150688 scopus 로고
    • Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes
    • Vinitsky A, Cardozo C, Sepp-Lorenzino L, Michaud C, Orlowski M, (1994) Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J Biol Chem 269: 29860-29866.
    • (1994) J Biol Chem , vol.269 , pp. 29860-29866
    • Vinitsky, A.1    Cardozo, C.2    Sepp-Lorenzino, L.3    Michaud, C.4    Orlowski, M.5
  • 17
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A, Michaud C, Powers JC, Orlowski M, (1992) Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31: 9421-9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 18
    • 0029564960 scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells
    • Imajoh-Ohmi S, Kawaguchi T, Sugiyama S, Tanaka K, Omura S, et al. (1995) Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem Biophys Res Commun 217: 1070-1077.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1070-1077
    • Imajoh-Ohmi, S.1    Kawaguchi, T.2    Sugiyama, S.3    Tanaka, K.4    Omura, S.5
  • 19
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: lessons from the first decade
    • Orlowski RZ, Kuhn DJ, (2008) Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res 14: 1649-1657.
    • (2008) Clin Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 20
    • 0030016329 scopus 로고    scopus 로고
    • Apoptosis induction resulting from proteasome inhibition
    • Shinohara K, Tomioka M, Nakano H, Tone S, Ito H, et al. (1996) Apoptosis induction resulting from proteasome inhibition. Biochem J 317 (Pt 2): 385-388.
    • (1996) Biochem J , vol.317 , Issue.PART 2 , pp. 385-388
    • Shinohara, K.1    Tomioka, M.2    Nakano, H.3    Tone, S.4    Ito, H.5
  • 21
    • 39049135494 scopus 로고    scopus 로고
    • Structure and activity of largazole, a potent antiproliferative agent from the Floridian marine cyanobacterium Symploca sp
    • Taori K, Paul VJ, Luesch H, (2008) Structure and activity of largazole, a potent antiproliferative agent from the Floridian marine cyanobacterium Symploca sp. J Am Chem Soc 130: 1806-1807.
    • (2008) J Am Chem Soc , vol.130 , pp. 1806-1807
    • Taori, K.1    Paul, V.J.2    Luesch, H.3
  • 22
    • 64049106355 scopus 로고    scopus 로고
    • Synthesis and histone deacetylase inhibitory activity of largazole analogs: alteration of the zinc-binding domain and macrocyclic scaffold
    • Bowers AA, West N, Newkirk TL, Troutman-Youngman AE, Schreiber SL, et al. (2009) Synthesis and histone deacetylase inhibitory activity of largazole analogs: alteration of the zinc-binding domain and macrocyclic scaffold. Org Lett 11: 1301-1304.
    • (2009) Org Lett , vol.11 , pp. 1301-1304
    • Bowers, A.A.1    West, N.2    Newkirk, T.L.3    Troutman-Youngman, A.E.4    Schreiber, S.L.5
  • 23
    • 68149161259 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of c7-demethyl largazole analogues
    • Chen F, Gao AH, Li J, Nan FJ, (2009) Synthesis and biological evaluation of c7-demethyl largazole analogues. Chem Med Chem 4: 1269-1272.
    • (2009) Chem Med Chem , vol.4 , pp. 1269-1272
    • Chen, F.1    Gao, A.H.2    Li, J.3    Nan, F.J.4
  • 24
    • 54049152858 scopus 로고    scopus 로고
    • A concise total synthesis of largazole, solution structure, and some preliminary structure activity relationships
    • Nasveschuk CG, Ungermannova D, Liu X, Phillips AJ, (2008) A concise total synthesis of largazole, solution structure, and some preliminary structure activity relationships. Org Lett 10: 3595-3598.
    • (2008) Org Lett , vol.10 , pp. 3595-3598
    • Nasveschuk, C.G.1    Ungermannova, D.2    Liu, X.3    Phillips, A.J.4
  • 25
    • 55949099039 scopus 로고    scopus 로고
    • Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase
    • Ghosh AK, Kulkarni S, (2008) Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase. Org Lett 10: 3907-3909.
    • (2008) Org Lett , vol.10 , pp. 3907-3909
    • Ghosh, A.K.1    Kulkarni, S.2
  • 26
    • 52049119362 scopus 로고    scopus 로고
    • Synthesis and biological activity of largazole and derivatives
    • Seiser T, Kamena F, Cramer N, (2008) Synthesis and biological activity of largazole and derivatives. Angew Chem Int Ed Engl 47: 6483-6485.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 6483-6485
    • Seiser, T.1    Kamena, F.2    Cramer, N.3
  • 27
    • 77953740289 scopus 로고    scopus 로고
    • Synthesis and biological characterization of the histone deacetylase inhibitor largazole and C7- modified analogues
    • Souto JA, Vaz E, Lepore I, Poppler AC, Franci G, et al. (2010) Synthesis and biological characterization of the histone deacetylase inhibitor largazole and C7- modified analogues. J Med Chem 53: 4654-4667.
    • (2010) J Med Chem , vol.53 , pp. 4654-4667
    • Souto, J.A.1    Vaz, E.2    Lepore, I.3    Poppler, A.C.4    Franci, G.5
  • 28
    • 79951632653 scopus 로고    scopus 로고
    • Total Syntheses of the Histone Deacetylase Inhibitors Largazole and 2-epi-Largazole: Application of N-Heterocyclic Carbene Mediated Acylations in Complex Molecule Synthesis
    • Wang B, Huang PH, Chen CS, Forsyth CJ, (2011) Total Syntheses of the Histone Deacetylase Inhibitors Largazole and 2-epi-Largazole: Application of N-Heterocyclic Carbene Mediated Acylations in Complex Molecule Synthesis. J Org Chem.
    • (2011) J Org Chem
    • Wang, B.1    Huang, P.H.2    Chen, C.S.3    Forsyth, C.J.4
  • 29
    • 55949094932 scopus 로고    scopus 로고
    • Synthesis and activity of largazole analogues with linker and macrocycle modification
    • Ying Y, Liu Y, Byeon SR, Kim H, Luesch H, et al. (2008) Synthesis and activity of largazole analogues with linker and macrocycle modification. Org Lett 10: 4021-4024.
    • (2008) Org Lett , vol.10 , pp. 4021-4024
    • Ying, Y.1    Liu, Y.2    Byeon, S.R.3    Kim, H.4    Luesch, H.5
  • 30
    • 46049100010 scopus 로고    scopus 로고
    • Total synthesis and molecular target of largazole, a histone deacetylase inhibitor
    • Ying Y, Taori K, Kim H, Hong J, Luesch H, (2008) Total synthesis and molecular target of largazole, a histone deacetylase inhibitor. J Am Chem Soc 130: 8455-8459.
    • (2008) J Am Chem Soc , vol.130 , pp. 8455-8459
    • Ying, Y.1    Taori, K.2    Kim, H.3    Hong, J.4    Luesch, H.5
  • 31
    • 77949831890 scopus 로고    scopus 로고
    • Total synthesis and biological evaluation of largazole and derivatives with promising selectivity for cancers cells
    • Zeng X, Yin B, Hu Z, Liao C, Liu J, et al. (2010) Total synthesis and biological evaluation of largazole and derivatives with promising selectivity for cancers cells. Org Lett 12: 1368-1371.
    • (2010) Org Lett , vol.12 , pp. 1368-1371
    • Zeng, X.1    Yin, B.2    Hu, Z.3    Liao, C.4    Liu, J.5
  • 32
    • 50249144006 scopus 로고    scopus 로고
    • Total synthesis and biological mode of action of largazole: a potent class I histone deacetylase inhibitor
    • Bowers A, West N, Taunton J, Schreiber SL, Bradner JE, et al. (2008) Total synthesis and biological mode of action of largazole: a potent class I histone deacetylase inhibitor. J Am Chem Soc 130: 11219-11222.
    • (2008) J Am Chem Soc , vol.130 , pp. 11219-11222
    • Bowers, A.1    West, N.2    Taunton, J.3    Schreiber, S.L.4    Bradner, J.E.5
  • 33
    • 24044471278 scopus 로고    scopus 로고
    • Ubiquitination of p27Kip1 requires physical interaction with cyclin E and probable phosphate recognition by SKP2
    • Ungermannova D, Gao Y, Liu X, (2005) Ubiquitination of p27Kip1 requires physical interaction with cyclin E and probable phosphate recognition by SKP2. J Biol Chem 280: 30301-30309.
    • (2005) J Biol Chem , vol.280 , pp. 30301-30309
    • Ungermannova, D.1    Gao, Y.2    Liu, X.3
  • 34
    • 76249092490 scopus 로고    scopus 로고
    • Structural basis of selective ubiquitination of TRF1 by SCFFbx4
    • Zeng Z, Wang W, Yang Y, Chen Y, Yang X, et al. (2010) Structural basis of selective ubiquitination of TRF1 by SCFFbx4. Dev Cell 18: 214-225.
    • (2010) Dev Cell , vol.18 , pp. 214-225
    • Zeng, Z.1    Wang, W.2    Yang, Y.3    Chen, Y.4    Yang, X.5
  • 35
    • 10944262307 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the Skp2-Cks1 binding interface
    • Wang W, Ungermannova D, Chen L, Liu X, (2004) Molecular and biochemical characterization of the Skp2-Cks1 binding interface. J Biol Chem 279: 51362-51369.
    • (2004) J Biol Chem , vol.279 , pp. 51362-51369
    • Wang, W.1    Ungermannova, D.2    Chen, L.3    Liu, X.4
  • 36
    • 70349525349 scopus 로고    scopus 로고
    • Discovery, biological activity, synthesis and potential therapeutic utility of naturally occurring histone deacetylase inhibitors
    • Newkirk TL, Bowers AA, Williams RM, (2009) Discovery, biological activity, synthesis and potential therapeutic utility of naturally occurring histone deacetylase inhibitors. Nat Prod Rep 26: 1293-1320.
    • (2009) Nat Prod Rep , vol.26 , pp. 1293-1320
    • Newkirk, T.L.1    Bowers, A.A.2    Williams, R.M.3
  • 37
    • 27644434674 scopus 로고    scopus 로고
    • A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program
    • Knuesel M, Cheung HT, Hamady M, Barthel KK, Liu X, (2005) A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program. Mol Cell Proteomics 4: 1626-1636.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1626-1636
    • Knuesel, M.1    Cheung, H.T.2    Hamady, M.3    Barthel, K.K.4    Liu, X.5
  • 38
    • 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: 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 39
    • 0036773256 scopus 로고    scopus 로고
    • Panepophenanthrin, from a mushroom strain, a novel inhibitor of the ubiquitin-activating enzyme
    • Sekizawa R, Ikeno S, Nakamura H, Naganawa H, Matsui S, et al. (2002) Panepophenanthrin, from a mushroom strain, a novel inhibitor of the ubiquitin-activating enzyme. J Nat Prod 65: 1491-1493.
    • (2002) J Nat Prod , vol.65 , pp. 1491-1493
    • Sekizawa, R.1    Ikeno, S.2    Nakamura, H.3    Naganawa, H.4    Matsui, S.5
  • 40
    • 9644281548 scopus 로고    scopus 로고
    • Himeic acid A: a new ubiquitin-activating enzyme inhibitor isolated from a marine-derived fungus, Aspergillus sp
    • Tsukamoto S, Hirota H, Imachi M, Fujimuro M, Onuki H, et al. (2005) Himeic acid A: a new ubiquitin-activating enzyme inhibitor isolated from a marine-derived fungus, Aspergillus sp. Bioorg Med Chem Lett 15: 191-194.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 191-194
    • Tsukamoto, S.1    Hirota, H.2    Imachi, M.3    Fujimuro, M.4    Onuki, H.5
  • 41
    • 77449103325 scopus 로고    scopus 로고
    • Therapeutic strategies within the ubiquitin proteasome system
    • Eldridge AG, O'Brien T, (2010) Therapeutic strategies within the ubiquitin proteasome system. Cell Death Differ 17: 4-13.
    • (2010) Cell Death Differ , vol.17 , pp. 4-13
    • Eldridge, A.G.1    O'Brien, T.2
  • 42
    • 35148886143 scopus 로고    scopus 로고
    • Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics
    • Yang Y, Kitagaki J, Dai RM, Tsai YC, Lorick KL, et al. (2007) Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics. Cancer Res 67: 9472-9481.
    • (2007) Cancer Res , vol.67 , pp. 9472-9481
    • Yang, Y.1    Kitagaki, J.2    Dai, R.M.3    Tsai, Y.C.4    Lorick, K.L.5
  • 43
    • 77249138804 scopus 로고    scopus 로고
    • Active site remodelling accompanies thioester bond formation in the SUMO E1
    • Olsen SK, Capili AD, Lu X, Tan DS, Lima CD, (2010) Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature 463: 906-912.
    • (2010) Nature , vol.463 , pp. 906-912
    • Olsen, S.K.1    Capili, A.D.2    Lu, X.3    Tan, D.S.4    Lima, C.D.5
  • 44
    • 77249098370 scopus 로고    scopus 로고
    • Designed semisynthetic protein inhibitors of Ub/Ubl E1 activating enzymes
    • Lu X, Olsen SK, Capili AD, Cisar JS, Lima CD, et al. (2010) Designed semisynthetic protein inhibitors of Ub/Ubl E1 activating enzymes. J Am Chem Soc 132: 1748-1749.
    • (2010) J Am Chem Soc , vol.132 , pp. 1748-1749
    • Lu, X.1    Olsen, S.K.2    Capili, A.D.3    Cisar, J.S.4    Lima, C.D.5
  • 45
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, Berger AJ, Gavin JM, et al. (2009) An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 458: 732-736.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3    Berger, A.J.4    Gavin, J.M.5
  • 46
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ
    • Brownell JE, Sintchak MD, Gavin JM, Liao H, Bruzzese FJ, et al. (2010) Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ. Mol Cell 37: 102-111.
    • (2010) Mol Cell , vol.37 , pp. 102-111
    • Brownell, J.E.1    Sintchak, M.D.2    Gavin, J.M.3    Liao, H.4    Bruzzese, F.J.5


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