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Volumn 26, Issue 4, 2016, Pages 499-510

Bacteria-host relationship: Ubiquitin ligases as weapons of invasion

Author keywords

bacteria; bacterial effectors; bacterial mimicry; ubiquitin ligases

Indexed keywords

UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 84960458024     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2016.30     Document Type: Review
Times cited : (92)

References (102)
  • 1
    • 0344413859 scopus 로고    scopus 로고
    • Temporal regulation of salmonella virulence effector function by proteasome-dependent protein degradation
    • Kubori T, Galán JE. Temporal regulation of salmonella virulence effector function by proteasome-dependent protein degradation. Cell 2003; 115:333-342.
    • (2003) Cell , vol.115 , pp. 333-342
    • Kubori, T.1    Galán, J.E.2
  • 2
    • 0032577563 scopus 로고    scopus 로고
    • S. Typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt WD, Chen LM, Schuebel KE, Bustelo XR, Galán JE. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 1998; 93:815-826.
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galán, J.E.5
  • 3
    • 0033923731 scopus 로고    scopus 로고
    • Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell
    • Stender S, Friebel A, Linder S, Rohde M, Mirold S, Hardt WD. Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell. Mol Microbiol 2000; 36:1206-1221.
    • (2000) Mol Microbiol , vol.36 , pp. 1206-1221
    • Stender, S.1    Friebel, A.2    Linder, S.3    Rohde, M.4    Mirold, S.5    Hardt, W.D.6
  • 4
    • 0035899360 scopus 로고    scopus 로고
    • Structural mimicry in bacterial virulence
    • Stebbins CE, Galán JE. Structural mimicry in bacterial virulence. Nature 2001; 412:701-705.
    • (2001) Nature , vol.412 , pp. 701-705
    • Stebbins, C.E.1    Galán, J.E.2
  • 5
    • 0033575956 scopus 로고    scopus 로고
    • A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y, Galán JE. A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999; 401:293-297.
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galán, J.E.2
  • 6
    • 43449122166 scopus 로고    scopus 로고
    • The type III secretion system tip complex and translocon
    • Mueller CA, Broz P, Cornelis GR. The type III secretion system tip complex and translocon. Mol Microbiol 2008; 68:1085-1095.
    • (2008) Mol Microbiol , vol.68 , pp. 1085-1095
    • Mueller, C.A.1    Broz, P.2    Cornelis, G.R.3
  • 7
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galán JE, Wolf-Watz H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 2006; 444:567-573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galán, J.E.1    Wolf-Watz, H.2
  • 9
    • 84941670513 scopus 로고    scopus 로고
    • Type III secretion systems: The bacterial flagellum and the injectisome
    • Diepold A, Armitage JP. Type III secretion systems: the bacterial flagellum and the injectisome. Philos Trans R Soc Lond B Biol Sci 2015; 370:20150020.
    • (2015) Philos Trans R Soc Lond B Biol Sci , vol.370 , pp. 20150020
    • Diepold, A.1    Armitage, J.P.2
  • 10
    • 84872113974 scopus 로고    scopus 로고
    • Interactions of pathogenic bacteria minireview with autophagy systems
    • Cemma M, Brumell JH. Interactions of pathogenic bacteria minireview with autophagy systems. Curr Biol 2012; 22:R540-R545.
    • (2012) Curr Biol , vol.22 , pp. R540-R545
    • Cemma, M.1    Brumell, J.H.2
  • 11
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • Birmingham CL, Smith AC, Bakowski MA, Yoshimori T, Brumell JH. Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J Biol Chem 2006; 281:11374-11383.
    • (2006) J Biol Chem , vol.281 , pp. 11374-11383
    • Birmingham, C.L.1    Smith, A.C.2    Bakowski, M.A.3    Yoshimori, T.4    Brumell, J.H.5
  • 12
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston TLM, Wandel MP, Muhlinen von N, Foeglein Á, Randow F. Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 2012; 482:414-418.
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.M.1    Wandel, M.P.2    Von N, M.3    Foeglein, Á.4    Randow, F.5
  • 13
    • 84947442809 scopus 로고    scopus 로고
    • Autophagy proteins promote repair of endosomal membranes damaged by the Salmonella type three secretion system 1
    • Kreibich S, Emmenlauer M, Fredlund J, et al. Autophagy proteins promote repair of endosomal membranes damaged by the Salmonella type three secretion system 1. Cell Host Microbe 2015; 18:527-537.
    • (2015) Cell Host Microbe , vol.18 , pp. 527-537
    • Kreibich, S.1    Emmenlauer, M.2    Fredlund, J.3
  • 14
    • 84901193479 scopus 로고    scopus 로고
    • Exploitation of the host ubiquitin system by human bacterial pathogens
    • Ashida H, Kim M, Sasakawa C. Exploitation of the host ubiquitin system by human bacterial pathogens. Nat Rev Microbiol 2014; 12:399-413.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 399-413
    • Ashida, H.1    Kim, M.2    Sasakawa, C.3
  • 15
    • 36549014181 scopus 로고    scopus 로고
    • Taking it step by step: Mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways
    • Capili AD, Lima CD. Taking it step by step: mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways. Curr Opin Struct Biol 2007; 17:726-735.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 726-735
    • Capili, A.D.1    Lima, C.D.2
  • 16
    • 84940479138 scopus 로고    scopus 로고
    • Regulating the regulators: Recent revelations in the control of E3 ubiquitin ligases
    • Vittal V, Stewart MD, Brzovic PS, Klevit RE. Regulating the regulators: Recent revelations in the control of E3 ubiquitin ligases. J Biol Chem 2015; 290:21244-21251.
    • (2015) J Biol Chem , vol.290 , pp. 21244-21251
    • Vittal, V.1    Stewart, M.D.2    Brzovic, P.S.3    Klevit, R.E.4
  • 17
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals
    • Ikeda F, Dikic I. Atypical ubiquitin chains: new molecular signals. EMBO Rep 2008; 9:536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 18
    • 84858124845 scopus 로고    scopus 로고
    • Generation and physiological roles of linear ubiquitin chains
    • Walczak H, Iwai K, Dikic I. Generation and physiological roles of linear ubiquitin chains. BMC Biol 2012; 10:23.
    • (2012) BMC Biol , vol.10 , pp. 23
    • Walczak, H.1    Iwai, K.2    Dikic, I.3
  • 19
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - From structures to functions
    • Dikic I, Wakatsuki S, Walters KJ. Ubiquitin-binding domains - from structures to functions. Nat Rev Mol Cell Biol 2009; 10:659-671.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 20
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich HD, Walden H. Ubiquitin signalling in DNA replication and repair. Nat Rev Mol Cell Biol 2010; 11:479-489.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 21
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zühl F, Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998; 92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 22
    • 56449118262 scopus 로고    scopus 로고
    • Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis
    • Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 2008; 322:1104-1107.
    • (2008) Science , vol.322 , pp. 1104-1107
    • Pearce, M.J.1    Mintseris, J.2    Ferreyra, J.3    Gygi, S.P.4    Darwin, K.H.5
  • 23
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 2009; 16:647-651.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 647-651
    • Striebel, F.1    Imkamp, F.2    Sutter, M.3    Steiner, M.4    Mamedov, A.5    Weber-Ban, E.6
  • 25
    • 78549254832 scopus 로고    scopus 로고
    • Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation
    • Wang T, Darwin KH, Li H. Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. Nat Struct Mol Biol 2010; 17:1352-1357.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1352-1357
    • Wang, T.1    Darwin, K.H.2    Li, H.3
  • 26
    • 77952575956 scopus 로고    scopus 로고
    • Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates
    • Burns KE, Pearce MJ, Darwin KH. Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates. J Bacteriol 2010; 192:2933-2935.
    • (2010) J Bacteriol , vol.192 , pp. 2933-2935
    • Burns, K.E.1    Pearce, M.J.2    Darwin, K.H.3
  • 27
    • 84925358668 scopus 로고    scopus 로고
    • Caught in action: Selecting peptide aptamers against intrinsically disordered proteins in live cells
    • Cobbert JD, DeMott C, Majumder S, et al. Caught in action: selecting peptide aptamers against intrinsically disordered proteins in live cells. Sci Rep 2015; 5:9402.
    • (2015) Sci Rep , vol.5 , pp. 9402
    • Cobbert, J.D.1    DeMott, C.2    Majumder, S.3
  • 28
    • 0041335630 scopus 로고    scopus 로고
    • The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. Tomato DC3000
    • Buell CR, Joardar V, Lindeberg M, et al. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc Natl Acad Sci USA 2003; 100:10181-10186.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10181-10186
    • Buell, C.R.1    Joardar, V.2    Lindeberg, M.3
  • 29
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds PN, Rathjen JP. Plant immunity: towards an integrated view of plant-pathogen interactions. Nat Rev Genet 2010; 11:539-548.
    • (2010) Nat Rev Genet , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 30
    • 79952452887 scopus 로고    scopus 로고
    • Effector-triggered immunity mediated by the Pto kinase
    • Oh CS, Martin GB. Effector-triggered immunity mediated by the Pto kinase. Trends Plant Sci 2011; 16:132-140.
    • (2011) Trends Plant Sci , vol.16 , pp. 132-140
    • Oh, C.S.1    Martin, G.B.2
  • 31
    • 33644527550 scopus 로고    scopus 로고
    • Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity
    • Abramovitch RB, Janjusevic R, Stebbins CE, Martin GB. Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity. Proc Natl Acad Sci USA 2006; 103:2851-2856.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2851-2856
    • Abramovitch, R.B.1    Janjusevic, R.2    Stebbins, C.E.3    Martin, G.B.4
  • 32
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • Janjusevic R, Abramovitch RB, Martin GB, Stebbins CE. A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 2006; 311:222-226.
    • (2006) Science , vol.311 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    Stebbins, C.E.4
  • 33
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng N, Schulman BA, Song L, et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 2002; 416:703-709.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1    Schulman, B.A.2    Song, L.3
  • 34
    • 34447542796 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity
    • Rosebrock TR, Zeng L, Brady JJ, Abramovitch RB, Xiao F, Martin GB. A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity. Nature 2007; 448:370-374.
    • (2007) Nature , vol.448 , pp. 370-374
    • Rosebrock, T.R.1    Zeng, L.2    Brady, J.J.3    Abramovitch, R.B.4    Xiao, F.5    Martin, G.B.6
  • 35
    • 65649140096 scopus 로고    scopus 로고
    • Host inhibition of a bacterial virulence effector triggers immunity to infection
    • Ntoukakis V, Mucyn TS, Gimenez-Ibanez S, et al. Host inhibition of a bacterial virulence effector triggers immunity to infection. Science 2009; 324:784-787.
    • (2009) Science , vol.324 , pp. 784-787
    • Ntoukakis, V.1    Mucyn, T.S.2    Gimenez-Ibanez, S.3
  • 37
    • 84863184187 scopus 로고    scopus 로고
    • Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions
    • Lin DY, Diao J, Chen J. Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions. Proc Natl Acad Sci USA 2012; 109:1925-1930.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 1925-1930
    • Lin, D.Y.1    Diao, J.2    Chen, J.3
  • 38
    • 78650931837 scopus 로고    scopus 로고
    • Biochemical and structural studies of a HECT-like ubiquitin ligase from Escherichia coli O157:H7
    • Lin DY, Diao J, Zhou D, Chen J. Biochemical and structural studies of a HECT-like ubiquitin ligase from Escherichia coli O157:H7. J Biol Chem 2010; 286:441-449.
    • (2010) J Biol Chem , vol.286 , pp. 441-449
    • Lin, D.Y.1    Diao, J.2    Zhou, D.3    Chen, J.4
  • 39
    • 37849010910 scopus 로고    scopus 로고
    • Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase
    • Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J. Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol 2007; 15:65-70.
    • (2007) Nat Struct Mol Biol , vol.15 , pp. 65-70
    • Diao, J.1    Zhang, Y.2    Huibregtse, J.M.3    Zhou, D.4    Chen, J.5
  • 40
    • 0033858046 scopus 로고    scopus 로고
    • The secreted effector protein of Salmonella Dublin, SopA, is translocated into eukaryotic cells and influences the induction of enteritis
    • Wood MW, Jones MA, Watson PR, et al. The secreted effector protein of Salmonella dublin, SopA, is translocated into eukaryotic cells and influences the induction of enteritis. Cell Microbiol 2000; 2:293-303.
    • (2000) Cell Microbiol , vol.2 , pp. 293-303
    • Wood, M.W.1    Jones, M.A.2    Watson, P.R.3
  • 41
    • 33845395048 scopus 로고    scopus 로고
    • Identification and characterization of NleI, a new non-LEE-encoded effector of enteropathogenic Escherichia coli (EPEC)
    • Li M, Rosenshine I, Yu HB, et al. Identification and characterization of NleI, a new non-LEE-encoded effector of enteropathogenic Escherichia coli (EPEC). Microbes Infect 2006; 8:2890-2898.
    • (2006) Microbes Infect , vol.8 , pp. 2890-2898
    • Li, M.1    Rosenshine, I.2    Yu, H.B.3
  • 42
    • 79955604109 scopus 로고    scopus 로고
    • The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation
    • Piscatelli H, Kotkar SA, McBee ME, et al. The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation. PLoS One 2011; 6:e19331.
    • (2011) PLoS One , vol.6
    • Piscatelli, H.1    Kotkar, S.A.2    McBee, M.E.3
  • 43
    • 33749515943 scopus 로고    scopus 로고
    • An extensive repertoire of type III secretion effectors in Escherichia coli O157 and the role of lambdoid phages in their dissemination
    • Tobe T, Beatson SA, Taniguchi H, et al. An extensive repertoire of type III secretion effectors in Escherichia coli O157 and the role of lambdoid phages in their dissemination. Proc Natl Acad Sci USA 2006; 103:14941-14946.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14941-14946
    • Tobe, T.1    Beatson, S.A.2    Taniguchi, H.3
  • 44
    • 84890136771 scopus 로고    scopus 로고
    • Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects
    • Scheffner M, Kumar S. Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects. Biochim Biophys Acta 2014; 1843:61-74.
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 61-74
    • Scheffner, M.1    Kumar, S.2
  • 45
    • 84930657235 scopus 로고    scopus 로고
    • Bacterial factors associated with lethal outcome of enteropathogenic Escherichia coli infection: Genomic case-control studies
    • Donnenberg MS, Hazen TH, Farag TH, et al. Bacterial factors associated with lethal outcome of enteropathogenic Escherichia coli infection: genomic case-control studies. PLoS Negl Trop Dis 2015; 9:e0003791.
    • (2015) PLoS Negl Trop Dis , vol.9
    • Donnenberg, M.S.1    Hazen, T.H.2    Farag, T.H.3
  • 46
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination
    • Aravind L, Koonin EV. The U box is a modified RING finger - a common domain in ubiquitination. Curr Biol 2000; 10:R132-R134.
    • (2000) Curr Biol , vol.10 , pp. R132-R134
    • Aravind, L.1    Koonin, E.V.2
  • 47
    • 0037459172 scopus 로고    scopus 로고
    • U-box proteins as a new family of ubiquitin ligases
    • Hatakeyama S, Nakayama K-II. U-box proteins as a new family of ubiquitin ligases. Biochem Biophys Res Commun 2003; 302:635-645.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 635-645
    • Hatakeyama, S.1    K-Ii, N.2
  • 48
    • 77954670354 scopus 로고    scopus 로고
    • NleG type 3 effectors from enterohaemorrhagic Escherichia coli are U-box E3 ubiquitin ligases
    • Wu B, Skarina T, Yee A, et al. NleG type 3 effectors from enterohaemorrhagic Escherichia coli are U-box E3 ubiquitin ligases. PLoS Pathog 2010; 6:e1000960.
    • (2010) PLoS Pathog , vol.6
    • Wu, B.1    Skarina, T.2    Yee, A.3
  • 49
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F, Wilm A, Dineen D, et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 2011; 7:539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3
  • 50
    • 77954296666 scopus 로고    scopus 로고
    • A new bioinformatics analysis tools framework at EMBL-EBI
    • Goujon M, McWilliam H, Li W, et al. A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res 2010; 38:W695-W699.
    • (2010) Nucleic Acids Res , vol.38 , pp. W695-W699
    • Goujon, M.1    McWilliam, H.2    Li, W.3
  • 51
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa H, Holm L. Advances and pitfalls of protein structural alignment. Curr Opin Struct Biol 2009; 19:341-348.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 52
    • 84937020102 scopus 로고    scopus 로고
    • The EHEC-host interactome reveals novel targets for the translocated intimin receptor
    • Blasche S, Arens S, Ceol A, et al. The EHEC-host interactome reveals novel targets for the translocated intimin receptor. Sci Rep 2014; 4:7531.
    • (2014) Sci Rep , vol.4 , pp. 7531
    • Blasche, S.1    Arens, S.2    Ceol, A.3
  • 53
    • 57649149094 scopus 로고    scopus 로고
    • The Legionella pneumophila replication vacuole: Making a cozy niche inside host cells
    • Isberg RR, O'Connor TJ, Heidtman M. The Legionella pneumophila replication vacuole: making a cozy niche inside host cells. Nat Rev Microbiol 2009; 7:13-24.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 13-24
    • Isberg, R.R.1    O'Connor, T.J.2    Heidtman, M.3
  • 54
    • 39849096721 scopus 로고    scopus 로고
    • Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions
    • Kubori T, Hyakutake A, Nagai H. Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. Mol Microbiol 2008; 67:1307-1319.
    • (2008) Mol Microbiol , vol.67 , pp. 1307-1319
    • Kubori, T.1    Hyakutake, A.2    Nagai, H.3
  • 55
    • 84938750845 scopus 로고    scopus 로고
    • Molecular characterization of LubX: Functional divergence of the U-box fold by Legionella pneumophila
    • Quaile AT, Urbanus ML, Stogios PJ, et al. Molecular characterization of LubX: functional divergence of the U-box fold by Legionella pneumophila. Structure 2015; 23:1459-1469.
    • (2015) Structure , vol.23 , pp. 1459-1469
    • Quaile, A.T.1    Urbanus, M.L.2    Stogios, P.J.3
  • 56
    • 77956644100 scopus 로고    scopus 로고
    • E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates
    • Ensminger AW, Isberg RR. E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates. Infect Immun 2010; 78:3905-3919.
    • (2010) Infect Immun , vol.78 , pp. 3905-3919
    • Ensminger, A.W.1    Isberg, R.R.2
  • 57
    • 83855160757 scopus 로고    scopus 로고
    • Host proteasomal degradation generates amino acids essential for intracellular bacterial growth
    • Price CTD, Al-Quadan T, Santic M, Rosenshine I, Kwaik YA. Host proteasomal degradation generates amino acids essential for intracellular bacterial growth. Science 2011; 334:1553-1557.
    • (2011) Science , vol.334 , pp. 1553-1557
    • Price, C.T.D.1    Al-Quadan, T.2    Santic, M.3    Rosenshine, I.4    Kwaik, Y.A.5
  • 58
    • 77953704524 scopus 로고    scopus 로고
    • The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication
    • Lomma M, Dervins-Ravault D, Rolando M, et al. The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication. Cell Microbiol 2010; 12:1272-1291.
    • (2010) Cell Microbiol , vol.12 , pp. 1272-1291
    • Lomma, M.1    Dervins-Ravault, D.2    Rolando, M.3
  • 60
    • 57149105701 scopus 로고    scopus 로고
    • Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
    • Singer AU, Rohde JR, Lam R, et al. Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Nat Struct Mol Biol 2008; 15:1293-1301.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1293-1301
    • Singer, A.U.1    Rohde, J.R.2    Lam, R.3
  • 61
    • 57149098210 scopus 로고    scopus 로고
    • Structure of a Shigella effector reveals a new class of ubiquitin ligases
    • Zhu Y, Li H, Hu L, et al. Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nat Struct Mol Biol 2008; 15:1302-1308.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1302-1308
    • Zhu, Y.1    Li, H.2    Hu, L.3
  • 62
    • 84908365192 scopus 로고    scopus 로고
    • The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family
    • Zouhir S, Bernal-Bayard J, Cordero Alba M, et al. The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family. Biochem J 2014; 464:135-144.
    • (2014) Biochem J , vol.464 , pp. 135-144
    • Zouhir, S.1    Bernal-Bayard, J.2    Cordero Alba, M.3
  • 63
    • 84892473685 scopus 로고    scopus 로고
    • Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase
    • Keszei AFA, Tang X, McCormick C, et al. Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol 2014; 34:362-373.
    • (2014) Mol Cell Biol , vol.34 , pp. 362-373
    • Keszei, A.F.A.1    Tang, X.2    McCormick, C.3
  • 64
    • 63849280748 scopus 로고    scopus 로고
    • A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases
    • Quezada CM, Hicks SW, Galán JE, Stebbins CE. A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases. Proc Natl Acad Sci USA 2009; 106:4864-4869.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4864-4869
    • Quezada, C.M.1    Hicks, S.W.2    Galán, J.E.3    Stebbins, C.E.4
  • 66
    • 0033636701 scopus 로고    scopus 로고
    • The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri
    • Buchrieser C, Glaser P, Rusniok C, et al. The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri. Mol Microbiol 2000; 38:760-771.
    • (2000) Mol Microbiol , vol.38 , pp. 760-771
    • Buchrieser, C.1    Glaser, P.2    Rusniok, C.3
  • 67
    • 0242416999 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T
    • Wei J, Goldberg MB, Burland V, et al. Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun 2003; 71:2775-2786.
    • (2003) Infect Immun , vol.71 , pp. 2775-2786
    • Wei, J.1    Goldberg, M.B.2    Burland, V.3
  • 68
    • 18644378721 scopus 로고    scopus 로고
    • Genome sequence of Shigella flexneri 2a: Insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157
    • Jin Q, Yuan Z, Xu J, et al. Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157. Nucleic Acids Res 2002; 30:4432-4441.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4432-4441
    • Jin, Q.1    Yuan, Z.2    Xu, J.3
  • 69
    • 33846199469 scopus 로고    scopus 로고
    • Shigella chromosomal IpaH proteins are secreted via the type III secretion system and act as effectors
    • Ashida H, Toyotome T, Nagai T, Sasakawa C. Shigella chromosomal IpaH proteins are secreted via the type III secretion system and act as effectors. Mol Microbiol 2007; 63:680-693.
    • (2007) Mol Microbiol , vol.63 , pp. 680-693
    • Ashida, H.1    Toyotome, T.2    Nagai, T.3    Sasakawa, C.4
  • 70
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response
    • Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response. Nat Cell Biol 2009; 12:66-73.
    • (2009) Nat Cell Biol , vol.12 , pp. 66-73
    • Ashida, H.1    Kim, M.2    Schmidt-Supprian, M.3    Ma, A.4    Ogawa, M.5    Sasakawa, C.6
  • 71
    • 0034110502 scopus 로고    scopus 로고
    • Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages
    • Fernandez-Prada CM, Hoover DL, Tall BD, Hartman AB, Kopelowitz J, Venkatesan MM. Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages. Infect Immun 2000; 68:3608-3619.
    • (2000) Infect Immun , vol.68 , pp. 3608-3619
    • Fernandez-Prada, C.M.1    Hoover, D.L.2    Tall, B.D.3    Hartman, A.B.4    Kopelowitz, J.5    Venkatesan, M.M.6
  • 72
    • 84908424472 scopus 로고    scopus 로고
    • Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages
    • Suzuki S, Mimuro H, Kim M, et al. Shigella IpaH7.8 E3 ubiquitin ligase targets glomulin and activates inflammasomes to demolish macrophages. Proc Natl Acad Sci USA 2014; 111:E4254-E4263.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E4254-E4263
    • Suzuki, S.1    Mimuro, H.2    Kim, M.3
  • 73
    • 84879542716 scopus 로고    scopus 로고
    • Shigella IpaH0722 E3 ubiquitin ligase effector targets TRAF2 to inhibit PKC-NF-κB activity in invaded epithelial cells
    • Ashida H, Nakano H, Sasakawa C. Shigella IpaH0722 E3 ubiquitin ligase effector targets TRAF2 to inhibit PKC-NF-κB activity in invaded epithelial cells. PLoS Pathog 2013; 9:e1003409.
    • (2013) PLoS Pathog , vol.9
    • Ashida, H.1    Nakano, H.2    Sasakawa, C.3
  • 74
    • 84873725296 scopus 로고    scopus 로고
    • Shigella flexneri T3SS effector IpaH4.5 modulates the host inflammatory response via interaction with NF-κB p65 protein
    • Wang F, Jiang Z, Li Y, et al. Shigella flexneri T3SS effector IpaH4.5 modulates the host inflammatory response via interaction with NF-κB p65 protein. Cell Microbiol 2012; 15:474-485.
    • (2012) Cell Microbiol , vol.15 , pp. 474-485
    • Wang, F.1    Jiang, Z.2    Li, Y.3
  • 75
    • 0032699917 scopus 로고    scopus 로고
    • Identification of a putative Salmonella enterica serotype typhimurium host range factor with homology to IpaH and YopM by signature-tagged mutagenesis
    • Tsolis RM, Townsend SM, Miao EA, et al. Identification of a putative Salmonella enterica serotype typhimurium host range factor with homology to IpaH and YopM by signature-tagged mutagenesis. Infect Immun 1999; 67:6385-6393.
    • (1999) Infect Immun , vol.67 , pp. 6385-6393
    • Tsolis, R.M.1    Townsend, S.M.2    Miao, E.A.3
  • 76
    • 0032701087 scopus 로고    scopus 로고
    • Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems
    • Miao EA, Scherer CA, Tsolis RM, et al. Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems. Mol Microbiol 1999; 34:850-864.
    • (1999) Mol Microbiol , vol.34 , pp. 850-864
    • Miao, E.A.1    Scherer, C.A.2    Tsolis, R.M.3
  • 77
    • 70350433251 scopus 로고    scopus 로고
    • Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin
    • Bernal-Bayard J, Ramos-Morales F. Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin. J Biol Chem 2009; 284:27587-27595.
    • (2009) J Biol Chem , vol.284 , pp. 27587-27595
    • Bernal-Bayard, J.1    Ramos-Morales, F.2
  • 78
    • 77952416144 scopus 로고    scopus 로고
    • The Salmonella type III secretion effector, Salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3
    • Bernal-Bayard J, Cardenal-Munoz E, Ramos-Morales F. The Salmonella type III secretion effector, Salmonella leucine-rich repeat protein (SlrP), targets the human chaperone ERdj3. J Biol Chem 2010; 285:16360-16368.
    • (2010) J Biol Chem , vol.285 , pp. 16360-16368
    • Bernal-Bayard, J.1    Cardenal-Munoz, E.2    Ramos-Morales, F.3
  • 79
    • 33645551769 scopus 로고    scopus 로고
    • A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1
    • Haraga A, Miller SI. A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1. Cell Microbiol 2006; 8:837-846.
    • (2006) Cell Microbiol , vol.8 , pp. 837-846
    • Haraga, A.1    Miller, S.I.2
  • 80
    • 79959884542 scopus 로고    scopus 로고
    • Quantitative mass spectrometry catalogues Salmonella pathogenicity island-2 effectors and identifies their cognate host binding partners
    • Auweter SD, Bhavsar AP, de Hoog CL, et al. Quantitative mass spectrometry catalogues Salmonella pathogenicity island-2 effectors and identifies their cognate host binding partners. J Biol Chem 2011; 286:24023-24035.
    • (2011) J Biol Chem , vol.286 , pp. 24023-24035
    • Auweter, S.D.1    Bhavsar, A.P.2    De Hoog, C.L.3
  • 81
    • 84884781065 scopus 로고    scopus 로고
    • The Salmonella type III effector SspH2 specifically exploits the NLR co-chaperone activity of SGT1 to subvert immunity
    • Bhavsar AP, Brown NF, Stoepel J, et al. The Salmonella type III effector SspH2 specifically exploits the NLR co-chaperone activity of SGT1 to subvert immunity. PLoS Pathog 2013; 9:e1003518.
    • (2013) PLoS Pathog , vol.9
    • Bhavsar, A.P.1    Brown, N.F.2    Stoepel, J.3
  • 82
    • 34547958577 scopus 로고    scopus 로고
    • Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain
    • Wiesner S, Ogunjimi AA, Wang HR, et al. Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain. Cell 2007; 130:651-662.
    • (2007) Cell , vol.130 , pp. 651-662
    • Wiesner, S.1    Ogunjimi, A.A.2    Wang, H.R.3
  • 83
    • 0025006850 scopus 로고
    • YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice
    • Leung KY, Reisner BS, Straley SC. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect Immun 1990; 58:3262-3271.
    • (1990) Infect Immun , vol.58 , pp. 3262-3271
    • Leung, K.Y.1    Reisner, B.S.2    Straley, S.C.3
  • 84
    • 0035965144 scopus 로고    scopus 로고
    • Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: A leucine-rich repeat protein with the shortest repeating unit
    • Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS. Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit. J Mol Biol 2001; 312:807-821.
    • (2001) J Mol Biol , vol.312 , pp. 807-821
    • Evdokimov, A.G.1    Anderson, D.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 85
    • 78651078179 scopus 로고    scopus 로고
    • The many faces of the YopM effector from plague causative bacterium Yersinia pestis and its implications for host immune modulation
    • Soundararajan V, Patel N, Subramanian V, Sasisekharan V, Sasisekharan R. The many faces of the YopM effector from plague causative bacterium Yersinia pestis and its implications for host immune modulation. Innate Immun 2011; 17:548-557.
    • (2011) Innate Immun , vol.17 , pp. 548-557
    • Soundararajan, V.1    Patel, N.2    Subramanian, V.3    Sasisekharan, V.4    Sasisekharan, R.5
  • 86
    • 0038719729 scopus 로고    scopus 로고
    • The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases
    • McDonald C, Vacratsis PO, Bliska JB, Dixon JE. The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases. J Biol Chem 2003; 278:18514-18523.
    • (2003) J Biol Chem , vol.278 , pp. 18514-18523
    • McDonald, C.1    Vacratsis, P.O.2    Bliska, J.B.3    Dixon, J.E.4
  • 88
    • 84871001488 scopus 로고    scopus 로고
    • The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing
    • LaRock CN, Cookson BT. The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing. Cell Host Microbe 2012; 12:799-805.
    • (2012) Cell Host Microbe , vol.12 , pp. 799-805
    • LaRock, C.N.1    Cookson, B.T.2
  • 89
    • 79251473377 scopus 로고    scopus 로고
    • Will the ubiquitin system furnish as many drug targets as protein kinases?
    • Cohen P, Tcherpakov M. Will the ubiquitin system furnish as many drug targets as protein kinases? Cell 2010; 143:686-693.
    • (2010) Cell , vol.143 , pp. 686-693
    • Cohen, P.1    Tcherpakov, M.2
  • 90
    • 36549047979 scopus 로고    scopus 로고
    • A high-throughput screen measuring ubiquitination of p53 by human mdm2
    • Murray MF, Jurewicz AJ, Martin JD, et al. A high-throughput screen measuring ubiquitination of p53 by human mdm2. J Biomol Screen 2007; 12:1050-1058.
    • (2007) J Biomol Screen , vol.12 , pp. 1050-1058
    • Murray, M.F.1    Jurewicz, A.J.2    Martin, J.D.3
  • 91
    • 3242687101 scopus 로고    scopus 로고
    • Development of a high throughput time-resolved fluorescence resonance energy transfer assay for TRAF6 ubiquitin polymerization
    • Hong CA, Swearingen E, Mallari R, et al. Development of a high throughput time-resolved fluorescence resonance energy transfer assay for TRAF6 ubiquitin polymerization. Assay Drug Dev Technol 2003; 1:175-180.
    • (2003) Assay Drug Dev Technol , vol.1 , pp. 175-180
    • Hong, C.A.1    Swearingen, E.2    Mallari, R.3
  • 92
    • 77954513389 scopus 로고    scopus 로고
    • An allosteric inhibitor of substrate recognition by the SCFCdc4 ubiquitin ligase
    • Orlicky S, Tang X, Neduva V, et al. An allosteric inhibitor of substrate recognition by the SCFCdc4 ubiquitin ligase. Nat Biotechnol 2010; 28:733-737.
    • (2010) Nat Biotechnol , vol.28 , pp. 733-737
    • Orlicky, S.1    Tang, X.2    Neduva, V.3
  • 93
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs, NF-κB activation, and TNFα-dependent apoptosis
    • Varfolomeev E, Blankenship JW, Wayson SM, et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-κB activation, and TNFα-dependent apoptosis. Cell 2007; 131:669-681.
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3
  • 94
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004; 303:844-848.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 95
    • 84901048406 scopus 로고    scopus 로고
    • High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy
    • Rossi M, Rotblat B, Ansell K, et al. High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy. Cell Death Dis 2014; 5:e1203.
    • (2014) Cell Death Dis , vol.5
    • Rossi, M.1    Rotblat, B.2    Ansell, K.3
  • 96
    • 84953896882 scopus 로고    scopus 로고
    • A generic platform for cellular screening against ubiquitin ligases
    • Maculins T, Carter N, Dorval T, et al. A generic platform for cellular screening against ubiquitin ligases. Sci Rep 2016; 6:18940.
    • (2016) Sci Rep , vol.6 , pp. 18940
    • Maculins, T.1    Carter, N.2    Dorval, T.3
  • 97
    • 30844443758 scopus 로고    scopus 로고
    • Herpesviral protein networks and their interaction with the human proteome
    • Uetz P, Dong YA, Zeretzke C, et al. Herpesviral protein networks and their interaction with the human proteome. Science 2006; 311:239-242.
    • (2006) Science , vol.311 , pp. 239-242
    • Uetz, P.1    Dong, Y.A.2    Zeretzke, C.3
  • 98
    • 79960957705 scopus 로고    scopus 로고
    • Independently evolved virulence effectors converge onto hubs in a plant immune system network
    • Mukhtar MS, Carvunis AR, Dreze M, et al. Independently evolved virulence effectors converge onto hubs in a plant immune system network. Science 2011; 333:596-601.
    • (2011) Science , vol.333 , pp. 596-601
    • Mukhtar, M.S.1    Carvunis, A.R.2    Dreze, M.3
  • 99
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • Hunter T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell 2007; 28:730-738.
    • (2007) Mol Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 100
    • 84923766339 scopus 로고    scopus 로고
    • How chemistry supports cell biology: The chemical toolbox at your service
    • Wijdeven RH, Neefjes J, Ovaa H. How chemistry supports cell biology: the chemical toolbox at your service. Trends Cell Biol 2014; 24:751-760.
    • (2014) Trends Cell Biol , vol.24 , pp. 751-760
    • Wijdeven, R.H.1    Neefjes, J.2    Ovaa, H.3
  • 101
    • 34547093612 scopus 로고    scopus 로고
    • Active-site directed probes to report enzymatic action in the ubiquitin proteasome system
    • Ovaa H. Active-site directed probes to report enzymatic action in the ubiquitin proteasome system. Nat Rev Cancer 2007; 7:613-620.
    • (2007) Nat Rev Cancer , vol.7 , pp. 613-620
    • Ovaa, H.1
  • 102
    • 84887639752 scopus 로고    scopus 로고
    • Development of activity-based probes for ubiquitin and ubiquitin-like protein signaling pathways
    • An H, Statsyuk AV. Development of activity-based probes for ubiquitin and ubiquitin-like protein signaling pathways. J Am Chem Soc 2013; 135:16948-16962.
    • (2013) J Am Chem Soc , vol.135 , pp. 16948-16962
    • An, H.1    Statsyuk, A.V.2


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