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Volumn 10, Issue 8, 2015, Pages

Erratum: Activity-based proteomic profiling of deubiquitinating enzymes in Salmonella-infected macrophages leads to identification of putative function of UCH-L5 in inflammasome regulation (PLoS ONE (2015) 10:8 (e0135531) DOI: 10.1371/journal.pone.0135531);Activity-based proteomic profiling of deubiquitinating enzymes in salmonella-infected macrophages leads to identification of putative function of UCH-L5 in inflammasome regulation

Author keywords

[No Author keywords available]

Indexed keywords

INFLAMMASOME; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; NIGERICIN; UBIQUITIN CARBOXYL TERMINAL HYDROLASE 4; UBIQUITIN CARBOXYL TERMINAL HYDROLASE 5; UBIQUITIN CARBOXYL TERMINAL HYDROLASE L3; UBIQUITIN CARBOXYL TERMINAL HYDROLASE L5; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 84942868601     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0138635     Document Type: Erratum
Times cited : (30)

References (33)
  • 1
    • 84896454183 scopus 로고    scopus 로고
    • National outbreaks of Salmonella infection in the UK, 2000-2011
    • PMID: 23721866
    • Harker KS, Lane C, Gormley FJ, Adak GK. National outbreaks of Salmonella infection in the UK, 2000- 2011. Epidemiology and infection. 2014; 142(3):601-7. doi: 10.1017/S0950268813001210 PMID: 23721866.
    • (2014) Epidemiology and Infection , vol.142 , Issue.3 , pp. 601-607
    • Harker, K.S.1    Lane, C.2    Gormley, F.J.3    Adak, G.K.4
  • 2
    • 84885656011 scopus 로고    scopus 로고
    • Distinguishable epidemics of multidrug-resistant Salmonella Typhimurium DT104 in different hosts
    • PMID: 24030491; PubMed Central PMCID:PMC4012302
    • Mather AE, Reid SW, Maskell DJ, Parkhill J, Fookes MC, Harris SR, et al. Distinguishable epidemics of multidrug-resistant Salmonella Typhimurium DT104 in different hosts. Science. 2013; 341 (6153):1514-7. doi: 10.1126/science.1240578 PMID: 24030491; PubMed Central PMCID:PMC4012302.
    • (2013) Science , vol.341 , Issue.6153 , pp. 1514-1517
    • Mather, A.E.1    Reid, S.W.2    Maskell, D.J.3    Parkhill, J.4    Fookes, M.C.5    Harris, S.R.6
  • 3
    • 84919457029 scopus 로고    scopus 로고
    • Ubiquitination as an efficient molecular strategy employed in Salmonella infection
    • Narayanan LA, Edelmann MJ. Ubiquitination as an efficient molecular strategy employed in Salmonella infection. Frontiers in Immunology. 2014; 5. doi: 10.3389/fimmu.2014.00558
    • (2014) Frontiers in Immunology , vol.5
    • Narayanan, L.A.1    Edelmann, M.J.2
  • 4
    • 84864060156 scopus 로고    scopus 로고
    • The Salmonella deubiquitinase SseL inhibits selective autophagy of cytosolic aggregates
    • Epub 2012/06/22. PMID: 22719249; PubMed Central PMCID: PMC3375275
    • Mesquita FS, Thomas M, Sachse M, Santos AJ, Figueira R, Holden DW. The Salmonella deubiquitinase SseL inhibits selective autophagy of cytosolic aggregates. PLoS pathogens. 2012; 8(6):e1002743. Epub 2012/06/22. doi: 10.1371/journal.ppat.1002743 PMID: 22719249; PubMed Central PMCID: PMC3375275.
    • (2012) PLoS Pathogens , vol.8 , Issue.6 , pp. e1002743
    • Mesquita, F.S.1    Thomas, M.2    Sachse, M.3    Santos, A.J.4    Figueira, R.5    Holden, D.W.6
  • 5
    • 84878887655 scopus 로고    scopus 로고
    • Deubiquitinating enzymes as promising drug targets for infectious diseases
    • Epub 2012/11/16. PMID: 23151130
    • Nanduri B, Suvarnapunya AE, Venkatesan M, Edelmann MJ. Deubiquitinating enzymes as promising drug targets for infectious diseases. Current pharmaceutical design. 2013; 19(18):3234-47. Epub 2012/11/16. PMID: 23151130.
    • (2013) Current Pharmaceutical Design , vol.19 , Issue.18 , pp. 3234-3247
    • Nanduri, B.1    Suvarnapunya, A.E.2    Venkatesan, M.3    Edelmann, M.J.4
  • 6
    • 77952715402 scopus 로고    scopus 로고
    • Post-translational modification of the deubiquitinating enzyme otubain 1 modulates active RhoA levels and susceptibility to Yersinia invasion
    • PMID: 20553488
    • Edelmann MJ, Kramer HB, Altun M, Kessler BM. Post-translational modification of the deubiquitinating enzyme otubain 1 modulates active RhoA levels and susceptibility to Yersinia invasion. FEBS Journal. 2010; 277(11):2515-30. doi: 10.1111/j.1742-4658.2010.07665.x PMID: 20553488
    • (2010) FEBS Journal , vol.277 , Issue.11 , pp. 2515-2530
    • Edelmann, M.J.1    Kramer, H.B.2    Altun, M.3    Kessler, B.M.4
  • 7
    • 33748192535 scopus 로고    scopus 로고
    • Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors
    • Epub 2006/09/09. S0092-8674(06) 01017-8 [pii] PMID: 16959567
    • Prehna G, Ivanov MI, Bliska JB, Stebbins CE. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell. 2006; 126(5):869-80. Epub 2006/09/09. S0092-8674(06) 01017-8 [pii] doi: 10.1016/j.cell.2006.06.056 PMID: 16959567.
    • (2006) Cell , vol.126 , Issue.5 , pp. 869-880
    • Prehna, G.1    Ivanov, M.I.2    Bliska, J.B.3    Stebbins, C.E.4
  • 8
    • 78651065175 scopus 로고    scopus 로고
    • The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton
    • PMID: 20608941
    • Basseres E, Coppotelli G, Pfirrmann T, Andersen JB, Masucci M, Frisan T. The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton. Cell Microbiol. 2010; 12(11):1622-33. doi: 10.1111/j.1462-5822.2010.01495.x PMID: 20608941.
    • (2010) Cell Microbiol , vol.12 , Issue.11 , pp. 1622-1633
    • Basseres, E.1    Coppotelli, G.2    Pfirrmann, T.3    Andersen, J.B.4    Masucci, M.5    Frisan, T.6
  • 9
    • 79951953010 scopus 로고    scopus 로고
    • Helicobacter pylori affects the cellular deubiquitinase USP7 and ubiquitin-regulated components TRAF6 and the tumour suppressor p53
    • Epub 2010/12/07. S1438-4221(10) 00107-4 [pii] PMID: 21131231
    • Coombs N, Sompallae R, Olbermann P, Gastaldello S, Goppel D, Masucci MG, et al. Helicobacter pylori affects the cellular deubiquitinase USP7 and ubiquitin-regulated components TRAF6 and the tumour suppressor p53. Int J Med Microbiol. 2010. Epub 2010/12/07. S1438-4221(10)00107-4 [pii] doi:10.1016/j.ijmm.2010.09.004 PMID: 21131231.
    • (2010) Int J Med Microbiol
    • Coombs, N.1    Sompallae, R.2    Olbermann, P.3    Gastaldello, S.4    Goppel, D.5    Masucci, M.G.6
  • 10
    • 42049086290 scopus 로고    scopus 로고
    • Tumor suppressor CYLD acts as a negative regulator for non-typeable Haemophilus influenza-induced inflammation in the middle ear and lung of mice
    • Epub 2007/10/11. PMID:17925880; PubMed Central PMCID: PMC2001183
    • Lim JH, Jono H, Koga T, Woo CH, Ishinaga H, Bourne P, et al. Tumor suppressor CYLD acts as a negative regulator for non-typeable Haemophilus influenza-induced inflammation in the middle ear and lung of mice. PLoS One. 2007; 2(10):e1032. Epub 2007/10/11. doi: 10.1371/journal.pone.0001032 PMID:17925880; PubMed Central PMCID: PMC2001183.
    • (2007) PLoS One , vol.2 , Issue.10 , pp. e1032
    • Lim, J.H.1    Jono, H.2    Koga, T.3    Woo, C.H.4    Ishinaga, H.5    Bourne, P.6
  • 11
    • 34447317818 scopus 로고    scopus 로고
    • The bacterium, nontypeable Haemophilus influenzae, enhances host antiviral response by inducing Toll-like receptor 7 expression: Evidence for negative regulation of host anti-viral response by CYLD
    • Epub 2007/07/05. EJB5899 [pii] PMID: 17608805
    • Sakai A, Koga T, Lim JH, Jono H, Harada K, Szymanski E, et al. The bacterium, nontypeable Haemophilus influenzae, enhances host antiviral response by inducing Toll-like receptor 7 expression: evidence for negative regulation of host anti-viral response by CYLD. FEBS J. 2007; 274(14):3655-68.Epub 2007/07/05. EJB5899 [pii] doi: 10.1111/j.1742-4658.2007.05899.x PMID: 17608805.
    • (2007) FEBS J , vol.274 , Issue.14 , pp. 3655-3668
    • Sakai, A.1    Koga, T.2    Lim, J.H.3    Jono, H.4    Harada, K.5    Szymanski, E.6
  • 12
    • 54049112664 scopus 로고    scopus 로고
    • CYLD is a crucial negative regulator of innate immune response in Escherichia coli pneumonia
    • Epub 2008/07/23. CMI1204 [pii] PMID: 18643924
    • Lim JH, Ha UH, Woo CH, Xu H, Li JD. CYLD is a crucial negative regulator of innate immune response in Escherichia coli pneumonia. Cell Microbiol. 2008; 10(11):2247-56. Epub 2008/07/23. CMI1204 [pii] doi: 10.1111/j.1462-5822.2008.01204.x PMID: 18643924.
    • (2008) Cell Microbiol , vol.10 , Issue.11 , pp. 2247-2256
    • Lim, J.H.1    Ha, U.H.2    Woo, C.H.3    Xu, H.4    Li, J.D.5
  • 13
    • 34548038609 scopus 로고    scopus 로고
    • Tumor suppressor CYLD regulates acute lung injury in lethal Streptococcus pneumoniae infections
    • Epub 2007/08/29. S1074-7613(07)00374-3 [pii] PMID: 17723219
    • Lim JH, Stirling B, Derry J, Koga T, Jono H, Woo CH, et al. Tumor suppressor CYLD regulates acute lung injury in lethal Streptococcus pneumoniae infections. Immunity. 2007; 27(2):349-60. Epub 2007/08/29. S1074-7613(07)00374-3 [pii] doi: 10.1016/j.immuni.2007.07.011 PMID: 17723219.
    • (2007) Immunity , vol.27 , Issue.2 , pp. 349-360
    • Lim, J.H.1    Stirling, B.2    Derry, J.3    Koga, T.4    Jono, H.5    Woo, C.H.6
  • 14
    • 84856085129 scopus 로고    scopus 로고
    • Inhibition of proteasome deubiquitinating activity as a new cancer therapy
    • Epub 2011/11/08. PMID: 22057347
    • D'Arcy P, Brnjic S, Olofsson MH, Fryknas M, Lindsten K, De Cesare M, et al. Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nature medicine. 2011; 17(12):1636-40. Epub 2011/11/08. doi: 10.1038/nm.2536 PMID: 22057347.
    • (2011) Nature Medicine , vol.17 , Issue.12 , pp. 1636-1640
    • D'Arcy, P.1    Brnjic, S.2    Olofsson, M.H.3    Fryknas, M.4    Lindsten, K.5    De Cesare, M.6
  • 15
    • 0018702930 scopus 로고
    • Chicken hematopoietic cells transformed by seven strains of defective avian leukemia viruses display three distinct phenotypes of differentiation
    • PMID: 227607
    • Beug H, von Kirchbach A, Doderlein G, Conscience JF, Graf T. Chicken hematopoietic cells transformed by seven strains of defective avian leukemia viruses display three distinct phenotypes of differentiation. Cell. 1979; 18(2):375-90. PMID: 227607.
    • (1979) Cell , vol.18 , Issue.2 , pp. 375-390
    • Beug, H.1    Von Kirchbach, A.2    Doderlein, G.3    Conscience, J.F.4    Graf, T.5
  • 16
    • 0343517154 scopus 로고    scopus 로고
    • Salmonella maintains the integrity of its intracellular vacuole through the action of SifA
    • PMID: 10880437; PubMed Central PMCID:PMC313946
    • Beuzon CR, Meresse S, Unsworth KE, Ruiz-Albert J, Garvis S, Waterman SR, et al. Salmonella maintains the integrity of its intracellular vacuole through the action of SifA. The EMBO journal. 2000; 19 (13):3235-49. doi: 10.1093/emboj/19.13.3235 PMID: 10880437; PubMed Central PMCID:PMC313946.
    • (2000) The EMBO Journal , vol.19 , Issue.13 , pp. 3235-3249
    • Beuzon, C.R.1    Meresse, S.2    Unsworth, K.E.3    Ruiz-Albert, J.4    Garvis, S.5    Waterman, S.R.6
  • 17
    • 84895895875 scopus 로고    scopus 로고
    • Global Analysis of Lysine Acetylation Suggests the Involvement of Protein Acetylation in Diverse Biological Processes in Rice (Oryza sativa)
    • Epub 2014/03/04. PMID:24586658; PubMed Central PMCID: PMC3930695
    • Nallamilli BR, Edelmann MJ, Zhong X, Tan F, Mujahid H, Zhang J, et al. Global Analysis of Lysine Acetylation Suggests the Involvement of Protein Acetylation in Diverse Biological Processes in Rice (Oryza sativa). PLoS One. 2014; 9(2):e89283. Epub 2014/03/04. doi: 10.1371/journal.pone.0089283 PMID:24586658; PubMed Central PMCID: PMC3930695.
    • (2014) PLoS One , vol.9 , Issue.2 , pp. e89283
    • Nallamilli, B.R.1    Edelmann, M.J.2    Zhong, X.3    Tan, F.4    Mujahid, H.5    Zhang, J.6
  • 18
    • 84887126250 scopus 로고    scopus 로고
    • Identification of palmitoyl protein thioesterase 1 in human thp1 monocytes and macrophages and characterization of unique biochemical activities for this enzyme
    • Wang R, Borazjani A, Matthews AT, Mangum LC, Edelmann MJ, Ross MK. Identification of Palmitoyl Protein Thioesterase 1 in Human THP1 Monocytes and Macrophages and Characterization of Unique Biochemical Activities for This Enzyme. Biochemistry. 2013; 52(43):7559-74. doi: 10.1021/bi401138sPMID: 24083319
    • (2013) Biochemistry , vol.52 , Issue.43 , pp. 7559-7574
    • Wang, R.1    Borazjani, A.2    Matthews, A.T.3    Mangum, L.C.4    Edelmann, M.J.5    Ross, M.K.6
  • 20
    • 82255181181 scopus 로고    scopus 로고
    • Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes
    • Epub 2011/11/29. PMID: 22118674
    • Altun M, Kramer HB, Willems LI, McDermott JL, Leach CA, Goldenberg SJ, et al. Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes. Chemistry & biology. 2011; 18(11):1401-12. Epub 2011/11/29. doi: 10.1016/j.chembiol.2011.08.018 PMID: 22118674.
    • (2011) Chemistry & Biology , vol.18 , Issue.11 , pp. 1401-1412
    • Altun, M.1    Kramer, H.B.2    Willems, L.I.3    McDermott, J.L.4    Leach, C.A.5    Goldenberg, S.J.6
  • 21
    • 79955941973 scopus 로고    scopus 로고
    • PTMs in conversation: Activity and function of deubiquitinating enzymes regulated via post-translational modifications
    • Epub 2011/04/12. PMID: 21480003; PubMed Central PMCID:PMC3094536
    • Kessler BM, Edelmann MJ. PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications. Cell biochemistry and biophysics. 2011; 60(1-2):21-38. Epub 2011/04/12. doi: 10.1007/s12013-011-9176-6 PMID: 21480003; PubMed Central PMCID:PMC3094536.
    • (2011) Cell Biochemistry and Biophysics , vol.60 , Issue.1-2 , pp. 21-38
    • Kessler, B.M.1    Edelmann, M.J.2
  • 22
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • Epub 2010/09/09. PMID: 20823120; PubMed Central PMCID:PMC3098602
    • Lee MJ, Lee BH, Hanna J, King RW, Finley D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Molecular & cellular proteomics: MCP. 2011; 10(5):R110 003871. Epub 2010/09/09. doi: 10.1074/mcp.R110.003871 PMID: 20823120; PubMed Central PMCID:PMC3098602.
    • (2011) Molecular & Cellular Proteomics: MCP , vol.10 , Issue.5 , pp. R110003871
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 23
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
    • Epub 2006/08/15. PMID: 16906146
    • Yao T, Song L, Xu W, DeMartino GN, Florens L, Swanson SK, et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature cell biology. 2006; 8(9):994-1002. Epub 2006/08/15. doi: 10.1038/ncb1460 PMID: 16906146.
    • (2006) Nature Cell Biology , vol.8 , Issue.9 , pp. 994-1002
    • Yao, T.1    Song, L.2    Xu, W.3    DeMartino, G.N.4    Florens, L.5    Swanson, S.K.6
  • 24
    • 84875130745 scopus 로고    scopus 로고
    • Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs
    • Epub 2013/01/24. PMID: 23341450; PubMed Central PMCID:PMC3597817
    • Peth A, Kukushkin N, Bosse M, Goldberg AL. Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. The Journal of biological chemistry. 2013; 288(11):7781-90. Epub 2013/01/24. doi: 10.1074/jbc.M112.441907 PMID: 23341450; PubMed Central PMCID:PMC3597817.
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.11 , pp. 7781-7790
    • Peth, A.1    Kukushkin, N.2    Bosse, M.3    Goldberg, A.L.4
  • 25
    • 84873834109 scopus 로고    scopus 로고
    • Deubiquitinases regulate the activity of caspase-1 and interleukin-1beta secretion via assembly of the inflammasome
    • Epub 2012/12/05. PMID: 23209292; PubMed Central PMCID: PMC3554938
    • Lopez-Castejon G, Luheshi NM, Compan V, High S, Whitehead RC, Flitsch S, et al. Deubiquitinases regulate the activity of caspase-1 and interleukin-1beta secretion via assembly of the inflammasome. The Journal of biological chemistry. 2013; 288(4):2721-33. Epub 2012/12/05. doi: 10.1074/jbc.M112.422238 PMID: 23209292; PubMed Central PMCID: PMC3554938.
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.4 , pp. 2721-2733
    • Lopez-Castejon, G.1    Luheshi, N.M.2    Compan, V.3    High, S.4    Whitehead, R.C.5    Flitsch, S.6
  • 26
    • 68649102975 scopus 로고    scopus 로고
    • Mechanisms of interleukin-1beta release
    • PMID: 19250700
    • Eder C. Mechanisms of interleukin-1beta release. Immunobiology. 2009; 214(7):543-53. doi: 10.1016/j.imbio.2008.11.007 PMID: 19250700.
    • (2009) Immunobiology , vol.214 , Issue.7 , pp. 543-553
    • Eder, C.1
  • 27
    • 84886897936 scopus 로고    scopus 로고
    • Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin
    • Epub 2013/10/09. PMID: 24100292; PubMed Central PMCID:PMC3798248
    • Fujita N, Morita E, Itoh T, Tanaka A, Nakaoka M, Osada Y, et al. Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin. The Journal of cell biology. 2013; 203 (1):115-28. Epub 2013/10/09. doi: 10.1083/jcb.201304188 PMID: 24100292; PubMed Central PMCID:PMC3798248.
    • (2013) The Journal of Cell Biology , vol.203 , Issue.1 , pp. 115-128
    • Fujita, N.1    Morita, E.2    Itoh, T.3    Tanaka, A.4    Nakaoka, M.5    Osada, Y.6
  • 28
    • 84865339202 scopus 로고    scopus 로고
    • Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection
    • Epub 2012/07/17. PMID: 22797665; PubMed Central PMCID: PMC3461347
    • Puri AW, Broz P, Shen A, Monack DM, Bogyo M. Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection. Nature chemical biology. 2012; 8(9):745-7. Epub 2012/07/17.doi: 10.1038/nchembio.1023 PMID: 22797665; PubMed Central PMCID: PMC3461347.
    • (2012) Nature Chemical Biology , vol.8 , Issue.9 , pp. 745-747
    • Puri, A.W.1    Broz, P.2    Shen, A.3    Monack, D.M.4    Bogyo, M.5
  • 29
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Epub 2012/09/06. PMID: 22948162; PubMed CentralPMCID: PMC3476327
    • Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. The Journal of biological chemistry. 2012;287(43):36617-22. Epub 2012/09/06. doi: 10.1074/jbc.M112.407130 PMID: 22948162; PubMed CentralPMCID: PMC3476327.
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.43 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3    Farias, A.4    Qin, F.5    Alnemri, E.S.6
  • 30
    • 79251513968 scopus 로고    scopus 로고
    • Pyroptosis: Macrophage suicide exposes hidden invaders
    • Epub 2011/01/25. PMID: 21256438
    • Brodsky IE, Medzhitov R. Pyroptosis: macrophage suicide exposes hidden invaders. Current biology: CB. 2011; 21(2):R72-5. Epub 2011/01/25. doi: 10.1016/j.cub.2010.12.008 PMID: 21256438.
    • (2011) Current Biology: CB , vol.21 , Issue.2 , pp. R72-R75
    • Brodsky, I.E.1    Medzhitov, R.2
  • 31
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • PMID: 20603313; PubMed CentralPMCID: PMC2916133
    • Broz P, Newton K, Lamkanfi M, Mariathasan S, Dixit VM, Monack DM. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. The Journal of experimental medicine. 2010; 207(8):1745-55. doi: 10.1084/jem.20100257 PMID: 20603313; PubMed CentralPMCID: PMC2916133.
    • (2010) The Journal of Experimental Medicine , vol.207 , Issue.8 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 32
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction
    • PMID: 22286270; PubMed Central PMCID: PMC4116819
    • Shi CS, Shenderov K, Huang NN, Kabat J, Abu-Asab M, Fitzgerald KA, et al. Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nature immunology. 2012; 13(3):255-63. doi: 10.1038/ni.2215 PMID: 22286270; PubMed Central PMCID: PMC4116819.
    • (2012) Nature Immunology , vol.13 , Issue.3 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6
  • 33
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • PMID: 23246432
    • Py BF, Kim MS, Vakifahmetoglu-Norberg H, Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Molecular cell. 2013; 49(2):331-8. doi: 10.1016/j.molcel.2012.11.009PMID: 23246432.
    • (2013) Molecular Cell , vol.49 , Issue.2 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4


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