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Volumn 22, Issue 9, 2012, Pages 1328-1338

Author Correction: Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms (Cell Research, (2012), 22, 9, (1328-1338), 10.1038/cr.2012.111);Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms

Author keywords

ISG54; structure biology

Indexed keywords


EID: 84865802844     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/s41422-022-00660-8     Document Type: Erratum
Times cited : (74)

References (46)
  • 1
    • 0021100660 scopus 로고
    • Interferoninduced 56,000 Mr protein and its mRNA in human cells: Molecular cloning and partial sequence of the cDNA
    • Chebath J, Merlin G, Metz R, Benech P, Revel M. Interferoninduced 56,000 Mr protein and its mRNA in human cells: molecular cloning and partial sequence of the cDNA. Nucleic Acids Res 1983; 11:1213-1226.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1213-1226
    • Chebath, J.1    Merlin, G.2    Metz, R.3    Benech, P.4    Revel, M.5
  • 2
    • 0022470806 scopus 로고
    • Molecular cloning, full-length sequence and preliminary characterization of a 56-kDa protein induced by human interferons
    • Wathelet M, Moutschen S, Defilippi P, et al. Molecular cloning, full-length sequence and preliminary characterization of a 56-kDa protein induced by human interferons. Eur J Biochem 1986; 155:11-17. (Pubitemid 16077753)
    • (1986) European Journal of Biochemistry , vol.155 , Issue.1 , pp. 11-17
    • Wathelet, M.1    Moutschen, S.2    Defilippi, P.3
  • 5
    • 0032400973 scopus 로고    scopus 로고
    • IFI60/ISG60/IFIT4, a new member of the human IFI54/IFIT2 family of interferon-stimulated genes
    • DOI 10.1006/geno.1998.5555
    • de Veer MJ, Sim H, Whisstock JC, Devenish RJ, Ralph SJ. IFI60/ISG60/IFIT4, a new member of the human IFI54/IFIT2 family of interferon-stimulated genes. Genomics 1998; 54:267-277. (Pubitemid 28553636)
    • (1998) Genomics , vol.54 , Issue.2 , pp. 267-277
    • De Veer, M.J.1    Sim, H.2    Whisstock, J.C.3    Devenish, R.J.4    Ralph, S.J.5
  • 6
    • 84863115198 scopus 로고    scopus 로고
    • Intrinsic antiviral immunity
    • Yan N, Chen ZJ. Intrinsic antiviral immunity. Nat Immunol 2012; 13:214-222.
    • (2012) Nat Immunol , vol.13 , pp. 214-222
    • Yan, N.1    Chen, Z.J.2
  • 7
    • 38449085054 scopus 로고    scopus 로고
    • The interferon-stimulated genes: Targets of direct signaling by interferons, double-stranded RNA, and viruses
    • Sen GC, Sarkar SN. The interferon-stimulated genes: targets of direct signaling by interferons, double-stranded RNA, and viruses. Curr Top Microbiol Immunol 2007; 316:233-250.
    • (2007) Curr Top Microbiol Immunol , vol.316 , pp. 233-250
    • Sen, G.C.1    Sarkar, S.N.2
  • 9
    • 84863714314 scopus 로고    scopus 로고
    • Interferoninduced Ifit2/ISG54 protects mice from lethal VSV neuropathogenesis
    • Fensterl V, Wetzel JL, Ramachandran S, et al. Interferoninduced Ifit2/ISG54 protects mice from lethal VSV neuropathogenesis. PLoS Pathog 2012; 8:e1002712.
    • (2012) PLoS Pathog , vol.8
    • Fensterl, V.1    Wetzel, J.L.2    Ramachandran, S.3
  • 10
    • 0033934285 scopus 로고    scopus 로고
    • Characterization of the interaction between the interferon-induced protein P56 and the Int6 protein encoded by a locus of insertion of the mouse mammary tumor virus
    • DOI 10.1128/JVI.74.4.1892-1899.2000
    • Guo J, Sen GC. Characterization of the interaction between the interferon-induced protein P56 and the Int6 protein encoded by a locus of insertion of the mouse mammary tumor virus. J Virol 2000; 74:1892-1899. (Pubitemid 30434048)
    • (2000) Journal of Virology , vol.74 , Issue.4 , pp. 1892-1899
    • Guo, J.1    Sen, G.C.2
  • 11
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To TPR or not to TPR?
    • Lamb JR, Tugendreich S, Hieter P. Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem Sci 1995; 20:257-259.
    • (1995) Trends Biochem Sci , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 12
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • DOI 10.1016/j.tibs.2003.10.007
    • D'Andrea LD, Regan L. TPR proteins: the versatile helix. Trends Biochem Sci 2003; 28:655-662. (Pubitemid 37500900)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 13
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • DOI 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N
    • Blatch GL, Lassle M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 1999; 21:932-939. (Pubitemid 29530602)
    • (1999) BioEssays , vol.21 , Issue.11 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 14
    • 33646143013 scopus 로고    scopus 로고
    • Ligand binding by TPR domains
    • Cortajarena AL, Regan L. Ligand binding by TPR domains. Protein Sci 2006; 15:1193-1198.
    • (2006) Protein Sci , vol.15 , pp. 1193-1198
    • Cortajarena, A.L.1    Regan, L.2
  • 15
    • 69949190148 scopus 로고    scopus 로고
    • Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure
    • Wang J, Dye BT, Rajashankar KR, Kurinov I, Schulman BA. Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure. Nat Struct Mol Biol 2009; 16:987-989.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 987-989
    • Wang, J.1    Dye, B.T.2    Rajashankar, K.R.3    Kurinov, I.4    Schulman, B.A.5
  • 16
    • 75849138999 scopus 로고    scopus 로고
    • AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin
    • Keiski CL, Harwich M, Jain S, et al. AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin. Structure 2010; 18:265-273.
    • (2010) Structure , vol.18 , pp. 265-273
    • Keiski, C.L.1    Harwich, M.2    Jain, S.3
  • 17
    • 33845961263 scopus 로고    scopus 로고
    • Distinct induction patterns and functions of two closely related interferon-inducible human genes, ISG54 and ISG56
    • DOI 10.1074/jbc.M605771200
    • Terenzi F, Hui DJ, Merrick WC, Sen GC. Distinct induction patterns and functions of two closely related interferoninducible human genes, ISG54 and ISG56. J Biol Chem 2006; 281:34064-34071. (Pubitemid 46036616)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34064-34071
    • Terenzi, F.1    Hui, D.J.2    Merrick, W.C.3    Sen, G.C.4
  • 18
    • 78549284909 scopus 로고    scopus 로고
    • 2′-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • Daffis S, Szretter KJ, Schriewer J, et al. 2′-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010; 468:452-456.
    • (2010) Nature , vol.468 , pp. 452-456
    • Daffis, S.1    Szretter, K.J.2    Schriewer, J.3
  • 19
    • 79959377900 scopus 로고    scopus 로고
    • IFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA
    • Pichlmair A, Lassnig C, Eberle CA, et al. IFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA. Nat Immunol 2011; 12:624-630.
    • (2011) Nat Immunol , vol.12 , pp. 624-630
    • Pichlmair, A.1    Lassnig, C.2    Eberle, C.A.3
  • 20
    • 66049088727 scopus 로고    scopus 로고
    • ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response
    • Li Y, Li C, Xue P, et al. ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response. Proc Natl Acad Sci USA 2009; 106:7945-7950.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7945-7950
    • Li, Y.1    Li, C.2    Xue, P.3
  • 22
    • 53349153323 scopus 로고    scopus 로고
    • IFN-induced protein with tetratricopeptide repeats 2 inhibits migration activity and increases survival of oral squamous cell carcinoma
    • Lai KC, Chang KW, Liu CJ, Kao SY, Lee TC. IFN-induced protein with tetratricopeptide repeats 2 inhibits migration activity and increases survival of oral squamous cell carcinoma. Mol Cancer Res 2008; 6:1431-1439.
    • (2008) Mol Cancer Res , vol.6 , pp. 1431-1439
    • Lai, K.C.1    Chang, K.W.2    Liu, C.J.3    Kao, S.Y.4    Lee, T.C.5
  • 23
    • 60749128384 scopus 로고    scopus 로고
    • Forced IFIT-2 expression represses LPS induced TNF-alpha expression at posttranscriptional levels
    • Berchtold S, Manncke B, Klenk J, Geisel J, Autenrieth IB, Bohn E. Forced IFIT-2 expression represses LPS induced TNF-alpha expression at posttranscriptional levels. BMC Immunol 2008; 9:75.
    • (2008) BMC Immunol , vol.9 , pp. 75
    • Berchtold, S.1    Manncke, B.2    Klenk, J.3    Geisel, J.4    Autenrieth, I.B.5    Bohn, E.6
  • 24
    • 0030872398 scopus 로고    scopus 로고
    • Modulation of the fate of cytoplasmic mRNA by AU-rich elements: Key sequence features controlling mrna deadenylation and decay
    • Xu N, Chen CY, Shyu AB. Modulation of the fate of cytoplasmic mRNA by AU-rich elements: key sequence features controlling mRNA deadenylation and decay. Mol Cell Biol 1997; 17:4611-4621. (Pubitemid 27318137)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.8 , pp. 4611-4621
    • Xu, N.1    Chen, C.-Y.A.2    Shyu, A.-B.3
  • 25
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007; 372:774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 77954386541 scopus 로고    scopus 로고
    • Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I
    • Wang Y, Ludwig J, Schuberth C, et al. Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I. Nat Struct Mol Biol 2010; 17:781-787.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 781-787
    • Wang, Y.1    Ludwig, J.2    Schuberth, C.3
  • 27
    • 77955481642 scopus 로고    scopus 로고
    • The structural basis of 5′ triphosphate double-stranded RNA recognition by RIG-I Cterminal domain
    • Lu C, Xu H, Ranjith-Kumar CT, et al. The structural basis of 5′ triphosphate double-stranded RNA recognition by RIG-I Cterminal domain. Structure 2010; 18:1032-1043.
    • (2010) Structure , vol.18 , pp. 1032-1043
    • Lu, C.1    Xu, H.2    Ranjith-Kumar, C.T.3
  • 28
    • 0035162672 scopus 로고    scopus 로고
    • ARED: Human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins
    • Bakheet T, Frevel M, Williams BR, Greer W, Khabar KS. ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins. Nucleic Acids Res 2001; 29:246-254. (Pubitemid 32054460)
    • (2001) Nucleic Acids Research , vol.29 , Issue.1 , pp. 246-254
    • Bakheet, T.1    Frevel, M.2    Williams, B.R.G.3    Greer, W.4    Khabar, K.S.A.5
  • 29
    • 77956727472 scopus 로고    scopus 로고
    • Post-transcriptional control during chronic inflammation and cancer: A focus on AU-rich elements
    • Khabar KS. Post-transcriptional control during chronic inflammation and cancer: a focus on AU-rich elements. Cell Mol Life Sci 2010; 67:2937-2955.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2937-2955
    • Khabar, K.S.1
  • 30
    • 70350093431 scopus 로고    scopus 로고
    • C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins
    • Ramsey AJ, Russell LC, Chinkers M. C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins. Biochem J 2009; 423:411-419.
    • (2009) Biochem J , vol.423 , pp. 411-419
    • Ramsey, A.J.1    Russell, L.C.2    Chinkers, M.3
  • 31
    • 0034671570 scopus 로고    scopus 로고
    • A new pathway of translational regulation mediated by eukaryotic initiation factor 3
    • DOI 10.1093/emboj/19.24.6891
    • Guo J, Hui DJ, Merrick WC, Sen GC. A new pathway of translational regulation mediated by eukaryotic initiation factor 3. EMBO J 2000; 19:6891-6899. (Pubitemid 32011682)
    • (2000) EMBO Journal , vol.19 , Issue.24 , pp. 6891-6899
    • Guo, J.1    Hui, D.J.2    Merrick, W.C.3    Sen, G.C.4
  • 32
    • 78651068887 scopus 로고    scopus 로고
    • Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein
    • Prikryl J, Rojas M, Schuster G, Barkan A. Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein. Proc Natl Acad Sci USA 2011; 108:415-420.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 415-420
    • Prikryl, J.1    Rojas, M.2    Schuster, G.3    Barkan, A.4
  • 33
    • 79953326716 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins stimulate mRNA adenylation/uridylation to activate mitochondrial translation in trypanosomes
    • Aphasizheva I, Maslov D, Wang X, Huang L, Aphasizhev R. Pentatricopeptide repeat proteins stimulate mRNA adenylation/uridylation to activate mitochondrial translation in trypanosomes. Mol Cell 2011; 42:106-117.
    • (2011) Mol Cell , vol.42 , pp. 106-117
    • Aphasizheva, I.1    Maslov, D.2    Wang, X.3    Huang, L.4    Aphasizhev, R.5
  • 34
    • 0033965922 scopus 로고    scopus 로고
    • The PPR motif - A TPR-related motif prevalent in plant organellar proteins
    • PII S0968000499015200
    • Small ID, Peeters N. The PPR motif-a TPR-related motif prevalent in plant organellar proteins. Trends Biochem Sci 2000; 25:46-47. (Pubitemid 30100363)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.2 , pp. 46-47
    • Small, I.D.1    Peeters, N.2
  • 35
    • 33744497839 scopus 로고    scopus 로고
    • Family of pentatricopeptide repeat proteins
    • Raczynska KD, Augustyniak H. [Family of pentatricopeptide repeat proteins]. Postepy Biochem 2005; 51:440-446.
    • (2005) Postepy Biochem , vol.51 , pp. 440-446
    • Raczynska, K.D.1    Augustyniak, H.2
  • 36
    • 0034846215 scopus 로고    scopus 로고
    • Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems
    • DOI 10.1007/s002530100690
    • Guerrero SA, Hecht HJ, Hofmann B, Biebl H, Singh M. Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems. Appl Microbiol Biotechnol 2001; 56:718-723. (Pubitemid 32831598)
    • (2001) Applied Microbiology and Biotechnology , vol.56 , Issue.5-6 , pp. 718-723
    • Guerrero, S.A.1    Hecht, H.-J.2    Hofmann, B.3    Biebl, H.4    Singh, M.5
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology, 1997; 276: Carter Jr CW, Sweet RM, Eds. Macromolecular Crystallography (part A), 1997; 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM. A short history of SHELX. Acta Crystallogr A 2008; 64:112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 39
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, Afonine PV, Bunkoczi G, et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010; 66:213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkoczi, G.3
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski AR, Macarthur WM, Moss SD, Thornton MJ. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993; 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, A.R.1    MacArthur, W.M.2    Moss, S.D.3    Thornton, M.J.4
  • 43
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-β signaling
    • DOI 10.1016/j.molcel.2005.08.014, PII S109727650501556X
    • Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell 2005; 19:727-740. (Pubitemid 41316668)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 727-740
    • Xu, L.-G.1    Wang, Y.-Y.2    Han, K.-J.3    Li, L.-Y.4    Zhai, Z.5    Shu, H.-B.6
  • 44
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation
    • DOI 10.1093/nar/24.4.596
    • Jordan M, Schallhorn A, Wurm FM. Transfecting mammalian cells: optimization of critical parameters affecting calciumphosphate precipitate formation. Nucleic Acids Res 1996; 24:596-601. (Pubitemid 26085833)
    • (1996) Nucleic Acids Research , vol.24 , Issue.4 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 45
    • 3142701675 scopus 로고    scopus 로고
    • Genomic sequence of an isolate of Newcastle disease virus isolated from an outbreak in geese: A novel six nucleotide insertion in the non-coding region of the nucleoprotein gene
    • Huang Y, Wan HQ, Liu HQ, Wu YT, Liu XF. Genomic sequence of an isolate of Newcastle disease virus isolated from an outbreak in geese: a novel six nucleotide insertion in the non-coding region of the nucleoprotein gene. Brief Report. Arch Virol 2004; 149:1445-1457. (Pubitemid 38927646)
    • (2004) Archives of Virology , vol.149 , Issue.7 , pp. 1445-1457
    • Huang, Y.1    Wan, H.Q.2    Liu, H.Q.3    Wu, Y.T.4    Liu, X.F.5


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