메뉴 건너뛰기




Volumn 1824, Issue 12, 2012, Pages 1401-1408

Solution structure and biophysical properties of MqsA, a Zn-containing antitoxin from Escherichia coli

Author keywords

Antitoxin structure; MqsA; NMR; solution structure; Toxin antitoxin; Zn fingers

Indexed keywords

ANTITOXIN; CYSTEINE; HELIX LOOP HELIX PROTEIN; PROTEIN MQSA; UNCLASSIFIED DRUG; ZINC DERIVATIVE;

EID: 84867669464     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.06.016     Document Type: Article
Times cited : (8)

References (66)
  • 1
    • 0033583045 scopus 로고
    • Forging a link between biofilms and disease
    • C. Potera Forging a link between biofilms and disease Science 283 1999 1837 1839
    • (1837) Science , vol.283 , Issue.1999 , pp. 1839
    • Potera, C.1
  • 2
    • 50349141358 scopus 로고
    • Treatment of staphylococcal infections with penicillin by intermittent sterilisation
    • J.W. Bigger Treatment of staphylococcal infections with penicillin by intermittent sterilisation Lancet 2 1944 497 500
    • (1944) Lancet , vol.2 , pp. 497-500
    • Bigger, J.W.1
  • 3
    • 0022745345 scopus 로고
    • Phenotypic tolerance: The search for beta-lactam antibiotics that kill nongrowing bacteria
    • E. Tuomanen Phenotypic tolerance: the search for beta-lactam antibiotics that kill nongrowing bacteria Rev. Infect. Dis. 8 Suppl. 3 1986 S279 S291
    • (1986) Rev. Infect. Dis. , vol.8 , Issue.SUPPL. 3
    • Tuomanen, E.1
  • 4
    • 33646549559 scopus 로고    scopus 로고
    • Increased persistence in Escherichia coli caused by controlled expression of toxins or other unrelated proteins
    • DOI 10.1128/JB.188.10.3494-3497.2006
    • N. Vazquez-Laslop, H. Lee, and A.A. Neyfakh Increased persistence in Escherichia coli caused by controlled expression of toxins or other unrelated proteins J. Bacteriol. 188 2006 3494 3497 (Pubitemid 43726213)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3494-3497
    • Vazquez-Laslop, N.1    Lee, H.2    Neyfakh, A.A.3
  • 5
    • 10044266575 scopus 로고    scopus 로고
    • Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli
    • DOI 10.1128/JB.186.24.8172-8180.2004
    • I. Keren, D. Shah, A. Spoering, N. Kaldalu, and K. Lewis Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli J. Bacteriol. 186 2004 8172 8180 (Pubitemid 39603206)
    • (2004) Journal of Bacteriology , vol.186 , Issue.24 , pp. 8172-8180
    • Keren, I.1    Shah, D.2    Spoering, A.3    Kaldalu, N.4    Lewis, K.5
  • 7
    • 34247148876 scopus 로고    scopus 로고
    • Current Opinion in Microbiology Cell Regulation (RNA special issue)
    • K. Gerdes, and E.G.H. Wagner RNA antitoxins Current Opinion in Microbiology Cell Regulation (RNA special issue) 10 2007 117 124
    • (2007) RNA Antitoxins , vol.10 , pp. 117-124
    • Gerdes, K.1    Wagner, E.G.H.2
  • 8
    • 80052196405 scopus 로고    scopus 로고
    • Diversity of bacterial type II toxin-antitoxin systems: A comprehensive search and functional analysis of novel families
    • R. Leplae, D. Geeraerts, R. Hallez, J. Guglielmini, P. Dreze, and L. Van Melderen Diversity of bacterial type II toxin-antitoxin systems: a comprehensive search and functional analysis of novel families Nucleic Acids Res. 39 2011 5513 5525
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5513-5525
    • Leplae, R.1    Geeraerts, D.2    Hallez, R.3    Guglielmini, J.4    Dreze, P.5    Van Melderen, L.6
  • 9
    • 77952567720 scopus 로고    scopus 로고
    • The Escherichia coli mqsR and ygiT genes encode a new toxin-antitoxin pair
    • 10.1128/JB.01266-09
    • V. Kasari, K. Kurg, T. Margus, T. Tenson, and N. Kaldalu The Escherichia coli mqsR and ygiT genes encode a new toxin-antitoxin pair J. Bacteriol. 192 2010 2908 2919 10.1128/JB.01266-09
    • (2010) J. Bacteriol. , vol.192 , pp. 2908-2919
    • Kasari, V.1    Kurg, K.2    Margus, T.3    Tenson, T.4    Kaldalu, N.5
  • 10
    • 0242407473 scopus 로고    scopus 로고
    • A Novel Family of Escherichia coli Toxin-Antitoxin Gene Pairs
    • DOI 10.1128/JB.185.22.6600-6608.2003
    • J.M. Brown, and K.J. Shaw A novel family of Escherichia coli toxin-antitoxin gene pairs J. Bacteriol. 185 2003 6600 6608 (Pubitemid 37385879)
    • (2003) Journal of Bacteriology , vol.185 , Issue.22 , pp. 6600-6608
    • Brown, J.M.1    Shaw, K.J.2
  • 11
    • 70350399514 scopus 로고    scopus 로고
    • MqsR, a crucial regulator for quorum sensing and biofilm formation, is a GCU-specific mRNA interferase in Escherichia coli
    • Y. Yamaguchi, J.H. Park, and M. Inouye MqsR, a crucial regulator for quorum sensing and biofilm formation, is a GCU-specific mRNA interferase in Escherichia coli J. Biol. Chem. 284 2009 28746 28753
    • (2009) J. Biol. Chem. , vol.284 , pp. 28746-28753
    • Yamaguchi, Y.1    Park, J.H.2    Inouye, M.3
  • 12
    • 79953808579 scopus 로고    scopus 로고
    • YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB
    • Q. Tan, N. Awano, and M. Inouye YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB Mol. Microbiol. 79 2011 109 118
    • (2011) Mol. Microbiol. , vol.79 , pp. 109-118
    • Tan, Q.1    Awano, N.2    Inouye, M.3
  • 14
    • 80755144025 scopus 로고    scopus 로고
    • Toxin-antitoxin systems in bacteria and archaea
    • Y. Yamaguchi, J.H. Park, and M. Inouye toxin-antitoxin systems in bacteria and archaea Annu. Rev. Genet. 45 2011 61 79
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 61-79
    • Yamaguchi, Y.1    Park, J.H.2    Inouye, M.3
  • 15
    • 34548496904 scopus 로고    scopus 로고
    • What is the benefit to Escherichia coli of having multiple toxin-antitoxin systems in its genome?
    • DOI 10.1128/JB.00527-07
    • V. Tsilibaris, G. Maenhaut-Michel, N. Mine, and L. Van Melderen What is the benefit to Escherichia coli of having multiple toxin-antitoxin systems in its genome? J. Bacteriol. 189 2007 6101 6108 (Pubitemid 47378616)
    • (2007) Journal of Bacteriology , vol.189 , Issue.17 , pp. 6101-6108
    • Tsilibaris, V.1    Maenhaut-Michel, G.2    Mine, N.3    Van Melderen, L.4
  • 17
    • 30744444010 scopus 로고    scopus 로고
    • Autoinducer 2 controls biofilm formation in Escherichia coli through a novel motility quorum-sensing regulator
    • MqsR, B3022
    • A.F. Gonzalez Barrios, R. Zuo, Y. Hashimoto, L. Yang, W.E. Bentley, and T.K. Wood Autoinducer 2 controls biofilm formation in Escherichia coli through a novel motility quorum-sensing regulator MqsR, B3022 J. Bacteriol. 188 2006 305 316
    • (2006) J. Bacteriol. , vol.188 , pp. 305-316
    • Gonzalez Barrios, A.F.1    Zuo, R.2    Hashimoto, Y.3    Yang, L.4    Bentley, W.E.5    Wood, T.K.6
  • 18
    • 74549170423 scopus 로고    scopus 로고
    • Three dimensional structure of the MqsR:MqsA complex: A novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties
    • B.L. Brown, S. Grigoriu, Y. Kim, J.M. Arruda, A. Davenport, T.K. Wood, W. Peti, and R. Page Three dimensional structure of the MqsR:MqsA complex: a novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties PLoS Pathog. 5 2009 e1000706
    • (2009) PLoS Pathog. , vol.5 , pp. 1000706
    • Brown, B.L.1    Grigoriu, S.2    Kim, Y.3    Arruda, J.M.4    Davenport, A.5    Wood, T.K.6    Peti, W.7    Page, R.8
  • 20
    • 72949116993 scopus 로고    scopus 로고
    • Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli
    • Y. Kim, and T.K. Wood Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli Biochem. Biophys. Res. Commun. 391 2010 209 213
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 209-213
    • Kim, Y.1    Wood, T.K.2
  • 23
    • 78751504273 scopus 로고    scopus 로고
    • Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation
    • B.L. Brown, T.K. Wood, W. Peti, and R. Page Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation J. Biol. Chem. 286 2010 2285 2296
    • (2010) J. Biol. Chem. , vol.286 , pp. 2285-2296
    • Brown, B.L.1    Wood, T.K.2    Peti, W.3    Page, R.4
  • 24
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010 10.1093/nar/gkp846
    • T.U. Consortium The Universal Protein Resource (UniProt) in 2010 10.1093/nar/gkp846 Nucleic Acids Res. 38 2010 D142 D148
    • (2010) Nucleic Acids Res. , vol.38
    • Consortium, T.U.1
  • 26
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: Recent updates and new developments
    • I. Letunic, T. Doerks, and P. Bork SMART 6: recent updates and new developments Nucleic Acids Res. 37 2009 D229 D232
    • (2009) Nucleic Acids Res. , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 29
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to Gal and Lac repressors
    • M.J. Weickert, and S. Adhya A family of bacterial regulators homologous to Gal and Lac repressors J. Biol. Chem. 267 1992 15869 15874
    • (1992) J. Biol. Chem. , vol.267 , pp. 15869-15874
    • Weickert, M.J.1    Adhya, S.2
  • 30
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • S.C. Schultz, G.C. Shields, and T.A. Steitz Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees Science 253 1991 1001 1007 (Pubitemid 21917242)
    • (1991) Science , vol.253 , Issue.5023 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 31
    • 0036130729 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin isoforms
    • DOI 10.1016/S0076-6879(02)47028-0
    • A. Vlamis-Gardikas, and A. Holmgren Thioredoxin and glutaredoxin isoforms Methods Enzymol. 347 2002 286 296 (Pubitemid 34234784)
    • (2002) Methods in Enzymology , vol.347 , pp. 286-296
    • Vlamis-Gardikas, A.1    Holmgren, A.2
  • 32
    • 68849104920 scopus 로고    scopus 로고
    • Assignment of (1)H, (13)C, and (15)N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs
    • E. Papadopoulos, M. Billeter, A. Gräslund, and A. Vlamis-Gardikas Assignment of (1)H, (13)C, and (15)N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs Biomol. NMR Assign. 1 2007 217 219
    • (2007) Biomol. NMR Assign. , vol.1 , pp. 217-219
    • Papadopoulos, E.1    Billeter, M.2    Gräslund, A.3    Vlamis-Gardikas, A.4
  • 33
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • PII S0079656598000259
    • M. Sattler, J. Schleucher, and C. Griesinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog. Nucl. Magn. Reson. Spectrosc. 34 1999 93 158 (Pubitemid 129595216)
    • (1999) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.34 , Issue.2 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 35
  • 36
    • 0000441606 scopus 로고    scopus 로고
    • GARANT - A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra
    • C. Bartels, P. Güntert, M. Billeter, and K. Wüthrich GARANT - a general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra J. Comput. Chem. 18 1997 139 149 (Pubitemid 127599839)
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.1 , pp. 139-149
    • Bartels, C.1    Guntert, P.2    Billeter, M.3    Wuthrich, K.4
  • 37
    • 0000714031 scopus 로고    scopus 로고
    • Automated sequence-specific NMR assignment of homologous proteins using the program GARANT
    • C. Bartels, M. Billeter, P. Güntert, and K. Wüthrich Automated sequence-specific NMR assignment of homologous proteins using the program GARANT J. Biomol. NMR 7 1996 207 213 (Pubitemid 126709559)
    • (1996) Journal of Biomolecular NMR , vol.7 , Issue.3 , pp. 207-213
    • Bartels, C.1    Billeter, M.2    Guntert, P.3    Wuthrich, K.4
  • 38
    • 0043027070 scopus 로고    scopus 로고
    • Fully automated sequence-specific resonance assignments of heteronuclear protein spectra
    • DOI 10.1023/A:1024765212223
    • D. Malmodin, C.H. Papavoine, and M. Billeter Fully automated sequence-specific resonance assignments of hetero- nuclear protein spectra J. Biomol. NMR 27 2003 69 79 (Pubitemid 36987111)
    • (2003) Journal of Biomolecular NMR , vol.27 , Issue.1 , pp. 69-79
    • Malmodin, D.1    Papavoine, C.H.M.2    Billeter, M.3
  • 39
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • P. Güntert, C. Mumenthaler, and K. Wüthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298 (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 40
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 41
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • T. Herrmann, P. Güntert, and K. Wüthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227 (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 (29-32) (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 44
    • 30144435044 scopus 로고    scopus 로고
    • NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles
    • DOI 10.1021/bi051313f
    • E. Papadopoulos, K. Oglecka, L. Maler, J. Jarvet, P.E. Wright, H.J. Dyson, and A. Gräslund NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles Biochemistry 45 2006 159 166 (Pubitemid 43054093)
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 159-166
    • Papadopoulos, E.1    Oglecka, K.2    Maler, L.3    Jarvet, J.4    Wright, P.E.5    Dyson, H.J.6    Graslund, A.7
  • 46
    • 0242580976 scopus 로고    scopus 로고
    • Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site
    • DOI 10.1074/jbc.M307818200
    • J.F. Collet, J.C. D'Souza, U. Jakob, and J.C. Bardwell Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site J. Biol. Chem. 278 2003 45325 45332 (Pubitemid 37432668)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45325-45332
    • Collet, J.-F.1    D'Souza, J.C.2    Jakob, U.3    Bardwell, J.C.A.4
  • 47
    • 0034623949 scopus 로고    scopus 로고
    • Redox switch of Hsp33 has a novel zinc-binding motif
    • DOI 10.1074/jbc.M005957200
    • U. Jakob, M. Eser, and J.C. Bardwell Redox switch of hsp33 has a novel zinc-binding motif J. Biol. Chem. 275 2000 38302 38310 (Pubitemid 32009152)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38302-38310
    • Jakob, U.1    Eser, M.2    Bardwell, J.C.A.3
  • 48
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • D.S. Wishart, B.D. Sykes, and F.M. Richards The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry 31 1992 1647 1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 49
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenstrom Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 50
    • 16644402680 scopus 로고    scopus 로고
    • Letter to the editor: NMR Structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups [3]
    • DOI 10.1023/B:JNMR.0000032609.72759.41
    • H. Iwai, G. Wider, and K. Wüthrich NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups J. Biomol. NMR 29 2004 395 398 (Pubitemid 38864839)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.3 , pp. 395-398
    • Iwai, H.1    Wider, G.2    Wuthrich, K.3
  • 52
    • 0028063876 scopus 로고
    • Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor
    • P. Sevilla-Sierra, G. Otting, and K. Wüthrich Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor J. Mol. Biol. 235 1994 1003 1020
    • (1994) J. Mol. Biol. , vol.235 , pp. 1003-1020
    • Sevilla-Sierra, P.1    Otting, G.2    Wüthrich, K.3
  • 53
    • 0030843294 scopus 로고    scopus 로고
    • Selection of carbonic anhydrase variants displayed on phage: Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics
    • DOI 10.1074/jbc.272.33.20364
    • J.A. Hunt, and C.A. Fierke Selection of carbonic anhydrase variants displayed on phage. Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics J. Biol. Chem. 272 1997 20364 20372 (Pubitemid 27355585)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20364-20372
    • Hunt, J.A.1    Fierke, C.A.2
  • 55
    • 58449087611 scopus 로고    scopus 로고
    • Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB
    • M.A. Schumacher, K.M. Piro, W. Xu, S. Hansen, K. Lewis, and R.G. Brennan Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB Science 323 2009 396 401
    • (2009) Science , vol.323 , pp. 396-401
    • Schumacher, M.A.1    Piro, K.M.2    Xu, W.3    Hansen, S.4    Lewis, K.5    Brennan, R.G.6
  • 56
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/MazF complex: Molecular bases of antidote-toxin recognition
    • DOI 10.1016/S1097-2765(03)00097-2
    • K. Kamada, F. Hanaoka, and S.K. Burley Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition Mol. Cell 11 2003 875 884 (Pubitemid 36569246)
    • (2003) Molecular Cell , vol.11 , Issue.4 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 57
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • DOI 10.1038/nsmb911
    • H. Takagi, Y. Kakuta, T. Okada, M. Yao, I. Tanaka, and M. Kimura Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects Nat. Struct. Mol. Biol. 12 2005 327 331 (Pubitemid 43093087)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.4 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 58
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • DOI 10.1016/j.molcel.2005.07.004, PII S1097276505014401
    • K. Kamada, and F. Hanaoka Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin Mol. Cell 19 2005 497 509 (Pubitemid 41140007)
    • (2005) Molecular Cell , vol.19 , Issue.4 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 59
    • 53149133857 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein
    • P. Kumar, B. Issac, E.J. Dodson, J.P. Turkenburg, and S.C. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein J. Mol. Biol. 383 2008 482 493
    • (2008) J. Mol. Biol. , vol.383 , pp. 482-493
    • Kumar, P.1    Issac, B.2    Dodson, E.J.3    Turkenburg, J.P.4    Mande, S.C.5
  • 60
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • G. Barbato, M. Ikura, L.E. Kay, R.W. Pastor, and A. Bax Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible Biochemistry 31 1992 5269 5278
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 61
    • 1942457231 scopus 로고    scopus 로고
    • Backbone dynamic properties of the central linker region of calcium-calmodulin in 35% trifluoroethanol
    • DOI 10.1016/j.jsb.2003.12.007, PII S1047847703003204
    • R.D. Brokx, R.M. Scheek, A.M. Weljie, and H.J. Vogel Backbone dynamic properties of the central linker region of calcium-calmodulin in 35% trifluoroethanol J. Struct. Biol. 146 2004 272 280 (Pubitemid 38507429)
    • (2004) Journal of Structural Biology , vol.146 , Issue.3 , pp. 272-280
    • Brokx, R.D.1    Scheek, R.M.2    Weljie, A.M.3    Vogel, H.J.4
  • 63
    • 70350680995 scopus 로고    scopus 로고
    • Coordination dynamics of zinc in proteins
    • W. Maret, and Y. Li Coordination dynamics of zinc in proteins Chem. Rev. 109 2009 4682 4707
    • (2009) Chem. Rev. , vol.109 , pp. 4682-4707
    • Maret, W.1    Li, Y.2
  • 64
    • 84867683026 scopus 로고    scopus 로고
    • Rescue of the p53 tumor suppressor by a rationally designed molecule
    • G. Selivanova, and A. Fersht Rescue of the p53 tumor suppressor by a rationally designed molecule Discov. Med. 4 2004 28 30
    • (2004) Discov. Med. , vol.4 , pp. 28-30
    • Selivanova, G.1    Fersht, A.2
  • 66
    • 0038018390 scopus 로고    scopus 로고
    • The biphenyl- and 4-chlorobiphenyl-catabolic transposon Tn4371, a member of a new family of genomic islands related to IncP and Ti plasmids
    • DOI 10.1128/AEM.69.8.4837-4845.2003
    • A. Toussaint, C. Merlin, S. Monchy, M.A. Benotmane, R. Leplae, M. Mergeay, and D. Springael The biphenyl- and 4-chlorobiphenyl-catabolic transposon Tn4371, a member of a new family of genomic islands related to IncP and Ti plasmids Appl. Environ. Microbiol. 69 2003 4837 4845 (Pubitemid 36992948)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.8 , pp. 4837-4845
    • Toussaint, A.1    Merlin, C.2    Monchy, S.3    Benotmane, M.A.4    Leplae, R.5    Mergeay, M.6    Springael, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.