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Volumn 46, Issue 43, 2007, Pages 12152-12163

Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: Indication for a functional role of differential stability

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENTIAL STABILITY; PROTEASE SENSITIVE; THERMOSTABILITY;

EID: 35649008288     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701037e     Document Type: Article
Times cited : (31)

References (63)
  • 1
    • 0032696759 scopus 로고    scopus 로고
    • Addiction modules and programmed cell death and antideath in bacterial cultures
    • Engelberg-Kulka, H., and Glaser, G. (1999) Addiction modules and programmed cell death and antideath in bacterial cultures, Annu. Rev. Microbiol. 53, 43-70.
    • (1999) Annu. Rev. Microbiol , vol.53 , pp. 43-70
    • Engelberg-Kulka, H.1    Glaser, G.2
  • 3
    • 0141707105 scopus 로고    scopus 로고
    • Toxins-antitoxins: Plasmid maintenance, programmed cell death, and cell cycle arrest
    • Hayes, F. (2003) Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest, Science 301, 1496-1499.
    • (2003) Science , vol.301 , pp. 1496-1499
    • Hayes, F.1
  • 4
    • 0036067108 scopus 로고    scopus 로고
    • Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins
    • Pedersen, K., Christensen, S. K., and Gerdes, K. (2002) Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins, Mol. Microbiol. 45, 501-510.
    • (2002) Mol. Microbiol , vol.45 , pp. 501-510
    • Pedersen, K.1    Christensen, S.K.2    Gerdes, K.3
  • 5
    • 10044283095 scopus 로고    scopus 로고
    • MazF-mediated cell death in Escherichia coli: A point of no return
    • Amitai, S., Yassin, Y., and Engelberg-Kulka, H. (2004) MazF-mediated cell death in Escherichia coli: a point of no return, J. Bacteriol. 186, 8295-8300.
    • (2004) J. Bacteriol , vol.186 , pp. 8295-8300
    • Amitai, S.1    Yassin, Y.2    Engelberg-Kulka, H.3
  • 6
    • 27944437497 scopus 로고    scopus 로고
    • Toxin-antitoxin modules as bacterial metabolic stress managers
    • Buts, L., Lah, J., Dao-Thi, M. H., Wyns, L., and Loris, R. (2005) Toxin-antitoxin modules as bacterial metabolic stress managers, Trends Biochem. Sci. 30, 672-679.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 672-679
    • Buts, L.1    Lah, J.2    Dao-Thi, M.H.3    Wyns, L.4    Loris, R.5
  • 7
    • 33750489399 scopus 로고    scopus 로고
    • Bacterial programmed cell death and multicellular behavior in bacteria
    • Engelberg-Kulka, H., Amitai, S., Kolodkin-Gal, I., and Hazan, R. (2006) Bacterial programmed cell death and multicellular behavior in bacteria, PLoS Genet. 2, e135.
    • (2006) PLoS Genet , vol.2
    • Engelberg-Kulka, H.1    Amitai, S.2    Kolodkin-Gal, I.3    Hazan, R.4
  • 8
    • 33748309126 scopus 로고    scopus 로고
    • Shutdown decay of mRNA
    • Condon, C. (2006) Shutdown decay of mRNA, Mol. Microbiol. 61, 573-583.
    • (2006) Mol. Microbiol , vol.61 , pp. 573-583
    • Condon, C.1
  • 9
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey, D. P., and Gerdes, K. (2005) Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes, Nucleic Acids Res. 33, 966-976.
    • (2005) Nucleic Acids Res , vol.33 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 10
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • Christensen, S. K., and Gerdes, K. (2003) RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA, Mol. Microbiol. 48, 1389-1400.
    • (2003) Mol. Microbiol , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 11
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen, S. K., Pedersen, K., Hansen, F. G., and Gerdes, K. (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA, J. Mol. Biol. 332, 809-819.
    • (2003) J. Mol. Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 12
    • 0035807805 scopus 로고    scopus 로고
    • RelE, a global inhibitor of translation, is activated during nutritional stress
    • Christensen, S. K., Mikkelsen, M., Pedersen, K., and Gerdes, K. (2001) RelE, a global inhibitor of translation, is activated during nutritional stress, Proc. Natl. Acad. Sci. U.S.A. 98, 14328-14333.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14328-14333
    • Christensen, S.K.1    Mikkelsen, M.2    Pedersen, K.3    Gerdes, K.4
  • 13
    • 34548496904 scopus 로고    scopus 로고
    • What is the benefit for E. coli to have multiple toxin-antitoxin systems in their genomes?
    • in press
    • Tsilibaris, V., Maenhaut-Michel, G., Mine, N., and Van Melderen, L. (2007) What is the benefit for E. coli to have multiple toxin-antitoxin systems in their genomes? J. Bacteriol. (in press).
    • (2007) J. Bacteriol
    • Tsilibaris, V.1    Maenhaut-Michel, G.2    Mine, N.3    Van Melderen, L.4
  • 14
    • 17144416850 scopus 로고    scopus 로고
    • Persister cells and the riddle of biofilm survival
    • Lewis, K. (2005) Persister cells and the riddle of biofilm survival, Biochemistry (Moscow) 70, 267-274.
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 267-274
    • Lewis, K.1
  • 15
    • 10044266575 scopus 로고    scopus 로고
    • Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli
    • Keren, I., Shah, D., Spoering, A., Kaldalu, N., and Lewis, K. (2004) Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli, J. Bacteriol. 186, 8172-8180.
    • (2004) J. Bacteriol , vol.186 , pp. 8172-8180
    • Keren, I.1    Shah, D.2    Spoering, A.3    Kaldalu, N.4    Lewis, K.5
  • 16
    • 33846064688 scopus 로고    scopus 로고
    • Toxin-antitoxin systems are ubiquitous and plasmid-encoded in vancomycin-resistant enterococci
    • Moritz, E. M., and Hergenrother, P. J. (2007) Toxin-antitoxin systems are ubiquitous and plasmid-encoded in vancomycin-resistant enterococci, Proc. Natl. Acad. Sci. U.S.A. 104, 311-316.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 311-316
    • Moritz, E.M.1    Hergenrother, P.J.2
  • 17
    • 0033614011 scopus 로고    scopus 로고
    • Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes
    • Gronlund, H., and Gerdes, K. (1999) Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes, J. Mol. Biol. 285, 1401-1415.
    • (1999) J. Mol. Biol , vol.285 , pp. 1401-1415
    • Gronlund, H.1    Gerdes, K.2
  • 18
    • 0028222452 scopus 로고
    • Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria
    • Van Melderen, L., Bernard, P., and Couturier, M. (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria, Mol. Microbiol. 11, 1151-1157.
    • (1994) Mol. Microbiol , vol.11 , pp. 1151-1157
    • Van Melderen, L.1    Bernard, P.2    Couturier, M.3
  • 19
    • 0028985596 scopus 로고
    • Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli
    • Lehnherr, H., and Yarmolinsky, M. B. (1995) Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 92, 3274-3277.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 3274-3277
    • Lehnherr, H.1    Yarmolinsky, M.B.2
  • 20
    • 0031690672 scopus 로고    scopus 로고
    • Efficiency of the pTF-FC2 pas poison-antidote stability system in Escherichia coli is affected by the host strain, and antidote degradation requires the lon protease
    • Smith, A. S., and Rawlings, D. E. (1998) Efficiency of the pTF-FC2 pas poison-antidote stability system in Escherichia coli is affected by the host strain, and antidote degradation requires the lon protease, J. Bacteriol. 180, 5458-5462.
    • (1998) J. Bacteriol , vol.180 , pp. 5458-5462
    • Smith, A.S.1    Rawlings, D.E.2
  • 21
    • 1642483754 scopus 로고    scopus 로고
    • Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: Involvement of the yefM-yoeB toxin-antitoxin system
    • Christensen, S. K., Maenhaut-Michel, G., Mine, N., Gottesman, S., Gerdes, K., and Van Melderen, L. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system, Mol. Microbiol. 51, 1705-1717.
    • (2004) Mol. Microbiol , vol.51 , pp. 1705-1717
    • Christensen, S.K.1    Maenhaut-Michel, G.2    Mine, N.3    Gottesman, S.4    Gerdes, K.5    Van Melderen, L.6
  • 22
    • 24044497249 scopus 로고    scopus 로고
    • The YoeB toxin is a folded protein that forms a physical complex with the unfolded YefM antitoxin. Implications for a structural-based differential stability of toxin-antitoxin systems
    • Cherny, I., Rockah, L., and Gazit, E. (2005) The YoeB toxin is a folded protein that forms a physical complex with the unfolded YefM antitoxin. Implications for a structural-based differential stability of toxin-antitoxin systems, J. Biol. Chem. 280, 30063-30072.
    • (2005) J. Biol. Chem , vol.280 , pp. 30063-30072
    • Cherny, I.1    Rockah, L.2    Gazit, E.3
  • 23
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal "addiction module" regulated by guanosine 3′,5′-bispyrophosphate: A model for programmed bacterial cell death
    • Aizenman, E., Engelberg-Kulka, H., and Glaser, G. (1996) An Escherichia coli chromosomal "addiction module" regulated by guanosine 3′,5′-bispyrophosphate: a model for programmed bacterial cell death, Proc. Natl. Acad. Sci. U.S.A. 93, 6059-6063.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-Kulka, H.2    Glaser, G.3
  • 24
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/MazF complex: Molecular bases of antidote-toxin recognition
    • Kamada, K., Hanaoka, F., and Burley, S. K. (2003) Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition, Mol. Cell 11, 875-884.
    • (2003) Mol. Cell , vol.11 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 25
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada, K., and Hanaoka, F. (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin, Mol. Cell 19, 497-509.
    • (2005) Mol. Cell , vol.19 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 26
    • 0037515721 scopus 로고    scopus 로고
    • Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA
    • Lah, J., Marianovsky, I., Glaser, G., Engelberg-Kulka, H., Kinne, J., Wyns, L., and Loris, R. (2003) Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA, J. Biol. Chem. 278, 14101-14111.
    • (2003) J. Biol. Chem , vol.278 , pp. 14101-14111
    • Lah, J.1    Marianovsky, I.2    Glaser, G.3    Engelberg-Kulka, H.4    Kinne, J.5    Wyns, L.6    Loris, R.7
  • 28
    • 20444458293 scopus 로고    scopus 로고
    • Energetics of structural transitions of the addiction antitoxin MazE: Is a programmed bacterial cell death dependent on the intrinsically flexible nature of the antitoxins?
    • Lah, J., Simic, M., Vesnaver, G., Marianovsky, I., Glaser, G., Engelberg-Kulka, H., and Loris, R. (2005) Energetics of structural transitions of the addiction antitoxin MazE: is a programmed bacterial cell death dependent on the intrinsically flexible nature of the antitoxins? J. Biol. Chem. 280, 17397-17407.
    • (2005) J. Biol. Chem , vol.280 , pp. 17397-17407
    • Lah, J.1    Simic, M.2    Vesnaver, G.3    Marianovsky, I.4    Glaser, G.5    Engelberg-Kulka, H.6    Loris, R.7
  • 29
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I., and Kimura, M. (2005) Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects, Nat. Struct. Mol. Biol. 12, 327-331.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 30
    • 1542379603 scopus 로고    scopus 로고
    • The YefM antitoxin defines a family of natively unfolded proteins: Implications as a novel antibacterial target
    • Cherny, I., and Gazit, E. (2004) The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target, J. Biol. Chem. 279, 8252-8261.
    • (2004) J. Biol. Chem , vol.279 , pp. 8252-8261
    • Cherny, I.1    Gazit, E.2
  • 31
    • 0036182510 scopus 로고    scopus 로고
    • The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins
    • Oberer, M., Zangger, K., Prytulla, S., and Keller, W. (2002) The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins, Biochem. J. 361, 41-47.
    • (2002) Biochem. J , vol.361 , pp. 41-47
    • Oberer, M.1    Zangger, K.2    Prytulla, S.3    Keller, W.4
  • 34
    • 0034705331 scopus 로고    scopus 로고
    • The thermodynamic stability of the proteins of the ccd plasmid addiction system
    • Dao-Thi, M. H., Messens, J., Wyns, L., and Backmann, J. (2000) The thermodynamic stability of the proteins of the ccd plasmid addiction system, J. Mol. Biol. 299, 1373-1386.
    • (2000) J. Mol. Biol , vol.299 , pp. 1373-1386
    • Dao-Thi, M.H.1    Messens, J.2    Wyns, L.3    Backmann, J.4
  • 36
    • 0029861722 scopus 로고    scopus 로고
    • ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions
    • Van Melderen, L., Thi, M. H., Lecchi, P., Gottesman, S., Couturier, M., and Maurizi, M. R. (1996) ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions, J. Biol. Chem. 271, 27730-27738.
    • (1996) J. Biol. Chem , vol.271 , pp. 27730-27738
    • Van Melderen, L.1    Thi, M.H.2    Lecchi, P.3    Gottesman, S.4    Couturier, M.5    Maurizi, M.R.6
  • 37
    • 0033546274 scopus 로고    scopus 로고
    • The Doc toxin and Phd antidote proteins of the bacteriophage P1 plasmid addiction system form a heterotrimeric complex
    • Gazit, E., and Sauer, R. T. (1999) The Doc toxin and Phd antidote proteins of the bacteriophage P1 plasmid addiction system form a heterotrimeric complex, J. Biol. Chem. 274, 16813-16818.
    • (1999) J. Biol. Chem , vol.274 , pp. 16813-16818
    • Gazit, E.1    Sauer, R.T.2
  • 38
    • 0033613864 scopus 로고    scopus 로고
    • Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system
    • Gazit, E., and Sauer, R. T. (1999) Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system, J. Biol. Chem. 274, 2652-2657.
    • (1999) J. Biol. Chem , vol.274 , pp. 2652-2657
    • Gazit, E.1    Sauer, R.T.2
  • 39
    • 0033401440 scopus 로고    scopus 로고
    • Thermodynamic properties and DNA binding of the ParD protein from the broad host-range plasmid RK2/RP4 killing system
    • Oberer, M., Lindner, H., Glatter, O., Kratky, C., and Keller, W. (1999) Thermodynamic properties and DNA binding of the ParD protein from the broad host-range plasmid RK2/RP4 killing system, Biol. Chem. 380, 1413-1420.
    • (1999) Biol. Chem , vol.380 , pp. 1413-1420
    • Oberer, M.1    Lindner, H.2    Glatter, O.3    Kratky, C.4    Keller, W.5
  • 40
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • Parsell, D. A., and Sauer, R. T. (1989) The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli, J. Biol. Chem. 264, 7590-7595.
    • (1989) J. Biol. Chem , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 41
    • 0033976914 scopus 로고    scopus 로고
    • Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress
    • Gerdes, K. (2000) Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress, J. Bacteriol. 182, 561-572.
    • (2000) J. Bacteriol , vol.182 , pp. 561-572
    • Gerdes, K.1
  • 43
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen, K., Zavialov, A. V., Pavlov, M. Y., Elf, J., Gerdes, K., and Ehrenberg, M. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site, Cell 112, 131-140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 44
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 45
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005) The interplay between structure and function in intrinsically unstructured proteins, FEBS Lett. 579, 3346-3354.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 46
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 47
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M. A., Chacon, P., Merelo, J. J., and Moran, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network, Protein Eng. 6, 383-390.
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 48
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (1999) Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy, Protein Sci. 8, 370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 49
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W., and Glockner, J. (1981) Estimation of globular protein secondary structure from circular dichroism, Biochemistry 20, 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 50
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson, W. C. (1999) Analyzing protein circular dichroism spectra for accurate secondary structures, Proteins 35, 307-312.
    • (1999) Proteins , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 51
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 52
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris, P. I., and Chapman, D. (1995) The conformational analysis of peptides using Fourier transform IR spectroscopy, Biopolymers 37, 251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 53
    • 0033642273 scopus 로고    scopus 로고
    • Sample preparation techniques for peptides and proteins analyzed by MALDI-MS
    • Kussmann, M., and Roepstorff, P. (2000) Sample preparation techniques for peptides and proteins analyzed by MALDI-MS, Methods Mol. Biol. 146, 405-424.
    • (2000) Methods Mol. Biol , vol.146 , pp. 405-424
    • Kussmann, M.1    Roepstorff, P.2
  • 54
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment, J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 55
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. (1999) Protein secondary structure prediction based on position-specific scoring matrices, J. Mol. Biol. 292, 195-202.
    • (1999) J. Mol. Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 56
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server, Bioinformatics 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 59
    • 0029743487 scopus 로고    scopus 로고
    • Autoregulation of the plasmid addiction Operon of bacteriophage P1
    • Magnuson, R., Lehnherr, H., Mukhopadhyay, G., and Yarmolinsky, M. B. (1996) Autoregulation of the plasmid addiction Operon of bacteriophage P1, J. Biol. Chem. 271, 18705-18710.
    • (1996) J. Biol. Chem , vol.271 , pp. 18705-18710
    • Magnuson, R.1    Lehnherr, H.2    Mukhopadhyay, G.3    Yarmolinsky, M.B.4
  • 60
    • 1642341084 scopus 로고    scopus 로고
    • Plasmid evolution and interaction between the plasmid addiction stability systems of two related broad-host-range IncQ-like plasmids
    • Deane, S. M., and Rawlings, D. E. (2004) Plasmid evolution and interaction between the plasmid addiction stability systems of two related broad-host-range IncQ-like plasmids, J. Bacteriol. 186, 2123-2133.
    • (2004) J. Bacteriol , vol.186 , pp. 2123-2133
    • Deane, S.M.1    Rawlings, D.E.2
  • 61
    • 33846897363 scopus 로고    scopus 로고
    • The yefM-yoeB toxin-antitoxin systems of Escherichia coli and Streptococcus pneumoniae: Functional and structural correlation
    • Nieto, C., Cherny, I., Khoo, S. K., de Lacoba, M. G., Chan, W. T., Yeo, C. C., Gazit, E., and Espinosa, M. (2007) The yefM-yoeB toxin-antitoxin systems of Escherichia coli and Streptococcus pneumoniae: functional and structural correlation, J. Bacteriol. 189, 1266-1278.
    • (2007) J. Bacteriol , vol.189 , pp. 1266-1278
    • Nieto, C.1    Cherny, I.2    Khoo, S.K.3    de Lacoba, M.G.4    Chan, W.T.5    Yeo, C.C.6    Gazit, E.7    Espinosa, M.8
  • 62
    • 34147093024 scopus 로고    scopus 로고
    • Functional interactions between coexisting toxin-antitoxin systems of the ccd family in Escherichia coli O157: H7
    • Wilbaux, M., Mine, N., Guerout, A. M., Mazel, D., and Van Melderen, L. (2007) Functional interactions between coexisting toxin-antitoxin systems of the ccd family in Escherichia coli O157: H7, J. Bacteriol. 189, 2712-2719.
    • (2007) J. Bacteriol , vol.189 , pp. 2712-2719
    • Wilbaux, M.1    Mine, N.2    Guerout, A.M.3    Mazel, D.4    Van Melderen, L.5
  • 63
    • 1542472730 scopus 로고    scopus 로고
    • New connections in the prokaryotic toxin-antitoxin network: Relationship with the eukaryotic nonsense-mediated RNA decay system
    • Anantharaman, V., and Aravind, L. (2003) New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system, GenomeBiology 4, R81.
    • (2003) GenomeBiology , vol.4
    • Anantharaman, V.1    Aravind, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.