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Volumn 16, Issue 4, 2005, Pages 741-750

Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CROSSLINKING; MASS SPECTROMETRY; MOLECULAR BIOLOGY;

EID: 22644437896     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc050043a     Document Type: Review
Times cited : (101)

References (50)
  • 1
    • 2342498275 scopus 로고    scopus 로고
    • Oligomerization is required for betaine-homocysteine S-methyltransferase function
    • Szegedi, S. S., and Garrow, T. A. (2004) Oligomerization is required for betaine-homocysteine S-methyltransferase function. Arch. Biochem. Biophys. 426, 32-42.
    • (2004) Arch. Biochem. Biophys. , vol.426 , pp. 32-42
    • Szegedi, S.S.1    Garrow, T.A.2
  • 2
    • 0042667015 scopus 로고    scopus 로고
    • Transmembrane organization of the Bacillus subtilis chemoreceptor McpB deduced by cysteine disulfide crosslinking
    • Bunn, M. W., and Ordal, G. W. (2003) Transmembrane organization of the Bacillus subtilis chemoreceptor McpB deduced by cysteine disulfide crosslinking. J. Mol. Biol. 331, 941-9.
    • (2003) J. Mol. Biol. , vol.331 , pp. 941-949
    • Bunn, M.W.1    Ordal, G.W.2
  • 3
    • 0037133698 scopus 로고    scopus 로고
    • Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking
    • Guan, L., Murphy, F. D., and Kaback, H. R. (2002) Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking. Proc. Natl. Acad. Sci. U.S.A. 99, 3475-80.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3475-3480
    • Guan, L.1    Murphy, F.D.2    Kaback, H.R.3
  • 4
    • 0041836334 scopus 로고    scopus 로고
    • Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli
    • Ermolova, N., Guan, L., and Kaback, H. R. (2003) Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 100, 10187-92.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 10187-10192
    • Ermolova, N.1    Guan, L.2    Kaback, H.R.3
  • 6
    • 0028960990 scopus 로고
    • Highly specific oxidative cross-linking of proteins mediated by a nickel-peptide complex
    • Brown, K. C., Yang, S. H., and Kodadek, T. (1995) Highly specific oxidative cross-linking of proteins mediated by a nickel-peptide complex. Biochemistry 34, 4733-9.
    • (1995) Biochemistry , vol.34 , pp. 4733-4739
    • Brown, K.C.1    Yang, S.H.2    Kodadek, T.3
  • 7
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • Fancy, D. A., and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light. Proc. Natl. Acad. Sci. U.S.A. 96, 6020-4.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 8
    • 0033596327 scopus 로고    scopus 로고
    • Photoinduced protein cross-linking mediated by palladium porphyrins
    • Kim, K., Fancy, D. A., Carney, D., and Kodadek, T. (1999) Photoinduced Protein Cross-Linking Mediated by Palladium Porphyrins. J. Am. Chem. Soc. 121, 11896-11897.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11896-11897
    • Kim, K.1    Fancy, D.A.2    Carney, D.3    Kodadek, T.4
  • 9
    • 0345531142 scopus 로고    scopus 로고
    • Using oxidative crosslinking and proximity labeling to quantitatively characterize protein-protein and protein-Peptide complexes
    • Amini, F., Denison, C., Lin, H. J., Kuo, L., and Kodadek, T. (2003) Using oxidative crosslinking and proximity labeling to quantitatively characterize protein-protein and protein-Peptide complexes. Chem. Biol. 10, 1115-27.
    • (2003) Chem. Biol. , vol.10 , pp. 1115-1127
    • Amini, F.1    Denison, C.2    Lin, H.J.3    Kuo, L.4    Kodadek, T.5
  • 10
    • 0037126841 scopus 로고    scopus 로고
    • Protein affinity labeling mediated by genetically encoded peptide tags
    • Amini, F., Kodadek, T., and Brown, K. C. (2002) Protein affinity labeling mediated by genetically encoded peptide tags. Angew. Chem., Int. Ed. 41, 356-9.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 356-359
    • Amini, F.1    Kodadek, T.2    Brown, K.C.3
  • 11
    • 0033970146 scopus 로고    scopus 로고
    • Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques
    • Fancy, D. A. (2000) Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques. Curr. Opin. Chem. Biol. 4, 28-33.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 28-33
    • Fancy, D.A.1
  • 12
    • 3442888009 scopus 로고    scopus 로고
    • New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein complexes
    • Melcher, K. (2004) New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein complexes. Curr. Protein Pept. Sci. 5, 287-96.
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 287-296
    • Melcher, K.1
  • 13
    • 0001268975 scopus 로고
    • Hydroxyl radical "footprinting": High-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein
    • Tullius, T. D., and Dombroski, B. A. (1986) Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein. Proc. Natl. Acad. Sci. U.S.A. 83, 5469-73.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 5469-5473
    • Tullius, T.D.1    Dombroski, B.A.2
  • 14
    • 0025208245 scopus 로고
    • Specific cleavage of a protein by an attached iron chelate
    • Rana, T. M., and Meares, C. F. (1990) Specific cleavage of a protein by an attached iron chelate. J. Am. Chem. Soc. 112, 2457-2458.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2457-2458
    • Rana, T.M.1    Meares, C.F.2
  • 15
    • 0036009245 scopus 로고    scopus 로고
    • The interaction between sigmaS, the stationary phase sigma factor, and the core enzyme of Escherichia coli RNA polymerase
    • Colland, F., Fujita, N., Ishihama, A., and Kolb, A. (2002) The interaction between sigmaS, the stationary phase sigma factor, and the core enzyme of Escherichia coli RNA polymerase. Genes Cells 7, 233-47.
    • (2002) Genes Cells , vol.7 , pp. 233-247
    • Colland, F.1    Fujita, N.2    Ishihama, A.3    Kolb, A.4
  • 16
    • 0141992120 scopus 로고    scopus 로고
    • Binding of TFIIB to RNA polymerase II: Mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex
    • Chen, H. T., and Hahn, S. (2003) Binding of TFIIB to RNA polymerase II: Mapping the binding site for the TFIIB zinc ribbon domain within the preinitiation complex. Mol. Cell 12, 437-47.
    • (2003) Mol. Cell , vol.12 , pp. 437-447
    • Chen, H.T.1    Hahn, S.2
  • 17
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz, P. J. (1993) Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 11, 1138-43.
    • (1993) Biotechnology (NY) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 18
    • 0020478659 scopus 로고
    • A new radioactive cross-linking reagent for studying the interactions of proteins
    • Schwartz, M. A., Das, O. P., and Hynes, R. O. (1982) A new radioactive cross-linking reagent for studying the interactions of proteins. J. Biol. Chem. 257, 2343-9.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2343-2349
    • Schwartz, M.A.1    Das, O.P.2    Hynes, R.O.3
  • 19
    • 0021487317 scopus 로고
    • 1251-labeled crosslinking reagent that is hydrophilic, photoactivatable, and cleavable through an azo linkage
    • Denny, J. B., and Blobel, G. (1984) 1251-labeled crosslinking reagent that is hydrophilic, photoactivatable, and cleavable through an azo linkage. Proc. Natl. Acad. Sci. U.S.A. 81, 5286-90.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 5286-5290
    • Denny, J.B.1    Blobel, G.2
  • 20
    • 0028465007 scopus 로고
    • Identification of the target of a transcription activator protein by protein-protein photocrosslinking
    • Chen, Y., Ebright, Y. W., and Ebright, R. H. (1994) Identification of the target of a transcription activator protein by protein-protein photocrosslinking. Science 265, 90-2.
    • (1994) Science , vol.265 , pp. 90-92
    • Chen, Y.1    Ebright, Y.W.2    Ebright, R.H.3
  • 22
    • 0034725391 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme using a novel trifunctional photo-cross-linking and affinity reagent
    • Alley, S. C., Ishmael, F. T., Jones, A. D., and Benkovic, S. J. (2000) Mapping Protein-Protein Interactions in the Bacteriophage T4 DNA Polymerase Holoenzyme Using a Novel Trifunctional Photo-cross-linking and Affinity Reagent. J. Am. Chem. Soc. 122, 6126-6127.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6126-6127
    • Alley, S.C.1    Ishmael, F.T.2    Jones, A.D.3    Benkovic, S.J.4
  • 23
    • 0035933521 scopus 로고    scopus 로고
    • Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit
    • Brown, C. E., Howe, L., Sousa, K., Alley, S. C., Carrozza, M. J., Tan, S., and Workman, J. L. (2001) Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit. Science 292, 2333-7.
    • (2001) Science , vol.292 , pp. 2333-2337
    • Brown, C.E.1    Howe, L.2    Sousa, K.3    Alley, S.C.4    Carrozza, M.J.5    Tan, S.6    Workman, J.L.7
  • 24
    • 18744398125 scopus 로고    scopus 로고
    • Large-scale database searching using tandem mass spectra: Looking up the answer in the back of the book
    • Sadygov, R. G., Cociorva, D., and Yates, J. R. (2004) Large-scale database searching using tandem mass spectra: Looking up the answer in the back of the book. Nature Methods 1, 195-202.
    • (2004) Nature Methods , vol.1 , pp. 195-202
    • Sadygov, R.G.1    Cociorva, D.2    Yates, J.R.3
  • 25
    • 0347988150 scopus 로고    scopus 로고
    • Lateral membrane protein associations of CD4 in lymphoid cells detected by cross-linking and mass spectrometry
    • Bernhard, O. K, Sheil, M. M., and Cunningham, A. L. (2004) Lateral membrane protein associations of CD4 in lymphoid cells detected by cross-linking and mass spectrometry. Biochemistry 43, 256-64.
    • (2004) Biochemistry , vol.43 , pp. 256-264
    • Bernhard, O.K.1    Sheil, M.M.2    Cunningham, A.L.3
  • 26
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier, L., Usherwood, Y. K., Chung, K. T., and Hendershot, L. M. (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13, 4456-69.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 27
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-9.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 29
    • 3242730298 scopus 로고    scopus 로고
    • Absolute quantification of specific proteins in complex mixtures using visible isotope-coded affinity tags
    • Lu, Y., Bottari, P., Turecek, F., Aebersold, R., and Gelb, M. H. (2004) Absolute quantification of specific proteins in complex mixtures using visible isotope-coded affinity tags. Anal.Chem 76, 4104-11.
    • (2004) Anal.Chem , vol.76 , pp. 4104-4111
    • Lu, Y.1    Bottari, P.2    Turecek, F.3    Aebersold, R.4    Gelb, M.H.5
  • 31
    • 0028859194 scopus 로고
    • Dibromobimane as a fluorescent crosslinking reagent
    • Kim, J. S., and Raines, R. T. (1995) Dibromobimane as a fluorescent crosslinking reagent. Anal. Biochem 225, 174-6.
    • (1995) Anal. Biochem. , vol.225 , pp. 174-176
    • Kim, J.S.1    Raines, R.T.2
  • 33
    • 0029789304 scopus 로고    scopus 로고
    • Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli
    • Wu, J., Voss, J., Hubbell, W. L., and Kaback, H. R. (1996) Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 93, 10123-7.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10123-10127
    • Wu, J.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 34
    • 0029661442 scopus 로고    scopus 로고
    • Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase
    • Bhattacharjee, H., and Rosen, B. P. (1996) Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase. J. Biol. Chem. 271, 24465-70.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24465-24470
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 35
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-Crystallin
    • Sharma, K. K., Kaur, H., and Rester, K. (1997) Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-Crystallin. Biochem. Biophys. Res. Commun. 239, 217-22.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Rester, K.3
  • 36
    • 0036558160 scopus 로고    scopus 로고
    • Identification of components of protein complexes using a fluorescent photo-cross-linker and mass spectrometry
    • Wine, R. N., Dial, J. M., Tomer, K. B., and Borchers, C. H. (2002) Identification of components of protein complexes using a fluorescent photo-cross-linker and mass spectrometry. Anal. Chem 74, 1939-45.
    • (2002) Anal. Chem. , vol.74 , pp. 1939-1945
    • Wine, R.N.1    Dial, J.M.2    Tomer, K.B.3    Borchers, C.H.4
  • 37
    • 0035914387 scopus 로고    scopus 로고
    • Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme
    • Alley, S. C., Trakselis, M. A., Mayer, M. U., Ishmael, F. T., Jones, A. D., and Benkovic, S. J. (2001) Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme. J. Biol. Chem. 276, 39340-9.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39340-39349
    • Alley, S.C.1    Trakselis, M.A.2    Mayer, M.U.3    Ishmael, F.T.4    Jones, A.D.5    Benkovic, S.J.6
  • 38
    • 2442604553 scopus 로고    scopus 로고
    • Mass spectrometric detection of affinity purified crosslinked peptides
    • Hurst, G. B., Lankford, T. K., and Kennel, S. J. (2004) Mass spectrometric detection of affinity purified crosslinked peptides. J. Am. Soc. Mass. Spectrom. 15, 832-9.
    • (2004) J. Am. Soc. Mass. Spectrom. , vol.15 , pp. 832-839
    • Hurst, G.B.1    Lankford, T.K.2    Kennel, S.J.3
  • 39
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck, A. J., and Van Den Heuvel, R. H. (2004) Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23, 368-89.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 40
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • German, J. J., Wallis, T. P., and Pitt, J. J. (2002) Protein disulfide bond determination by mass spectrometry. Mass Spectrom. Rev. 21, 183-216.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 183-216
    • German, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 41
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • Young, M. M., Tang, N., Hempel, J. C., Oshiro, C. M., Taylor, E. W., Kuntz, I. D., Gibson, B. W., and Dollinger, G. (2000) High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 97, 5802-6.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5    Kuntz, I.D.6    Gibson, B.W.7    Dollinger, G.8
  • 42
    • 0037236038 scopus 로고    scopus 로고
    • A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry
    • Kruppa, G. H., Schoeniger, J., and Young, M. M. (2003) A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. Rapid. Commun. Mass Spectrom. 17, 155-62.
    • (2003) Rapid. Commun. Mass Spectrom. , vol.17 , pp. 155-162
    • Kruppa, G.H.1    Schoeniger, J.2    Young, M.M.3
  • 44
    • 9344221072 scopus 로고    scopus 로고
    • Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry
    • Chu, F., Shan, S. O., Moustakas, D. T., Alber, F., Egea, P. F., Stroud, R. M., Walter, P., and Burlingame, A. L. (2004) Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101, 16454-9.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16454-16459
    • Chu, F.1    Shan, S.O.2    Moustakas, D.T.3    Alber, F.4    Egea, P.F.5    Stroud, R.M.6    Walter, P.7    Burlingame, A.L.8
  • 45
    • 1942470540 scopus 로고    scopus 로고
    • Mapping the topology and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTI-CRMS: Direct demonstration of multiple binding modes
    • Schulz, D. M., Ihling, C., Clore, G. M., and Sinz, A. (2004) Mapping the topology and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTI-CRMS: direct demonstration of multiple binding modes. Biochemistry 43, 4703-15,
    • (2004) Biochemistry , vol.43 , pp. 4703-4715
    • Schulz, D.M.1    Ihling, C.2    Clore, G.M.3    Sinz, A.4
  • 46
    • 0345549549 scopus 로고    scopus 로고
    • Non-canonical amino acids in protein engineering
    • Link, A. J., Mock, M. L., and Tirrell, D. A. (2003) Non-canonical amino acids in protein engineering. Curr. Opin. Biotechnol. 14, 603-9.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 603-609
    • Link, A.J.1    Mock, M.L.2    Tirrell, D.A.3
  • 47
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli
    • Chin, J. W., Martin, A. B., King, D. S., Wang, L., and Schultz, P. G. (2002) Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli. Proc. Natl. Acad. Sci. U.S.A. 99, 11020-4.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 48
    • 0036523420 scopus 로고    scopus 로고
    • Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues
    • Kirshenbaum, K., Carrico, I. S., and Tirrell, D. A. (2002) Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues. Chembiochem 3, 235-7.
    • (2002) Chembiochem , vol.3 , pp. 235-237
    • Kirshenbaum, K.1    Carrico, I.S.2    Tirrell, D.A.3
  • 49
    • 0037870583 scopus 로고    scopus 로고
    • Breaking the degeneracy of the genetic code
    • Kwon, I., Kirshenbaum, K., and Tirrell, D. A. (2003) Breaking the degeneracy of the genetic code. J. Am. Chem. Soc. 125, 7512-3.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7512-7513
    • Kwon, I.1    Kirshenbaum, K.2    Tirrell, D.A.3


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