메뉴 건너뛰기




Volumn 17, Issue 1, 2006, Pages 525-538

Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; GOLGI MATRIX PROTEIN; MATRIX PROTEIN; MEMBRANE PROTEIN; PROTEIN P58; PROTEIN SEC13; UNCLASSIFIED DRUG;

EID: 30044439559     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-05-0447     Document Type: Article
Times cited : (49)

References (54)
  • 1
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller, C., Andersson, H., Kappeler, F., and Hauri, H. P. (1999). The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat. Cell Biol. 1, 330-334.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.P.4
  • 2
    • 16844374025 scopus 로고    scopus 로고
    • Golgi positioning: Are we looking at the right MAP?
    • Barr, F. A., and Egerer, J. (2005). Golgi positioning: are we looking at the right MAP? J. Cell Biol. 168, 993-998.
    • (2005) J. Cell Biol. , vol.168 , pp. 993-998
    • Barr, F.A.1    Egerer, J.2
  • 3
    • 0032526720 scopus 로고    scopus 로고
    • Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae
    • Barr, F. A., Nakamura, N., and Warren, G. (1998). Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J. 17, 3258-3268.
    • (1998) EMBO J. , vol.17 , pp. 3258-3268
    • Barr, F.A.1    Nakamura, N.2    Warren, G.3
  • 4
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr, F. A., Puype, M., Vandekerckhove, J., and Warren, G. (1997). GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91, 253-262.
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 5
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr, F. A., and Short, B. (2003). Golgins in the structure and dynamics of the Golgi apparatus. Curr. Opin. Cell Biol. 15, 405-413.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 6
    • 0028796834 scopus 로고
    • Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes
    • Barroso, M., Nelson, D. S., and Sztul, E. (1995). Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes. Proc. Natl. Acad. Sci. USA 92, 527-531.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 527-531
    • Barroso, M.1    Nelson, D.S.2    Sztul, E.3
  • 7
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • Ben-Tekaya, H., Miura, K., Pepperkok, R., and Hauri, H. P. (2005). Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci. 118, 357-367.
    • (2005) J. Cell Sci. , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 8
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • Bevis, B. J., Hammond, A. T., Reinke, C. A., and Glick, B. S. (2002). De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat. Cell Biol. 4, 750-756.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 750-756
    • Bevis, B.J.1    Hammond, A.T.2    Reinke, C.A.3    Glick, B.S.4
  • 10
    • 0034618073 scopus 로고    scopus 로고
    • Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments
    • Dirac-Svejstrup, A. B., Shorter, J., Waters, M. G., and Warren, G. (2000). Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments. J. Cell Biol. 150, 475-488.
    • (2000) J. Cell Biol. , vol.150 , pp. 475-488
    • Dirac-Svejstrup, A.B.1    Shorter, J.2    Waters, M.G.3    Warren, G.4
  • 11
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes
    • Donaldson, J. G., Cassel, D., Kahn, R. A., and Klausner, R. D. (1992a). ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89, 6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 12
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J. G., Finazzi, D., and Klausner, R. D. (1992b). Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 360, 350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 13
    • 0026034357 scopus 로고
    • Beta-COP, a 110 kD protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin
    • Duden, R., Griffiths, G., Frank, R., Argos, P., and Kreis, T. E. (1991). Beta-COP, a 110 kD protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin. Cell 64, 649-665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 14
    • 0025916210 scopus 로고
    • Diversity and origin of rheumatologic autoantibodies
    • Fritzler, M. J., and Salazar, M. (1991). Diversity and origin of rheumatologic autoantibodies. Clin. Microbiol. Rev. 4, 256-269.
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 256-269
    • Fritzler, M.J.1    Salazar, M.2
  • 15
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • Garcia-Mata, R., Szul, T., Alvarez, C., and Sztul, E. (2003). ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol. Biol. Cell 14, 2250-2261.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2250-2261
    • Garcia-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 16
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham, A. K., and Munro, S. (2003). Long coiled-coil proteins and membrane traffic. Biochim. Biophys. Acta 1641, 71-85.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 17
    • 0026063240 scopus 로고
    • A 58-kDa resident protein of the cis-Golgi cisterna is not terminally glycosylated
    • Hendricks, L. C., Gabel, C. A., Suh, K., and Farquhar, M. G. (1991). A 58-kDa resident protein of the cis-Golgi cisterna is not terminally glycosylated. J. Biol. Chem. 266, 17559-17565.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17559-17565
    • Hendricks, L.C.1    Gabel, C.A.2    Suh, K.3    Farquhar, M.G.4
  • 19
    • 18244407270 scopus 로고    scopus 로고
    • Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress
    • Jiang, S., and Storrie, B. (2005). Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress. Mol. Biol. Cell 16, 2586-2596.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2586-2596
    • Jiang, S.1    Storrie, B.2
  • 20
    • 4344702375 scopus 로고    scopus 로고
    • Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase HeLa cells
    • Kasap, M., Thomas, S., Danaher, E., Holton, V., Jiang, S., and Storrie, B. (2004). Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase HeLa cells. Traffic 5, 595-605.
    • (2004) Traffic , vol.5 , pp. 595-605
    • Kasap, M.1    Thomas, S.2    Danaher, E.3    Holton, V.4    Jiang, S.5    Storrie, B.6
  • 21
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., Donaldson, J. G., and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 22
    • 0032895860 scopus 로고    scopus 로고
    • Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COP1 dissociation
    • Lee, T. H., and Linstedt, A. D. (1999). Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COP1 dissociation. Mol. Biol. Cell 10, 1445-1462.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1445-1462
    • Lee, T.H.1    Linstedt, A.D.2
  • 23
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt, A. D., and Hauri, H. P. (1993). Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.P.2
  • 24
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C., and Klausner, R. D. (1990). Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 26
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe, M., Rabouille, C., Nakamura, N., Watson, R., Jackman, M., Jamsa, E., Rahman, D., Pappin, D. J., and Warren, G. (1998). Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell 94, 783-793.
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3    Watson, R.4    Jackman, M.5    Jamsa, E.6    Rahman, D.7    Pappin, D.J.8    Warren, G.9
  • 27
    • 0032939863 scopus 로고    scopus 로고
    • Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: Immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family
    • Mandel, U., Hassan, H., Therkildsen, M. H., Rygaard, J., Jakobsen, M. H., Juhl, B. R., Dabelsteen, E., and Clausen, H. (1999). Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Glycobiology 9, 43-52.
    • (1999) Glycobiology , vol.9 , pp. 43-52
    • Mandel, U.1    Hassan, H.2    Therkildsen, M.H.3    Rygaard, J.4    Jakobsen, M.H.5    Juhl, B.R.6    Dabelsteen, E.7    Clausen, H.8
  • 29
    • 0036902478 scopus 로고    scopus 로고
    • Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex
    • Matanis, T., et al. (2002). Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex. Nat. Cell Biol. 4, 986-992.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 986-992
    • Matanis, T.1
  • 30
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., Lowe, M., Levine, T. P., Rabouille, C., and Warren, G. (1997). The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89, 445-455.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 31
    • 0032547807 scopus 로고    scopus 로고
    • The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function
    • Nelson, D. S., Alvarez, C., Gao, Y. S., Garcia-Mata, R., Fialkowski, E., and Sztul, E. (1998). The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function. J. Cell Biol. 143, 319-331.
    • (1998) J. Cell Biol. , vol.143 , pp. 319-331
    • Nelson, D.S.1    Alvarez, C.2    Gao, Y.S.3    Garcia-Mata, R.4    Fialkowski, E.5    Sztul, E.6
  • 32
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu, T. K., Pfeifer, A. C., Lippincott-Schwartz, J., and Jackson, C. L. (2005). Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16, 1213-1222.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 33
    • 12344267982 scopus 로고    scopus 로고
    • Unique and shared features of Golgi complex autoantigens
    • Nozawa, K., Fritzler, M. J., and Chan, E. K. (2005). Unique and shared features of Golgi complex autoantigens. Autoimmun. Rev. 4, 35-41.
    • (2005) Autoimmun. Rev. , vol.4 , pp. 35-41
    • Nozawa, K.1    Fritzler, M.J.2    Chan, E.K.3
  • 36
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G. (1975). Intracellular aspects of the process of protein synthesis. Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 37
    • 0037418595 scopus 로고    scopus 로고
    • The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus
    • Panic, B., Whyte, J. R., and Munro, S. (2003). The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr. Biol. 13, 405-410.
    • (2003) Curr. Biol. , vol.13 , pp. 405-410
    • Panic, B.1    Whyte, J.R.2    Munro, S.3
  • 38
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin a acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • Peyroche, A., Antonny, B., Robineau, S., Acker, J., Cherfils, J., and Jackson, C. L. (1999). Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3, 275-285.
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 39
    • 0345306582 scopus 로고    scopus 로고
    • Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum
    • Puri, S., and Linstedt, A. D. (2003). Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum. Mol. Biol. Cell 14, 5011-5018.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5011-5018
    • Puri, S.1    Linstedt, A.D.2
  • 40
    • 0035889084 scopus 로고    scopus 로고
    • Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components Giantin and GM130
    • Puthenveedu, M. A., and Linstedt, A. D. (2001). Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components Giantin and GM130. J. Cell Biol. 155, 227-238.
    • (2001) J. Cell Biol. , vol.155 , pp. 227-238
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 42
    • 0034718846 scopus 로고    scopus 로고
    • Matrix proteins can generate the higher order architecture of the Golgi apparatus
    • Seemann, J., Jokitalo, E., Pypaert, M., and Warren, G. (2000). Matrix proteins can generate the higher order architecture of the Golgi apparatus. Nature 407, 1022-1026.
    • (2000) Nature , vol.407 , pp. 1022-1026
    • Seemann, J.1    Jokitalo, E.2    Pypaert, M.3    Warren, G.4
  • 43
  • 44
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter, J., Watson, R., Giannakou, M. E., Clarke, M., Warren, G., and Barr, F. A. (1999). GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18, 4949-4960.
    • (1999) EMBO J. , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 45
    • 0036701880 scopus 로고    scopus 로고
    • ARF1 regulatory factors and COPI vesicle formation
    • Spang, A. (2002). ARF1 regulatory factors and COPI vesicle formation. Curr. Opin. Cell Biol. 14, 423-427.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 423-427
    • Spang, A.1
  • 46
    • 0034285087 scopus 로고    scopus 로고
    • Breaking the COPI monopoly on Golgi recycling
    • Storrie, B., Pepperkok, R., and Nilsson, T. (2000). Breaking the COPI monopoly on Golgi recycling. Trends Cell Biol. 10, 385-391.
    • (2000) Trends Cell Biol. , vol.10 , pp. 385-391
    • Storrie, B.1    Pepperkok, R.2    Nilsson, T.3
  • 47
    • 21844468961 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division
    • Sütterlin, C., Polishchuk, R., Pecot, M., and Malhotra, V. (2005). The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division. Mol. Biol. Cell 16, 3211-3222.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3211-3222
    • Sütterlin, C.1    Polishchuk, R.2    Pecot, M.3    Malhotra, V.4
  • 48
    • 0028823747 scopus 로고
    • Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A
    • Tang, B. L., Low, S. H., and Hong, W. (1995). Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A. Eur. J. Cell Biol. 68, 199-205.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 199-205
    • Tang, B.L.1    Low, S.H.2    Hong, W.3
  • 49
    • 2142753950 scopus 로고    scopus 로고
    • Tension in tubulovesicular networks of Golgi and endoplasmic reticulum membranes
    • Upadhyaya, A., and Sheetz, M. P. (2004). Tension in tubulovesicular networks of Golgi and endoplasmic reticulum membranes. Biophys. J. 86, 2923-2928.
    • (2004) Biophys. J. , vol.86 , pp. 2923-2928
    • Upadhyaya, A.1    Sheetz, M.P.2
  • 50
    • 0013086420 scopus 로고    scopus 로고
    • Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130
    • Vasile, E., Perez, T., Nakamura, N., and Krieger, M. (2003). Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130. Traffic 4, 254-272.
    • (2003) Traffic , vol.4 , pp. 254-272
    • Vasile, E.1    Perez, T.2    Nakamura, N.3    Krieger, M.4
  • 53
    • 0031910288 scopus 로고    scopus 로고
    • Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins
    • Yang, W., and Storrie, B. (1998). Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins. Mol. Biol. Cell 9, 191-207.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 191-207
    • Yang, W.1    Storrie, B.2
  • 54
    • 0033544712 scopus 로고    scopus 로고
    • Golgi membranes are absorbed into and reemerge from the ER during mitosis
    • Zaal, K. J., et al. (1999). Golgi membranes are absorbed into and reemerge from the ER during mitosis. Cell 99, 589-601.
    • (1999) Cell , vol.99 , pp. 589-601
    • Zaal, K.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.