메뉴 건너뛰기




Volumn 134, Issue 1, 2003, Pages 1-8

Ubiquitylation as a quality control system for intracellular proteins

Author keywords

Molecular chaperone; Quality control; U box protein; Ubiquitin; Ubiquitin ligase

Indexed keywords

CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; PROTEIN UFD2; U BOX PROTEIN; UBIQUITIN; UBIQUITIN CHAIN ASSEMBLY FACTOR; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 0042320478     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg106     Document Type: Review
Times cited : (53)

References (59)
  • 1
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 2
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies: Symptoms of cellular indigestion?
    • Kopito, R.R. and Sitia, R. (2000) Aggresomes and Russell bodies: Symptoms of cellular indigestion? EMBO Rep. 1, 225-231
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 3
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L., and Kopito, R.R. (1998) Aggresomes: A cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 4
    • 0036677215 scopus 로고    scopus 로고
    • Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells
    • Namekata, K., Nishimura, N., and Kimura, H. (2002) Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells. J. Neurochem. 82, 819-827
    • (2002) J. Neurochem. , vol.82 , pp. 819-827
    • Namekata, K.1    Nishimura, N.2    Kimura, H.3
  • 5
    • 0032752558 scopus 로고    scopus 로고
    • PMP22 accumulation in aggresomes: Implications for CMT1A pathology
    • Notterpek, L., Ryan, M.C., Tobler, A.R., and Shooter, E.M. (1999) PMP22 accumulation in aggresomes: Implications for CMT1A pathology. Neurobiol. Dis. 6, 450-460
    • (1999) Neurobiol. Dis. , vol.6 , pp. 450-460
    • Notterpek, L.1    Ryan, M.C.2    Tobler, A.R.3    Shooter, E.M.4
  • 6
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata, R., Bebok, Z., Sorscher, E.J., and Sztul, E.S. (1999) Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. 146, 1239-1254
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 7
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in HeLa cells: Indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik, C., Schroeter, D., Wilk, S., Lamprecht, J., and Paweletz, N. (1996) Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur. J. Cell Biol. 71, 311-318
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 311-318
    • Wojcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 8
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • Kopito, R.R. and Ron, D. (2000) Conformational disease. Nature Cell Biol. 2, 207-209
    • (2000) Nature Cell Biol. , vol.2 , pp. 207-209
    • Kopito, R.R.1    Ron, D.2
  • 9
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: Two ubiquitin-like systems. Nature Rev. Mol. Cell. Biol. 2, 211-216
    • (2001) Nature Rev. Mol. Cell. Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 10
    • 0024370374 scopus 로고
    • Endocytosis and autophagy in dying neurons: An ultrastructural study in chick embryos
    • Hornung, J.P., Koppel, H., and Clarke, P.G. (1989) Endocytosis and autophagy in dying neurons: an ultrastructural study in chick embryos. J. Comp. Neurol. 283, 425-437
    • (1989) J. Comp. Neurol. , vol.283 , pp. 425-437
    • Hornung, J.P.1    Koppel, H.2    Clarke, P.G.3
  • 12
    • 0036668073 scopus 로고    scopus 로고
    • Autophagy in hypothalamic neurones of rats expressing a familial neurohypophysial diabetes insipidus transgene
    • Davies, J. and Murphy, D. (2002) Autophagy in hypothalamic neurones of rats expressing a familial neurohypophysial diabetes insipidus transgene. J. Neuroendocrinol. 14, 629-637
    • (2002) J. Neuroendocrinol. , vol.14 , pp. 629-637
    • Davies, J.1    Murphy, D.2
  • 13
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A.M. (2001) Themes and variations on ubiquitylation. Nature Rev. Mol. Cell. Biol. 2, 169-178
    • (2001) Nature Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H. and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol. Rev. 82, 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 16
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings, C.J., Reinstein, E., Sun, Y.L., Antalffy, B., Jiang, Y.H., Ciechanover, A., Orr, H.T., Beaudet, A.L., and Zoghbi, H.Y. (1999) Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 24, 879-892
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.L.3    Antalffy, B.4    Jiang, Y.H.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 19
    • 0021679940 scopus 로고
    • The yeast ubiquitin gene: Head to tail repeats encoding a polyubiquitin precursor protein
    • Ozkaynak, E., Finley, D., and Varshavsky, A. (1984) The yeast ubiquitin gene: head to tail repeats encoding a polyubiquitin precursor protein. Nature 312, 663-666
    • (1984) Nature , vol.312 , pp. 663-666
    • Ozkaynak, E.1    Finley, D.2    Varshavsky, A.3
  • 20
    • 0023115331 scopus 로고
    • The dynamics of ubiquitin pools within cultured human lung fibroblasts
    • Haas, A.L. and Bright, P.M. (1987) The dynamics of ubiquitin pools within cultured human lung fibroblasts. J. Biol. Chem. 262, 345-351
    • (1987) J. Biol. Chem. , vol.262 , pp. 345-351
    • Haas, A.L.1    Bright, P.M.2
  • 21
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley, D., Ozkaynak, E., and Varshavsky, A. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48, 1035-1046
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozkaynak, E.2    Varshavsky, A.3
  • 22
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B., and Varshavsky, A. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338, 394-401
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 23
    • 0020804563 scopus 로고
    • Ubiquitin: Roles in protein modification and breakdown
    • Hershko, A. (1983) Ubiquitin: roles in protein modification and breakdown. Cell 34, 11-12
    • (1983) Cell , vol.34 , pp. 11-12
    • Hershko, A.1
  • 24
  • 25
    • 0034604520 scopus 로고    scopus 로고
    • Degradation of the Epstein-Barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway: Targeting via ubiquitination of the N-terminal residue
    • Aviel, S., Winberg, G., Massucci, M., and Ciechanover, A. (2000) Degradation of the Epstein-Barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway: Targeting via ubiquitination of the N-terminal residue. J. Biol. Chem. 275, 23491-23499
    • (2000) J. Biol. Chem. , vol.275 , pp. 23491-23499
    • Aviel, S.1    Winberg, G.2    Massucci, M.3    Ciechanover, A.4
  • 26
  • 28
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M.H., Rubin, D.M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V.A., and Finley, D. (1998) A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94, 615-623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 29
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C., Ota, I.M., and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 30
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H.D., Mayer, T.U., and Jentsch, S. (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 31
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger: A common domain in ubiquitination
    • Aravind, L. and Koonin, E.V. (2000) The U box is a modified RING finger: a common domain in ubiquitination. Curr. Biol. 10, R132-R134
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 33
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A.L., and Finley, D. (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 34
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason, T. and Ellison, M.J. (1994) Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14, 7876-7883
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 35
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk, H.A. and Yaffe, M.P. (1999) A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145, 1199-1208
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 36
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease
    • Soetens, O., De Craene, J.O., and Andre, B. (2001) Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276, 43949-43957
    • (2001) Gap1. J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    De Craene, J.O.2    Andre, B.3
  • 37
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence, J., Gali, R.R., Dittmar, G., Sherman, F., Karin, M., and Finley, D. (2000) Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102, 67-76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 38
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C.M., and Chen, Z.J. (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.M.8    Chen, Z.J.9
  • 39
  • 40
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang, J., Ballinger, C.A., Wu, Y., Dai, Q., Cyr, D.M., Hohfeld, J., and Patterson, C. (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 44
    • 0036472341 scopus 로고    scopus 로고
    • The human homologue of the yeast polyubiquitination factor Ufd2p is cleaved by caspase 6 and granzyme B during apoptosis
    • Mahoney, J.A., Odin, J.A., White, S.M., Shaffer, D., Koff, A., Casciola-Rosen, L., and Rosen, A. (2002) The human homologue of the yeast polyubiquitination factor Ufd2p is cleaved by caspase 6 and granzyme B during apoptosis. Biochem. J. 361, 587-595
    • (2002) Biochem. J. , vol.361 , pp. 587-595
    • Mahoney, J.A.1    Odin, J.A.2    White, S.M.3    Shaffer, D.4    Koff, A.5    Casciola-Rosen, L.6    Rosen, A.7
  • 46
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y.H., Meyer, H.H., and Rapoport, T.A. (2001) The AAA ATPase Cdc48/ p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.H.1    Meyer, H.H.2    Rapoport, T.A.3
  • 47
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002) Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 49
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell, P., Ballinger, C.A., J., J., Wu, Y., Thompson, L.J., Hohfeld, J., and Patterson, C. (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nature Cell Biol. 3, 93-96
    • (2001) Nature Cell Biol. , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Wu, Y.3    Thompson, L.J.4    Hohfeld, J.5    Patterson, C.6
  • 50
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G.C., Patterson, C., Zhang, W., Younger, J.M., and Cyr, D.M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nature Cell Biol. 3, 100-105
    • (2001) Nature Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 51
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T., and Tanaka, K. (2001) CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO rep. 2, 1133-1138
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 52
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K., and Takahashi, R. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10, 55-67
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.6    Takahashi, R.7
  • 53
    • 0035375052 scopus 로고    scopus 로고
    • Interaction of the RING finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes
    • Pringa, E., Martinez-Noel, G., Muller, U., and Harbers, K. (2001) Interaction of the RING finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. J. Biol. Chem. 276, 19617-19623
    • (2001) J. Biol. Chem. , vol.276 , pp. 19617-19623
    • Pringa, E.1    Martinez-Noel, G.2    Muller, U.3    Harbers, K.4
  • 54
    • 0030020702 scopus 로고    scopus 로고
    • Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c
    • Wang, B.B., Hayenga, K.J., Payan, D.G., and Fisher, J.M. (1996) Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c. Biochem. J. 314, 313-319
    • (1996) Biochem. J. , vol.314 , pp. 313-319
    • Wang, B.B.1    Hayenga, K.J.2    Payan, D.G.3    Fisher, J.M.4
  • 55
    • 0026663165 scopus 로고
    • PRP38 encodes a yeast protein required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels
    • Blanton, S., Srinivasan, A., and Rymond, B.C. (1992) PRP38 encodes a yeast protein required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels. Mol. Cell. Biol. 12, 3939-3947
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3939-3947
    • Blanton, S.1    Srinivasan, A.2    Rymond, B.C.3
  • 57
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays, N.W., Gardner, R.G., Seelig, L.P., Joazeiro, C.A., and Hampton, R.Y. (2001) Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nature Cell Biol. 3, 24-29
    • (2001) Nature Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 58
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang, S.Y., Ferrone, M., Yang, C.H., Jensen, J.P., Tiwari, S., and Weissman, A.M. (2001) The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 98, 14422-14427
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.Y.1    Ferrone, M.2    Yang, C.H.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.