메뉴 건너뛰기




Volumn 41, Issue 4, 2011, Pages 926-935

PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo

Author keywords

Antigen processing; CD8+ T cell; Immunoproteasome; MHC class I; PA28

Indexed keywords

CELL PROTEIN; GAMMA INTERFERON; LARGE MULTIFUNCTIONAL PEPTIDASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDASE; PROTEASOME; PROTEIN MECL 1; PROTEIN PA28; UNCLASSIFIED DRUG;

EID: 79953035505     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201041040     Document Type: Article
Times cited : (51)

References (48)
  • 1
    • 34250167524 scopus 로고    scopus 로고
    • Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes
    • Deol, P., Zaiss, D. M., Monaco, J. J. and Sijts, A. J., Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes. J. Immunol. 2007. 178: 7557-7562.
    • (2007) J. Immunol. , vol.178 , pp. 7557-7562
    • Deol, P.1    Zaiss, D.M.2    Monaco, J.J.3    Sijts, A.J.4
  • 3
    • 0031568653 scopus 로고    scopus 로고
    • MHC affinity, peptide liberation, T cell repertoire, and immunodominance all contribute to the paucity of MHC class I-restricted peptides recognized by antiviral CTL
    • Deng, Y., Yewdell, J. W., Eisenlohr, L. C. and Bennink, J. R., MHC affinity, peptide liberation, T cell repertoire, and immunodominance all contribute to the paucity of MHC class I-restricted peptides recognized by antiviral CTL. J. Immunol. 1997. 158: 1507-1515.
    • (1997) J. Immunol. , vol.158 , pp. 1507-1515
    • Deng, Y.1    Yewdell, J.W.2    Eisenlohr, L.C.3    Bennink, J.R.4
  • 4
    • 0035806246 scopus 로고    scopus 로고
    • Immunoproteasomes shape immunodominance hierarchies of antiviral CD8(+) T cells at the levels of T cell repertoire and presentation of viral antigens
    • Chen, W., Norbury, C. C., Cho, Y., Yewdell, J. W. and Bennink, J. R., Immunoproteasomes shape immunodominance hierarchies of antiviral CD8(+) T cells at the levels of T cell repertoire and presentation of viral antigens. J. Exp. Med. 2001. 193: 1319-1326.
    • (2001) J. Exp. Med. , vol.193 , pp. 1319-1326
    • Chen, W.1    Norbury, C.C.2    Cho, Y.3    Yewdell, J.W.4    Bennink, J.R.5
  • 5
    • 0034193031 scopus 로고    scopus 로고
    • MHC class I antigen processing of an adenovirus CTL epitope is linked to the levels of immunoproteasomes in infected cells
    • Sijts, A. J., Standera, S., Toes, R. E., Ruppert, T., Beekman, N. J., van Veelen, P. A., Ossendorp, F. A. et al., MHC class I antigen processing of an adenovirus CTL epitope is linked to the levels of immunoproteasomes in infected cells. J. Immunol. 2000. 164: 4500-4506.
    • (2000) J. Immunol. , vol.164 , pp. 4500-4506
    • Sijts, A.J.1    Standera, S.2    Toes, R.E.3    Ruppert, T.4    Beekman, N.J.5    van Veelen, P.A.6    Ossendorp, F.A.7
  • 6
    • 0034698738 scopus 로고    scopus 로고
    • Differential influence on cytotoxic T lymphocyte epitope presentation by controlled expression of either proteasome immunosubunits or PA28
    • van Hall, T., Sijts, A., Camps, M., Offringa, R., Melief, C., Kloetzel, P. M. and Ossendorp, F., Differential influence on cytotoxic T lymphocyte epitope presentation by controlled expression of either proteasome immunosubunits or PA28. J. Exp. Med. 2000. 192: 483-494.
    • (2000) J. Exp. Med. , vol.192 , pp. 483-494
    • van Hall, T.1    Sijts, A.2    Camps, M.3    Offringa, R.4    Melief, C.5    Kloetzel, P.M.6    Ossendorp, F.7
  • 7
    • 0034662001 scopus 로고    scopus 로고
    • Overexpression of the proteasome subunits LMP2, LMP7, and MECL-1, but not PA28 alpha/beta, enhances the presentation of an immunodominant lymphocytic choriomeningitis virus T cell epitope
    • Schwarz, K., van Den Broek, M., Kostka, S., Kraft, R., Soza, A., Schmidtke, G., Kloetzel, P. M. and Groettrup, M., Overexpression of the proteasome subunits LMP2, LMP7, and MECL-1, but not PA28 alpha/beta, enhances the presentation of an immunodominant lymphocytic choriomeningitis virus T cell epitope. J. Immunol. 2000. 165: 768-778.
    • (2000) J. Immunol. , vol.165 , pp. 768-778
    • Schwarz, K.1    van Den Broek, M.2    Kostka, S.3    Kraft, R.4    Soza, A.5    Schmidtke, G.6    Kloetzel, P.M.7    Groettrup, M.8
  • 8
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. and Goldberg, A. L., Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 1996. 65: 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 10
    • 0035883047 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface
    • Hallermalm, K., Seki, K., Wei, C., Castelli, C., Rivoltini, L., Kiessling, R. and Levitskaya, J., Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface. Blood 2001. 98: 1108-1115.
    • (2001) Blood , vol.98 , pp. 1108-1115
    • Hallermalm, K.1    Seki, K.2    Wei, C.3    Castelli, C.4    Rivoltini, L.5    Kiessling, R.6    Levitskaya, J.7
  • 11
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit
    • Nandi, D., Jiang, H. and Monaco, J. J., Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit. J. Immunol. 1996. 156: 2361-2364.
    • (1996) J. Immunol. , vol.156 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 12
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes, B., Hengel, H., Ruppert, T., Multhaup, G., Koszinowski, U. H. and Kloetzel, P. M., Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 1994. 179: 901-909.
    • (1994) J. Exp. Med. , vol.179 , pp. 901-909
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Kloetzel, P.M.6
  • 13
    • 0027983803 scopus 로고
    • Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease
    • Realini, C., Dubiel, W., Pratt, G., Ferrell, K. and Rechsteiner, M., Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease. J. Biol. Chem. 1994. 269: 20727-20732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20727-20732
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferrell, K.4    Rechsteiner, M.5
  • 14
    • 20444399554 scopus 로고    scopus 로고
    • Differential expression regulation of the alpha and beta subunits of the PA28 proteasome activator in mature dendritic cells
    • Ossendorp, F., Fu, N., Camps, M., Granucci, F., Gobin, S. J., van den Elsen, P. J., Schuurhuis, D. et al., Differential expression regulation of the alpha and beta subunits of the PA28 proteasome activator in mature dendritic cells. J. Immunol. 2005. 174: 7815-7822.
    • (2005) J. Immunol. , vol.174 , pp. 7815-7822
    • Ossendorp, F.1    Fu, N.2    Camps, M.3    Granucci, F.4    Gobin, S.J.5    van den Elsen, P.J.6    Schuurhuis, D.7
  • 15
    • 0030840661 scopus 로고    scopus 로고
    • Expression and subcellular localization of mouse 20S proteasome activator complex PA28
    • Soza, A., Knuehl, C., Groettrup, M., Henklein, P., Tanaka, K. and Kloetzel, P. M., Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett. 1997. 413: 27-34.
    • (1997) FEBS Lett. , vol.413 , pp. 27-34
    • Soza, A.1    Knuehl, C.2    Groettrup, M.3    Henklein, P.4    Tanaka, K.5    Kloetzel, P.M.6
  • 16
    • 0032730872 scopus 로고    scopus 로고
    • Dendritic cells up-regulate immunoproteasomes and the proteasome regulator PA28 during maturation
    • Macagno, A., Gilliet, M., Sallusto, F., Lanzavecchia, A., Nestle, F. O. and Groettrup, M., Dendritic cells up-regulate immunoproteasomes and the proteasome regulator PA28 during maturation. Eur. J. Immunol. 1999. 29: 4037-4042.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 4037-4042
    • Macagno, A.1    Gilliet, M.2    Sallusto, F.3    Lanzavecchia, A.4    Nestle, F.O.5    Groettrup, M.6
  • 19
    • 0035756029 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in MHC class I antigen processing: implications for vaccine design
    • Sijts, A., Zaiss, D. and Kloetzel, P. M., The role of the ubiquitin-proteasome pathway in MHC class I antigen processing: implications for vaccine design. Curr. Mol. Med. 2001. 1: 665-676.
    • (2001) Curr. Mol. Med. , vol.1 , pp. 665-676
    • Sijts, A.1    Zaiss, D.2    Kloetzel, P.M.3
  • 20
    • 23244457800 scopus 로고    scopus 로고
    • Immunoproteasome-deficient mice mount largely normal CD8+ T cell responses to lymphocytic choriomeningitis virus infection and DNA vaccination
    • Nussbaum, A. K., Rodriguez-Carreno, M. P., Benning, N., Botten, J. and Whitton, J. L., Immunoproteasome-deficient mice mount largely normal CD8+ T cell responses to lymphocytic choriomeningitis virus infection and DNA vaccination. J. Immunol. 2005. 175: 1153-1160.
    • (2005) J. Immunol. , vol.175 , pp. 1153-1160
    • Nussbaum, A.K.1    Rodriguez-Carreno, M.P.2    Benning, N.3    Botten, J.4    Whitton, J.L.5
  • 21
    • 77955596988 scopus 로고    scopus 로고
    • Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress
    • Seifert, U., Bialy, L. P., Ebstein, F., Bech-Otschir, D., Voigt, A., Schroter, F., Prozorovski, T. et al., Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress. Cell 2010. 142: 613-624.
    • (2010) Cell , vol.142 , pp. 613-624
    • Seifert, U.1    Bialy, L.P.2    Ebstein, F.3    Bech-Otschir, D.4    Voigt, A.5    Schroter, F.6    Prozorovski, T.7
  • 22
    • 0033608969 scopus 로고    scopus 로고
    • Proteasome activator 11S REG or PA28: Recombinant REG alpha/REG beta hetero-oligomers are heptamers
    • Zhang, Z., Krutchinsky, A., Endicott, S., Realini, C., Rechsteiner, M. and Standing, K. G., Proteasome activator 11S REG or PA28: Recombinant REG alpha/REG beta hetero-oligomers are heptamers. Biochemistry 1999. 38: 5651-5658.
    • (1999) Biochemistry , vol.38 , pp. 5651-5658
    • Zhang, Z.1    Krutchinsky, A.2    Endicott, S.3    Realini, C.4    Rechsteiner, M.5    Standing, K.G.6
  • 23
    • 0030602834 scopus 로고    scopus 로고
    • Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands
    • Dick, T. P., Ruppert, T., Groettrup, M., Kloetzel, P. M., Kuehn, L., Koszinowski, U. H., Stevanovic, S. et al., Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell 1996. 86: 253-262.
    • (1996) Cell , vol.86 , pp. 253-262
    • Dick, T.P.1    Ruppert, T.2    Groettrup, M.3    Kloetzel, P.M.4    Kuehn, L.5    Koszinowski, U.H.6    Stevanovic, S.7
  • 25
    • 17944369433 scopus 로고    scopus 로고
    • Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta
    • Murata, S., Udono, H., Tanahashi, N., Hamada, N., Watanabe, K., Adachi, K., Yamano, T. et al., Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta. EMBO J. 2001. 20: 5898-5907.
    • (2001) EMBO J. , vol.20 , pp. 5898-5907
    • Murata, S.1    Udono, H.2    Tanahashi, N.3    Hamada, N.4    Watanabe, K.5    Adachi, K.6    Yamano, T.7
  • 27
    • 0037099735 scopus 로고    scopus 로고
    • Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing
    • Yamano, T., Murata, S., Shimbara, N., Tanaka, N., Chiba, T., Tanaka, K., Yui, K. and Udono, H., Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing. J. Exp. Med. 2002. 196: 185-196.
    • (2002) J. Exp. Med. , vol.196 , pp. 185-196
    • Yamano, T.1    Murata, S.2    Shimbara, N.3    Tanaka, N.4    Chiba, T.5    Tanaka, K.6    Yui, K.7    Udono, H.8
  • 28
    • 33645091895 scopus 로고    scopus 로고
    • Proteasomes and antigen presentation: evidence that a KEKE motif does not promote presentation of the class I epitope SIINFEKL
    • Gonciarz-Swiatek, M. and Rechsteiner, M., Proteasomes and antigen presentation: evidence that a KEKE motif does not promote presentation of the class I epitope SIINFEKL. Mol. Immunol. 2006. 43: 1993-2001.
    • (2006) Mol. Immunol. , vol.43 , pp. 1993-2001
    • Gonciarz-Swiatek, M.1    Rechsteiner, M.2
  • 29
    • 33646053214 scopus 로고    scopus 로고
    • T cells lacking immunoproteasome subunits MECL-1 and LMP7 hyperproliferate in response to polyclonal mitogens
    • Caudill, C. M., Jayarapu, K., Elenich, L., Monaco, J. J., Colbert, R. A. and Griffin, T. A., T cells lacking immunoproteasome subunits MECL-1 and LMP7 hyperproliferate in response to polyclonal mitogens. J. Immunol. 2006. 176: 4075-4082.
    • (2006) J. Immunol. , vol.176 , pp. 4075-4082
    • Caudill, C.M.1    Jayarapu, K.2    Elenich, L.3    Monaco, J.J.4    Colbert, R.A.5    Griffin, T.A.6
  • 30
    • 0037093234 scopus 로고    scopus 로고
    • Expression of the proteasome activator PA28 rescues the presentation of a cytotoxic T lymphocyte epitope on melanoma cells
    • Sun, Y., Sijts, A. J., Song, M., Janek, K., Nussbaum, A. K., Kral, S., Schirle, M. et al., Expression of the proteasome activator PA28 rescues the presentation of a cytotoxic T lymphocyte epitope on melanoma cells. Cancer Res. 2002. 62: 2875-2882.
    • (2002) Cancer Res. , vol.62 , pp. 2875-2882
    • Sun, Y.1    Sijts, A.J.2    Song, M.3    Janek, K.4    Nussbaum, A.K.5    Kral, S.6    Schirle, M.7
  • 31
    • 0036105112 scopus 로고    scopus 로고
    • The effect of the interferon-gamma-inducible processing machinery on the generation of a naturally tumor-associated human cytotoxic T lymphocyte epitope within a wild-type and mutant p53 sequence context
    • Kuckelkorn, U., Ferreira, E. A., Drung, I., Liewer, U., Kloetzel, P. M. and Theobald, M., The effect of the interferon-gamma-inducible processing machinery on the generation of a naturally tumor-associated human cytotoxic T lymphocyte epitope within a wild-type and mutant p53 sequence context. Eur. J. Immunol. 2002. 32: 1368-1375.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1368-1375
    • Kuckelkorn, U.1    Ferreira, E.A.2    Drung, I.3    Liewer, U.4    Kloetzel, P.M.5    Theobald, M.6
  • 32
    • 0034614889 scopus 로고    scopus 로고
    • Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes
    • Sijts, A. J., Ruppert, T., Rehermann, B., Schmidt, M., Koszinowski, U. and Kloetzel, P. M., Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes. J. Exp. Med. 2000. 191: 503-514.
    • (2000) J. Exp. Med. , vol.191 , pp. 503-514
    • Sijts, A.J.1    Ruppert, T.2    Rehermann, B.3    Schmidt, M.4    Koszinowski, U.5    Kloetzel, P.M.6
  • 33
    • 0035796461 scopus 로고    scopus 로고
    • Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products
    • Toes, R. E., Nussbaum, A. K., Degermann, S., Schirle, M., Emmerich, N. P., Kraft, M., Laplace, C. et al., Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products. J. Exp. Med. 2001. 194: 1-12.
    • (2001) J. Exp. Med. , vol.194 , pp. 1-12
    • Toes, R.E.1    Nussbaum, A.K.2    Degermann, S.3    Schirle, M.4    Emmerich, N.P.5    Kraft, M.6    Laplace, C.7
  • 35
    • 40749155440 scopus 로고    scopus 로고
    • The proteasome immunosubunit multicatalytic endopeptidase complex-like 1 is a T-cell-intrinsic factor influencing homeostatic expansion
    • Zaiss, D. M., de Graaf, N. and Sijts, A. J., The proteasome immunosubunit multicatalytic endopeptidase complex-like 1 is a T-cell-intrinsic factor influencing homeostatic expansion. Infect. Immun. 2008. 76: 1207-1213.
    • (2008) Infect. Immun. , vol.76 , pp. 1207-1213
    • Zaiss, D.M.1    de Graaf, N.2    Sijts, A.J.3
  • 39
    • 0035892754 scopus 로고    scopus 로고
    • Immunoproteasomes largely replace constitutive proteasomes during an antiviral and antibacterial immune response in the liver
    • Khan, S., van den Broek, M., Schwarz, K., de Giuli, R., Diener, P. A. and Groettrup, M., Immunoproteasomes largely replace constitutive proteasomes during an antiviral and antibacterial immune response in the liver. J. Immunol. 2001. 167: 6859-6868.
    • (2001) J. Immunol. , vol.167 , pp. 6859-6868
    • Khan, S.1    van den Broek, M.2    Schwarz, K.3    de Giuli, R.4    Diener, P.A.5    Groettrup, M.6
  • 41
    • 4644249095 scopus 로고    scopus 로고
    • Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus
    • Basler, M., Youhnovski, N., Van Den Broek, M., Przybylski, M. and Groettrup, M., Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus. J. Immunol. 2004. 173: 3925-3934.
    • (2004) J. Immunol. , vol.173 , pp. 3925-3934
    • Basler, M.1    Youhnovski, N.2    Van Den Broek, M.3    Przybylski, M.4    Groettrup, M.5
  • 42
    • 0037083612 scopus 로고    scopus 로고
    • Cutting edge: CD4 and CD8 T cells are intrinsically different in their proliferative responses
    • Foulds, K. E., Zenewicz, L. A., Shedlock, D. J., Jiang, J., Troy, A. E. and Shen, H., Cutting edge: CD4 and CD8 T cells are intrinsically different in their proliferative responses. J. Immunol. 2002. 168: 1528-1532.
    • (2002) J. Immunol. , vol.168 , pp. 1528-1532
    • Foulds, K.E.1    Zenewicz, L.A.2    Shedlock, D.J.3    Jiang, J.4    Troy, A.E.5    Shen, H.6
  • 44
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • Griffin, T. A., Nandi, D., Cruz, M., Fehling, H. J., Kaer, L. V., Monaco, J. J. and Colbert, R. A., Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J. Exp. Med. 1998. 187: 97-104.
    • (1998) J. Exp. Med. , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Kaer, L.V.5    Monaco, J.J.6    Colbert, R.A.7
  • 45
    • 0030852963 scopus 로고    scopus 로고
    • Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system
    • Niedermann, G., Grimm, R., Geier, E., Maurer, M., Realini, C., Gartmann, C., Soll, J. et al., Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system. J. Exp. Med. 1997. 186: 209-220.
    • (1997) J. Exp. Med. , vol.186 , pp. 209-220
    • Niedermann, G.1    Grimm, R.2    Geier, E.3    Maurer, M.4    Realini, C.5    Gartmann, C.6    Soll, J.7
  • 46
    • 33646575879 scopus 로고    scopus 로고
    • Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway
    • Kunisawa, J. and Shastri, N., Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. Immunity 2006. 24: 523-534.
    • (2006) Immunity , vol.24 , pp. 523-534
    • Kunisawa, J.1    Shastri, N.2
  • 47
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava, P. K., Udono, H., Blachere, N. E. and Li, Z., Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 1994. 39: 93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 48
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering, A. M., Koop, A. L., Teoh, C. Y., Ermak, G., Grune, T. and Davies, K. J. A., The immunoproteasome, the 20S proteasome and PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem. J. 2010. 432: 585-594.
    • (2010) Biochem. J. , vol.432 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.