메뉴 건너뛰기




Volumn 591, Issue , 2016, Pages 132-140

Mammalian proteasome subtypes: Their diversity in structure and function

Author keywords

Posttranslational modification; Proteasome; Subpopulation; Subtype; Subunit iso proteoform

Indexed keywords

CELL PROTEIN; PROTEASOME; PROTEINASE;

EID: 84953286231     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2015.12.012     Document Type: Review
Times cited : (71)

References (131)
  • 1
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka, and A.L. Goldberg Structure and functions of the 20S and 26S proteasomes Annu. Rev. Biochem. 65 1996 801 847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 2
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • D.H. Wolf, and W. Hilt The proteasome: a proteolytic nanomachine of cell regulation and waste disposal Biochim. Biophys. Acta 1695 2004 19 31
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 3
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • M. Groll, and R. Huber Substrate access and processing by the 20S proteasome core particle Int. J. Biochem. Cell Biol. 35 2003 606 616
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 8
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 9
    • 33644515991 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From an idea to the patient bed
    • A. Ciechanover The ubiquitin proteolytic system: from an idea to the patient bed Proc. Am. Thorac. Soc. 3 2006 21 31
    • (2006) Proc. Am. Thorac. Soc. , vol.3 , pp. 21-31
    • Ciechanover, A.1
  • 10
    • 84896032345 scopus 로고    scopus 로고
    • Paradigms of protein degradation by the proteasome
    • T. Inobe, and A. Matouschek Paradigms of protein degradation by the proteasome Curr. Opin. Struct. Biol. 24 2014 156 164
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 156-164
    • Inobe, T.1    Matouschek, A.2
  • 12
    • 84922220547 scopus 로고    scopus 로고
    • PA28alphabeta: The enigmatic magic ring of the proteasome?
    • P. Cascio PA28alphabeta: the enigmatic magic ring of the proteasome? Biomolecules 4 2014 566 584
    • (2014) Biomolecules , vol.4 , pp. 566-584
    • Cascio, P.1
  • 13
    • 79955751471 scopus 로고    scopus 로고
    • Proteasome activator 200: The heat is on
    • R110 006890
    • A.F. Savulescu, and M.H. Glickman Proteasome activator 200: the heat is on Mol. Cell. Proteom. 10 2011 R110 006890
    • (2011) Mol. Cell. Proteom. , vol.10
    • Savulescu, A.F.1    Glickman, M.H.2
  • 14
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • N. Tanahashi, Y. Murakami, Y. Minami, N. Shimbara, K.B. Hendil, and K. Tanaka Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis J. Biol. Chem. 275 2000 14336 14345
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 15
    • 84874620572 scopus 로고    scopus 로고
    • Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics
    • B. Fabre, T. Lambour, J. Delobel, F. Amalric, B. Monsarrat, O. Burlet-Schiltz, and M.P. Bousquet-Dubouch Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics Mol. Cell. Proteom. 12 2013 687 699
    • (2013) Mol. Cell. Proteom. , vol.12 , pp. 687-699
    • Fabre, B.1    Lambour, T.2    Delobel, J.3    Amalric, F.4    Monsarrat, B.5    Burlet-Schiltz, O.6    Bousquet-Dubouch, M.P.7
  • 17
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • M. Rechsteiner, and C.P. Hill Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors Trends Cell Biol. 15 2005 27 33
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 18
    • 0025886546 scopus 로고
    • Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes
    • M.G. Brown, J. Driscoll, and J.J. Monaco Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes Nature 353 1991 355 357
    • (1991) Nature , vol.353 , pp. 355-357
    • Brown, M.G.1    Driscoll, J.2    Monaco, J.J.3
  • 19
    • 0026728649 scopus 로고
    • Proteasomes are regulated by interferon gamma: Implications for antigen processing
    • Y. Yang, J.B. Waters, K. Fruh, and P.A. Peterson Proteasomes are regulated by interferon gamma: implications for antigen processing Proc. Natl. Acad. Sci. U. S. A. 89 1992 4928 4932
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4928-4932
    • Yang, Y.1    Waters, J.B.2    Fruh, K.3    Peterson, P.A.4
  • 20
    • 0027281826 scopus 로고
    • MHC-linked low-molecular mass polypeptide subunits define distinct subsets of proteasomes. Implications for divergent function among distinct proteasome subsets
    • M.G. Brown, J. Driscoll, and J.J. Monaco MHC-linked low-molecular mass polypeptide subunits define distinct subsets of proteasomes. Implications for divergent function among distinct proteasome subsets J. Immunol. 151 1993 1193 1204
    • (1993) J. Immunol. , vol.151 , pp. 1193-1204
    • Brown, M.G.1    Driscoll, J.2    Monaco, J.J.3
  • 21
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • J. Driscoll, M.G. Brown, D. Finley, and J.J. Monaco MHC-linked LMP gene products specifically alter peptidase activities of the proteasome Nature 365 1993 262 264
    • (1993) Nature , vol.365 , pp. 262-264
    • Driscoll, J.1    Brown, M.G.2    Finley, D.3    Monaco, J.J.4
  • 22
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • M. Gaczynska, K.L. Rock, and A.L. Goldberg Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes Nature 365 1993 264 267
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 23
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • B. Boes, H. Hengel, T. Ruppert, G. Multhaup, U.H. Koszinowski, and P.M. Kloetzel Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes J. Exp. Med. 179 1994 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
  • 25
    • 0034634389 scopus 로고    scopus 로고
    • Different proteasome subtypes in a single tissue exhibit different enzymatic properties
    • B. Dahlmann, T. Ruppert, L. Kuehn, S. Merforth, and P.M. Kloetzel Different proteasome subtypes in a single tissue exhibit different enzymatic properties J. Mol. Biol. 303 2000 643 653
    • (2000) J. Mol. Biol. , vol.303 , pp. 643-653
    • Dahlmann, B.1    Ruppert, T.2    Kuehn, L.3    Merforth, S.4    Kloetzel, P.M.5
  • 26
    • 72949105782 scopus 로고    scopus 로고
    • Multiple cardiac proteasome subtypes differ in their susceptibility to proteasome inhibitors
    • A. Kloss, S. Meiners, A. Ludwig, and B. Dahlmann Multiple cardiac proteasome subtypes differ in their susceptibility to proteasome inhibitors Cardiovasc. Res. 85 2009 367 375
    • (2009) Cardiovasc. Res. , vol.85 , pp. 367-375
    • Kloss, A.1    Meiners, S.2    Ludwig, A.3    Dahlmann, B.4
  • 29
    • 77957970501 scopus 로고    scopus 로고
    • The proteasome antechamber maintains substrates in an unfolded state
    • A.M. Ruschak, T.L. Religa, S. Breuer, S. Witt, and L.E. Kay The proteasome antechamber maintains substrates in an unfolded state Nature 467 2010 868 871
    • (2010) Nature , vol.467 , pp. 868-871
    • Ruschak, A.M.1    Religa, T.L.2    Breuer, S.3    Witt, S.4    Kay, L.E.5
  • 30
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • D.M. Smith, S.C. Chang, S. Park, D. Finley, Y. Cheng, and A.L. Goldberg Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry Mol. Cell. 27 2007 731 744
    • (2007) Mol. Cell. , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 32
    • 0031819536 scopus 로고    scopus 로고
    • The MHC class I ligand-generating system: Roles of immunoproteasomes and the interferon-gamma-inducible proteasome activator PA28
    • K. Tanaka, and M. Kasahara The MHC class I ligand-generating system: roles of immunoproteasomes and the interferon-gamma-inducible proteasome activator PA28 Immunol. Rev. 163 1998 161 176
    • (1998) Immunol. Rev. , vol.163 , pp. 161-176
    • Tanaka, K.1    Kasahara, M.2
  • 33
    • 79958772781 scopus 로고    scopus 로고
    • The role of the proteasome in the generation of MHC class I ligands and immune responses
    • E.J. Sijts, and P.M. Kloetzel The role of the proteasome in the generation of MHC class I ligands and immune responses Cell. Mol. Life Sci. 68 2011 1491 1502
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1491-1502
    • Sijts, E.J.1    Kloetzel, P.M.2
  • 34
    • 0030613816 scopus 로고    scopus 로고
    • Reactions of [14C]-3,4-dichloroisocoumarin with subunits of pituitary and spleen multicatalytic proteinase complexes (proteasomes)
    • M. Orlowski, C. Cardozo, A.M. Eleuteri, R. Kohanski, C.M. Kam, and J.C. Powers Reactions of [14C]-3,4-dichloroisocoumarin with subunits of pituitary and spleen multicatalytic proteinase complexes (proteasomes) Biochemistry 36 1997 13946 13953
    • (1997) Biochemistry , vol.36 , pp. 13946-13953
    • Orlowski, M.1    Cardozo, C.2    Eleuteri, A.M.3    Kohanski, R.4    Kam, C.M.5    Powers, J.C.6
  • 35
    • 0034254726 scopus 로고    scopus 로고
    • How Stat1 mediates constitutive gene expression: A complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene
    • M. Chatterjee-Kishore, K.L. Wright, J.P. Ting, and G.R. Stark How Stat1 mediates constitutive gene expression: a complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene EMBO J. 19 2000 4111 4122
    • (2000) EMBO J. , vol.19 , pp. 4111-4122
    • Chatterjee-Kishore, M.1    Wright, K.L.2    Ting, J.P.3    Stark, G.R.4
  • 36
    • 84944788684 scopus 로고    scopus 로고
    • Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes
    • J. Liepe, H.G. Holzhutter, E. Bellavista, P.M. Kloetzel, M.P. Stumpf, and M. Mishto Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes Elife 4 2015 e07545
    • (2015) Elife , vol.4 , pp. e07545
    • Liepe, J.1    Holzhutter, H.G.2    Bellavista, E.3    Kloetzel, P.M.4    Stumpf, M.P.5    Mishto, M.6
  • 37
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • K.L. Rock, and A.L. Goldberg Degradation of cell proteins and the generation of MHC class I-presented peptides Annu. Rev. Immunol. 17 1999 739 779
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 38
    • 0035756029 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in MHC class I antigen processing: Implications for vaccine design
    • A. Sijts, D. Zaiss, and P.M. Kloetzel The role of the ubiquitin-proteasome pathway in MHC class I antigen processing: implications for vaccine design Curr. Mol. Med. 1 2001 665 676
    • (2001) Curr. Mol. Med. , vol.1 , pp. 665-676
    • Sijts, A.1    Zaiss, D.2    Kloetzel, P.M.3
  • 39
    • 0242468319 scopus 로고    scopus 로고
    • Bioinformatic analysis of functional differences between the immunoproteasome and the constitutive proteasome
    • C. Kesmir, V. van Noort, R.J. de Boer, and P. Hogeweg Bioinformatic analysis of functional differences between the immunoproteasome and the constitutive proteasome Immunogenetics 55 2003 437 449
    • (2003) Immunogenetics , vol.55 , pp. 437-449
    • Kesmir, C.1    Van Noort, V.2    De Boer, R.J.3    Hogeweg, P.4
  • 40
    • 0842277344 scopus 로고    scopus 로고
    • The components of the proteasome system and their role in MHC class I antigen processing
    • E. Krüger, U. Kuckelkorn, A. Sijts, and P. Kloetzel The components of the proteasome system and their role in MHC class I antigen processing Rev. Physiol. Biochem. Pharmacol. 148 2003 81 104
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.148 , pp. 81-104
    • Krüger, E.1    Kuckelkorn, U.2    Sijts, A.3    Kloetzel, P.4
  • 44
    • 33845399734 scopus 로고    scopus 로고
    • Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes
    • M.K. Callahan, E.A. Wohlfert, A. Menoret, and P.K. Srivastava Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes J. Immunol. 177 2006 8393 8399
    • (2006) J. Immunol. , vol.177 , pp. 8393-8399
    • Callahan, M.K.1    Wohlfert, E.A.2    Menoret, A.3    Srivastava, P.K.4
  • 45
    • 4544233720 scopus 로고    scopus 로고
    • Expression of proteasome subunits low molecular mass polypeptide (LMP) 2 and LMP7 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy
    • H.X. Wang, H.M. Wang, Q.L. Li, H.Y. Lin, D. Qian, and C. Zhu Expression of proteasome subunits low molecular mass polypeptide (LMP) 2 and LMP7 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy Biol. Reprod. 71 2004 1317 1324
    • (2004) Biol. Reprod. , vol.71 , pp. 1317-1324
    • Wang, H.X.1    Wang, H.M.2    Li, Q.L.3    Lin, H.Y.4    Qian, D.5    Zhu, C.6
  • 46
    • 31944432777 scopus 로고    scopus 로고
    • Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line
    • H.X. Wang, H.M. Wang, H.Y. Lin, Q. Yang, H. Zhang, B.K. Tsang, and C. Zhu Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line J. Cell. Physiol. 206 2006 616 623
    • (2006) J. Cell. Physiol. , vol.206 , pp. 616-623
    • Wang, H.X.1    Wang, H.M.2    Lin, H.Y.3    Yang, Q.4    Zhang, H.5    Tsang, B.K.6    Zhu, C.7
  • 47
    • 33644656207 scopus 로고    scopus 로고
    • LMP2 knock-out mice have reduced proteasome activities and increased levels of oxidatively damaged proteins
    • Q. Ding, S. Martin, E. Dimayuga, A.J. Bruce-Keller, and J.N. Keller LMP2 knock-out mice have reduced proteasome activities and increased levels of oxidatively damaged proteins Antioxid. Redox Signal 8 2006 130 135
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 130-135
    • Ding, Q.1    Martin, S.2    Dimayuga, E.3    Bruce-Keller, A.J.4    Keller, J.N.5
  • 51
    • 78649558302 scopus 로고    scopus 로고
    • Immunoproteasomes are essential for survival and expansion of T cells in virus-infected mice
    • J. Moebius, M. van den Broek, M. Groettrup, and M. Basler Immunoproteasomes are essential for survival and expansion of T cells in virus-infected mice Eur. J. Immunol. 40 2010 3439 3449
    • (2010) Eur. J. Immunol. , vol.40 , pp. 3439-3449
    • Moebius, J.1    Van Den Broek, M.2    Groettrup, M.3    Basler, M.4
  • 52
    • 84866986070 scopus 로고    scopus 로고
    • Proteasome protease mediated regulation of cytokine induction and inflammation
    • N. Qureshi, D.C. Morrison, and J. Reis Proteasome protease mediated regulation of cytokine induction and inflammation Biochim. Biophys. Acta 1823 2012 2087 2093
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 2087-2093
    • Qureshi, N.1    Morrison, D.C.2    Reis, J.3
  • 53
    • 84927511820 scopus 로고    scopus 로고
    • The immunoproteasome and viral infection: A complex regulator of inflammation
    • M.K. McCarthy, and J.B. Weinberg The immunoproteasome and viral infection: a complex regulator of inflammation Front. Microbiol. 6 2015 21
    • (2015) Front. Microbiol. , vol.6 , pp. 21
    • McCarthy, M.K.1    Weinberg, J.B.2
  • 54
    • 77954008149 scopus 로고    scopus 로고
    • Targeting the proteasome: Partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis
    • N. Schmidt, E. Gonzalez, A. Visekruna, A.A. Kuhl, C. Loddenkemper, H. Mollenkopf, S.H. Kaufmann, U. Steinhoff, and T. Joeris Targeting the proteasome: partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis Gut 59 2010 896 906
    • (2010) Gut , vol.59 , pp. 896-906
    • Schmidt, N.1    Gonzalez, E.2    Visekruna, A.3    Kuhl, A.A.4    Loddenkemper, C.5    Mollenkopf, H.6    Kaufmann, S.H.7    Steinhoff, U.8    Joeris, T.9
  • 56
    • 84879492973 scopus 로고    scopus 로고
    • Cytokine-induced oxidative stress in cardiac inflammation and heart failure-how the ubiquitin proteasome system targets this vicious cycle
    • A. Voigt, A. Rahnefeld, P.M. Kloetzel, and E. Kruger Cytokine-induced oxidative stress in cardiac inflammation and heart failure-how the ubiquitin proteasome system targets this vicious cycle Front. Physiol. 4 2013 42
    • (2013) Front. Physiol. , vol.4 , pp. 42
    • Voigt, A.1    Rahnefeld, A.2    Kloetzel, P.M.3    Kruger, E.4
  • 58
    • 21544475903 scopus 로고    scopus 로고
    • IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • S. Heink, D. Ludwig, P.M. Kloetzel, and E. Kruger IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response Proc. Natl. Acad. Sci. U. S. A. 102 2005 9241 9246
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Kruger, E.4
  • 59
    • 0028136465 scopus 로고
    • Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7
    • M. Gaczynska, K.L. Rock, T. Spies, and A.L. Goldberg Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7 Proc. Natl. Acad. Sci. U. S. A. 91 1994 9213 9217
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9213-9217
    • Gaczynska, M.1    Rock, K.L.2    Spies, T.3    Goldberg, A.L.4
  • 60
    • 0034604384 scopus 로고    scopus 로고
    • Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes
    • E. Witt, D. Zantopf, M. Schmidt, R. Kraft, P.M. Kloetzel, and E. Kruger Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes J. Mol. Biol. 301 2000 1 9
    • (2000) J. Mol. Biol. , vol.301 , pp. 1-9
    • Witt, E.1    Zantopf, D.2    Schmidt, M.3    Kraft, R.4    Kloetzel, P.M.5    Kruger, E.6
  • 63
    • 84920830622 scopus 로고    scopus 로고
    • Elucidating the catalytic subunit composition of distinct proteasome subtypes: A crosslinking approach employing bifunctional activity-based probes
    • K. Cornish Carmony, L.K. Sharma, D.M. Lee, J.E. Park, W. Lee, and K.B. Kim Elucidating the catalytic subunit composition of distinct proteasome subtypes: a crosslinking approach employing bifunctional activity-based probes Chembiochem 16 2015 284 292
    • (2015) Chembiochem , vol.16 , pp. 284-292
    • Cornish Carmony, K.1    Sharma, L.K.2    Lee, D.M.3    Park, J.E.4    Lee, W.5    Kim, K.B.6
  • 64
    • 52649181646 scopus 로고    scopus 로고
    • Automated online sequential isotope labeling for protein quantitation applied to proteasome tissue-specific diversity
    • R. Raijmakers, C.R. Berkers, A. de Jong, H. Ovaa, A.J. Heck, and S. Mohammed Automated online sequential isotope labeling for protein quantitation applied to proteasome tissue-specific diversity Mol. Cell. Proteom. 7 2008 1755 1762
    • (2008) Mol. Cell. Proteom. , vol.7 , pp. 1755-1762
    • Raijmakers, R.1    Berkers, C.R.2    De Jong, A.3    Ovaa, H.4    Heck, A.J.5    Mohammed, S.6
  • 65
    • 0030793290 scopus 로고    scopus 로고
    • The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome
    • M. Groettrup, S. Standera, R. Stohwasser, and P.M. Kloetzel The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome Proc. Natl. Acad. Sci. U. S. A. 94 1997 8970 8975
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8970-8975
    • Groettrup, M.1    Standera, S.2    Stohwasser, R.3    Kloetzel, P.M.4
  • 66
    • 0029940895 scopus 로고    scopus 로고
    • 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences
    • R. Stohwasser, U. Kuckelkorn, R. Kraft, S. Kostka, and P.M. Kloetzel 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences FEBS Lett. 383 1996 109 113
    • (1996) FEBS Lett. , vol.383 , pp. 109-113
    • Stohwasser, R.1    Kuckelkorn, U.2    Kraft, R.3    Kostka, S.4    Kloetzel, P.M.5
  • 67
    • 34250167524 scopus 로고    scopus 로고
    • Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes
    • P. Deol, D.M. Zaiss, J.J. Monaco, and A.J. Sijts Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes J. Immunol. 178 2007 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
  • 68
    • 84879663141 scopus 로고    scopus 로고
    • Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses
    • D. Zanker, J. Waithman, J.W. Yewdell, and W. Chen Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses J. Immunol. 191 2013 52 59
    • (2013) J. Immunol. , vol.191 , pp. 52-59
    • Zanker, D.1    Waithman, J.2    Yewdell, J.W.3    Chen, W.4
  • 69
    • 84857065362 scopus 로고    scopus 로고
    • Proteasome subtypes and the processing of tumor antigens: Increasing antigenic diversity
    • N. Vigneron, and B.J. Van den Eynde Proteasome subtypes and the processing of tumor antigens: increasing antigenic diversity Curr. Opin. Immunol. 24 2011 84 91
    • (2011) Curr. Opin. Immunol. , vol.24 , pp. 84-91
    • Vigneron, N.1    Van Den Eynde, B.J.2
  • 70
    • 34548566134 scopus 로고    scopus 로고
    • Intermediate-type 20 S proteasomes in HeLa cells: "asymmetric" subunit composition, diversity and adaptation
    • N. Klare, M. Seeger, K. Janek, P.R. Jungblut, and B. Dahlmann Intermediate-type 20 S proteasomes in HeLa cells: "asymmetric" subunit composition, diversity and adaptation J. Mol. Biol. 373 2007 1 10
    • (2007) J. Mol. Biol. , vol.373 , pp. 1-10
    • Klare, N.1    Seeger, M.2    Janek, K.3    Jungblut, P.R.4    Dahlmann, B.5
  • 71
    • 84899723316 scopus 로고    scopus 로고
    • Characterization of the testis-specific proteasome subunit alpha4s in mammals
    • H. Uechi, J. Hamazaki, and S. Murata Characterization of the testis-specific proteasome subunit alpha4s in mammals J. Biol. Chem. 289 2014 12365 12374
    • (2014) J. Biol. Chem. , vol.289 , pp. 12365-12374
    • Uechi, H.1    Hamazaki, J.2    Murata, S.3
  • 74
    • 44749085669 scopus 로고    scopus 로고
    • Thymoproteasome: Probable role in generating positively selecting peptides
    • S. Murata, Y. Takahama, and K. Tanaka Thymoproteasome: probable role in generating positively selecting peptides Curr. Opin. Immunol. 20 2008 192 196
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 192-196
    • Murata, S.1    Takahama, Y.2    Tanaka, K.3
  • 76
    • 84857313367 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity
    • E.M. Huber, M. Basler, R. Schwab, W. Heinemeyer, C.J. Kirk, M. Groettrup, and M. Groll Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity Cell 148 2012 727 738
    • (2012) Cell , vol.148 , pp. 727-738
    • Huber, E.M.1    Basler, M.2    Schwab, R.3    Heinemeyer, W.4    Kirk, C.J.5    Groettrup, M.6    Groll, M.7
  • 77
    • 84870294017 scopus 로고    scopus 로고
    • Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC-MS
    • V. Dechavanne, F. Vilbois, L. Glez, and B. Antonsson Purification and separation of the 20S immunoproteasome from the constitutive proteasome and identification of the subunits by LC-MS Protein Expr. Purif. 87 2013 100 110
    • (2013) Protein Expr. Purif. , vol.87 , pp. 100-110
    • Dechavanne, V.1    Vilbois, F.2    Glez, L.3    Antonsson, B.4
  • 78
  • 79
    • 33748344059 scopus 로고    scopus 로고
    • Comprehensive quantitative proteome analysis of 20S proteasome subtypes from rat liver by isotope coded affinity tag and 2-D gel-based approaches
    • F. Schmidt, B. Dahlmann, K. Janek, A. Kloss, M. Wacker, R. Ackermann, B. Thiede, and P.R. Jungblut Comprehensive quantitative proteome analysis of 20S proteasome subtypes from rat liver by isotope coded affinity tag and 2-D gel-based approaches Proteomics 6 2006 4622 4632
    • (2006) Proteomics , vol.6 , pp. 4622-4632
    • Schmidt, F.1    Dahlmann, B.2    Janek, K.3    Kloss, A.4    Wacker, M.5    Ackermann, R.6    Thiede, B.7    Jungblut, P.R.8
  • 83
    • 33750476672 scopus 로고    scopus 로고
    • Circulating proteasomes are functional and have a subtype pattern distinct from 20S proteasomes in major blood cells
    • A. Zoeger, M. Blau, K. Egerer, E. Feist, and B. Dahlmann Circulating proteasomes are functional and have a subtype pattern distinct from 20S proteasomes in major blood cells Clin. Chem. 52 2006 2079 2086
    • (2006) Clin. Chem. , vol.52 , pp. 2079-2086
    • Zoeger, A.1    Blau, M.2    Egerer, K.3    Feist, E.4    Dahlmann, B.5
  • 84
    • 34249811193 scopus 로고    scopus 로고
    • The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity
    • F. Gillardon, A. Kloss, M. Berg, M. Neumann, K. Mechtler, B. Hengerer, and B. Dahlmann The 20S proteasome isolated from Alzheimer's disease brain shows post-translational modifications but unchanged proteolytic activity J. Neurochem. 101 2007 1483 1490
    • (2007) J. Neurochem. , vol.101 , pp. 1483-1490
    • Gillardon, F.1    Kloss, A.2    Berg, M.3    Neumann, M.4    Mechtler, K.5    Hengerer, B.6    Dahlmann, B.7
  • 86
    • 84874625369 scopus 로고    scopus 로고
    • Proteoform: A single term describing protein complexity
    • L.M. Smith, and N.L. Kelleher Proteoform: a single term describing protein complexity Nat. Methods 10 2013 186 187
    • (2013) Nat. Methods , vol.10 , pp. 186-187
    • Smith, L.M.1    Kelleher, N.L.2
  • 87
    • 31544452256 scopus 로고    scopus 로고
    • Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency
    • S. Heink, B. Fricke, D. Ludwig, P.M. Kloetzel, and E. Kruger Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency Cancer Res. 66 2006 649 652
    • (2006) Cancer Res. , vol.66 , pp. 649-652
    • Heink, S.1    Fricke, B.2    Ludwig, D.3    Kloetzel, P.M.4    Kruger, E.5
  • 88
    • 84922248914 scopus 로고    scopus 로고
    • Genetics of proteasome diseases
    • A.V. Gomes Genetics of proteasome diseases Sci. Cairo 2013 2013 637629
    • (2013) Sci. Cairo , vol.2013 , pp. 637629
    • Gomes, A.V.1
  • 91
    • 84921548263 scopus 로고    scopus 로고
    • Proteasome-associated autoinflammatory syndromes: Advances in pathogeneses, clinical presentations, diagnosis, and management
    • A. McDermott, J. Jacks, M. Kessler, P.D. Emanuel, and L. Gao Proteasome-associated autoinflammatory syndromes: advances in pathogeneses, clinical presentations, diagnosis, and management Int. J. Dermatol 54 2015 121 129
    • (2015) Int. J. Dermatol , vol.54 , pp. 121-129
    • McDermott, A.1    Jacks, J.2    Kessler, M.3    Emanuel, P.D.4    Gao, L.5
  • 94
    • 34247522791 scopus 로고    scopus 로고
    • Exploring proteasome complexes by proteomic approaches
    • O. Drews, C. Zong, and P. Ping Exploring proteasome complexes by proteomic approaches Proteomics 7 2007 1047 1058
    • (2007) Proteomics , vol.7 , pp. 1047-1058
    • Drews, O.1    Zong, C.2    Ping, P.3
  • 95
    • 52049127000 scopus 로고    scopus 로고
    • Role of proteasomes in transcription and their regulation by covalent modifications
    • A.G. Mittenberg, T.N. Moiseeva, and N.A. Barlev Role of proteasomes in transcription and their regulation by covalent modifications Front. Biosci. 13 2008 7184 7192
    • (2008) Front. Biosci. , vol.13 , pp. 7184-7192
    • Mittenberg, A.G.1    Moiseeva, T.N.2    Barlev, N.A.3
  • 97
    • 57649146490 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes
    • C. Zong, G.W. Young, Y. Wang, H. Lu, N. Deng, O. Drews, and P. Ping Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes Proteomics 8 2008 5025 5037
    • (2008) Proteomics , vol.8 , pp. 5025-5037
    • Zong, C.1    Young, G.W.2    Wang, Y.3    Lu, H.4    Deng, N.5    Drews, O.6    Ping, P.7
  • 99
    • 80051736289 scopus 로고    scopus 로고
    • Proteomics to study the diversity and dynamics of proteasome complexes: From fundamentals to the clinic
    • M.P. Bousquet-Dubouch, B. Fabre, B. Monsarrat, and O. Burlet-Schiltz Proteomics to study the diversity and dynamics of proteasome complexes: from fundamentals to the clinic Expert Rev. Proteom. 8 2011 459 481
    • (2011) Expert Rev. Proteom. , vol.8 , pp. 459-481
    • Bousquet-Dubouch, M.P.1    Fabre, B.2    Monsarrat, B.3    Burlet-Schiltz, O.4
  • 101
    • 84899928291 scopus 로고    scopus 로고
    • Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond
    • Z. Cui, S.B. Scruggs, J.E. Gilda, P. Ping, and A.V. Gomes Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond J. Mol. Cell. Cardiol. 71 2014 32 42
    • (2014) J. Mol. Cell. Cardiol. , vol.71 , pp. 32-42
    • Cui, Z.1    Scruggs, S.B.2    Gilda, J.E.3    Ping, P.4    Gomes, A.V.5
  • 104
    • 84874055523 scopus 로고    scopus 로고
    • High resolution quantitative proteomics of HeLa cells protein species using stable isotope labeling with amino acids in cell culture(SILAC), two-dimensional gel electrophoresis(2DE) and nano-liquid chromatography coupled to an LTQ-OrbitrapMass spectrometer
    • B. Thiede, C.J. Koehler, M. Strozynski, A. Treumann, R. Stein, U. Zimny-Arndt, M. Schmid, and P.R. Jungblut High resolution quantitative proteomics of HeLa cells protein species using stable isotope labeling with amino acids in cell culture(SILAC), two-dimensional gel electrophoresis(2DE) and nano-liquid chromatography coupled to an LTQ-OrbitrapMass spectrometer Mol. Cell. Proteom. 12 2013 529 538
    • (2013) Mol. Cell. Proteom. , vol.12 , pp. 529-538
    • Thiede, B.1    Koehler, C.J.2    Strozynski, M.3    Treumann, A.4    Stein, R.5    Zimny-Arndt, U.6    Schmid, M.7    Jungblut, P.R.8
  • 105
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase alpha subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • C.M. Benedict, L. Ren, and G.A. Clawson Nuclear multicatalytic proteinase alpha subunit RRC3: differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment Biochemistry 34 1995 9587 9598
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.M.1    Ren, L.2    Clawson, G.A.3
  • 106
    • 0033785045 scopus 로고    scopus 로고
    • Age-related alterations of proteasome structure and function in aging epidermis
    • A.L. Bulteau, I. Petropoulos, and B. Friguet Age-related alterations of proteasome structure and function in aging epidermis Exp. Gerontol. 35 2000 767 777
    • (2000) Exp. Gerontol. , vol.35 , pp. 767-777
    • Bulteau, A.L.1    Petropoulos, I.2    Friguet, B.3
  • 107
    • 2442676283 scopus 로고    scopus 로고
    • Hyperphosphorylation of rat liver proteasome subunits: The effects of ethanol and okadaic acid are compared
    • F. Bardag-Gorce, R. Venkatesh, J. Li, B.A. French, and S.W. French Hyperphosphorylation of rat liver proteasome subunits: the effects of ethanol and okadaic acid are compared Life Sci. 75 2004 585 597
    • (2004) Life Sci. , vol.75 , pp. 585-597
    • Bardag-Gorce, F.1    Venkatesh, R.2    Li, J.3    French, B.A.4    French, S.W.5
  • 108
    • 62849098196 scopus 로고    scopus 로고
    • Characterization and differential expression of a newly identified phosphorylated isoform of the human 20S proteasome ß7 subunit in tumor vs. Normal cell lines
    • R. Eang, E. Girbal-Neuhauser, B. Xu, and E.J. Gairin Characterization and differential expression of a newly identified phosphorylated isoform of the human 20S proteasome ß7 subunit in tumor vs. normal cell lines Fund. Clin. Pharmacol. 23 2009 215 224
    • (2009) Fund. Clin. Pharmacol. , vol.23 , pp. 215-224
    • Eang, R.1    Girbal-Neuhauser, E.2    Xu, B.3    Gairin, E.J.4
  • 112
    • 84878268667 scopus 로고    scopus 로고
    • Structural insights into proteasome activation by the 19S regulatory particle
    • A. Ehlinger, and K.J. Walters Structural insights into proteasome activation by the 19S regulatory particle Biochemistry 52 2013 3618 3628
    • (2013) Biochemistry , vol.52 , pp. 3618-3628
    • Ehlinger, A.1    Walters, K.J.2
  • 114
    • 24044488987 scopus 로고    scopus 로고
    • Mechanism of direct degradation of IkappaBalpha by 20S proteasome
    • B. Alvarez-Castelao, and J.G. Castano Mechanism of direct degradation of IkappaBalpha by 20S proteasome FEBS Lett. 579 2005 4797 4802
    • (2005) FEBS Lett. , vol.579 , pp. 4797-4802
    • Alvarez-Castelao, B.1    Castano, J.G.2
  • 115
    • 0032488219 scopus 로고    scopus 로고
    • Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state
    • L. Petropoulos, and J. Hiscott Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state Virology 252 1998 189 199
    • (1998) Virology , vol.252 , pp. 189-199
    • Petropoulos, L.1    Hiscott, J.2
  • 116
    • 0034685805 scopus 로고    scopus 로고
    • Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex
    • Z. Zhang, N. Torii, A. Furusaka, N. Malayaman, Z. Hu, and T.J. Liang Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex J. Biol. Chem. 275 2000 15157 15165
    • (2000) J. Biol. Chem. , vol.275 , pp. 15157-15165
    • Zhang, Z.1    Torii, N.2    Furusaka, A.3    Malayaman, N.4    Hu, Z.5    Liang, T.J.6
  • 117
    • 2442673028 scopus 로고    scopus 로고
    • The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes
    • J. Dong, W. Chen, A. Welford, and A. Wandinger-Ness The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes J. Biol. Chem. 279 2004 21334 21342
    • (2004) J. Biol. Chem. , vol.279 , pp. 21334-21342
    • Dong, J.1    Chen, W.2    Welford, A.3    Wandinger-Ness, A.4
  • 118
    • 0035370123 scopus 로고    scopus 로고
    • Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7
    • S. Cho, Y.J. Choi, J.M. Kim, S.T. Jeong, J.H. Kim, S.H. Kim, and S.E. Ryu Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7 FEBS Lett. 498 2001 62 66
    • (2001) FEBS Lett. , vol.498 , pp. 62-66
    • Cho, S.1    Choi, Y.J.2    Kim, J.M.3    Jeong, S.T.4    Kim, J.H.5    Kim, S.H.6    Ryu, S.E.7
  • 119
    • 0042847104 scopus 로고    scopus 로고
    • The proteasome as a lipopolysaccharide-binding protein in macrophages: Differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events
    • N. Qureshi, P.Y. Perera, J. Shen, G. Zhang, A. Lenschat, G. Splitter, D.C. Morrison, and S.N. Vogel The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events J. Immunol. 171 2003 1515 1525
    • (2003) J. Immunol. , vol.171 , pp. 1515-1525
    • Qureshi, N.1    Perera, P.Y.2    Shen, J.3    Zhang, G.4    Lenschat, A.5    Splitter, G.6    Morrison, D.C.7    Vogel, S.N.8
  • 120
    • 84991980677 scopus 로고    scopus 로고
    • Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation
    • R. Sanchez-Lanzas, and J.G. Castano Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation Biomolecules 4 2014 1140 1154
    • (2014) Biomolecules , vol.4 , pp. 1140-1154
    • Sanchez-Lanzas, R.1    Castano, J.G.2
  • 121
    • 80053619565 scopus 로고    scopus 로고
    • Gel-based proteomics analysis of the heterogeneity of 20S proteasomes from four human pancreatic cancer cell lines
    • X. Wang, Z. Zhao, Y. Luo, G. Chen, and Z. Li Gel-based proteomics analysis of the heterogeneity of 20S proteasomes from four human pancreatic cancer cell lines Proteom. Clin. Appl. 5 2011 484 492
    • (2011) Proteom. Clin. Appl. , vol.5 , pp. 484-492
    • Wang, X.1    Zhao, Z.2    Luo, Y.3    Chen, G.4    Li, Z.5
  • 122
    • 67650160542 scopus 로고    scopus 로고
    • Comparative expression analysis and characterization of 20S proteasomes in human intestinal tissues: The proteasome pattern as diagnostic tool for IBD patients
    • A. Visekruna, T. Joeris, N. Schmidt, M. Lawrenz, J.P. Ritz, H.J. Buhr, and U. Steinhoff Comparative expression analysis and characterization of 20S proteasomes in human intestinal tissues: the proteasome pattern as diagnostic tool for IBD patients Inflamm. Bowel Dis. 15 2009 526 533
    • (2009) Inflamm. Bowel Dis. , vol.15 , pp. 526-533
    • Visekruna, A.1    Joeris, T.2    Schmidt, N.3    Lawrenz, M.4    Ritz, J.P.5    Buhr, H.J.6    Steinhoff, U.7
  • 126
    • 51649100549 scopus 로고    scopus 로고
    • Scaled-down purification protocol to access proteomic analysis of 20S proteasome from human tissue samples: Comparison of normal and tumor colorectal cells
    • M. Ducoux-Petit, S. Uttenweiler-Joseph, F. Brichory, M.P. Bousquet-Dubouch, O. Burlet-Schiltz, J.F. Haeuw, and B. Monsarrat Scaled-down purification protocol to access proteomic analysis of 20S proteasome from human tissue samples: comparison of normal and tumor colorectal cells J. Proteome Res. 7 2008 2852 2859
    • (2008) J. Proteome Res. , vol.7 , pp. 2852-2859
    • Ducoux-Petit, M.1    Uttenweiler-Joseph, S.2    Brichory, F.3    Bousquet-Dubouch, M.P.4    Burlet-Schiltz, O.5    Haeuw, J.F.6    Monsarrat, B.7
  • 127
    • 70350442776 scopus 로고    scopus 로고
    • A relatively simple and economical protocol for proteomic analyses of human 20S proteasome: Compatible with both scaled-up and scaled-down purifications
    • G. Chen, Y. Luo, X. Wang, Z. Zhao, H. Liu, H. Zhang, and Z. Li A relatively simple and economical protocol for proteomic analyses of human 20S proteasome: compatible with both scaled-up and scaled-down purifications Electrophoresis 30 2009 2422 2430
    • (2009) Electrophoresis , vol.30 , pp. 2422-2430
    • Chen, G.1    Luo, Y.2    Wang, X.3    Zhao, Z.4    Liu, H.5    Zhang, H.6    Li, Z.7
  • 128
  • 129
    • 38749115417 scopus 로고    scopus 로고
    • Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits
    • A. Busse, M. Kraus, I.K. Na, A. Rietz, C. Scheibenbogen, C. Driessen, I.W. Blau, E. Thiel, and U. Keilholz Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits Cancer 112 2008 659 670
    • (2008) Cancer , vol.112 , pp. 659-670
    • Busse, A.1    Kraus, M.2    Na, I.K.3    Rietz, A.4    Scheibenbogen, C.5    Driessen, C.6    Blau, I.W.7    Thiel, E.8    Keilholz, U.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.