메뉴 건너뛰기




Volumn 33, Issue 1, 2014, Pages

Histone deacetylase 8 is deregulated in urothelial cancer but not a target for efficient treatment

Author keywords

Cell cycle arrest; Histone deacetylase 8; Histone deacetylase inhibitor; Urothelial bladder cancer

Indexed keywords

HISTONE DEACETYLASE 8; HISTONE DEACETYLASE INHIBITOR; MESSENGER RNA; SMALL INTERFERING RNA; THYMIDYLATE SYNTHASE; HDAC8 PROTEIN, HUMAN; HISTONE DEACETYLASE; HYDROXAMIC ACID; REPRESSOR PROTEIN;

EID: 84904080238     PISSN: None     EISSN: 17569966     Source Type: Journal    
DOI: 10.1186/s13046-014-0059-8     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 78049485263 scopus 로고    scopus 로고
    • Estimates of worldwide burden of cancer in 2008: GLOBOCAN 2008
    • 10.1002/ijc.25516 21351269
    • Estimates of worldwide burden of cancer in 2008: GLOBOCAN 2008. J Ferlay, HR Shin, F Bray, D Forman, C Mathers, DM Parkin, Int J Cancer 2010 127 2893 2917 10.1002/ijc.25516 21351269
    • (2010) Int J Cancer , vol.127 , pp. 2893-2917
    • Ferlay, J.1    Shin, H.R.2    Bray, F.3    Forman, D.4    Mathers, C.5    Parkin, D.M.6
  • 4
    • 33745597921 scopus 로고    scopus 로고
    • Long-term survival results of a randomized trial comparing gemcitabine/cisplatin and methotrexate/vinblastine/doxorubicin/cisplatin in patients with locally advanced and metastatic bladder cancer
    • 10.1093/annonc/mdj965 16807438
    • Long-term survival results of a randomized trial comparing gemcitabine/cisplatin and methotrexate/vinblastine/doxorubicin/cisplatin in patients with locally advanced and metastatic bladder cancer. JT Roberts, H von der Maase, L Sengelov, PF Conte, L Dogliotti, T Oliver, MJ Moore, A Zimmermann, M Arning, Ann Oncol 2006 17 Suppl 5 &22118 122 10.1093/annonc/mdj965 16807438
    • (2006) Ann Oncol , vol.17 , Issue.SUPPL. 5 , pp. 22118-22122
    • Roberts, J.T.1    Von Der Maase, H.2    Sengelov, L.3    Conte, P.F.4    Dogliotti, L.5    Oliver, T.6    Moore, M.J.7    Zimmermann, A.8    Arning, M.9
  • 6
    • 84859174608 scopus 로고    scopus 로고
    • Histone-modifying enzymes: Regulators of developmental decisions and drivers of human disease
    • 10.2217/epi.12.3 22449188
    • Histone-modifying enzymes: regulators of developmental decisions and drivers of human disease. JS Butler, E Koutelou, AC Schibler, SY Dent, Epigenomics 2012 4 163 177 10.2217/epi.12.3 22449188
    • (2012) Epigenomics , vol.4 , pp. 163-177
    • Butler, J.S.1    Koutelou, E.2    Schibler, A.C.3    Dent, S.Y.4
  • 7
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: From mechanism to therapy
    • 10.1016/j.cell.2012.06.013 22770212
    • Cancer epigenetics: from mechanism to therapy. MA Dawson, T Kouzarides, Cell 2012 150 12 27 10.1016/j.cell.2012.06.013 22770212
    • (2012) Cell , vol.150 , pp. 12-27
    • Dawson, M.A.1    Kouzarides, T.2
  • 11
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • 10.1042/BJ20021321 12429021
    • Histone deacetylases (HDACs): characterization of the classical HDAC family. AJ de Ruijter, AH van Gennip, HN Caron, S Kemp, AB van Kuilenburg, Biochem J 2003 370 737 749 10.1042/BJ20021321 12429021
    • (2003) Biochem J , vol.370 , pp. 737-749
    • De Ruijter, A.J.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.5
  • 12
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • 10.1016/j.jmb.2004.02.006 15050820
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. IV Gregoretti, YM Lee, HV Goodson, J Mol Biol 2004 338 17 31 10.1016/j.jmb.2004.02.006 15050820
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 13
    • 61849144810 scopus 로고    scopus 로고
    • HDAC family: What are the cancer relevant targets?
    • 10.1016/j.canlet.2008.08.016 18824292
    • HDAC family: What are the cancer relevant targets? O Witt, HE Deubzer, T Milde, I Oehme, Cancer Lett 2009 277 8 21 10.1016/j.canlet.2008.08.016 18824292
    • (2009) Cancer Lett , vol.277 , pp. 8-21
    • Witt, O.1    Deubzer, H.E.2    Milde, T.3    Oehme, I.4
  • 14
    • 38549157208 scopus 로고    scopus 로고
    • Association of patterns of class i histone deacetylase expression with patient prognosis in gastric cancer: A retrospective analysis
    • 10.1016/S1470-2045(08)70004-4 18207460
    • Association of patterns of class I histone deacetylase expression with patient prognosis in gastric cancer: a retrospective analysis. W Weichert, A Roske, V Gekeler, T Beckers, MP Ebert, M Pross, M Dietel, C Denkert, C Rocken, Lancet Oncol 2008 9 139 148 10.1016/S1470-2045(08)70004-4 18207460
    • (2008) Lancet Oncol , vol.9 , pp. 139-148
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Ebert, M.P.5    Pross, M.6    Dietel, M.7    Denkert, C.8    Rocken, C.9
  • 15
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • 10.1038/sj.bjc.6604199 18212746
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. W Weichert, A Roske, V Gekeler, T Beckers, C Stephan, K Jung, FR Fritzsche, S Niesporek, C Denkert, M Dietel, G Kristiansen, Br J Cancer 2008 98 604 610 10.1038/sj.bjc.6604199 18212746
    • (2008) Br J Cancer , vol.98 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6    Fritzsche, F.R.7    Niesporek, S.8    Denkert, C.9    Dietel, M.10    Kristiansen, G.11
  • 16
    • 50949104573 scopus 로고    scopus 로고
    • Expression of class i histone deacetylases indicates poor prognosis in endometrioid subtypes of ovarian and endometrial carcinomas
    • 18714364
    • Expression of class I histone deacetylases indicates poor prognosis in endometrioid subtypes of ovarian and endometrial carcinomas. W Weichert, C Denkert, A Noske, S Darb-Esfahani, M Dietel, SE Kalloger, DG Huntsman, M Kobel, Neoplasia 2008 10 1021 1027 18714364
    • (2008) Neoplasia , vol.10 , pp. 1021-1027
    • Weichert, W.1    Denkert, C.2    Noske, A.3    Darb-Esfahani, S.4    Dietel, M.5    Kalloger, S.E.6    Huntsman, D.G.7    Kobel, M.8
  • 17
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • 10.1038/nrm2346 18292778
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. XJ Yang, E Seto, Nat Rev Mol Cell Biol 2008 9 206 218 10.1038/nrm2346 18292778
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 206-218
    • Yang, X.J.1    Seto, E.2
  • 18
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • 10.1038/38664 9311776
    • Histone acetylation in chromatin structure and transcription. M Grunstein, Nature 1997 389 349 352 10.1038/38664 9311776
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 19
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • 10.1126/science.1175371 19608861
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions. C Choudhary, C Kumar, F Gnad, ML Nielsen, M Rehman, TC Walther, JV Olsen, M Mann, Science 2009 325 834 840 10.1126/science.1175371 19608861
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 20
    • 79952105783 scopus 로고    scopus 로고
    • The biology of lysine acetylation integrates transcriptional programming and metabolism
    • 10.1186/1743-7075-8-12
    • The biology of lysine acetylation integrates transcriptional programming and metabolism. J Patel, RR Pathak, S Mujtaba, Nutr Metabol 2011 8 12 10.1186/1743-7075-8-12
    • (2011) Nutr Metabol , vol.8 , pp. 12
    • Patel, J.1    Pathak, R.R.2    Mujtaba, S.3
  • 21
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • 10.1016/S0092-8674(00)80521-8 9288740
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. W Gu, RG Roeder, Cell 1997 90 595 606 10.1016/S0092-8674(00) 80521-8 9288740
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 22
    • 48249132443 scopus 로고    scopus 로고
    • Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion
    • 10.1126/science.1157774 18653893
    • Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion. T Rolef Ben-Shahar, S Heeger, C Lehane, P East, H Flynn, M Skehel, F Uhlmann, Science 2008 321 563 566 10.1126/science.1157774 18653893
    • (2008) Science , vol.321 , pp. 563-566
    • Rolef Ben-Shahar, T.1    Heeger, S.2    Lehane, C.3    East, P.4    Flynn, H.5    Skehel, M.6    Uhlmann, F.7
  • 23
    • 84873173538 scopus 로고    scopus 로고
    • Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes
    • 23181831
    • Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes. Y Li, D Shin, SH Kwon, FEBS J 2013 280 775 793 23181831
    • (2013) FEBS J , vol.280 , pp. 775-793
    • Li, Y.1    Shin, D.2    Kwon, S.H.3
  • 24
    • 84896470334 scopus 로고    scopus 로고
    • Small-molecule inhibitors of histone deacetylase for the treatment of cancer and non-cancer diseases: A patent review (2011 - 2013)
    • 10.1517/13543776.2014.877446 24397271
    • Small-molecule inhibitors of histone deacetylase for the treatment of cancer and non-cancer diseases: a patent review (2011-2013). S Valente, A Mai, Expert Opin Ther Pat 2014 24 4 401 15 10.1517/13543776.2014.877446 24397271
    • (2014) Expert Opin Ther Pat , vol.24 , Issue.4 , pp. 401-415
    • Valente, S.1    Mai, A.2
  • 25
    • 84874410182 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors (HDACIs): Multitargeted anticancer agents
    • 23459471
    • Histone deacetylase inhibitors (HDACIs): multitargeted anticancer agents. K Ververis, A Hiong, TC Karagiannis, PV Licciardi, Biologics 2013 7 47 60 23459471
    • (2013) Biologics , vol.7 , pp. 47-60
    • Ververis, K.1    Hiong, A.2    Karagiannis, T.C.3    Licciardi, P.V.4
  • 27
    • 0034685766 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human class i histone deacetylase that functions as a transcription repressor
    • 10.1074/jbc.M908988199 10748112
    • Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. E Hu, Z Chen, T Fredrickson, Y Zhu, R Kirkpatrick, GF Zhang, K Johanson, CM Sung, R Liu, J Winkler, J Biol Chem 2000 275 15254 15264 10.1074/jbc.M908988199 10748112
    • (2000) J Biol Chem , vol.275 , pp. 15254-15264
    • Hu, E.1    Chen, Z.2    Fredrickson, T.3    Zhu, Y.4    Kirkpatrick, R.5    Zhang, G.F.6    Johanson, K.7    Sung, C.M.8    Liu, R.9    Winkler, J.10
  • 29
    • 0034663486 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human histone deacetylase, HDAC8
    • 10.1042/0264-6021:3500199 10926844
    • Cloning and characterization of a novel human histone deacetylase, HDAC8. JJ Buggy, ML Sideris, P Mak, DD Lorimer, B McIntosh, JM Clark, Biochem J 2000 350 Pt 1 199 205 10.1042/0264-6021:3500199 10926844
    • (2000) Biochem J , vol.350 , pp. 199-205
    • Buggy, J.J.1    Sideris, M.L.2    Mak, P.3    Lorimer, D.D.4    McIntosh, B.5    Clark, J.M.6
  • 30
    • 0346725952 scopus 로고    scopus 로고
    • Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
    • 10.1128/MCB.24.2.765-773.2004 14701748
    • Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. H Lee, N Rezai-Zadeh, E Seto, Mol Cell Biol 2004 24 765 773 10.1128/MCB.24.2.765-773.2004 14701748
    • (2004) Mol Cell Biol , vol.24 , pp. 765-773
    • Lee, H.1    Rezai-Zadeh, N.2    Seto, E.3
  • 32
    • 16644369899 scopus 로고    scopus 로고
    • Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class i HDAC profiles between epithelial and stromal cells
    • 15590418
    • Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class I HDAC profiles between epithelial and stromal cells. D Waltregny, B North, F Van Mellaert, J de Leval, E Verdin, V Castronovo, Eur J Histochem 2004 48 273 290 15590418
    • (2004) Eur J Histochem , vol.48 , pp. 273-290
    • Waltregny, D.1    North, B.2    Van Mellaert, F.3    De Leval, J.4    Verdin, E.5    Castronovo, V.6
  • 33
    • 3242793175 scopus 로고    scopus 로고
    • Expression of histone deacetylase 8, a class i histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues
    • 10.1016/S0002-9440(10)63320-2 15277229
    • Expression of histone deacetylase 8, a class I histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues. D Waltregny, L De Leval, W Glenisson, S Ly Tran, BJ North, A Bellahcene, U Weidle, E Verdin, V Castronovo, Am J Pathol 2004 165 553 564 10.1016/S0002-9440(10)63320-2 15277229
    • (2004) Am J Pathol , vol.165 , pp. 553-564
    • Waltregny, D.1    De Leval, L.2    Glenisson, W.3    Ly Tran, S.4    North, B.J.5    Bellahcene, A.6    Weidle, U.7    Verdin, E.8    Castronovo, V.9
  • 35
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • 10.1038/leu.2008.9 18256683
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas. S Balasubramanian, J Ramos, W Luo, M Sirisawad, E Verner, JJ Buggy, Leukemia 2008 22 1026 1034 10.1038/leu.2008.9 18256683
    • (2008) Leukemia , vol.22 , pp. 1026-1034
    • Balasubramanian, S.1    Ramos, J.2    Luo, W.3    Sirisawad, M.4    Verner, E.5    Buggy, J.J.6
  • 36
    • 84890080778 scopus 로고    scopus 로고
    • The up-regulation of histone deacetylase 8 promotes proliferation and inhibits apoptosis in hepatocellular carcinoma
    • 10.1007/s10620-013-2867-7 24077923
    • The up-regulation of histone deacetylase 8 promotes proliferation and inhibits apoptosis in hepatocellular carcinoma. J Wu, C Du, Z Lv, C Ding, J Cheng, H Xie, L Zhou, S Zheng, Dig Dis Sci 2013 58 3545 3553 10.1007/s10620-013-2867-7 24077923
    • (2013) Dig Dis Sci , vol.58 , pp. 3545-3553
    • Wu, J.1    Du, C.2    Lv, Z.3    Ding, C.4    Cheng, J.5    Xie, H.6    Zhou, L.7    Zheng, S.8
  • 38
    • 33745822471 scopus 로고    scopus 로고
    • Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation
    • 10.1128/MCB.01971-05 16809764
    • Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. H Lee, N Sengupta, A Villagra, N Rezai-Zadeh, E Seto, Mol Cell Biol 2006 26 5259 5269 10.1128/MCB.01971-05 16809764
    • (2006) Mol Cell Biol , vol.26 , pp. 5259-5269
    • Lee, H.1    Sengupta, N.2    Villagra, A.3    Rezai-Zadeh, N.4    Seto, E.5
  • 39
    • 84886292827 scopus 로고    scopus 로고
    • Changes in histone deacetylase (HDAC) expression patterns and activity of HDAC inhibitors in urothelial cancers
    • 10.1016/j.urolonc.2012.06.015 22944197
    • Changes in histone deacetylase (HDAC) expression patterns and activity of HDAC inhibitors in urothelial cancers. G Niegisch, J Knievel, A Koch, C Hader, U Fischer, P Albers, WA Schulz, Urol Oncol 2013 31 1770 1779 10.1016/j.urolonc.2012.06.015 22944197
    • (2013) Urol Oncol , vol.31 , pp. 1770-1779
    • Niegisch, G.1    Knievel, J.2    Koch, A.3    Hader, C.4    Fischer, U.5    Albers, P.6    Schulz, W.A.7
  • 40
    • 0037229621 scopus 로고    scopus 로고
    • Activities of MAP-kinase pathways in normal uroepithelial cells and urothelial carcinoma cell lines
    • 10.1006/excr.2002.5647 12490193
    • Activities of MAP-kinase pathways in normal uroepithelial cells and urothelial carcinoma cell lines. S Swiatkowski, HH Seifert, C Steinhoff, A Prior, I Thievessen, F Schliess, WA Schulz, Exp Cell Res 2003 282 48 57 10.1006/excr.2002.5647 12490193
    • (2003) Exp Cell Res , vol.282 , pp. 48-57
    • Swiatkowski, S.1    Seifert, H.H.2    Steinhoff, C.3    Prior, A.4    Thievessen, I.5    Schliess, F.6    Schulz, W.A.7
  • 41
    • 34247376560 scopus 로고    scopus 로고
    • Design and evaluation of 'Linkerless' hydroxamic acids as selective HDAC8 inhibitors
    • 10.1016/j.bmcl.2007.02.064 17346959
    • Design and evaluation of 'Linkerless' hydroxamic acids as selective HDAC8 inhibitors. K Krennhrubec, BL Marshall, M Hedglin, E Verdin, SM Ulrich, Bioorg Med Chem Lett 2007 17 2874 2878 10.1016/j.bmcl.2007.02.064 17346959
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 2874-2878
    • Krennhrubec, K.1    Marshall, B.L.2    Hedglin, M.3    Verdin, E.4    Ulrich, S.M.5
  • 42
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • 10.1016/0022-1759(91)90198-O
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. I Nicoletti, G Migliorati, MC Pagliacci, F Grignani, C Riccardi, J Immunol Meth 1991 139 271 279 10.1016/0022-1759(91) 90198-O
    • (1991) J Immunol Meth , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 43
    • 34250782684 scopus 로고    scopus 로고
    • Extraction, purification and analysis of histones
    • 10.1038/nprot.2007.202
    • Extraction, purification and analysis of histones. D Shechter, HL Dormann, CD Allis, SB Hake, Nat Protocol 2007 2 1445 1457 10.1038/nprot.2007.202
    • (2007) Nat Protocol , vol.2 , pp. 1445-1457
    • Shechter, D.1    Dormann, H.L.2    Allis, C.D.3    Hake, S.B.4
  • 44
    • 77954928123 scopus 로고    scopus 로고
    • Expression signature of E2F1 and its associated genes predict superficial to invasive progression of bladder tumors
    • 10.1200/JCO.2009.25.0977 20421545
    • Expression signature of E2F1 and its associated genes predict superficial to invasive progression of bladder tumors. JS Lee, SH Leem, SY Lee, SC Kim, ES Park, SB Kim, SK Kim, YJ Kim, WJ Kim, IS Chu, J Clin Oncol 2010 28 2660 2667 10.1200/JCO.2009.25.0977 20421545
    • (2010) J Clin Oncol , vol.28 , pp. 2660-2667
    • Lee, J.S.1    Leem, S.H.2    Lee, S.Y.3    Kim, S.C.4    Park, E.S.5    Kim, S.B.6    Kim, S.K.7    Kim, Y.J.8    Kim, W.J.9    Chu, I.S.10
  • 45
  • 46
    • 34547684065 scopus 로고    scopus 로고
    • HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
    • 10.1038/sj.onc.1210614 17694087
    • HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination. C Boyault, K Sadoul, M Pabion, S Khochbin, Oncogene 2007 26 5468 5476 10.1038/sj.onc.1210614 17694087
    • (2007) Oncogene , vol.26 , pp. 5468-5476
    • Boyault, C.1    Sadoul, K.2    Pabion, M.3    Khochbin, S.4
  • 48
    • 84901698457 scopus 로고    scopus 로고
    • Limited efficacy of specific HDAC6 inhibition in urothelial cancer cells
    • 10.4161/cbt.28469
    • Limited efficacy of specific HDAC6 inhibition in urothelial cancer cells. L Rosik, G Niegisch, U Fischer, M Jung, WA Schulz, MJ Hoffmann, Canc Biol Ther 2014 15 742 57 10.4161/cbt.28469
    • (2014) Canc Biol Ther , vol.15 , pp. 742-757
    • Rosik, L.1    Niegisch, G.2    Fischer, U.3    Jung, M.4    Schulz, W.A.5    Hoffmann, M.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.