메뉴 건너뛰기




Volumn 2011, Issue 5, 2011, Pages 11-32

Repercussion of mitochondria deformity induced by anti-Hsp90 drug 17AAG in human tumor cells

Author keywords

17AAG; Hsp90; Mitochondria; Tumor cells; m

Indexed keywords

CISPLATIN; CURCUMIN; CYTOCHALASIN D; CYTOCHROME C; DIGITONIN; HEAT SHOCK PROTEIN 90; HYDROGEN PEROXIDE; NOVOBIOCIN; PACLITAXEL; RADICICOL; REACTIVE OXYGEN METABOLITE; TANESPIMYCIN; VINCRISTINE;

EID: 80053907818     PISSN: None     EISSN: 11773928     Source Type: Journal    
DOI: 10.4137/DTI.S6582     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molec ular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G. The 90-kDa molec ular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther. 1998;79:129-68.
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 3
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood). 2003;228:111-33.
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 4
    • 33846861747 scopus 로고    scopus 로고
    • Targeting of multiple signaling by heat shock protein 90 molecular chaperone inhibitors
    • Powers MV, Workman P. Targeting of multiple signaling by heat shock protein 90 molecular chaperone inhibitors. Endocr Relat Cancer. 2006;13: S125-135.
    • (2006) Endocr Relat Cancer , vol.13
    • Powers, M.V.1    Workman, P.2
  • 5
    • 0037458627 scopus 로고    scopus 로고
    • Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis
    • Vanden Berghe T, Kalai M, van Loo G, Declercq W, Vandenabeele P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J Biol Chem. 2003;278:5622-9.
    • (2003) J Biol Chem , vol.278 , pp. 5622-5629
    • Berghe, V.T.1    Kalai, M.2    van Loo, G.3    Declercq, W.4    Vandenabeele, P.5
  • 6
    • 0037069929 scopus 로고    scopus 로고
    • Chemotherapy: Targeting the mitochon drial death pathway
    • Debatin K, Poncet D, Kroemer G. Chemotherapy: targeting the mitochon drial death pathway. Oncogene. 2002;21:8786-803.
    • (2002) Oncogene , vol.21 , pp. 8786-8803
    • Debatin, K.1    Poncet, D.2    Kroemer, G.3
  • 7
    • 0004207650 scopus 로고
    • Plenum Press, New York, NY, USA
    • Tzagoloff A. Mitochondria, Plenum Press, New York, NY, USA; 1982.
    • (1982) Mitochondria
    • Tzagoloff, A.1
  • 8
    • 33748518966 scopus 로고    scopus 로고
    • Superoxide dismutase: An emerging target for cancer therapeutics
    • Hileman EO, Achanta G, Huang P. Superoxide dismutase: an emerging target for cancer therapeutics. Expert Opin Ther Targets. 2001;5:697-710.
    • (2001) Expert Opin Ther Targets , vol.5 , pp. 697-710
    • Hileman, E.O.1    Achanta, G.2    Huang, P.3
  • 9
    • 33644870379 scopus 로고    scopus 로고
    • Oxidative phosphorylation dysfunction modulates expression of extracellular matrix-remodeling genes and invasion
    • Van Waveren C, Sun Y, Cheung HS, Moraes CT. Oxidative phosphorylation dysfunction modulates expression of extracellular matrix-remodeling genes and invasion. Carcinogenesis. 2006;27:409-18.
    • (2006) Carcinogenesis , vol.27 , pp. 409-418
    • van Waveren, C.1    Sun, Y.2    Cheung, H.S.3    Moraes, C.T.4
  • 11
    • 0019200299 scopus 로고
    • Phospholipid composition of inner and outer mitochondrial membranes isolated from Yoshida hepatoma AH-130
    • Garcea R, Canuto RA, Guatero B, Biocca M, Feo F. Phospholipid composition of inner and outer mitochondrial membranes isolated from Yoshida hepatoma AH-130. (1980) Cancer Lett. 1980;11:133-9.
    • (1980) Cancer Lett , vol.11 , pp. 133-139
    • Garcea, R.1    Canuto, R.A.2    Guatero, B.3    Biocca, M.4    Feo, F.5
  • 12
    • 33645527573 scopus 로고    scopus 로고
    • Cancer cell mitochondria are direct proapoptotic targets for the marine antitumor drug lamellarin D
    • Kluza J, Gallego MA, Loyens A, etal. Cancer cell mitochondria are direct proapoptotic targets for the marine antitumor drug lamellarin D. Cancer Res. 2006;66:3177-87.
    • (2006) Cancer Res , vol.66 , pp. 3177-3187
    • Kluza, J.1    Gallego, M.A.2    Loyens, A.3
  • 13
    • 2942531063 scopus 로고    scopus 로고
    • Mitochondrial defects in cancer
    • Carew JS, Huang P. Mitochondrial defects in cancer. Mol Cancer. 2002;9:1-9.
    • (2002) Mol Cancer , vol.9 , pp. 1-9
    • Carew, J.S.1    Huang, P.2
  • 14
    • 33846390427 scopus 로고    scopus 로고
    • Building the power house: Recent advances in mito- chondrial studies through proteomics and systems biology
    • Vo TD, Palsson BO. Building the power house: recent advances in mito- chondrial studies through proteomics and systems biology. Am J Physiol Cell Physiol. 2007;292:C164-77.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Vo, T.D.1    Palsson, B.O.2
  • 15
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • Kroemer G. Mitochondrial control of apoptosis: an introduction. Biochem Biophys Res Commun. 2003;304:433-5.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 17
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power- transmitting cables
    • Skulachev VP. Mitochondrial filaments and clusters as intracellular power- transmitting cables. Trends Biochem Sci. 2001;26:23-9.
    • (2001) Trends Biochem Sci , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 18
    • 39749149059 scopus 로고    scopus 로고
    • Cancer: Defeating the immortal
    • Kroemer G. Cancer: defeating the immortal. Cancer Biol Ther. 2007;6: 1324-8.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1324-1328
    • Kroemer, G.1
  • 19
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 20
    • 1542328907 scopus 로고    scopus 로고
    • Hsp90 inhibition: A new strategy to inhibit protein kinases
    • Sreedhar AS, Soti C, Csermely P. Hsp90 inhibition: a new strategy to inhibit protein kinases. Biochim Biophys Acta. 2004;1697:233-42.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 233-242
    • Sreedhar, A.S.1    Soti, C.2    Csermely, P.3
  • 21
    • 36148976786 scopus 로고    scopus 로고
    • Hsp90 inhibitors disrupt mitochondrial homeostasis in cancer cells
    • Neckers L, Kern A, Tsutsumi S. Hsp90 inhibitors disrupt mitochondrial homeostasis in cancer cells. Chem Biol. 2007;14:1204-6.
    • (2007) Chem Biol , vol.14 , pp. 1204-1206
    • Neckers, L.1    Kern, A.2    Tsutsumi, S.3
  • 22
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn J. Behavior of mitochondria in the living cell. Inst Rev Cytol. 1990;122:1-63.
    • (1990) Inst Rev Cytol , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 24
    • 0032905925 scopus 로고    scopus 로고
    • Subcellular heterogeneity of mitochondrial membrane potential: Relationship with organelle distribution and intercellular contacts in normal, hypoxic and apoptotic cells
    • Diaz G, Setzu MD, Zucca A, Isola R, et al. Subcellular heterogeneity of mitochondrial membrane potential: relationship with organelle distribution and intercellular contacts in normal, hypoxic and apoptotic cells. J Cell Sci. 1999;112:1077-84.
    • (1999) J Cell Sci , vol.112 , pp. 1077-1084
    • Diaz, G.1    Setzu, M.D.2    Zucca, A.3    Isola, R.4
  • 25
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90inhibitors
    • Kamal A, Thao L, Sensintaffar J, etal. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90inhibitors. Nature. 2003;425:407-10.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 26
    • 51649086458 scopus 로고    scopus 로고
    • Mitochondrial swelling measurement in situ by optimized spatial filtering: Astrocyte-neuron differences
    • Gerencser AA, Doczi J, Torocsik B, Bossy-Wetzel E, Adam-Vizi V. Mitochondrial swelling measurement in situ by optimized spatial filtering: astrocyte-neuron differences. Biophys J. 2008;95:2583-98.
    • (2008) Biophys J , vol.95 , pp. 2583-2598
    • Gerencser, A.A.1    Doczi, J.2    Torocsik, B.3    Bossy-Wetzel, E.4    Adam-Vizi, V.5
  • 27
    • 0000955838 scopus 로고
    • Water uptake and extrusion by mitochondria in relation to oxidative phosphorylation
    • Lehninger AL. Water uptake and extrusion by mitochondria in relation to oxidative phosphorylation. Physiol Rev. 1962;42:467-517.
    • (1962) Physiol Rev , vol.42 , pp. 467-517
    • Lehninger, A.L.1
  • 28
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function
    • He L, Lemasters JJ. Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function. FEBS Lett. 2002;512:1-7.
    • (2002) FEBS Lett , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 29
    • 0032570577 scopus 로고    scopus 로고
    • Cytochrome c in the apoptotic and antioxidant cascades
    • Skulachev VP. Cytochrome c in the apoptotic and antioxidant cascades. FEBS Lett. 1998;423:275-80.
    • (1998) FEBS Lett , vol.423 , pp. 275-280
    • Skulachev, V.P.1
  • 31
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • Mitchell P. Keilin's respiratory chain concept and its chemiosmotic consequences. Science. 1979;206:1148-59.
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 32
    • 22044432618 scopus 로고    scopus 로고
    • Control of mitochondrial shape
    • Jensen RE. Control of mitochondrial shape. Curr Opin Cell Biol. 2005;17: 384-8.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 384-388
    • Jensen, R.E.1
  • 33
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Akinaga S, Soga S, et al. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones. 1998;3:100-8.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3
  • 34
    • 55749086986 scopus 로고    scopus 로고
    • Cisplatin differently affects amino terminal and carboxyl terminal domains of HSP90
    • Ishida R, Takaoka Y, Yamamoto S, et al. Cisplatin differently affects amino terminal and carboxyl terminal domains of HSP90. FEBS Letts. 2008;582:3879-83.
    • (2008) FEBS Letts , vol.582 , pp. 3879-3883
    • Ishida, R.1    Takaoka, Y.2    Yamamoto, S.3
  • 35
    • 61649098007 scopus 로고    scopus 로고
    • Novobiocin and Additional Inhibitors of the Hsp90 C-Terminal Nucleotide-binding Pocket
    • Donnelly A, Blahh BSJ. Novobiocin and Additional Inhibitors of the Hsp90 C-Terminal Nucleotide-binding Pocket. Curr Med Chem. 2008;15: 2702-17.
    • (2008) Curr Med Chem , vol.15 , pp. 2702-2717
    • Donnelly, A.1    Blahh, B.S.J.2
  • 37
    • 30344441143 scopus 로고    scopus 로고
    • Loss of mitochondrial membrane potential is associated with increase in mitochondrial volume: Physiological role in neurones
    • Safiulina D, Veksler V, Zharkovsky A, Kaasik A. Loss of mitochondrial membrane potential is associated with increase in mitochondrial volume: physiological role in neurones. Cell Physiol. 2006;206:347-53.
    • (2006) Cell Physiol , vol.206 , pp. 347-353
    • Safiulina, D.1    Veksler, V.2    Zharkovsky, A.3    Kaasik, A.4
  • 38
    • 45249092773 scopus 로고    scopus 로고
    • Oxidative stress caused by blocking of mitochondrial complex I H(+) pumping as a link in aging/disease vicious cycle
    • Dlaskova A, Hlavata L, Jezek P. Oxidative stress caused by blocking of mitochondrial complex I H(+) pumping as a link in aging/disease vicious cycle. Int J Biochem Cell Biol. 2008;40:792-1805.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 792-1805
    • Dlaskova, A.1    Hlavata, L.2    Jezek, P.3
  • 39
    • 51049094187 scopus 로고    scopus 로고
    • Reduced cytosolic protein synthesis suppresses mitochondrial degeneration
    • Wang X, Zuo X, Kucejova B, Chen XJ. Reduced cytosolic protein synthesis suppresses mitochondrial degeneration. Nat Cell Biol. 2008;10: 1090-7.
    • (2008) Nat Cell Biol , vol.10 , pp. 1090-1097
    • Wang, X.1    Zuo, X.2    Kucejova, B.3    Chen, X.J.4
  • 40
    • 0037236792 scopus 로고    scopus 로고
    • Anticancer potential of curcumin: Preclinical and clinical studies
    • Aggarwal BB, Kumar A, Bharti AC. Anticancer potential of curcumin: preclinical and clinical studies. Anticancer Res. 2003;23:63-398.
    • (2003) Anticancer Res , vol.23 , pp. 63-398
    • Aggarwal, B.B.1    Kumar, A.2    Bharti, A.C.3
  • 41
    • 0042818097 scopus 로고    scopus 로고
    • Hsp90 inhibition accelerates cell lysis. Anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibi- tors involving both superoxide- and Hsp90-dependent events
    • Sreedhar AS, Mihaly K, Pato B, et al. Hsp90 inhibition accelerates cell lysis. Anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibi- tors involving both superoxide- and Hsp90-dependent events. J Biol Chem. 2003;278:35231-40.
    • (2003) J Biol Chem , vol.278 , pp. 35231-35240
    • Sreedhar, A.S.1    Mihaly, K.2    Pato, B.3
  • 42
    • 0034778433 scopus 로고    scopus 로고
    • Digitonin enhances the antitumor effect of cisplatin during isolated lung perfusion
    • Tanaka T, Kaneda Y, Li TS, Matsuoka T, Zempo N, Esato K. Digitonin enhances the antitumor effect of cisplatin during isolated lung perfusion. Ann Thorac Surg. 2001;72:1173-8.
    • (2001) Ann Thorac Surg , vol.72 , pp. 1173-1178
    • Tanaka, T.1    Kaneda, Y.2    Li, T.S.3    Matsuoka, T.4    Zempo, N.5    Esato, K.6
  • 43
    • 0036313059 scopus 로고    scopus 로고
    • Calcium- induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane
    • Brustovetsky N, Brustovetsky T, Jemmerson R, Dubinsky JM. Calcium- induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane. J Neurochem. 2002;80:207-18.
    • (2002) J Neurochem , vol.80 , pp. 207-218
    • Brustovetsky, N.1    Brustovetsky, T.2    Jemmerson, R.3    Dubinsky, J.M.4
  • 44
    • 0026333907 scopus 로고
    • Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of T{stroke}rypanosoma cruzi in situ
    • Vercesi AE, Bernardes CF, Hoffmann ME, Gadelha FR, Docampo R. Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of T{stroke}rypanosoma cruzi in situ. J Biol Chem. 1991;266:14431-4.
    • (1991) J Biol Chem , vol.266 , pp. 14431-14434
    • Vercesi, A.E.1    Bernardes, C.F.2    Hoffmann, M.E.3    Gadelha, F.R.4    Docampo, R.5
  • 45
    • 75849158230 scopus 로고    scopus 로고
    • The gene ontology in 2010: Extensions and refinements
    • Gene Ontology Consortium
    • Gene Ontology Consortium. The gene ontology in 2010: extensions and refinements. Nucleic Acids Res. 2010;38:D331-5.
    • (2010) Nucleic Acids Res , vol.38
  • 46
    • 58149200954 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • Sayers EW, Barrett T, Benson DA etal. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 2009;37: D5-15.
    • (2009) Nucleic Acids Res , vol.37
    • Sayers, E.W.1    Barrett, T.2    Benson, D.A.3
  • 47
    • 0010527137 scopus 로고    scopus 로고
    • Characterization of the 90 kDa heat shock protein (Hsp90) -associated ATP/GTPase
    • Nardai G, Schnaider T, Soti C, et al. Characterization of the 90 kDa heat shock protein (Hsp90) -associated ATP/GTPase. J Biosci. 1996;21: 179-90.
    • (1996) J Biosci , vol.21 , pp. 179-190
    • Nardai, G.1    Schnaider, T.2    Soti, C.3
  • 48
    • 0035295778 scopus 로고    scopus 로고
    • Mitochondria in apoptosis and human disease
    • Oslon M, Kronbluth S. Mitochondria in apoptosis and human disease. Curr Mol Med. 2001;1:91-122.
    • (2001) Curr Mol Med , vol.1 , pp. 91-122
    • Oslon, M.1    Kronbluth, S.2
  • 49
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chap-erone network
    • Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chap-erone network. Cell. 2007;131:257-70.
    • (2007) Cell , vol.131 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 50
    • 77957554723 scopus 로고    scopus 로고
    • Preclinical characterization of mito- chondria-targeted small molecule hsp90inhibitors, gamitrinibs, in advanced prostate cancer
    • Kang BH, Siegelin MD, Plescia J, etal. Preclinical characterization of mito- chondria-targeted small molecule hsp90inhibitors, gamitrinibs, in advanced prostate cancer. Clin Cancer Res. 2010;16:4779-88.
    • (2010) Clin Cancer Res , vol.16 , pp. 4779-4788
    • Kang, B.H.1    Siegelin, M.D.2    Plescia, J.3
  • 51
    • 65649128567 scopus 로고    scopus 로고
    • Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90
    • Kang BH, Plescia J, Song HY, et al. Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90. JClin Invest. 2009;119:454-64.
    • (2009) JClin Invest , vol.119 , pp. 454-464
    • Kang, B.H.1    Plescia, J.2    Song, H.Y.3
  • 52
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevi- siae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari J, Marshall WF, Straight A, Murray A, Sedat JW, Walter P. Mitochondrial transmission during mating in Saccharomyces cerevi- siae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol Biol Cell. 1997;8: 1233-42.
    • (1997) Mol Biol Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 53
    • 0034650725 scopus 로고    scopus 로고
    • Geldanamycin disrupts platelet-membrane structure, leading to membrane permeabilization and inhibition of platelet aggregation
    • Suttitanamongkol S, Gear AR, Polanowska-Grabowska R. Geldanamycin disrupts platelet-membrane structure, leading to membrane permeabilization and inhibition of platelet aggregation. Biochem J. 2000;345 Pt 2: 307-14.
    • (2000) Biochem J , vol.345 , Issue.PART 2 , pp. 307-314
    • Suttitanamongkol, S.1    Gear, A.R.2    Polanowska-Grabowska, R.3
  • 54
    • 10744224439 scopus 로고    scopus 로고
    • Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria
    • Mooth VK, Bunkenborg J, Olsen JV, et al. Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell. 2003;115:629-40.
    • (2003) Cell , vol.115 , pp. 629-640
    • Mooth, V.K.1    Bunkenborg, J.2    Olsen, J.V.3
  • 55
    • 77953589749 scopus 로고    scopus 로고
    • Mammalian mitochondrial proteomics: Insights into mitochondrial functions and mitochondria-related diseases
    • Chen X, Li J, Hou J, Xie Z, Yang F. Mammalian mitochondrial proteomics: insights into mitochondrial functions and mitochondria-related diseases. Expert Rev Proteomics. 2010;7:333-45.
    • (2010) Expert Rev Proteomics , vol.7 , pp. 333-345
    • Chen, X.1    Li, J.2    Hou, J.3    Xie, Z.4    Yang, F.5
  • 56
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of protein
    • O'Farrell PH. High resolution two-dimensional electrophoresis of protein. JBiol Chem. 1975;250:4007-21.
    • (1975) JBiol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 57
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE. Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol. 2000;16:483-519
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.