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Volumn 32, Issue 1, 2015, Pages 211-221

Oxidative stress protection by exogenous delivery of rhhsp70 chaperone to the retinal pigment epithelium (RPE), a possible therapeutic strategy against RPE degeneration

Author keywords

AMD; Hsp70; Oxidative stress; Protein delivery; RPE

Indexed keywords

HEAT SHOCK PROTEIN 70; HYDROGEN PEROXIDE; INTERLEUKIN 6; RECOMBINANT PROTEIN;

EID: 84939878208     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-014-1456-6     Document Type: Article
Times cited : (38)

References (44)
  • 1
    • 33749440219 scopus 로고    scopus 로고
    • Mechanisms of disease: Age-related macular degeneration
    • 17021323 10.1056/NEJMra062326
    • de Jong PTVM. Mechanisms of disease: Age-related macular degeneration. N Engl J Med. 2006;355(14):1474-85.
    • (2006) N. Engl. J. Med. , vol.355 , Issue.14 , pp. 1474-1485
    • De Jong, P.1
  • 3
    • 84880797112 scopus 로고    scopus 로고
    • Autophagy and heterophagy dysregulation leads to retinal pigment epithelium dysfunction and development of age-related macular degeneration
    • 1:CAS:528:DC%2BC2cXlsF2ktw%3D%3D 3722332 23590900
    • Kaarniranta K, Sinha D, Blasiak J, Kauppinen A, Vereb Z, Salminen A, et al. Autophagy and heterophagy dysregulation leads to retinal pigment epithelium dysfunction and development of age-related macular degeneration. Autophagy. 2013;9(7):973-84.
    • (2013) Autophagy , vol.9 , Issue.7 , pp. 973-984
    • Kaarniranta, K.1    Sinha, D.2    Blasiak, J.3    Kauppinen, A.4    Vereb, Z.5    Salminen, A.6
  • 4
    • 84863726788 scopus 로고    scopus 로고
    • Consequences of oxidative stress in age-related macular degeneration
    • 1:CAS:528:DC%2BC38XhtVShurfN 3392472 22510306
    • Jarrett SG, Boulton ME. Consequences of oxidative stress in age-related macular degeneration. Mol Aspects Med. 2012;33(4):399-417.
    • (2012) Mol Aspects Med , vol.33 , Issue.4 , pp. 399-417
    • Jarrett, S.G.1    Boulton, M.E.2
  • 5
    • 0021323978 scopus 로고
    • Aging human RPE: Morphometric analysis of macular, equatorial, and peripheral cells
    • 1:STN:280:DyaL2c7jsV2isQ%3D%3D 6698741
    • Feeney-Burns L, Hilderbrand ES, Eldridge S. Aging human RPE: morphometric analysis of macular, equatorial, and peripheral cells. Invest Ophthalmol Vis Sci. 1984;25(2):195-200.
    • (1984) Invest. Ophthalmol. Vis. Sci. , vol.25 , Issue.2 , pp. 195-200
    • Feeney-Burns, L.1    Hilderbrand, E.S.2    Eldridge, S.3
  • 6
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • 1:CAS:528:DC%2BD3MXisleis7k%3D 11182078
    • Sherman MY, Goldberg AL. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron. 2001;29(1):15-32.
    • (2001) Neuron , vol.29 , Issue.1 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 7
    • 84874832163 scopus 로고    scopus 로고
    • Protein homeostasis as a therapeutic target for diseases of protein conformation
    • 1:CAS:528:DC%2BC3sXmtVajs74%3D 3955168 23339312
    • Calamini B, Morimoto RI. Protein homeostasis as a therapeutic target for diseases of protein conformation. Curr Top Med Chem. 2012;12(22):2623-40.
    • (2012) Curr. Top. Med. Chem. , vol.12 , Issue.22 , pp. 2623-2640
    • Calamini, B.1    Morimoto, R.I.2
  • 8
    • 77449157041 scopus 로고    scopus 로고
    • Crosstalk between Hsp70 molecular chaperone, lysosomes and proteasomes in autophagy-mediated proteolysis in human retinal pigment epithelial cells
    • 19017362 10.1111/j.1582-4934.2008.00577.x
    • Ryhänen T, Hyttinen JMT, Kopitz J, Rilla K, Kuusisto E, Mannermaa E, et al. Crosstalk between Hsp70 molecular chaperone, lysosomes and proteasomes in autophagy-mediated proteolysis in human retinal pigment epithelial cells. J Cell Mol Med. 2009;13(9B):3616-31.
    • (2009) J. Cell. Mol. Med. , vol.13 , Issue.9 , pp. 3616-3631
    • Ryhänen, T.1    Hyttinen, J.M.T.2    Kopitz, J.3    Rilla, K.4    Kuusisto, E.5    Mannermaa, E.6
  • 9
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto RI. The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb Symp Quant Biol. 2011;76 (91-99
    • (2011) Cold Spring Harb Symp Quant Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 11
    • 0030322758 scopus 로고    scopus 로고
    • Diminished heat shock response in the aged myocardium
    • 1:CAS:528:DyaK2sXlvVOqtA%3D%3D 376462 9222610
    • Locke M, Tanguay RM. Diminished heat shock response in the aged myocardium. Cell Stress Chaperones. 1996;1(4):251-60.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.4 , pp. 251-260
    • Locke, M.1    Tanguay, R.M.2
  • 12
    • 0029945392 scopus 로고    scopus 로고
    • Age-related decrease in the inductability of heat shock protein 72 in normal human skin
    • 1:STN:280:DyaK283oslOltg%3D%3D 8763420
    • Muramatsu T, Hatoko M, Tada H, Shirai T, Ohnishi T. Age-related decrease in the inductability of heat shock protein 72 in normal human skin. Br J Dermatol. 1996;134(6):1035-8.
    • (1996) Br. J. Dermatol. , vol.134 , Issue.6 , pp. 1035-1038
    • Muramatsu, T.1    Hatoko, M.2    Tada, H.3    Shirai, T.4    Ohnishi, T.5
  • 13
    • 0035900779 scopus 로고    scopus 로고
    • Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations
    • 1:CAS:528:DC%2BD3MXptlelur0%3D 11551913
    • Katayama T, Imaizumi K, Honda A, Yoneda T, Kudo T, Takeda M, et al. Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations. J Biol Chem. 2001;276(46):43446-54.
    • (2001) J. Biol. Chem. , vol.276 , Issue.46 , pp. 43446-43454
    • Katayama, T.1    Imaizumi, K.2    Honda, A.3    Yoneda, T.4    Kudo, T.5    Takeda, M.6
  • 14
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • 1:CAS:528:DC%2BD3sXksVWqsb8%3D 12783846
    • Cowan KJ, Diamond MI, Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum Mol Genet. 2003;12(12):1377-91.
    • (2003) Hum. Mol. Genet. , vol.12 , Issue.12 , pp. 1377-1391
    • Cowan, K.J.1    Diamond, M.I.2    Welch, W.J.3
  • 15
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3
    • 1:CAS:528:DC%2BD3sXkvVKjt70%3D 12832059
    • Wen FC, Li YH, Tsai HF, Lin CH, Li C, Liu CS, et al. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. FEBS Lett. 2003;546(2-3):307-14.
    • (2003) FEBS Lett. , vol.546 , Issue.2-3 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3    Lin, C.H.4    Li, C.5    Liu, C.S.6
  • 16
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • 1:CAS:528:DC%2BD2cXkvVSrs7c%3D 15115766
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, Mestril R, et al. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum Mol Genet. 2004;13(13):1389-405.
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6
  • 17
    • 34447331291 scopus 로고    scopus 로고
    • Hsp27 overexpression in the R6/2 mouse model of Huntington's disease: Chronic neurodegeneration does not induce Hsp27 activation
    • 1:CAS:528:DC%2BD2sXntVKqsLk%3D 17360721
    • Zourlidou A, Gidalevitz T, Kristiansen M, Landles C, Woodman B, Wells DJ, et al. Hsp27 overexpression in the R6/2 mouse model of Huntington's disease: chronic neurodegeneration does not induce Hsp27 activation. Hum Mol Genet. 2007;16(9):1078-90.
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.9 , pp. 1078-1090
    • Zourlidou, A.1    Gidalevitz, T.2    Kristiansen, M.3    Landles, C.4    Woodman, B.5    Wells, D.J.6
  • 18
    • 33645401537 scopus 로고    scopus 로고
    • Proteomics of the retinal pigment epithelium reveals altered protein expression at progressive stages of age-related macular degeneration
    • 16505012 10.1167/iovs.05-0976
    • Nordgaard CL, Berg KM, Kapphahn R, Reilly C, Feng X, Olsen TW, et al. Proteomics of the retinal pigment epithelium reveals altered protein expression at progressive stages of age-related macular degeneration. Invest Ophthalmol Vis Sci. 2006;47(3):815-22.
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , Issue.3 , pp. 815-822
    • Nordgaard, C.L.1    Berg, K.M.2    Kapphahn, R.3    Reilly, C.4    Feng, X.5    Olsen, T.W.6
  • 19
    • 33947383078 scopus 로고    scopus 로고
    • Changes in select redox proteins of the retinal pigment epithelium in age-related macular degeneration
    • 1:CAS:528:DC%2BD2sXjsVWitb0%3D 2365890 17280640
    • Decanini A, Nordgaard CL, Feng X, Ferrington DA, Olsen TW. Changes in select redox proteins of the retinal pigment epithelium in age-related macular degeneration. Am J Ophthalmol. 2007;143(4):607-15.
    • (2007) Am J. Ophthalmol. , vol.143 , Issue.4 , pp. 607-615
    • Decanini, A.1    Nordgaard, C.L.2    Feng, X.3    Ferrington, D.A.4    Olsen, T.W.5
  • 20
    • 48249104648 scopus 로고    scopus 로고
    • Mitochondrial proteomics of the retinal pigment epithelium at progressive stages of age-related macular degeneration
    • 18344451 10.1167/iovs.07-1352
    • Nordgaard CL, Karunadharma PP, Feng X, Olsen TW, Ferrington DA. Mitochondrial proteomics of the retinal pigment epithelium at progressive stages of age-related macular degeneration. Invest Ophthalmol Vis Sci. 2008;49(7):2848-55.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , Issue.7 , pp. 2848-2855
    • Nordgaard, C.L.1    Karunadharma, P.P.2    Feng, X.3    Olsen, T.W.4    Ferrington, D.A.5
  • 22
    • 4644284867 scopus 로고    scopus 로고
    • Survival of retinal pigment epithelium after exposure to prolonged oxidative injury: A detailed gene expression and cellular analysis
    • 15452088
    • Strunnikova N, Zhang C, Teichberg D, Cousins SW, Baffi J, Becker KG, et al. Survival of retinal pigment epithelium after exposure to prolonged oxidative injury: A detailed gene expression and cellular analysis. Invest Ophthalmol Vis Sci. 2004;45(10):3767-77.
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , Issue.10 , pp. 3767-3777
    • Strunnikova, N.1    Zhang, C.2    Teichberg, D.3    Cousins, S.W.4    Baffi, J.5    Becker, K.G.6
  • 23
    • 58149398237 scopus 로고    scopus 로고
    • Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
    • 1:CAS:528:DC%2BD1MXnvFCksLs%3D 18989099
    • Kurz T, Brunk UT. Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form. Autophagy. 2009;5(1):93-5.
    • (2009) Autophagy , vol.5 , Issue.1 , pp. 93-95
    • Kurz, T.1    Brunk, U.T.2
  • 24
    • 84887372043 scopus 로고    scopus 로고
    • Autophagy of iron-binding proteins may contribute to the oxidative stress resistance of ARPE-19 cells
    • Karlsson M, Frennesson C, Gustafsson T, Brunk UT, Nilsson SEG, Kurz T. Autophagy of iron-binding proteins may contribute to the oxidative stress resistance of ARPE-19 cells. Exp Eye Res. 2013;116 (359-365.
    • (2013) Exp Eye Res , vol.116 , pp. 359-365
    • Karlsson, M.1    Frennesson, C.2    Gustafsson, T.3    Brunk, U.T.4    Seg, N.5    Kurz, T.6
  • 26
    • 80055015419 scopus 로고    scopus 로고
    • Celastrol regulates innate immunity response via NF-kappa B and Hsp70 in human retinal pigment epithelial cells
    • 1:CAS:528:DC%2BC3MXht1WqtLnL 21683142
    • Paimela T, Hyttinen JMT, Viiri J, Ryhänen T, Karjalainen RO, Salminen A, et al. Celastrol regulates innate immunity response via NF-kappa B and Hsp70 in human retinal pigment epithelial cells. Pharmacol Res. 2011;64(5):501-8.
    • (2011) Pharmacol. Res. , vol.64 , Issue.5 , pp. 501-508
    • Paimela, T.1    Hyttinen, J.M.T.2    Viiri, J.3    Ryhänen, T.4    Karjalainen, R.O.5    Salminen, A.6
  • 27
    • 84861144268 scopus 로고    scopus 로고
    • Proteomic profiling of human retinal pigment epithelium exposed to an advanced glycation-modified substrate
    • 1:CAS:528:DC%2BC38Xjt1Crtb0%3D 3673018 22081232
    • Glenn JV, Mahaffy H, Dasari S, Oliver M, Chen M, Boulton ME, et al. Proteomic profiling of human retinal pigment epithelium exposed to an advanced glycation-modified substrate. Graefes Arch Clin Exp Ophthalmol. 2012;250(3):349-59.
    • (2012) Graefes Arch. Clin. Exp. Ophthalmol. , vol.250 , Issue.3 , pp. 349-359
    • Glenn, J.V.1    Mahaffy, H.2    Dasari, S.3    Oliver, M.4    Chen, M.5    Boulton, M.E.6
  • 29
    • 0024595042 scopus 로고
    • Re-examination and further development of a precise and rapid Dye method for measuring cell-growth cell kill
    • 1:STN:280:DyaL1M3ls1OitA%3D%3D 2470825
    • Hansen MB, Nielsen SE, Berg K. Re-examination and further development of a precise and rapid Dye method for measuring cell-growth cell kill. J Immunol Methods. 1989;119(2):203-10.
    • (1989) J. Immunol. Methods , vol.119 , Issue.2 , pp. 203-210
    • Hansen, M.B.1    Nielsen, S.E.2    Berg, K.3
  • 30
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • 1:CAS:528:DyaK1cXkslSqur4%3D 9674429
    • Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell. 1998;94(1):73-82.
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 31
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • 1:CAS:528:DyaK1MXns1Oqtrw%3D 24133 10570141
    • Goloubinoff P, Mogk A, Ben Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci U S A. 1999;96(24):13732-7.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.24 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Ben Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 32
    • 84880515581 scopus 로고    scopus 로고
    • Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
    • 1:CAS:528:DC%2BC3sXhtFeksbvK 3774407 23737532
    • Mattoo RUH, Sharma SK, Priya S, Finka A, Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem. 2013;288(29):21399-411.
    • (2013) J. Biol. Chem. , vol.288 , Issue.29 , pp. 21399-21411
    • Mattoo, R.U.H.1    Sharma, S.K.2    Priya, S.3    Finka, A.4    Goloubinoff, P.5
  • 33
    • 84866398752 scopus 로고    scopus 로고
    • Intraocular pharmacokinetics of ranibizumab following a single intravitreal injection in humans
    • 1:CAS:528:DC%2BC38XhtV2itLvN 22818800
    • Krohne TU, Liu ZP, Holz FG, Meyer CH. Intraocular pharmacokinetics of ranibizumab following a single intravitreal injection in humans. Am J Ophthalmol. 2012;154(4):682-6.
    • (2012) Am J. Ophthalmol. , vol.154 , Issue.4 , pp. 682-686
    • Krohne, T.U.1    Liu, Z.P.2    Holz, F.G.3    Meyer, C.H.4
  • 34
    • 84875435647 scopus 로고    scopus 로고
    • Pharmacokinetics of ranibizumab in patients with neovascular Age-related macular degeneration: A population approach
    • 1:CAS:528:DC%2BC3sXnsVCgsLg%3D 23361508
    • Xu L, Lu T, Tuomi L, Jumbe N, Lu JF, Eppler S, et al. Pharmacokinetics of ranibizumab in patients with neovascular Age-related macular degeneration: a population approach. Invest Ophthalmol Vis Sci. 2013;54(3):1616-24.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , Issue.3 , pp. 1616-1624
    • Xu, L.1    Lu, T.2    Tuomi, L.3    Jumbe, N.4    Lu, J.F.5    Eppler, S.6
  • 35
    • 84876460284 scopus 로고    scopus 로고
    • Antiapoptotic properties of alpha-crystallin-derived peptide chaperones and characterization of their uptake transporters in human RPE cells
    • 1:CAS:528:DC%2BC3sXhtVyjsb3I 3632268 23532520
    • Sreekumar PG, Chothe P, Sharma KK, Baid R, Kompella U, Spee C, et al. Antiapoptotic properties of alpha-crystallin-derived peptide chaperones and characterization of their uptake transporters in human RPE cells. Invest Ophthalmol Vis Sci. 2013;54(4):2787-98.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , Issue.4 , pp. 2787-2798
    • Sreekumar, P.G.1    Chothe, P.2    Sharma, K.K.3    Baid, R.4    Kompella, U.5    Spee, C.6
  • 36
    • 0037392838 scopus 로고    scopus 로고
    • Vitreous is a barrier in nonviral gene transfer by cationic lipids and polymers
    • 12739764 10.1023/A:1023238530504
    • Pitkänen L, Ruponen M, Nieminen J, Urtti A. Vitreous is a barrier in nonviral gene transfer by cationic lipids and polymers. Pharm Res. 2003;20(4):576-83.
    • (2003) Pharm. Res. , vol.20 , Issue.4 , pp. 576-583
    • Pitkänen, L.1    Ruponen, M.2    Nieminen, J.3    Urtti, A.4
  • 37
    • 34848928410 scopus 로고    scopus 로고
    • Intravitreal injections of GDNF-loaded biodegradable microspheres are neuroprotective in a rat model of glaucoma
    • 1:CAS:528:DC%2BD2sXhtleqt73F 17960131
    • Jiang C, Moore MJ, Zhang X, Klassen H, Langer R, Young M. Intravitreal injections of GDNF-loaded biodegradable microspheres are neuroprotective in a rat model of glaucoma. Mol Vis. 2007;13(198-99):1783-92.
    • (2007) Mol. Vis. , vol.13 , Issue.198 , pp. 1783-1792
    • Jiang, C.1    Moore, M.J.2    Zhang, X.3    Klassen, H.4    Langer, R.5    Young, M.6
  • 38
    • 80855130893 scopus 로고    scopus 로고
    • Retinal ganglion cells survival in a glaucoma model by GDNF/Vit e PLGA microspheres prepared according to a novel microencapsulation procedure
    • 1:CAS:528:DC%2BC3MXhsVGntrvI 21704662
    • Checa-Casalengua P, Jiang CH, Bravo-Osuna I, Tucker BA, Molina-Martinez IT, Young MJ, et al. Retinal ganglion cells survival in a glaucoma model by GDNF/Vit E PLGA microspheres prepared according to a novel microencapsulation procedure. J Control Release. 2011;156(1):92-100.
    • (2011) J. Control. Release , vol.156 , Issue.1 , pp. 92-100
    • Checa-Casalengua, P.1    Jiang, C.H.2    Bravo-Osuna, I.3    Tucker, B.A.4    Molina-Martinez, I.T.5    Young, M.J.6
  • 40
    • 34548055674 scopus 로고    scopus 로고
    • Prolonged protective effect of basic fibroblast growth factor-impregnated nanoparticles in royal college of surgeons rats
    • 17591912 10.1167/iovs.06-1242
    • Sakai T, Kuno N, Takamatsu F, Kimura E, Kohno H, Okano K, et al. Prolonged protective effect of basic fibroblast growth factor-impregnated nanoparticles in royal college of surgeons rats. Invest Ophthalmol Vis Sci. 2007;48(7):3381-7.
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , Issue.7 , pp. 3381-3387
    • Sakai, T.1    Kuno, N.2    Takamatsu, F.3    Kimura, E.4    Kohno, H.5    Okano, K.6
  • 41
    • 66349109049 scopus 로고    scopus 로고
    • Preparation, characterization, and in vivo evaluation of nanoliposomes-encapsulated bevacizumab (avastin) for intravitreal administration
    • Abrishami M, Ganavati SZ, Soroush D, Rouhbakhsh M, Jaafari MR, Malaekeh-Nikouei B. Preparation, characterization, and in vivo evaluation of nanoliposomes-encapsulated bevacizumab (avastin) for intravitreal administration. Retina-J Ret Vit Dis. 2009;29(5):699-703.
    • (2009) Retina-J Ret Vit Dis , vol.29 , Issue.5 , pp. 699-703
    • Abrishami, M.1    Ganavati, S.Z.2    Soroush, D.3    Rouhbakhsh, M.4    Jaafari, M.R.5    Malaekeh-Nikouei, B.6
  • 42
    • 79955032437 scopus 로고    scopus 로고
    • Ciliary neurotrophic factor delivered by encapsulated cell intraocular implants for treatment of geographic atrophy in age-related macular degeneration
    • 1:CAS:528:DC%2BC3MXltVOqsrc%3D 3076847 21444807
    • Zhang K, Hopkins JJ, Heier JS, Birch DG, Halperin LS, Albini TA, et al. Ciliary neurotrophic factor delivered by encapsulated cell intraocular implants for treatment of geographic atrophy in age-related macular degeneration. Proc Natl Acad Sci U S A. 2011;108(15):6241-5.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.15 , pp. 6241-6245
    • Zhang, K.1    Hopkins, J.J.2    Heier, J.S.3    Birch, D.G.4    Halperin, L.S.5    Albini, T.A.6
  • 43
    • 77955432662 scopus 로고    scopus 로고
    • Delivery of drug macromolecules from thermally responsive gel implants to the posterior eye
    • 1:CAS:528:DC%2BC3cXpvVKht70%3D
    • Ninawe PR, Hatziavramidis D, Parulekar SJ. Delivery of drug macromolecules from thermally responsive gel implants to the posterior eye. Chem Eng Sci. 2010;65(18):5170-7.
    • (2010) Chem. Eng. Sci. , vol.65 , Issue.18 , pp. 5170-5177
    • Ninawe, P.R.1    Hatziavramidis, D.2    Parulekar, S.J.3


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