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Volumn 89, Issue 2, 2011, Pages 162-175

Differential expression and induction of small heat shock proteins in rat brain and cultured hippocampal neurons

Author keywords

crystallin; Hippocampus; Neuroprotection; Small heat shock proteins; Stress tolerance

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 25; MESSENGER RNA; RNA; SMALL HEAT SHOCK PROTEIN;

EID: 78650187121     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.22536     Document Type: Article
Times cited : (65)

References (66)
  • 5
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M. 1992. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 712: 288-294.
    • (1992) Circ Res , vol.712 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 7
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and nonocular tissues
    • Bhat SP, Nagineni CN. 1989. Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and nonocular tissues. Biochem Biophys Res Commun 1581: 319-325.
    • (1989) Biochem Biophys Res Commun , vol.1581 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 8
    • 0025636488 scopus 로고
    • Isolation and characterization of five new soluble placental tissue proteins (PP22, PP23, PP24, PP25, PP26)
    • Bohn H, Winckler W. 1991. Isolation and characterization of five new soluble placental tissue proteins (PP22, PP23, PP24, PP25, PP26). Arch Gynecol Obstet 2483: 111-115.
    • (1991) Arch Gynecol Obstet , vol.2483 , pp. 111-115
    • Bohn, H.1    Winckler, W.2
  • 9
    • 40549112638 scopus 로고    scopus 로고
    • Reference genes for normalization: a study of rat brain tissue
    • Bonefeld BE, Elfving B, Wegener G. 2008. Reference genes for normalization: a study of rat brain tissue. Synapse 624: 302-309.
    • (2008) Synapse , vol.624 , pp. 302-309
    • Bonefeld, B.E.1    Elfving, B.2    Wegener, G.3
  • 11
    • 34247272428 scopus 로고    scopus 로고
    • Therapeutic potential of H11 kinase for the ischemic heart
    • Danan IJ, Rashed ER, Depre C. 2007. Therapeutic potential of H11 kinase for the ischemic heart. Cardiovasc Drug Rev 251: 14-29.
    • (2007) Cardiovasc Drug Rev , vol.251 , pp. 14-29
    • Danan, I.J.1    Rashed, E.R.2    Depre, C.3
  • 12
    • 33745496759 scopus 로고    scopus 로고
    • The emerging complexity of the vertebrate cilium: new functional roles for an ancient organelle
    • Davis EE, Brueckner M, Katsanis N. 2006. The emerging complexity of the vertebrate cilium: new functional roles for an ancient organelle. Dev Cell 111: 9-19.
    • (2006) Dev Cell , vol.111 , pp. 9-19
    • Davis, E.E.1    Brueckner, M.2    Katsanis, N.3
  • 14
  • 16
    • 1342281718 scopus 로고    scopus 로고
    • Neuronal primary cilia: a review
    • Fuchs JL, Schwark HD. 2004. Neuronal primary cilia: a review. Cell Biol Int 282: 111-118.
    • (2004) Cell Biol Int , vol.282 , pp. 111-118
    • Fuchs, J.L.1    Schwark, H.D.2
  • 18
    • 0027193606 scopus 로고
    • Development and tissue-specific distribution of mouse small heat shock protein hsp25
    • Gernold M, Knauf U, Gaestel M, Stahl J, Kloetzel PM. 1993. Development and tissue-specific distribution of mouse small heat shock protein hsp25. Dev Genet 142: 103-111.
    • (1993) Dev Genet , vol.142 , pp. 103-111
    • Gernold, M.1    Knauf, U.2    Gaestel, M.3    Stahl, J.4    Kloetzel, P.M.5
  • 19
    • 33750806555 scopus 로고    scopus 로고
    • Ischemia-induced phosphorylation and translocation of stress protein alpha B-crystallin to Z lines of myocardium
    • Golenhofen N, Ness W, Koob R, Htun P, Schaper W, Drenckhahn D. 1998. Ischemia-induced phosphorylation and translocation of stress protein alpha B-crystallin to Z lines of myocardium. Am J Physiol 2745: H1457-H1464.
    • (1998) Am J Physiol , vol.2745
    • Golenhofen, N.1    Ness, W.2    Koob, R.3    Htun, P.4    Schaper, W.5    Drenckhahn, D.6
  • 20
    • 0036517816 scopus 로고    scopus 로고
    • Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin
    • Golenhofen N, Arbeiter A, Koob R, Drenckhahn D. 2002. Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin. J Mol Cell Cardiol 343: 309-319.
    • (2002) J Mol Cell Cardiol , vol.343 , pp. 309-319
    • Golenhofen, N.1    Arbeiter, A.2    Koob, R.3    Drenckhahn, D.4
  • 22
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • Gusev NB, Bogatcheva NV, Marston SB. 2002. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Moscow) 675: 511-519.
    • (2002) Biochemistry (Moscow) , vol.675 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 24
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: the structure and function of small heat-shock proteins
    • Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. 2005. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 1210: 842-846.
    • (2005) Nat Struct Mol Biol , vol.1210 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 25
    • 0001726511 scopus 로고
    • A new method for the quantitative determination of antibody and antigen protein, with a sensitivity to five micrograms
    • Heinzel W, Vogt A, Kallee E, Faller W. 1965. A new method for the quantitative determination of antibody and antigen protein, with a sensitivity to five micrograms. J Lab Clin Med 66: 334-340.
    • (1965) J Lab Clin Med , vol.66 , pp. 334-340
    • Heinzel, W.1    Vogt, A.2    Kallee, E.3    Faller, W.4
  • 26
    • 10044254417 scopus 로고    scopus 로고
    • Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model
    • 11023
    • Hollander JM, Martin JL, Belke DD, Scott BT, Swanson E, Krishnamoorthy V, Dillmann WH. 2004. Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model. Circulation 11023: 3544-3552.
    • (2004) Circulation , pp. 3544-3552
    • Hollander, J.M.1    Martin, J.L.2    Belke, D.D.3    Scott, B.T.4    Swanson, E.5    Krishnamoorthy, V.6    Dillmann, W.H.7
  • 27
    • 0026575146 scopus 로고
    • Translocation and induction of alpha B crystallin by heat shock in rat glioma (GA-1) cells
    • Inaguma Y, Shinohara H, Goto S, Kato K. 1992. Translocation and induction of alpha B crystallin by heat shock in rat glioma (GA-1) cells. Biochem Biophys Res Commun 1822: 844-850.
    • (1992) Biochem Biophys Res Commun , vol.1822 , pp. 844-850
    • Inaguma, Y.1    Shinohara, H.2    Goto, S.3    Kato, K.4
  • 29
    • 0025101570 scopus 로고
    • Cellular distribution of alpha B-crystallin in nonlenticular tissues
    • Iwaki T, Kume-Iwaki A, Goldman JE. 1990. Cellular distribution of alpha B-crystallin in nonlenticular tissues. J Histochem Cytochem 381: 31-39.
    • (1990) J Histochem Cytochem , vol.381 , pp. 31-39
    • Iwaki, T.1    Kume-Iwaki, A.2    Goldman, J.E.3
  • 32
    • 77955665257 scopus 로고    scopus 로고
    • Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB
    • Kappe G, Boelens WC, de Jong WW. 2010. Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB. Cell Stress Chaperones 154: 457-461.
    • (2010) Cell Stress Chaperones , vol.154 , pp. 457-461
    • Kappe, G.1    Boelens, W.C.2    de Jong, W.W.3
  • 33
    • 0025877859 scopus 로고
    • Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system
    • 10741
    • Kato K, Shinohara H, Kurobe N, Inaguma Y, Shimizu K, Ohshima K. 1991. Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system. Biochim Biophys Acta 10741: 201-208.
    • (1991) Biochim Biophys Acta , pp. 201-208
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Inaguma, Y.4    Shimizu, K.5    Ohshima, K.6
  • 34
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin
    • 26921
    • Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita R, Asano T. 1994. Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin. J Biol Chem 26921: 15302-15309.
    • (1994) J Biol Chem , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3    Hasegawa, K.4    Morishita, R.5    Asano, T.6
  • 35
    • 0029065339 scopus 로고
    • An immunohistochemical study of heat shock protein-27 in the hippocampus in a gerbil model of cerebral ischemia and ischemic tolerance
    • Kato H, Araki T, Itoyama Y, Kogure K, Kato K. 1995. An immunohistochemical study of heat shock protein-27 in the hippocampus in a gerbil model of cerebral ischemia and ischemic tolerance. Neuroscience 681: 65-71.
    • (1995) Neuroscience , vol.681 , pp. 65-71
    • Kato, H.1    Araki, T.2    Itoyama, Y.3    Kogure, K.4    Kato, K.5
  • 37
    • 0030665373 scopus 로고    scopus 로고
    • Expression and subcellular localization of p42IP4/centaurin-alpha, a brain-specific, high-affinity receptor for inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate in rat brain
    • Kreutz MR, Bockers TM, Sabel BA, Hulser E, Stricker R, Reiser G. 1997. Expression and subcellular localization of p42IP4/centaurin-alpha, a brain-specific, high-affinity receptor for inositol 1, 3, 4, 5-tetrakisphosphate and phosphatidylinositol 3, 4, 5-trisphosphate in rat brain. Eur J Neurosci 910: 2110-2124.
    • (1997) Eur J Neurosci , vol.910 , pp. 2110-2124
    • Kreutz, M.R.1    Bockers, T.M.2    Sabel, B.A.3    Hulser, E.4    Stricker, R.5    Reiser, G.6
  • 38
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J. 1984. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods 103-4: 203-209.
    • (1984) J Biochem Biophys Methods , vol.103-104 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 227259
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227259: 680-685.
    • (1970) Nature , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 68949198337 scopus 로고    scopus 로고
    • Alpha A-crystallin and alpha B-crystallin, newly identified interaction proteins of protease-activated receptor-2, rescue astrocytes from C2-ceramide- and staurosporine-induced cell death
    • Li R, Rohatgi T, Hanck T, Reiser G. 2009. Alpha A-crystallin and alpha B-crystallin, newly identified interaction proteins of protease-activated receptor-2, rescue astrocytes from C2-ceramide- and staurosporine-induced cell death. J Neurochem 1105: 1433-1444.
    • (2009) J Neurochem , vol.1105 , pp. 1433-1444
    • Li, R.1    Rohatgi, T.2    Hanck, T.3    Reiser, G.4
  • 41
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. 1986. The heat-shock response. Annu Rev Biochem 55: 1151-1191.
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 42
    • 34748840772 scopus 로고    scopus 로고
    • Regulation of hypothalamic expression of KiSS-1 and GPR54 genes by metabolic factors: analyses using mouse models and a cell line
    • 14810
    • Luque RM, Kineman RD, Tena-Sempere M. 2007. Regulation of hypothalamic expression of KiSS-1 and GPR54 genes by metabolic factors: analyses using mouse models and a cell line. Endocrinology 14810: 4601-4611.
    • (2007) Endocrinology , pp. 4601-4611
    • Luque, R.M.1    Kineman, R.D.2    Tena-Sempere, M.3
  • 44
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry CE, Jennings RB, Reimer KA. 1986. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 745: 1124-1136.
    • (1986) Circulation , vol.745 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 45
    • 0028104679 scopus 로고
    • Cognitive deficits induced by global cerebral ischaemia: relationship to brain damage and reversal by transplants
    • Nunn J, Hodges H. 1994. Cognitive deficits induced by global cerebral ischaemia: relationship to brain damage and reversal by transplants. Behav Brain Res 651: 1-31.
    • (1994) Behav Brain Res , vol.651 , pp. 1-31
    • Nunn, J.1    Hodges, H.2
  • 46
    • 39049111571 scopus 로고    scopus 로고
    • Correlation between the progressive cytoplasmic expression of a novel small heat shock protein (Hsp16.2) and malignancy in brain tumors
    • Pozsgai E, Gomori E, Szigeti A, Boronkai A, Gallyas FJr, Sumegi B, Bellyei S. 2007. Correlation between the progressive cytoplasmic expression of a novel small heat shock protein (Hsp16.2) and malignancy in brain tumors. BMC Cancer 7: 233.
    • (2007) BMC Cancer , vol.7 , pp. 233
    • Pozsgai, E.1    Gomori, E.2    Szigeti, A.3    Boronkai, A.4    Gallyas Jr, F.5    Sumegi, B.6    Bellyei, S.7
  • 47
    • 42749092501 scopus 로고    scopus 로고
    • Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization
    • Quraishe S, Asuni A, Boelens WC, O'Connor V, Wyttenbach A. 2008. Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization. Neuroscience 1532: 483-491.
    • (2008) Neuroscience , vol.1532 , pp. 483-491
    • Quraishe, S.1    Asuni, A.2    Boelens, W.C.3    O'Connor, V.4    Wyttenbach, A.5
  • 48
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • Ray PS, Martin JL, Swanson EA, Otani H, Dillmann WH, Das DK. 2001. Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 152: 393-402.
    • (2001) FASEB J , vol.152 , pp. 393-402
    • Ray, P.S.1    Martin, J.L.2    Swanson, E.A.3    Otani, H.4    Dillmann, W.H.5    Das, D.K.6
  • 49
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • Ritossa FM. 1962. A new puffing pattern induced by a temperature shock and DNP in Drosophila. Experientia 18: 571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 50
    • 4444337502 scopus 로고    scopus 로고
    • Mathematics of quantitative kinetic PCR and the application of standard curves
    • Rutledge RG, Côté C. 2003. Mathematics of quantitative kinetic PCR and the application of standard curves. Nucleic Acids Res 3116: e93.
    • (2003) Nucleic Acids Res , vol.3116
    • Rutledge, R.G.1    Côté, C.2
  • 51
    • 0032902813 scopus 로고    scopus 로고
    • Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium
    • Shama KM, Suzuki A, Harada K, Fujitani N, Kimura H, Ohno S, Yoshida K. 1999. Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium. Cell Struct Funct 241: 1-4.
    • (1999) Cell Struct Funct , vol.241 , pp. 1-4
    • Shama, K.M.1    Suzuki, A.2    Harada, K.3    Fujitani, N.4    Kimura, H.5    Ohno, S.6    Yoshida, K.7
  • 52
    • 67349215120 scopus 로고    scopus 로고
    • AlphaB-crystallin suppresses oxidative stress-induced astrocyte apoptosis by inhibiting caspase-3 activation
    • Shin JH, Kim SW, Lim CM, Jeong JY, Piao CS, Lee JK. 2009. AlphaB-crystallin suppresses oxidative stress-induced astrocyte apoptosis by inhibiting caspase-3 activation. Neurosci Res 644: 355-361.
    • (2009) Neurosci Res , vol.644 , pp. 355-361
    • Shin, J.H.1    Kim, S.W.2    Lim, C.M.3    Jeong, J.Y.4    Piao, C.S.5    Lee, J.K.6
  • 54
    • 58149402446 scopus 로고    scopus 로고
    • Hsp27 protects against ischemic brain injury via attenuation of a novel stress-response cascade upstream of mitochondrial cell death signaling
    • Stetler RA, Cao G, Gao Y, Zhang F, Wang S, Weng Z, Vosler P, Zhang L, Signore A, Graham SH, Chen J. 2008. Hsp27 protects against ischemic brain injury via attenuation of a novel stress-response cascade upstream of mitochondrial cell death signaling. J Neurosci 2849: 13038-13055.
    • (2008) J Neurosci , vol.2849 , pp. 13038-13055
    • Stetler, R.A.1    Cao, G.2    Gao, Y.3    Zhang, F.4    Wang, S.5    Weng, Z.6    Vosler, P.7    Zhang, L.8    Signore, A.9    Graham, S.H.10    Chen, J.11
  • 55
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • 27211
    • Sun Y, MacRae TH. 2005. The small heat shock proteins and their role in human disease. FEBS J 27211: 2613-2627.
    • (2005) FEBS J , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 56
    • 0038638997 scopus 로고    scopus 로고
    • Dual perinatal and developmental expression of the small heat shock proteins [FC12]aB-crystallin and Hsp27 in different tissues of the developing piglet
    • Tallot P, Grongnet JF, David JC. 2003. Dual perinatal and developmental expression of the small heat shock proteins [FC12]aB-crystallin and Hsp27 in different tissues of the developing piglet. Biol Neonate 834: 281-288.
    • (2003) Biol Neonate , vol.834 , pp. 281-288
    • Tallot, P.1    Grongnet, J.F.2    David, J.C.3
  • 57
    • 70349781683 scopus 로고    scopus 로고
    • Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes
    • 31518
    • Tucker NR, Shelden EA. 2009. Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes. Exp Cell Res 31518: 3176-3186.
    • (2009) Exp Cell Res , pp. 3176-3186
    • Tucker, N.R.1    Shelden, E.A.2
  • 58
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F. 2002. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 37: RESEARCH0034.
    • (2002) Genome Biol , vol.37
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 60
    • 0242407366 scopus 로고    scopus 로고
    • Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig
    • Verschuure P, Tatard C, Boelens WC, Grongnet JF, David JC. 2003. Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Eur J Cell Biol 8210: 523-530.
    • (2003) Eur J Cell Biol , vol.8210 , pp. 523-530
    • Verschuure, P.1    Tatard, C.2    Boelens, W.C.3    Grongnet, J.F.4    David, J.C.5
  • 61
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos MJ, Hageman J, Carra S, Kampinga HH. 2008. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 4727: 7001-7011.
    • (2008) Biochemistry , vol.4727 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 62
    • 39749113234 scopus 로고    scopus 로고
    • Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases
    • Wang J, Martin E, Gonzales V, Borchelt DR, Lee MK. 2008. Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases. Neurobiol Aging 294: 586-597.
    • (2008) Neurobiol Aging , vol.294 , pp. 586-597
    • Wang, J.1    Martin, E.2    Gonzales, V.3    Borchelt, D.R.4    Lee, M.K.5
  • 63
    • 0026460892 scopus 로고
    • Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch WJ. 1992. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol Rev 724: 1063-1081.
    • (1992) Physiol Rev , vol.724 , pp. 1063-1081
    • Welch, W.J.1
  • 64
    • 33646190092 scopus 로고    scopus 로고
    • Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity
    • Wilhelmus MM, Boelens WC, Otte-Holler I, Kamps B, Kusters B, Maat-Schieman ML, de Waal RM, Verbeek MM. 2006a. Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity. Acta Neuropathol 1112: 139-149.
    • (2006) Acta Neuropathol , vol.1112 , pp. 139-149
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Holler, I.3    Kamps, B.4    Kusters, B.5    Maat-Schieman, M.L.6    de Waal, R.M.7    Verbeek, M.M.8


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