메뉴 건너뛰기




Volumn 324, Issue 4, 2004, Pages 1199-1203

pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27 kDa (HspB1)

Author keywords

Acidosis; Phosphorylation; Small heat shock proteins; Structure

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 24; HEAT SHOCK PROTEIN 27; OLIGOMER; SERINE; UNCLASSIFIED DRUG; HSPB1 PROTEIN, HUMAN; TUMOR PROTEIN;

EID: 14344264502     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.176     Document Type: Article
Times cited : (22)

References (31)
  • 1
    • 0036809333 scopus 로고    scopus 로고
    • SHsps and their role in the chaperone network
    • M. Haslbeck sHsps and their role in the chaperone network Cell. Mol. Life Sci. 59 2002 1649 1657
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1649-1657
    • Haslbeck, M.1
  • 2
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • J. Horwitz Alpha-crystallin Exp. Eye Res. 76 2003 145 153
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 3
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • N. Mounier, and A.P. Arrigo Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 7 2002 167 176
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 4
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • K.K. Kim, R. Kim, and S.H. Kim Crystal structure of a small heat-shock protein Nature 394 1998 595 599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 6
    • 2542451125 scopus 로고    scopus 로고
    • Essential role of the N-terminal WD/EPF motif in the phosphorylation- activated protective function of mammalian Hsp27
    • J.R. Theriault, H. Lambert, A.T. Chavez-Zobel, G. Charest, P. Lavigne, and J. Landry Essential role of the N-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27 J. Biol. Chem. 279 2004 23463 23471
    • (2004) J. Biol. Chem. , vol.279 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6
  • 7
    • 0033591453 scopus 로고    scopus 로고
    • The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species
    • M. Ehrnsperger, H. Lilie, M. Gaestel, and J. Buchner The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species J. Biol. Chem. 274 1999 14867 14874
    • (1999) J. Biol. Chem. , vol.274 , pp. 14867-14874
    • Ehrnsperger, M.1    Lilie, H.2    Gaestel, M.3    Buchner, J.4
  • 9
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to αb-crystallin
    • K. Kato, S. Goto, Y. Inaguma, K. Hasegawa, R. Morishita, and T. Asano Purification and characterization of a 20-kDa protein that is highly homologous to αB-crystallin J. Biol. Chem. 269 1994 15302 15309
    • (1994) J. Biol. Chem. , vol.269 , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3    Hasegawa, K.4    Morishita, R.5    Asano, T.6
  • 10
    • 0036186869 scopus 로고    scopus 로고
    • Hsp27: Novel regulator of intracellular redox state
    • A.-P. Arrigo Hsp27: novel regulator of intracellular redox state IUBMB Life 52 2001 303 307
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.-P.1
  • 11
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • J.L. Martin, R. Mestril, R. Hilal-Dandan, L.L. Brunton, and W.H. Dillmann Small heat shock proteins and protection against ischemic injury in cardiac myocytes Circulation 96 1997 4343 4348
    • (1997) Circulation , vol.96 , pp. 4343-4348
    • Martin, J.L.1    Mestril, R.2    Hilal-Dandan, R.3    Brunton, L.L.4    Dillmann, W.H.5
  • 12
    • 0033841185 scopus 로고    scopus 로고
    • Ischemic preconditioning: Potential role for constitutive low molecular weight stress protein translocation and phosphorylation?
    • P. Eaton, W.I. Award, J.I. Miller, D.J. Hears, and M.J. Shattock Ischemic preconditioning: potential role for constitutive low molecular weight stress protein translocation and phosphorylation? J. Mol. Cell. Cardiol. 32 2000 680 685
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 680-685
    • Eaton, P.1    Award, W.I.2    Miller, J.I.3    Hears, D.J.4    Shattock, M.J.5
  • 13
    • 0036085215 scopus 로고    scopus 로고
    • Increased expression of HSP 27 protects canine myocytes from simulated ischemia-reperfusion injury
    • R.S.V. Heide Increased expression of HSP 27 protects canine myocytes from simulated ischemia-reperfusion injury Am. J. Physiol. Heart Circ. Physiol. 282 2002 H935 H941
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282
    • Heide, R.S.V.1
  • 15
    • 0035964739 scopus 로고    scopus 로고
    • α-A- and α-B-crystallin prevent irreversible acidification-induced protein denaturation
    • K. Wang α-A- and α-B-crystallin prevent irreversible acidification-induced protein denaturation Biochem. Biophys. Res. Commun. 287 2001 642 647
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 642-647
    • Wang, K.1
  • 18
    • 0035831438 scopus 로고    scopus 로고
    • Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelet
    • E. Butt, D. Immler, H. Meyer, A. Kotlyarov, K. Laass, and M. Gaestel Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelet J. Biol. Chem. 276 2001 7108 7113
    • (2001) J. Biol. Chem. , vol.276 , pp. 7108-7113
    • Butt, E.1    Immler, D.2    Meyer, H.3    Kotlyarov, A.4    Laass, K.5    Gaestel, M.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 21
    • 0029841943 scopus 로고    scopus 로고
    • Exposed hydrophobic sites in factor VIII and isolated subunits
    • K. Sudhakar, and P.J. Fay Exposed hydrophobic sites in factor VIII and isolated subunits J. Biol. Chem. 271 1996 23015 23021
    • (1996) J. Biol. Chem. , vol.271 , pp. 23015-23021
    • Sudhakar, K.1    Fay, P.J.2
  • 22
    • 0034673175 scopus 로고    scopus 로고
    • PH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin
    • T. Hochgrebe, G.J. Pankhurst, J. Wilce, and S.B. Easterbrook-Smith pH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin Biochemistry 39 2000 1411 1419
    • (2000) Biochemistry , vol.39 , pp. 1411-1419
    • Hochgrebe, T.1    Pankhurst, G.J.2    Wilce, J.3    Easterbrook-Smith, S.B.4
  • 23
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 24
    • 0035895908 scopus 로고    scopus 로고
    • Phosphorylation-induced changes of the oligomeric state of αb-crystallin
    • H. Ito, K. Kamei, I. Iwamoto, Y. Inaguma, D. Nohara, and K. Kato Phosphorylation-induced changes of the oligomeric state of αB-crystallin J. Biol. Chem. 276 2001 5346 5352
    • (2001) J. Biol. Chem. , vol.276 , pp. 5346-5352
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Nohara, D.5    Kato, K.6
  • 25
    • 0036402632 scopus 로고    scopus 로고
    • C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αb-crystallin
    • J.H. Liao, J.-S. Lee, and H. Chiou C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-crystallin Biochem. Biophys. Res. Commun. 297 2002 309 316
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 309-316
    • Liao, J.H.1    Lee, J.-S.2    Chiou, H.3
  • 26
    • 0032077161 scopus 로고    scopus 로고
    • The effect of the intersubunit disulfide bond on the structure and functional properties of the small heat shock protein Hsp25
    • A. Zavialov, R. Benndorf, M. Ehrnsperger, V. Zav'yalov, I. Dudich, J. Buchner, and M. Gaestel The effect of the intersubunit disulfide bond on the structure and functional properties of the small heat shock protein Hsp25 Int. J. Biol. Macromol. 22 1998 163 173
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 163-173
    • Zavialov, A.1    Benndorf, R.2    Ehrnsperger, M.3    Zav'Yalov, V.4    Dudich, I.5    Buchner, J.6    Gaestel, M.7
  • 27
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1′-bis(4-anilino)naphthalene-5,5′-disulfonic acid with α-crystallin
    • K. Sharma, H. Kaur, G.S. Kumar, and K. Kester Interaction of 1,1′-bis(4-anilino)naphthalene-5,5′-disulfonic acid with α-crystallin J. Biol. Chem. 273 1998 8965 8970
    • (1998) J. Biol. Chem. , vol.273 , pp. 8965-8970
    • Sharma, K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 30
    • 2342496707 scopus 로고    scopus 로고
    • Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress
    • Y. Katoh, M. Fujimoto, K. Nakamura, S. Inouye, K. Sugahara, H. Izu, and A. Nakai Hsp25, a member of the Hsp30 family, promotes inclusion formation in response to stress FEBS Lett. 565 2004 28 32
    • (2004) FEBS Lett. , vol.565 , pp. 28-32
    • Katoh, Y.1    Fujimoto, M.2    Nakamura, K.3    Inouye, S.4    Sugahara, K.5    Izu, H.6    Nakai, A.7
  • 31
    • 0034613078 scopus 로고    scopus 로고
    • Self-complementary motifs (SCM) in α-crystallin small heat shock proteins
    • P.N. Farnsworth, and K. Singh Self-complementary motifs (SCM) in α-crystallin small heat shock proteins FEBS Lett. 482 2000 175 179
    • (2000) FEBS Lett. , vol.482 , pp. 175-179
    • Farnsworth, P.N.1    Singh, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.