메뉴 건너뛰기




Volumn 8, Issue , 2002, Pages 359-366

Decreased heat stability and increased chaperone requirement of modified human βB1-crystallins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; LENS PROTEIN; MONOMER; OLIGOMER;

EID: 0041339004     PISSN: 10900535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (53)

References (23)
  • 2
    • 0030614501 scopus 로고    scopus 로고
    • Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens
    • Lampi KJ, Ma Z, Shih M, Shearer TR, Smith JB, Smith DL, David LL. Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. J Biol Chem 1997; 272:2268-75.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2268-2275
    • Lampi, K.J.1    Ma, Z.2    Shih, M.3    Shearer, T.R.4    Smith, J.B.5    Smith, D.L.6    David, L.L.7
  • 4
    • 0030893023 scopus 로고    scopus 로고
    • Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1
    • Ajaz MS, Ma Z, Smith DL, Smith JB. Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1. J Biol Chem 1997; 272:11250-5.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11250-11255
    • Ajaz, M.S.1    Ma, Z.2    Smith, D.L.3    Smith, J.B.4
  • 5
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 1998; 67:21-30.
    • (1998) Exp. Eye Res. , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5    Smith, J.B.6
  • 6
    • 0029664615 scopus 로고    scopus 로고
    • The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension
    • David LL, Lampi KJ, Lund AL, Smith JB. The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension. J Biol Chem 1996; 271:4273-9.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4273-4279
    • David, L.L.1    Lampi, K.J.2    Lund, A.L.3    Smith, J.B.4
  • 7
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson SR, Hasan A, Smith DL, Smith JB. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp Eye Res 2000; 71:195-207.
    • (2000) Exp. Eye Res. , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 8
    • 0034609357 scopus 로고    scopus 로고
    • Increased deamidation of asparagine during human senile cataractogenesis
    • Takemoto L, Bolye D. Increased deamidation of asparagine during human senile cataractogenesis. Mol Vis 2000; 6:164-8 .
    • (2000) Mol. Vis. , vol.6 , pp. 164-168
    • Takemoto, L.1    Bolye, D.2
  • 9
    • 0003789150 scopus 로고    scopus 로고
    • Identification and characterization of post-translational modifications in human lens beta crystallins during the aging process
    • [dissertation] Lincoln (NE): University of Nebraska-Lincoln
    • Zhang Z. Identification and characterization of post-translational modifications in human lens beta crystallins during the aging process [dissertation]. Lincoln (NE): University of Nebraska-Lincoln; 2001.
    • (2001)
    • Zhang, Z.1
  • 11
    • 0029803592 scopus 로고    scopus 로고
    • The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin
    • Werten PJ, Carver JA, Jaenicke R, de Jong WW. The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin. Protein Eng 1996; 9:1021-8.
    • (1996) Protein Eng. , vol.9 , pp. 1021-1028
    • Werten, P.J.1    Carver, J.A.2    Jaenicke, R.3    de Jong, W.W.4
  • 12
    • 58149365344 scopus 로고
    • WET solvent suppression and its application to LC NMR and high-resolution NMR spectroscopy
    • Smallcombe SH, Patt SL, Keifer PA. WET solvent suppression and its application to LC NMR and high-resolution NMR spectroscopy. Journal of Magnetic Resonance, Series A 1995; 117:295-303.
    • (1995) Journal of Magnetic Resonance, Series A , vol.117 , pp. 295-303
    • Smallcombe, S.H.1    Patt, S.L.2    Keifer, P.A.3
  • 13
    • 0034771090 scopus 로고    scopus 로고
    • Association behaviour of human betaB1-crystallin and its truncated forms
    • Bateman OA, Lubsen NH, Slingsby C. Association behaviour of human betaB1-crystallin and its truncated forms. Exp Eye Res 2001; 73:321-31.
    • (2001) Exp. Eye Res. , vol.73 , pp. 321-331
    • Bateman, O.A.1    Lubsen, N.H.2    Slingsby, C.3
  • 14
    • 0028099860 scopus 로고
    • Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions
    • Cooper PG, Aquilina JA, Truscott RJ, Carver JA. Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions. Exp Eye Res 1994; 59:607-19.
    • (1994) Exp. Eye Res. , vol.59 , pp. 607-619
    • Cooper, P.G.1    Aquilina, J.A.2    Truscott, R.J.3    Carver, J.A.4
  • 15
    • 0034740569 scopus 로고    scopus 로고
    • Resistance of human betaB2-crystallin to in vivo modification
    • Zhang Z, David LL, Smith DL, Smith JB. Resistance of human betaB2-crystallin to in vivo modification. Exp Eye Res 2001; 73:203-11.
    • (2001) Exp. Eye Res. , vol.73 , pp. 203-211
    • Zhang, Z.1    David, L.L.2    Smith, D.L.3    Smith, J.B.4
  • 16
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens alpha-crystallins
    • Lund AL, Smith JB, Smith DL. Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res 1996; 63:661-72.
    • (1996) Exp. Eye Res. , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 17
    • 0028280702 scopus 로고
    • Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions
    • Nalini V, Bax B, Driessen H, Moss DS, Lindley PF, Slingsby C. Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions. J Mol Biol 1994; 236:1250-8.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1250-1258
    • Nalini, V.1    Bax, B.2    Driessen, H.3    Moss, D.S.4    Lindley, P.F.5    Slingsby, C.6
  • 19
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci U S A 1999; 96:6137-42.
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 21
    • 0032983631 scopus 로고    scopus 로고
    • Probing the structure and interactions of crystallin proteins by NMR spectroscopy
    • Carver JA. Probing the structure and interactions of crystallin proteins by NMR spectroscopy. Prog Retin Eye Res 1999; 18:431-62.
    • (1999) Prog. Retin Eye Res. , vol.18 , pp. 431-462
    • Carver, J.A.1
  • 22
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
    • Carver JA, Lindner RA. NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Int J Biol Macromol 1998; 22:197-209.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 23
    • 0035727359 scopus 로고    scopus 로고
    • Proteolysis by m-calpain enhances in vitro light scattering by crystallins from human and bovine lenses
    • Shih M, David LL, Lampi KJ, Ma H, Fukiage C, Azuma M, Shearer TR. Proteolysis by m-calpain enhances in vitro light scattering by crystallins from human and bovine lenses. Curr Eye Res 2001; 22:458-69.
    • (2001) Curr. Eye Res. , vol.22 , pp. 458-469
    • Shih, M.1    David, L.L.2    Lampi, K.J.3    Ma, H.4    Fukiage, C.5    Azuma, M.6    Shearer, T.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.