메뉴 건너뛰기




Volumn 3, Issue 9, 2008, Pages

Interaction of C-terminal truncated human αA-crystallins with target proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; ALPHA CRYSTALLIN; AMINE; ARGININE; BETA CRYSTALLIN; BETA L CRYSTALLIN; CHAPERONE; CYSTEINE; FLUORESCENT DYE; UNCLASSIFIED DRUG;

EID: 52649126857     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003175     Document Type: Article
Times cited : (14)

References (23)
  • 1
    • 0015910905 scopus 로고
    • the amino- acid sequence of the alphaA2 chain of bovine alpha-crystallin
    • Van Der Ouderra FJ, De Jong WW, Bloemendal H (1973) the amino- acid sequence of the alphaA2 chain of bovine alpha-crystallin. Eur J Biochem 39: 207-222.
    • (1973) Eur J Biochem , vol.39 , pp. 207-222
    • Van Der Ouderra, F.J.1    De Jong, W.W.2    Bloemendal, H.3
  • 3
    • 0016778248 scopus 로고
    • The amino-acid sequence of the A chain of human alpha-crystallin
    • De Jong WW, Terwindt EC, Bloemendal H (1975) The amino-acid sequence of the A chain of human alpha-crystallin. FEBS Lett 58: 310-313.
    • (1975) FEBS Lett , vol.58 , pp. 310-313
    • De Jong, W.W.1    Terwindt, E.C.2    Bloemendal, H.3
  • 4
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin
    • Ingolia TD, Craig EA (1982) Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc Natl Acad Sci USA 79: 2360-2364.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 5
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz J (1992) α-Crystallin can function as a molecular chaperone. Proc: Natl Acad Sci USA 89: 10449-10.
    • (1992) Proc: Natl Acad Sci USA , vol.89 , pp. 10449-10510
    • Horwitz, J.1
  • 6
    • 0028282965 scopus 로고
    • the chaperone activiy of bovine alpha-crystallin. Interaction with other lens crystallins in native and denatured states
    • Wang K, Spector A (1994) the chaperone activiy of bovine alpha-crystallin. Interaction with other lens crystallins in native and denatured states. J Biol Chem 269: 13601-13608.
    • (1994) J Biol Chem , vol.269 , pp. 13601-13608
    • Wang, K.1    Spector, A.2
  • 7
    • 0028973109 scopus 로고
    • Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens
    • Rao PV, Huang QL, Horwitz J, Zigler JS (1995) Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta 1245: 439-447.
    • (1995) Biochim Biophys Acta , vol.1245 , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler, J.S.4
  • 8
    • 0022423148 scopus 로고
    • Domain structure and evolution in α-crystallins and small heat shock proteins
    • Wistow G (1985) Domain structure and evolution in α-crystallins and small heat shock proteins. FEBS Lett 18: 1-6.
    • (1985) FEBS Lett , vol.18 , pp. 1-6
    • Wistow, G.1
  • 9
    • 0029144240 scopus 로고
    • Identification of the in vivo truncation sites at the C-terminal region of alpha-A-crystallin from aged bovine and human lens
    • Takrmoto LJ (1995) Identification of the in vivo truncation sites at the C-terminal region of alpha-A-crystallin from aged bovine and human lens. Curr Eye Res 14: 837-841.
    • (1995) Curr Eye Res , vol.14 , pp. 837-841
    • Takrmoto, L.J.1
  • 10
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens alpha-crystallins
    • Lund AL, Smith JB, Smith DL (1996) Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res 63: 661-672.
    • (1996) Exp Eye Res , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 11
    • 0037082138 scopus 로고    scopus 로고
    • Posttranslational modification of human Α-crystallin: Correlation with electrophoretic migration
    • Colvis C, Garland D (2002) Posttranslational modification of human Α-crystallin: correlation with electrophoretic migration. Arch Biochem Biophys 397: 319-323.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 319-323
    • Colvis, C.1    Garland, D.2
  • 12
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallin identified by HPLC and mass spectrometry
    • Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB (1998) Age-related changes in human lens crystallin identified by HPLC and mass spectrometry. Exp Eye Res 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
  • 13
    • 0028216737 scopus 로고
    • Posttranslational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer LR, Zhou X, Yang Z, Sun Y, Smith DL, et al. (1994) Posttranslational modifications of water-soluble human lens crystallins from young adults. J Biol Chem 269: 12494-12502.
    • (1994) J Biol Chem , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Sun, Y.4    Smith, D.L.5
  • 14
    • 0031889967 scopus 로고    scopus 로고
    • Quantitation of specific cleavage sites at the C-terminal region of alpha-A-crystallin from human lenses of different age
    • Takemoto LJ (1998) Quantitation of specific cleavage sites at the C-terminal region of alpha-A-crystallin from human lenses of different age. Exp Eye Res 66: 263-266.
    • (1998) Exp Eye Res , vol.66 , pp. 263-266
    • Takemoto, L.J.1
  • 15
    • 0036784934 scopus 로고    scopus 로고
    • Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses
    • Thampi P, Hassan A, Smith JB, Abraham EC (2002) Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 43: 3265-3272.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3265-3272
    • Thampi, P.1    Hassan, A.2    Smith, J.B.3    Abraham, E.C.4
  • 17
    • 0034992086 scopus 로고    scopus 로고
    • Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin
    • Shroff NP, Bera S, Cherian-Shaw M, Abraham EC (2001) Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin. Mol Cell Biochem 220: 127-133.
    • (2001) Mol Cell Biochem , vol.220 , pp. 127-133
    • Shroff, N.P.1    Bera, S.2    Cherian-Shaw, M.3    Abraham, E.C.4
  • 18
    • 0037039153 scopus 로고    scopus 로고
    • The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin
    • Bera S, Abraham EC (2002) The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin. Biochemistry 41: 297-305.
    • (2002) Biochemistry , vol.41 , pp. 297-305
    • Bera, S.1    Abraham, E.C.2
  • 19
    • 38649094555 scopus 로고    scopus 로고
    • C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin
    • Kallur LS, Aziz A, Abraham EC (2008) C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin. Mol Cell Biochem 308: 85-91.
    • (2008) Mol Cell Biochem , vol.308 , pp. 85-91
    • Kallur, L.S.1    Aziz, A.2    Abraham, E.C.3
  • 20
    • 33845967487 scopus 로고    scopus 로고
    • The effect of dextran on subunit exchange of the molecular chaperone αA-crystallin
    • Ghahghghaei A, Rekas A, Price WE, Carver JA (2007) The effect of dextran on subunit exchange of the molecular chaperone αA-crystallin. Biochim Biophys Acta 1774: 102-111.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 102-111
    • Ghahghghaei, A.1    Rekas, A.2    Price, W.E.3    Carver, J.A.4
  • 21
    • 0034673151 scopus 로고    scopus 로고
    • Mutation of R116C results in highly oligomerized αA-crystallin with modified structure and defective chaperone-like function
    • Shroff NP, Cherian-Shaw M, Bera S, Abraham EC (2000) Mutation of R116C results in highly oligomerized αA-crystallin with modified structure and defective chaperone-like function. Biochemistry 39: 1420-1426.
    • (2000) Biochemistry , vol.39 , pp. 1420-1426
    • Shroff, N.P.1    Cherian-Shaw, M.2    Bera, S.3    Abraham, E.C.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.