메뉴 건너뛰기




Volumn 13, Issue , 2007, Pages 1873-1877

Comparison of two tandem mass spectrometry-based methods for analyzing the proteome of healthy human lens fibers

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; FILENSIN; GAMMA CRYSTALLIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LENS PROTEIN; RETINAL DEHYDROGENASE; TRYPSIN;

EID: 34948907351     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (17)
  • 1
    • 18444391517 scopus 로고    scopus 로고
    • MacCoss MJ, McDonald WH, Saraf A, Sadygov R, Clark JM, Tasto JJ, Gould KL, Wolters D, Washburn M, Weiss A, Clark JI, Yates JR 3rd. Shotgun identification of protein modifications from protein complexes and lens tissue. Proc Natl Acad Sci U S A 2002; 99:7900-5.
    • MacCoss MJ, McDonald WH, Saraf A, Sadygov R, Clark JM, Tasto JJ, Gould KL, Wolters D, Washburn M, Weiss A, Clark JI, Yates JR 3rd. Shotgun identification of protein modifications from protein complexes and lens tissue. Proc Natl Acad Sci U S A 2002; 99:7900-5.
  • 3
    • 0032612938 scopus 로고    scopus 로고
    • Klose J. Large-gel 2-D electrophoresis. Methods Mol Biol 1999; 112:147-72.
    • Klose J. Large-gel 2-D electrophoresis. Methods Mol Biol 1999; 112:147-72.
  • 4
    • 0035582244 scopus 로고    scopus 로고
    • Wolters DA, Washburn MP, Yates JR 3rd. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 2001; 73:5683-90.
    • Wolters DA, Washburn MP, Yates JR 3rd. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 2001; 73:5683-90.
  • 6
    • 12744280774 scopus 로고    scopus 로고
    • AMASS: Software for automatically validating the quality of MS/MS spectrum from. SEQUEST results
    • Sun W, Li F, Wang J, Zheng D, Gao Y. AMASS: software for automatically validating the quality of MS/MS spectrum from. SEQUEST results. Mol Cell Proteomics 2004; 3:1194-9.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1194-1199
    • Sun, W.1    Li, F.2    Wang, J.3    Zheng, D.4    Gao, Y.5
  • 7
    • 3142729873 scopus 로고    scopus 로고
    • RScore: A peptide randomicity score for evaluating tandem mass spectra
    • Li F, Sun W, Gao Y, Wang J. RScore: a peptide randomicity score for evaluating tandem mass spectra. Rapid Commun Mass Spectrom. 2004; 18:1655-9.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 1655-1659
    • Li, F.1    Sun, W.2    Gao, Y.3    Wang, J.4
  • 8
    • 3242731195 scopus 로고    scopus 로고
    • Liu H, Sadygov RG, Yates JR 3rd. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 2004; 76:4193-201.
    • Liu H, Sadygov RG, Yates JR 3rd. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 2004; 76:4193-201.
  • 9
    • 0033051101 scopus 로고    scopus 로고
    • Link AJ, Eng J, Schieltz DM, Carmack E, Mize GJ, Morris DR, Garvik BM, Yates JR 3rd. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol 1999; 17:676-82.
    • Link AJ, Eng J, Schieltz DM, Carmack E, Mize GJ, Morris DR, Garvik BM, Yates JR 3rd. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol 1999; 17:676-82.
  • 10
    • 0035106351 scopus 로고    scopus 로고
    • Washburn MP, Wolters D, Yates JR 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001; 19:242-7.
    • Washburn MP, Wolters D, Yates JR 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001; 19:242-7.
  • 11
    • 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
  • 12
    • 0021116455 scopus 로고
    • Why the eye lens is transparent
    • Benedek G. Why the eye lens is transparent. Nature 1983; 302:383-4.
    • (1983) Nature , vol.302 , pp. 383-384
    • Benedek, G.1
  • 13
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens betaB2-crystallin destabilizes the dimer
    • Lampi KJ, Amyx KK, Ahmann P, Steel EA. Deamidation in human lens betaB2-crystallin destabilizes the dimer. Biochemistry 2006; 45:3146-53.
    • (2006) Biochemistry , vol.45 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 14
    • 0042121150 scopus 로고    scopus 로고
    • Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate
    • Zhang Z, Smith DL, Smith JB. Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate. Exp Eye Res 2003; 77:259-72.
    • (2003) Exp Eye Res , vol.77 , pp. 259-272
    • Zhang, Z.1    Smith, D.L.2    Smith, J.B.3
  • 15
    • 20444501631 scopus 로고    scopus 로고
    • Phosphoproteome analysis of hereditary cataractous rat lens alpha-crystallin
    • Kamei A, Takamura S, Nagai M, Takeuchi N. Phosphoproteome analysis of hereditary cataractous rat lens alpha-crystallin. Biol Pharm Bull 2004; 27:1923-31.
    • (2004) Biol Pharm Bull , vol.27 , pp. 1923-1931
    • Kamei, A.1    Takamura, S.2    Nagai, M.3    Takeuchi, N.4
  • 16
    • 0036137567 scopus 로고    scopus 로고
    • Lens proteomics: Analysis of rat crystallin sequences and two-dimensional electrophoresis map
    • Lampi KJ, Shih M, Ueda Y, Shearer TR, David LL. Lens proteomics: analysis of rat crystallin sequences and two-dimensional electrophoresis map. Invest Ophthalmol Vis Sci 2002, 43:216-24.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 216-224
    • Lampi, K.J.1    Shih, M.2    Ueda, Y.3    Shearer, T.R.4    David, L.L.5
  • 17
    • 0036139647 scopus 로고    scopus 로고
    • Lens proteomics: The accumulation of crystallin modifications in the mouse lens with age
    • Ueda Y, Duncan MK, David LL. Lens proteomics: the accumulation of crystallin modifications in the mouse lens with age. Invest Ophthalmol Vis Sci 2002; 43:205-15.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 205-215
    • Ueda, Y.1    Duncan, M.K.2    David, L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.