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Volumn 44, Issue 5, 2009, Pages 803-812

Detection and structural features of the βB2-B3-crystallin heterodimer by radical probe mass spectrometry (RP-MS)

Author keywords

Ampersandbetacolon crystallin; Heterodimer; Mass spectrometry; Oxidation; Radical; Radical probe

Indexed keywords

AMPERSANDBETACOLON-CRYSTALLIN; CRYSTALLIN; DENATURING CONDITIONS; ELECTROSPRAY; GEL ELECTROPHORESIS; HETERODIMER; IONISATION; MONOMERIC FORMS; N-TERMINAL DOMAINS; RADICAL; RADICAL PROBE; STRUCTURAL FEATURE; TIME OF FLIGHT;

EID: 66249127927     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1560     Document Type: Article
Times cited : (6)

References (27)
  • 2
    • 0033551420 scopus 로고    scopus 로고
    • Formation of βA3/βB2-crystallin mixed complexes: Involvement of N- and C- terminal extensions
    • P.J. Werten, R. A. Lindner, J. A. Carver, W. W. de Jong. Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C- terminal extensions. Biochimica EtBiophysica Acta 1999, 1432, 286.
    • (1999) Biochimica EtBiophysica Acta , vol.1432 , pp. 286
    • Werten, P.J.1    Lindner, R.A.2    Carver, J.A.3    de Jong, W.W.4
  • 4
    • 0023813177 scopus 로고
    • Age-related increase in concentration and aggregation of degraded polypeptides in human lenses
    • O. P. Srivastava. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Experimental Eye Research 1988,47, 525.
    • (1988) Experimental Eye Research , vol.47 , pp. 525
    • Srivastava, O.P.1
  • 6
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β- crystallins favor heterologous association
    • C. Slingsby, O. A. Bateman. Quaternary interactions in eye lens β-crystallins: basic and acidic subunits of β- crystallins favor heterologous association. Biochemistry 1990,29,6592.
    • (1990) Biochemistry , vol.29 , pp. 6592
    • Slingsby, C.1    Bateman, O.A.2
  • 8
    • 66249110680 scopus 로고
    • Formation and crystallization of the eye lens heterodimer of βB2-βB3-crystallin
    • C. Slingsby, O. A. Bateman. Formation and crystallization of the eye lens heterodimer of βB2-βB3-crystallin. Experimental Eye Research 1994, 79, 377.
    • (1994) Experimental Eye Research , vol.79 , pp. 377
    • Slingsby, C.1    Bateman, O.A.2
  • 9
    • 0025835886 scopus 로고
    • Isolation and characterization of cDNAs encoding beta A2- and beta A4-crystallins: Heterologous interactions in the predicted beta A4-beta B2 heterodimer
    • G. L. van Rens, H. P. Driessen, V. Nalini, C. Slingsby, W. W. de Jong, H. Bloemendal. Isolation and characterization of cDNAs encoding beta A2- and beta A4-crystallins: heterologous interactions in the predicted beta A4-beta B2 heterodimer. Gene 1991,30,179.
    • (1991) Gene , vol.30 , pp. 179
    • van Rens, G.L.1    Driessen, H.P.2    Nalini, V.3    Slingsby, C.4    de Jong, W.W.5    Bloemendal, H.6
  • 10
    • 23244468386 scopus 로고    scopus 로고
    • Effect of oxidized β B3-crystallin peptide on lens βL-crystallin: Interaction with βB2-crystallin
    • E. G. P. Udupa, K. K. Sharma. Effect of oxidized β B3-crystallin peptide on lens βL-crystallin: interaction with βB2-crystallin. Investigative Ophthalmology & Visual Science 2005,46, 2514.
    • (2005) Investigative Ophthalmology & Visual Science , vol.46 , pp. 2514
    • Udupa, E.G.P.1    Sharma, K.K.2
  • 12
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
    • S. D. Maleknia, M. D. Brenowitz, M. R. Chance. Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry. Analytical Chemistry 1999,71, 3965.
    • (1999) Analytical Chemistry , vol.71 , pp. 3965
    • Maleknia, S.D.1    Brenowitz, M.D.2    Chance, M.R.3
  • 13
    • 0035497782 scopus 로고    scopus 로고
    • Radical approaches to probe protein structure, folding and interactions by mass spectrometry
    • S. D. Maleknia, K. M. Downard. Radical approaches to probe protein structure, folding and interactions by mass spectrometry. Mass SpectrometryReviews 2001, 20, 388.
    • (2001) Mass SpectrometryReviews , vol.20 , pp. 388
    • Maleknia, S.D.1    Downard, K.M.2
  • 15
    • 0242500901 scopus 로고    scopus 로고
    • Study of the RNase S- protein S-peptide complex using a radical probe and electrospray ionization mass spectrometry
    • J. W. H. Wong, S. D. Maleknia, K. M. Downard. Study of the RNase S- protein S-peptide complex using a radical probe and electrospray ionization mass spectrometry. Analytical Chemistry 2003,75,1557.
    • (2003) Analytical Chemistry , vol.75 , pp. 1557
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 16
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • S. D. Maleknia, K. M. Downard. Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry. European Journal of Biochemistry 2001, 268, 5578.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 5578
    • Maleknia, S.D.1    Downard, K.M.2
  • 17
    • 4644253428 scopus 로고    scopus 로고
    • Photochemical and electrophysical production of radicals on millisecond timescales. A probe of protein structure, dynamics and interactions
    • J. W. H. Wong, S. D. Maleknia, K. M. Downard. Photochemical and electrophysical production of radicals on millisecond timescales. A probe of protein structure, dynamics and interactions. Photochemistryand PhotobiologySciences 2004, 3, 741.
    • (2004) Photochemistryand PhotobiologySciences , vol.3 , pp. 741
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 18
    • 84889286164 scopus 로고    scopus 로고
    • Genesis and application of radical probe mass spectrometry (RP-MS) to study protein interactions
    • K. M. Downard ed, John Wiley and Sons: New Jersey
    • S. D. Maleknia, K. M. Downard. Genesis and application of radical probe mass spectrometry (RP-MS) to study protein interactions. In MassSpectrometryofProtein Interactions, K. M. Downard (ed.). John Wiley and Sons: New Jersey, 2007,109.
    • (2007) MassSpectrometryofProtein Interactions , pp. 109
    • Maleknia, S.D.1    Downard, K.M.2
  • 19
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • K.Takamoto, M.R.Chance. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annual Review of Biophysics and Biomolecular Structure 2006,35,251.
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 251
    • Takamoto, K.1    Chance, M.R.2
  • 20
    • 34548048810 scopus 로고    scopus 로고
    • Effects of protein concentration on the extent of gamma-ray-mediated oxidative labeling studied by electrospray mass spectrometry
    • X. Tong, J. C. Wren, L. Konermann. Effects of protein concentration on the extent of gamma-ray-mediated oxidative labeling studied by electrospray mass spectrometry. Analytical Chemistry 2007, 79, 6376.
    • (2007) Analytical Chemistry , vol.79 , pp. 6376
    • Tong, X.1    Wren, J.C.2    Konermann, L.3
  • 21
    • 33750632747 scopus 로고    scopus 로고
    • Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin
    • D. Hambly, M. Gross. Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin. InternationalJournalofMassSpectrometry2007, 259, 124.
    • (2007) InternationalJournalofMassSpectrometry , vol.259 , pp. 124
    • Hambly, D.1    Gross, M.2
  • 22
    • 13444309381 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry
    • J. W. H. Wong, S. D. Maleknia, K. M. Downard. Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry. Journal of the American Society for Mass Spectrometry2005, 16, 225.
    • (2005) Journal of the American Society for Mass Spectrometry , vol.16 , pp. 225
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 23
    • 23944445066 scopus 로고    scopus 로고
    • Onset of oxidative damage in alpha-crystallin by radical probe mass spectrometry
    • W.-K. Shum, S. D. Maleknia, K. M. Downard. Onset of oxidative damage in alpha-crystallin by radical probe mass spectrometry. AnalyticalBiochemistry2005, 344, 247.
    • (2005) AnalyticalBiochemistry , vol.344 , pp. 247
    • Shum, W.-K.1    Maleknia, S.D.2    Downard, K.M.3
  • 24
    • 33750543205 scopus 로고    scopus 로고
    • Interaction between alpha and upsilon- crystallin common to the eye of the australian platypus by radical probe mass spectrometry
    • S. Issa, K. M. Downard. Interaction between alpha and upsilon- crystallin common to the eye of the australian platypus by radical probe mass spectrometry. Journal of Mass Spectrometry 2006, 41, 1298.
    • (2006) Journal of Mass Spectrometry , vol.41 , pp. 1298
    • Issa, S.1    Downard, K.M.2
  • 25
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionisation orthogonal time-of-flight instrument
    • N.Tahallah, M.Pinkse, C. S. Maier, A. J. R.Heck. The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionisation orthogonal time-of-flight instrument. Rapid Communications in Mass Spectrometry. 2001, 15, 596.
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , pp. 596
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.R.4
  • 26
    • 84889465822 scopus 로고    scopus 로고
    • Direct characterization of protein complexes by electrospray ionization mass spectrometry and ion mobility analysis
    • M. Downard ed, John Wiley and Sons: New Jersey
    • J. A. Loo, C. K. Kaddis. Direct characterization of protein complexes by electrospray ionization mass spectrometry and ion mobility analysis. In Mass Spectrometry of Protein Interactions,K. M. Downard (ed.). John Wiley and Sons: New Jersey, 2007,1.
    • (2007) Mass Spectrometry of Protein Interactions,K , pp. 1
    • Loo, J.A.1    Kaddis, C.K.2
  • 27
    • 33747889776 scopus 로고    scopus 로고
    • PROXIMO - A docking new algorithm to model protein complexes using data from radical probe mass spectrometry
    • S. K. Gerega, K. M. Downard. PROXIMO - A docking new algorithm to model protein complexes using data from radical probe mass spectrometry. Bioinformatics 2006,22,1702.
    • (2006) Bioinformatics , vol.22 , pp. 1702
    • Gerega, S.K.1    Downard, K.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.