메뉴 건너뛰기




Volumn 11, Issue , 2005, Pages 1211-1219

Quantitative measurement of deamidation in lens βB2-crystallin and peptides by direct electrospray injection and fragmentation in a Fourier transform mass spectrometer

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; BETA CRYSTALLIN; GLUTAMIC ACID; GLYCINE; PEPTIDE DERIVATIVE;

EID: 29644438539     PISSN: 10900535     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (37)

References (33)
  • 1
    • 28944448458 scopus 로고    scopus 로고
    • Molecular clocks: Deamidation of asparaginyl and glutaminyl residues in peptides and proteins
    • Cave Junction (OR): Althouse Press
    • Robinson NE, Robinson AB. Molecular clocks: deamidation of asparaginyl and glutaminyl residues in peptides and proteins. Cave Junction (OR): Althouse Press; 2004.
    • (2004)
    • Robinson, N.E.1    Robinson, A.B.2
  • 3
    • 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
  • 4
    • 0014819315 scopus 로고
    • Controlled deamidation of peptides and proteins: An experimental hazard and a possible biological timer
    • Robinson AB, McKerrow JH, Cary P. Controlled deamidation of peptides and proteins: an experimental hazard and a possible biological timer. Proc Natl Acad Sci U S A 1970; 66:753-7.
    • (1970) Proc Natl Acad Sci U S A , vol.66 , pp. 753-757
    • Robinson, A.B.1    McKerrow, J.H.2    Cary, P.3
  • 5
    • 0016360069 scopus 로고
    • Deamidation of glutaminyl and asparaginyl residues in peptides and proteins
    • Robinson AB, Rudd CJ. Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr Top Cell Regul 1974; 8:247-95.
    • (1974) Curr Top Cell Regul , vol.8 , pp. 247-295
    • Robinson, A.B.1    Rudd, C.J.2
  • 8
    • 1842525883 scopus 로고    scopus 로고
    • Amide molecular clocks in drosophila proteins: Potential regulators of aging and other processes
    • Robinson NE, Robinson AB. Amide molecular clocks in drosophila proteins: potential regulators of aging and other processes. Mech Ageing Dev 2004; 125:259-67.
    • (2004) Mech Ageing Dev , vol.125 , pp. 259-267
    • Robinson, N.E.1    Robinson, A.B.2
  • 9
    • 0014216748 scopus 로고
    • Multiple molecular forms of bovine heart cytochrome c. V.A comparative study of their physicochemical properties and their reactions in biological systems
    • Flatmark T. Multiple molecular forms of bovine heart cytochrome c. V.A comparative study of their physicochemical properties and their reactions in biological systems. J Biol Chem 1967; 242:2454-9.
    • (1967) J Biol Chem , vol.242 , pp. 2454-2459
    • Flatmark, T.1
  • 10
    • 0014408806 scopus 로고
    • Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy 3 in vivo
    • Flatmark T, Sletten K. Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy 3 in vivo. J Biol Chem 1968; 243:1623-9.
    • (1968) J Biol Chem , vol.243 , pp. 1623-1629
    • Flatmark, T.1    Sletten, K.2
  • 11
    • 0016219368 scopus 로고
    • Sequence dependent deamidation rates for model peptides of cytochrome C
    • Robinson AB, McKerrow JH, Legaz M. Sequence dependent deamidation rates for model peptides of cytochrome C. Int J Pept Protein Res 1974; 6:31-5.
    • (1974) Int J Pept Protein Res , vol.6 , pp. 31-35
    • Robinson, A.B.1    McKerrow, J.H.2    Legaz, M.3
  • 12
    • 0015373660 scopus 로고
    • Deamidation in vivo of an asparagine residue of rabbit muscle aldolase
    • Midelfort CF, Mehler AH. Deamidation in vivo of an asparagine residue of rabbit muscle aldolase. Proc Natl Acad Sci U S A 1972; 69:1816-9.
    • (1972) Proc Natl Acad Sci U S A , vol.69 , pp. 1816-1819
    • Midelfort, C.F.1    Mehler, A.H.2
  • 13
    • 0015953478 scopus 로고
    • Primary sequence dependence of the deamidation of rabbit muscle aldolase
    • McKerrow JH, Robinson AB. Primary sequence dependence of the deamidation of rabbit muscle aldolase. Science 1974; 183:85.
    • (1974) Science , vol.183 , pp. 85
    • McKerrow, J.H.1    Robinson, A.B.2
  • 14
    • 0038856860 scopus 로고
    • Structural analysis of altered proteins
    • Adelman RC, Roth GS, editors. Boca Raton (FL): CRC Press
    • Gracy RW, Lu HS, Yuan PM, Talent JM. Structural analysis of altered proteins. In Adelman RC, Roth GS, editors. Altered Proteins and Aging. Boca Raton (FL): CRC Press; 1983. p27-34.
    • (1983) Altered Proteins and Aging , pp. 27-34
    • Gracy, R.W.1    Lu, H.S.2    Yuan, P.M.3    Talent, J.M.4
  • 15
    • 3543041226 scopus 로고    scopus 로고
    • Molecular wear and tear leads to terminal marking and the unstable isoforms of aging
    • Gracy RW, Talent JM, Zvaigzne AI. Molecular wear and tear leads to terminal marking and the unstable isoforms of aging. J Exp Zool 1998; 282:18-27.
    • (1998) J Exp Zool , vol.282 , pp. 18-27
    • Gracy, R.W.1    Talent, J.M.2    Zvaigzne, A.I.3
  • 17
    • 1642430931 scopus 로고    scopus 로고
    • Resistance to antineoplastic therapy. The oncogenic tyrosine kinase-Bcl-x(L) axis
    • Weintraub SJ, Manson SR, Deverman BE. Resistance to antineoplastic therapy. The oncogenic tyrosine kinase-Bcl-x(L) axis. Cancer Cell 2004; 5:3-4.
    • (2004) Cancer Cell , vol.5 , pp. 3-4
    • Weintraub, S.J.1    Manson, S.R.2    Deverman, B.E.3
  • 18
    • 0032578419 scopus 로고    scopus 로고
    • Deamidation of specific glutamine residues from alpha-A crystallin during aging of the human lens
    • Takemoto L, Boyle D. Deamidation of specific glutamine residues from alpha-A crystallin during aging of the human lens. Biochemistry 1998; 37:13681-5.
    • (1998) Biochemistry , vol.37 , pp. 13681-13685
    • Takemoto, L.1    Boyle, D.2
  • 19
    • 0037047002 scopus 로고    scopus 로고
    • Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure
    • Lapko VN, Purkiss AG, Smith DL, Smith JB. Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure. Biochemistry 2002; 41:8638-48.
    • (2002) Biochemistry , vol.41 , pp. 8638-8648
    • Lapko, V.N.1    Purkiss, A.G.2    Smith, D.L.3    Smith, J.B.4
  • 21
    • 1342268073 scopus 로고    scopus 로고
    • Laser light-scattering evidence for an altered association of beta B1-crystallin deamidated in the connecting peptide
    • Harms MJ, Wilmarth PA, Kapfer DM, Steel EA, David LL, Bachinger HP, Lampi KJ. Laser light-scattering evidence for an altered association of beta B1-crystallin deamidated in the connecting peptide. Protein Sci 2004; 13:678-86.
    • (2004) Protein Sci , vol.13 , pp. 678-686
    • Harms, M.J.1    Wilmarth, P.A.2    Kapfer, D.M.3    Steel, E.A.4    David, L.L.5    Bachinger, H.P.6    Lampi, K.J.7
  • 22
    • 0034609357 scopus 로고    scopus 로고
    • Increased deamidation of asparagine during human senile cataractogenesis
    • Takemoto L, Boyle 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    Boyle, D.2
  • 23
    • 0345825772 scopus 로고    scopus 로고
    • Existence of deamidated alphaB-crystallin fragments in normal and cataractous human lenses
    • Srivastava OP, Srivastava K. Existence of deamidated alphaB-crystallin fragments in normal and cataractous human lenses. Mol Vis 2003; 9:110-8 .
    • (2003) Mol Vis , vol.9 , pp. 110-118
    • Srivastava, O.P.1    Srivastava, K.2
  • 24
    • 17444406699 scopus 로고    scopus 로고
    • Identification of protein modifications using MS/MS de novo sequencing and the OpenSea alignment algorithm
    • Mar-Apr
    • Searle BC, Dasari S, Wilmarth PA, Turner M, Reddy AP, David LL, Nagalla SR. Identification of protein modifications using MS/MS de novo sequencing and the OpenSea alignment algorithm. J Proteome Res 2005 Mar-Apr; 4:546-54.
    • (2005) J Proteome Res , vol.4 , pp. 546-554
    • Searle, B.C.1    Dasari, S.2    Wilmarth, P.A.3    Turner, M.4    Reddy, A.P.5    David, L.L.6    Nagalla, S.R.7
  • 26
    • 0034989185 scopus 로고    scopus 로고
    • Mass spectrometric evaluation of synthetic peptides as primary structure models for peptide and protein deamidation
    • Robinson NE, Robinson AB, Merrifield RB. Mass spectrometric evaluation of synthetic peptides as primary structure models for peptide and protein deamidation. J Pept Res 2001; 57:483-93.
    • (2001) J Pept Res , vol.57 , pp. 483-493
    • Robinson, N.E.1    Robinson, A.B.2    Merrifield, R.B.3
  • 28
    • 0035894272 scopus 로고    scopus 로고
    • Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides
    • Schmid DG, von der Mulbe FD, Fleckenstein B, Weinschenk T, Jung G. Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides. Anal Chem 2001; 73:6008-13.
    • (2001) Anal Chem , vol.73 , pp. 6008-6013
    • Schmid, D.G.1    von der Mulbe, F.D.2    Fleckenstein, B.3    Weinschenk, T.4    Jung, G.5
  • 30
    • 0033973532 scopus 로고    scopus 로고
    • Effect of lysine residues on the deamidation reaction of asparagine side chains
    • Capasso S, Balboni G, Di Cerbo P. Effect of lysine residues on the deamidation reaction of asparagine side chains. Biopolymers 2000; 53:213-9.
    • (2000) Biopolymers , vol.53 , pp. 213-219
    • Capasso, S.1    Balboni, G.2    Di Cerbo, P.3
  • 31
    • 0033636448 scopus 로고    scopus 로고
    • Kinetic and thermodynamic control of the relative yield of the deamidation of asparagine and isomerization of aspartic acid residues
    • Capasso S, Di Cerbo P. Kinetic and thermodynamic control of the relative yield of the deamidation of asparagine and isomerization of aspartic acid residues. J Pept Res 2000; 56:382-7.
    • (2000) J Pept Res , vol.56 , pp. 382-387
    • Capasso, S.1    Di Cerbo, P.2
  • 33
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.