메뉴 건너뛰기




Volumn 428, Issue 1, 2012, Pages 1-3

An electrophoretic approach to screen for glutamine deamidation

Author keywords

BN PAGE; Glutamine deamidation; SDS PAGE; Transglutaminase; V8 in gel digestion

Indexed keywords

AMINO ACIDS; CHEMICAL REACTIONS; DIAGNOSIS; DIFFUSERS (OPTICAL); ELECTROPHORESIS; RECOMBINANT PROTEINS; SULFUR COMPOUNDS;

EID: 84862676614     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2012.05.016     Document Type: Article
Times cited : (6)

References (21)
  • 1
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • H.T. Wright Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins Crit. Rev. Biochem. Mol. Biol. 26 1991 1 52
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 2
    • 67449146916 scopus 로고    scopus 로고
    • Glutamine-specific N-terminal amidase, a component of the N-end rule pathway
    • H. Wang, K.I. Piatkov, C.S. Brower, and A. Varshavsky Glutamine-specific N-terminal amidase, a component of the N-end rule pathway Mol. Cell 34 2009 686 695
    • (2009) Mol. Cell , vol.34 , pp. 686-695
    • Wang, H.1    Piatkov, K.I.2    Brower, C.S.3    Varshavsky, A.4
  • 3
    • 79958723000 scopus 로고    scopus 로고
    • Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins
    • H. Iwasa, S. Meshitsuka, K. Hongo, T. Mizobata, and Y. Kawata Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins J. Biol. Chem. 286 2011 21796 21805
    • (2011) J. Biol. Chem. , vol.286 , pp. 21796-21805
    • Iwasa, H.1    Meshitsuka, S.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 4
    • 0034695932 scopus 로고    scopus 로고
    • Intracellular distribution of mammalian protein kinase: A catalytic subunit altered by conserved Asn2 deamidation
    • R. Pepperkok, A. Hotz-Wagenblatt, N. Konig, A. Girod, D. Bossemeyer, and V. Kinzel Intracellular distribution of mammalian protein kinase: a catalytic subunit altered by conserved Asn2 deamidation J. Cell Biol. 148 2000 715 726
    • (2000) J. Cell Biol. , vol.148 , pp. 715-726
    • Pepperkok, R.1    Hotz-Wagenblatt, A.2    Konig, N.3    Girod, A.4    Bossemeyer, D.5    Kinzel, V.6
  • 5
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • J. Cui, Q. Yao, S. Li, X. Ding, Q. Lu, H. Mao, L. Liu, N. Zheng, S. Chen, and F. Shao Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family Science 329 2010 1215 1218
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5    Mao, H.6    Liu, L.7    Zheng, N.8    Chen, S.9    Shao, F.10
  • 6
    • 80052338389 scopus 로고    scopus 로고
    • Macromolecular deterioration as the ultimate constraint on human lifespan
    • R.J. Truscott Macromolecular deterioration as the ultimate constraint on human lifespan Ageing Res. Rev. 10 2011 397 403
    • (2011) Ageing Res. Rev. , vol.10 , pp. 397-403
    • Truscott, R.J.1
  • 7
    • 77951818488 scopus 로고    scopus 로고
    • Glutamine deamidation: Differentiation of glutamic acid and γ-glutamic acid in peptides by electron capture dissociation
    • X. Li, C. Lin, and P.B. O'Connor Glutamine deamidation: differentiation of glutamic acid and γ-glutamic acid in peptides by electron capture dissociation Anal. Chem. 82 2010 3606 3615
    • (2010) Anal. Chem. , vol.82 , pp. 3606-3615
    • Li, X.1    Lin, C.2    O'Connor, P.B.3
  • 8
    • 60149093608 scopus 로고    scopus 로고
    • Glutamine deamidation of a recombinant monoclonal antibody
    • H. Liu, G. Gaza-Bulseco, and C. Chumsae Glutamine deamidation of a recombinant monoclonal antibody Rapid Commun. Mass Spectrom. 22 2008 4081 4088
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 4081-4088
    • Liu, H.1    Gaza-Bulseco, G.2    Chumsae, C.3
  • 9
    • 79960404170 scopus 로고    scopus 로고
    • Proteins from Erwinia asparaginase Erwinase and E. coli asparaginase 2 MEDAC for treatment of human leukemia show a multitude of modifications for which the consequences are completely unclear
    • N. Bae, A. Pollak, and G. Lubec Proteins from Erwinia asparaginase Erwinase and E. coli asparaginase 2 MEDAC for treatment of human leukemia show a multitude of modifications for which the consequences are completely unclear Electrophoresis 32 2011 1824 1828
    • (2011) Electrophoresis , vol.32 , pp. 1824-1828
    • Bae, N.1    Pollak, A.2    Lubec, G.3
  • 10
    • 32044444785 scopus 로고    scopus 로고
    • A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation
    • DOI 10.1016/j.cell.2005.11.046, PII S0092867406000651
    • X. Chao, T.J. Muff, S.Y. Park, S. Zhang, A.M. Pollard, G.W. Ordal, A.M. Bilwes, and B.R. Crane A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation Cell 124 2006 561 571 (Pubitemid 43199441)
    • (2006) Cell , vol.124 , Issue.3 , pp. 561-571
    • Chao, X.1    Muff, T.J.2    Park, S.-Y.3    Zhang, S.4    Pollard, A.M.5    Ordal, G.W.6    Bilwes, A.M.7    Crane, B.R.8
  • 11
    • 0026185519 scopus 로고
    • Deamidation via cyclic imide of asparaginyl peptides: Dependence on salts, buffers, and organic solvents
    • S. Capasso, L. Mazzarella, and A. Zagari Deamidation via cyclic imide of asparaginyl peptides: dependence on salts, buffers, and organic solvents Pept. Res. 4 1991 234 238
    • (1991) Pept. Res. , vol.4 , pp. 234-238
    • Capasso, S.1    Mazzarella, L.2    Zagari, A.3
  • 12
    • 0000162485 scopus 로고
    • The enzymatic deamidation of proteins
    • M.J. Mycek, and H. Waelsch The enzymatic deamidation of proteins J. Biol. Chem. 235 1960 3513 3517
    • (1960) J. Biol. Chem. , vol.235 , pp. 3513-3517
    • Mycek, M.J.1    Waelsch, H.2
  • 13
    • 47749153411 scopus 로고    scopus 로고
    • Transglutaminase induces protofibril-like amyloid β-protein assemblies that are protease-resistant and inhibit long-term potentiation
    • D.M. Hartley, C. Zhao, A.C. Speier, G.A. Woodard, S. Li, Z. Li, and T. Walz Transglutaminase induces protofibril-like amyloid β-protein assemblies that are protease-resistant and inhibit long-term potentiation J. Biol. Chem. 283 2008 16790 16800
    • (2008) J. Biol. Chem. , vol.283 , pp. 16790-16800
    • Hartley, D.M.1    Zhao, C.2    Speier, A.C.3    Woodard, G.A.4    Li, S.5    Li, Z.6    Walz, T.7
  • 14
    • 79953317964 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated glutamine deamidation of β-amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregation
    • A.W. Schmid, E. Condemi, G. Tuchscherer, D. Chiappe, M. Mutter, H. Vogel, M. Moniatte, and Y.O. Tsybin Tissue transglutaminase-mediated glutamine deamidation of β-amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregation J. Biol. Chem. 286 2011 12172 12188
    • (2011) J. Biol. Chem. , vol.286 , pp. 12172-12188
    • Schmid, A.W.1    Condemi, E.2    Tuchscherer, G.3    Chiappe, D.4    Mutter, M.5    Vogel, H.6    Moniatte, M.7    Tsybin, Y.O.8
  • 15
    • 54049147249 scopus 로고    scopus 로고
    • The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions
    • J. Stamnaes, B. Fleckenstein, and L.M. Sollid The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions Biochim. Biophys. Acta 1784 2008 1804 1811
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1804-1811
    • Stamnaes, J.1    Fleckenstein, B.2    Sollid, L.M.3
  • 16
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • D.W. Cleveland, S.G. Fischer, M.W. Kirschner, and U.K. Laemmli Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis J. Biol. Chem. 252 1977 1102 1106 (Pubitemid 8043094)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.3 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 17
    • 53049091572 scopus 로고    scopus 로고
    • A receptor subunits representing strongly hydrophobic transmembrane proteins
    • A receptor subunits representing strongly hydrophobic transmembrane proteins J. Proteome Res. 7 2008 3498 3506
    • (2008) J. Proteome Res. , vol.7 , pp. 3498-3506
    • Kang, S.U.1    Fuchs, K.2    Sieghart, W.3    Lubec, G.4
  • 18
    • 14744268457 scopus 로고    scopus 로고
    • In vivo deamidation characterization of monoclonal antibody by LC/MS/MS
    • DOI 10.1021/ac0494174
    • L. Huang, J. Lu, V.J. Wroblewski, J.M. Beals, and R.M. Riggin In vivo deamidation characterization of monoclonal antibody by LC/MS/MS Anal. Chem. 77 2005 1432 1439 (Pubitemid 40327884)
    • (2005) Analytical Chemistry , vol.77 , Issue.5 , pp. 1432-1439
    • Huang, L.1    Lu, J.2    Wroblewski, V.J.3    Beals, J.M.4    Riggin, R.M.5
  • 19
    • 8544266059 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein
    • Y.H. Yong, S. Yamaguchi, Y.S. Gu, T. Mori, and Y. Matsumura Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein J. Agric. Food Chem. 52 2004 7094 7100
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 7094-7100
    • Yong, Y.H.1    Yamaguchi, S.2    Gu, Y.S.3    Mori, T.4    Matsumura, Y.5
  • 20
    • 84857879076 scopus 로고    scopus 로고
    • Mass spectrometrical identification of hippocampal NMDA receptor subunits NR1, NR2A-D, and five novel phosphorylation sites on NR2A and NR2B
    • M. Ghafari, H. Höger, S. Keihan Falsafi, N. Russo-Schlaff, A. Pollak, and G. Lubec Mass spectrometrical identification of hippocampal NMDA receptor subunits NR1, NR2A-D, and five novel phosphorylation sites on NR2A and NR2B J. Proteome Res. 11 2012 1891 1896
    • (2012) J. Proteome Res. , vol.11 , pp. 1891-1896
    • Ghafari, M.1    Höger, H.2    Keihan Falsafi, S.3    Russo-Schlaff, N.4    Pollak, A.5    Lubec, G.6
  • 21
    • 0142148054 scopus 로고    scopus 로고
    • Identification of transglutaminase-mediated deamidation sites in a recombinant α-gliadin by advanced mass-spectrometric methodologies
    • DOI 10.1110/ps.03185903
    • M.F. Mazzeo, B. De Giulio, S. Senger, M. Rossi, A. Malorni, and R.A. Siciliano Identification of transglutaminase-mediated deamidation sites in a recombinant α-gliadin by advanced mass-spectrometric methodologies Protein Sci. 12 2003 2434 2442 (Pubitemid 37310785)
    • (2003) Protein Science , vol.12 , Issue.11 , pp. 2434-2442
    • Mazzeo, M.F.1    De Giulio, B.2    Senger, S.3    Rossi, M.4    Malorni, A.5    Siciliano, R.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.