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Volumn 19, Issue 6, 2012, Pages 688-697

Local flexibility facilitates oxidization of buried methionine residues

Author keywords

Bioinformatics; Disorder score; Flexibility; Intrinsic disorder; Methionine oxidation; Solvent accessible surface area

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; ALPHA SYNUCLEIN; ALR585 PROTEIN; AMINO ACID; AMYLOID BETA PROTEIN[1-42]; APOLIPOPROTEIN A1; BACTERIORHODOPSIN; CALCITONIN; CAM PROTEIN; CATALASE; CELLOBIOSE QUINONE OXIDOREDUCTASE; CYCLOHEXANONE MONOOXYGENASE; CYSTEINE; DJ 1 PROTEIN; DOPAMINE 2 RECEPTOR; ERYTHROPOIETIN; HEMOGLOBIN A; HUMAN GROWTH HORMONE; KININOGEN; METHIONINE; PRIO PROTEIN; PROTEIN; PRRDH PROTEIN; PSEUDOZYMA ANTARCTICA LIPASE B; REACTIVE OXYGEN METABOLITE; SERUM ALBUMIN; THROMBOMODULIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL M6; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 84861939035     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986612800494084     Document Type: Article
Times cited : (21)

References (92)
  • 1
    • 0017733498 scopus 로고
    • Interconversion of methionine and methionine sulfoxide
    • Savige, W.E.; Fontana, A. Interconversion of methionine and methionine sulfoxide. Methods Enzymol., 1977, 47, 453-459.
    • (1977) Methods Enzymol. , vol.47 , pp. 453-459
    • Savige, W.E.1    Fontana, A.2
  • 2
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman, K.B.; Ames, B.N. The free radical theory of aging matures. Physiol. Rev., 1998, 78, 547-581. (Pubitemid 28182903)
    • (1998) Physiological Reviews , vol.78 , Issue.2 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 3
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • DOI 10.1016/j.febslet.2006.03.028, PII S0014579306003309
    • Friguet, B. Oxidized protein degradation and repair in ageing and oxidative stress. FEBS lett., 2006, 580, 2910-2916. (Pubitemid 43729157)
    • (2006) FEBS Letters , vol.580 , Issue.12 , pp. 2910-2916
    • Friguet, B.1
  • 4
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • DOI 10.1007/s00726-003-0011-2
    • Stadtman, E.R.; Levine, R.L. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino acids, 2003, 25, 207-218. (Pubitemid 38043943)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 5
    • 0015870249 scopus 로고
    • Free radical theory of aging
    • Harman, D. Free radical theory of aging. Triangle, 1973, 12, 153-158.
    • (1973) Triangle , vol.12 , pp. 153-158
    • Harman, D.1
  • 6
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • Berlett, B.S.; Stadtman, E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem., 1997, 272, 20313-20316. (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 7
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • DOI 10.1021/tx960133r
    • Stadtman, E.R.; Berlett, B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol., 1997, 10, 485-494. (Pubitemid 27217204)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 8
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: Protein carbonyl content as a marker of damage
    • Chevion, M.; Berenshtein, E.; Stadtman, E.R. Human studies related to protein oxidation: protein carbonyl content as a marker of damage. Free Radic. Res., 2000, 33 Suppl, S99-108.
    • (2000) Free Radic. Res. , vol.33 , Issue.SUPPL.
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 9
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T.; Holbrook, N.J. Oxidants, oxidative stress and the biology of ageing. Nature, 2000, 408, 239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 10
    • 2342440118 scopus 로고    scopus 로고
    • Peripheral markers of oxidative stress and excitotoxicity in neurodegenerative disorders: Tools for diagnosis and therapy?
    • Facheris, M.; Beretta, S.; Ferrarese, C. Peripheral markers of oxidative stress and excitotoxicity in neurodegenerative disorders: tools for diagnosis and therapy? J. Alzheimers Dis., 2004, 6, 177-184. (Pubitemid 38560254)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.2 , pp. 177-184
    • Facheris, M.1    Beretta, S.2    Ferrarese, C.3
  • 11
    • 33846811473 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants: A link to disease and prevention?
    • DOI 10.1016/j.jnutbio.2006.12.003, PII S0955286306002713
    • Seifried, H.E. Oxidative stress and antioxidants: a link to disease and prevention? J. Nutr. Biochem., 2007, 18, 168-171. (Pubitemid 46216808)
    • (2007) Journal of Nutritional Biochemistry , vol.18 , Issue.3 , pp. 168-171
    • Seifried, H.E.1
  • 13
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • DOI 10.1007/s00726-003-0016-x
    • Hawkins, C.L.; Pattison, D.I.; Davies, M.J. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino acids, 2003, 25, 259-274. (Pubitemid 38041264)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 14
    • 0001388811 scopus 로고
    • Oxidation with hydrogen peroxide
    • Neumann, N.P. Oxidation with hydrogen peroxide. Methods Enzymol., 1972, 25, 393-400.
    • (1972) Methods Enzymol. , vol.25 , pp. 393-400
    • Neumann, N.P.1
  • 15
    • 0035968194 scopus 로고    scopus 로고
    • Mechanism of the formation and proteolytic release of H2O2-induced dityrosine and tyrosine oxidation products in hemoglobin and red blood cells
    • Giulivi, C.; Davies, K.J., Mechanism of the formation and proteolytic release of H2O2-induced dityrosine and tyrosine oxidation products in hemoglobin and red blood cells. J. Biol. Chem., 2001, 276, 24129-24136.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24129-24136
    • Giulivi, C.1    Davies, K.J.2
  • 16
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt, W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic. Biol. Med., 1995, 18, 93-105.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 17
    • 3142775571 scopus 로고    scopus 로고
    • 13C]methionine-labeled DNA polymerase β
    • DOI 10.1021/bi049641n
    • Bose-Basu, B.; DeRose, E.F.; Kirby, T.W.; Mueller, G.A.; Beard, W.A.; Wilson, S.H.; London, R.E. Dynamic characterization of a DNA repair enzyme: NMR studies of [methyl-13C]methioninelabeled DNA polymerase beta. Biochemistry, 2004, 43, 8911-8922. (Pubitemid 38924426)
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 8911-8922
    • Bose-Basu, B.1    DeRose, E.F.2    Kirby, T.W.3    Mueller, G.A.4    Beard, W.A.5    Wilson, S.H.6    London, R.E.7
  • 18
    • 0037082115 scopus 로고    scopus 로고
    • Redox processes of methionine relevant to β-amyloid oxidation and Alzheimer's disease
    • DOI 10.1006/abbi.2001.2621
    • Schoneich, C. Redox processes of methionine relevant to betaamyloid oxidation and Alzheimer's disease. Arch. Biochem. Biophys., 2002, 397, 370-376. (Pubitemid 34852305)
    • (2002) Archives of Biochemistry and Biophysics , vol.397 , Issue.2 , pp. 370-376
    • Schoneich, C.1
  • 19
    • 1042302134 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation
    • DOI 10.1016/j.abb.2003.10.001
    • Stadtman, E.R. Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation. Arch. Biochem. Biophys., 2004, 423, 2-5. (Pubitemid 38198207)
    • (2004) Archives of Biochemistry and Biophysics , vol.423 , Issue.1 , pp. 2-5
    • Stadtman, E.R.1
  • 21
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • DOI 10.1016/j.bbapap.2004.08.007, PII S1570963904002183, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Davies, M.J. The oxidative environment and protein damage. Biochim. Biophys. Acta, 2005, 1703, 93-109. (Pubitemid 40170433)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 93-109
    • Davies, M.J.1
  • 23
    • 76649124599 scopus 로고    scopus 로고
    • Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I
    • Wong, Y.Q.; Binger, K.J.; Howlett, G.J.; Griffin, M.D. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proc. Natl. Acad. Sci. USA, 2010, 107, 1977-1982.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1977-1982
    • Wong, Y.Q.1    Binger, K.J.2    Howlett, G.J.3    Griffin, M.D.4
  • 24
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of Methionine Residues of Proteins: Biological Consequences
    • Stadtman, E.R.; Moskovitz, J.; Levine, R.L. Oxidation of methionine residues of proteins: biological consequences. Antioxid. Redox Signal., 2003, 5, 577-582. (Pubitemid 37315145)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 25
    • 0036289894 scopus 로고    scopus 로고
    • GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation
    • DOI 10.1016/S0006-291X(02)00575-2, PII S0006291X02005752
    • Melkani, G.C.; Zardeneta, G.; Mendoza, J.A. GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation. Biochem. Biophys. Res. Commun., 2002, 294, 893-899. (Pubitemid 34687200)
    • (2002) Biochemical and Biophysical Research Communications , vol.294 , Issue.4 , pp. 893-899
    • Melkani, G.C.1    Zardeneta, G.2    Mendoza, J.A.3
  • 26
    • 27144440590 scopus 로고    scopus 로고
    • Inactivation of protease inhibitors and lysozyme by hypochlorous acid: Role of side-chain oxidation and protein unfolding in loss of biological function
    • DOI 10.1021/tx050207b
    • Hawkins, C.L.; Davies, M.J., Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function. Chem. Res. Toxicol., 2005, 18, 1600-1610. (Pubitemid 41504481)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.10 , pp. 1600-1610
    • Hawkins, C.L.1    Davies, M.J.2
  • 28
    • 0141905917 scopus 로고    scopus 로고
    • Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
    • DOI 10.1042/BJ20030685
    • Chapman, A.L.; Winterbourn, C.C.; Brennan, S.O.; Jordan, T.W.; Kettle, A.J. Characterization of non-covalent oligomers of proteins treated with hypochlorous acid. Biochem. j., 2003, 375, 33-40. (Pubitemid 37255379)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 33-40
    • Chapman, A.L.P.1    Winterbourn, C.C.2    Brennan, S.O.3    Jordan, T.W.4    Kettle, A.J.5
  • 29
    • 33846525435 scopus 로고    scopus 로고
    • Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes
    • DOI 10.1016/j.freeradbiomed.2006.11.019, PII S089158490600757X
    • Bonini, M.G.; Siraki, A.G.; Atanassov, B.S.; Mason, R.P. Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes. Free Radic. Biol. Med., 2007, 42, 530-540. (Pubitemid 46162122)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.4 , pp. 530-540
    • Bonini, M.G.1    Siraki, A.G.2    Atanassov, B.S.3    Mason, R.P.4
  • 30
    • 55449092300 scopus 로고    scopus 로고
    • Bleach activates a redox-regulated chaperone by oxidative protein unfolding
    • Winter, J.; Ilbert, M.; Graf, P.C.; Ozcelik, D.; Jakob, U. Bleach activates a redox-regulated chaperone by oxidative protein unfolding. Cell, 2008, 135, 691-701.
    • (2008) Cell , vol.135 , pp. 691-701
    • Winter, J.1    Ilbert, M.2    Graf, P.C.3    Ozcelik, D.4    Jakob, U.5
  • 31
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune, T.; Reinheckel, T.; Davies, K.J. Degradation of oxidized proteins in mammalian cells. FASEB J., 1997, 11, 526-534. (Pubitemid 27274426)
    • (1997) FASEB Journal , vol.11 , Issue.7 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 33
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human α-synuclein in vitro
    • DOI 10.1016/S0014-5793(02)02638-8, PII S0014579302026388
    • Uversky, V.N.; Yamin, G.; Souillac, P.O.; Goers, J.; Glaser, C.B.; Fink, A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS lett., 2002, 517, 239-244. (Pubitemid 34327667)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 34
    • 12844272205 scopus 로고    scopus 로고
    • Methionine oxidation, α-synuclein and Parkinson's disease
    • DOI 10.1016/j.bbapap.2004.10.008, PII S1570963904002900, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Glaser, C.B.; Yamin, G.; Uversky, V.N.; Fink, A.L., Methionine oxidation, alpha-synuclein and Parkinson's disease. Biochim. Biophys. Acta, 2005, 1703, 157-169. (Pubitemid 40170439)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 157-169
    • Glaser, C.B.1    Yamin, G.2    Uversky, V.N.3    Fink, A.L.4
  • 35
    • 9144274018 scopus 로고    scopus 로고
    • Role of Individual Methionines in the Fibrillation of Methionine-Oxidized α-Synuclein
    • DOI 10.1021/bi049979h
    • Hokenson, M.J.; Uversky, V.N.; Goers, J.; Yamin, G.; Munishkina, L.A.; Fink, A.L. Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein. Biochemistry, 2004, 43, 4621-4633. (Pubitemid 38500591)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4621-4633
    • Hokenson, M.J.1    Uversky, V.N.2    Goers, J.3    Yamin, G.4    Munishkina, L.A.5    Fink, A.L.6
  • 36
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionine-oxidized α-synuclein
    • DOI 10.1074/jbc.M303302200
    • Yamin, G.; Glaser, C.B.; Uversky, V.N.; Fink, A.L. Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. J. Biol. Chem., 2003, 278, 27630-27635. (Pubitemid 36899949)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 37
    • 74849125564 scopus 로고    scopus 로고
    • Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intramolecular long-range interactions
    • Zhou, W.; Long, C.; Reaney, S.H.; Di Monte, D.A.; Fink, A.L.; Uversky, V.N. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intramolecular long-range interactions. Biochim. Biophys. Acta, 2010, 1802, 322-330.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 322-330
    • Zhou, W.1    Long, C.2    Reaney, S.H.3    Di Monte, D.A.4    Fink, A.L.5    Uversky, V.N.6
  • 38
    • 70149091474 scopus 로고    scopus 로고
    • Oxidation of methionine residues: The missing link between stress and signalling responses in plants
    • Emes, M.J., Oxidation of methionine residues: the missing link between stress and signalling responses in plants. Biochem. J., 2009, 422, e1-2.
    • (2009) Biochem. J. , vol.422
    • Emes, M.J.1
  • 39
    • 70149092747 scopus 로고    scopus 로고
    • Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis
    • Hardin, S.C.; Larue, C.T.; Oh, M.H.; Jain, V.; Huber, S.C. Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis. Biochem. J., 2009, 422, 305-312.
    • (2009) Biochem. J. , vol.422 , pp. 305-312
    • Hardin, S.C.1    Larue, C.T.2    Oh, M.H.3    Jain, V.4    Huber, S.C.5
  • 40
    • 73849134745 scopus 로고    scopus 로고
    • Clearance and phosphorylation of alpha-synuclein are inhibited in methionine sulfoxide reductase a null yeast cells
    • Oien, D.B.; Shinogle, H.E.; Moore, D.S.; Moskovitz, J. Clearance and phosphorylation of alpha-synuclein are inhibited in methionine sulfoxide reductase a null yeast cells. J. Mol. Neurosci., 2009, 39, 323-332.
    • (2009) J. Mol. Neurosci. , vol.39 , pp. 323-332
    • Oien, D.B.1    Shinogle, H.E.2    Moore, D.S.3    Moskovitz, J.4
  • 41
    • 2542574135 scopus 로고    scopus 로고
    • The influence of oxidation on proteolysis in raw milk
    • DOI 10.1017/S0022029903006654
    • Wiking, L.; Nielsen, J.H., The influence of oxidation on proteolysis in raw milk. J. Dairy Res., 2004, 71, 196-200. (Pubitemid 38693295)
    • (2004) Journal of Dairy Research , vol.71 , Issue.2 , pp. 196-200
    • Wiking, L.1    Nielsen, J.H.2
  • 42
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • DOI 10.1016/j.bbapap.2004.09.003, PII S1570963904002419, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Moskovitz, J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta, 2005, 1703, 213-219. (Pubitemid 40170444)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 213-219
    • Moskovitz, J.1
  • 43
    • 0038745648 scopus 로고    scopus 로고
    • Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants
    • DOI 10.1016/S0006-291X(03)00685-5
    • Abulimiti, A.; Qiu, X.; Chen, J.; Liu, Y.; Chang, Z. Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants. Biochem. Biophys. Res. Commun., 2003, 305, 87-93. (Pubitemid 36535412)
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , Issue.1 , pp. 87-93
    • Abulimiti, A.1    Qiu, X.2    Chen, J.3    Liu, Y.4    Chang, Z.5
  • 44
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo, S.; Levine, R.L. Methionine in proteins defends against oxidative stress. FASEB J., 2009, 23, 464-472.
    • (2009) FASEB J. , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 45
    • 2442456741 scopus 로고    scopus 로고
    • -)
    • DOI 10.1074/jbc.M310045200
    • Khor, H.K.; Fisher, M.T.; Schoneich, C. Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO-). J. Biol. Chem., 2004, 279, 19486-19493. (Pubitemid 38623383)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 19486-19493
    • Khor, H.K.1    Fisher, M.T.2    Schoneich, C.3
  • 47
    • 78651282637 scopus 로고    scopus 로고
    • Helicobacter pylori: A ROSinducing bacterial species in the stomach
    • Handa, O.; Naito, Y.; Yoshikawa, T. Helicobacter pylori: a ROSinducing bacterial species in the stomach. Inflamm. Res., 2010, 59, 997-1003.
    • (2010) Inflamm. Res. , vol.59 , pp. 997-1003
    • Handa, O.1    Naito, Y.2    Yoshikawa, T.3
  • 50
    • 79952443164 scopus 로고    scopus 로고
    • Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II
    • Snijder, J.; Rose, R.J.; Raijmakers, R.; Heck, A.J. Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II. J. Struct. Biol., 2011, 174, 187-195.
    • (2011) J. Struct. Biol. , vol.174 , pp. 187-195
    • Snijder, J.1    Rose, R.J.2    Raijmakers, R.3    Heck, A.J.4
  • 51
    • 21844479556 scopus 로고    scopus 로고
    • Mediating molecular recognition by methionine oxidation: Conformational switching by oxidation of methionine in the carboxyl-terminal domain of calmodulin
    • DOI 10.1021/bi0504963
    • Anbanandam, A.; Bieber Urbauer, R.J.; Bartlett, R.K.; Smallwood, H.S.; Squier, T.C.; Urbauer, J.L. Mediating molecular recognition by methionine oxidation: conformational switching by oxidation of methionine in the carboxyl-terminal domain of calmodulin. Biochemistry, 2005, 44, 9486-9496. (Pubitemid 40962047)
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9486-9496
    • Anbanandam, A.1    Bieber Urbauer, R.J.2    Bartlett, R.K.3    Smallwood, H.S.4    Squier, T.C.5    Urbauer, J.L.6
  • 53
    • 33847794081 scopus 로고    scopus 로고
    • Analysis of the oxidative damage-induced conformational changes of apo- and holocalmodulin by dose-dependent protein oxidative surface mapping
    • DOI 10.1529/biophysj.106.099093
    • Sharp, J.S.; Tomer, K.B. Analysis of the oxidative damage-induced conformational changes of apo-and holocalmodulin by dosedependent protein oxidative surface mapping. Biophys. j., 2007, 92, 1682-1692. (Pubitemid 46393479)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1682-1692
    • Sharp, J.S.1    Tomer, K.B.2
  • 55
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • DOI 10.1016/S0065-3233(02)62004-2
    • Dunker, A.K.; Brown, C.J.; Obradovic, Z. Identification and functions of usefully disordered proteins. Adv. Protein Chem., 2002, 62, 25-49. (Pubitemid 35204867)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 56
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol., 2005, 6, 197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 57
    • 0015217648 scopus 로고
    • A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus I. Experimental procedures and chain tracing
    • Arnone, A.; Bier, C.J.; Cotton, F.A.; Day, V.W.; Hazen, E.E., Jr.; Richardson, D.C.; Yonath, A.; Richardson, J.S. A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing. J. Biol. Chem., 1971, 246, 2302-2316.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2302-2316
    • Arnone, A.1    Bier, C.J.2    Cotton, F.A.3    Day, V.W.4    Hazen Jr., E.E.5    Richardson, D.C.6    Yonath, A.7    Richardson, J.S.8
  • 59
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol., 1999, 293, 321-331. (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 60
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are natively unfolded proteins unstructured under physiologic conditions? Proteins 2000 41 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 62
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • Tompa, P., Intrinsically unstructured proteins. Trends Biochem. Sci., 2002, 27, 527-533. (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 63
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • DOI 10.1016/j.str.2003.10.002
    • Linding, R.; Jensen, L.J.; Diella, F.; Bork, P.; Gibson, T.J.; Russell, R.B. Protein disorder prediction: implications for structural proteomics. Structure, 2003, 11, 1453-1459. (Pubitemid 37412427)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5    Russell, R.B.6
  • 64
    • 68949213019 scopus 로고    scopus 로고
    • A generic method for assignment of reliability scores applied to solvent accessibility predictions
    • Petersen, B.; Petersen, T.N.; Andersen, P.; Nielsen, M.; Lundegaard, C. A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct. Biol., 2009, 9, 51.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 51
    • Petersen, B.1    Petersen, T.N.2    Andersen, P.3    Nielsen, M.4    Lundegaard, C.5
  • 65
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 66
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia, C. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol., 1976, 105, 1-12.
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-12
    • Chothia, C.1
  • 67
    • 0037340834 scopus 로고    scopus 로고
    • Real value prediction of solvent accessibility from amino acid sequence
    • DOI 10.1002/prot.10328
    • Ahmad, S.; Gromiha, M.M.; Sarai, A. Real value prediction of solvent accessibility from amino acid sequence. Proteins, 2003, 50, 629-635. (Pubitemid 36330487)
    • (2003) Proteins: Structure, Function and Genetics , vol.50 , Issue.4 , pp. 629-635
    • Ahmad, S.1    Gromiha, M.M.2    Sarai, A.3
  • 70
    • 50349086362 scopus 로고    scopus 로고
    • The twilight zone between protein order and disorder
    • Szilagyi, A.; Gyorffy, D.; Zavodszky, P. The twilight zone between protein order and disorder. Biophys. j., 2008, 95, 1612-1626.
    • (2008) Biophys. J. , vol.95 , pp. 1612-1626
    • Szilagyi, A.1    Gyorffy, D.2    Zavodszky, P.3
  • 71
    • 80051563770 scopus 로고    scopus 로고
    • Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides
    • Xue, B.; Soeria-Atmadja, D.; Gustafsson, M.G.; Hammerling, U.; Dunker, A.K.; Uversky, V.N. Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins, 2011, 79, 2595-2606.
    • (2011) Proteins , vol.79 , pp. 2595-2606
    • Xue, B.1    Soeria-Atmadja, D.2    Gustafsson, M.G.3    Hammerling, U.4    Dunker, A.K.5    Uversky, V.N.6
  • 73
    • 78650008114 scopus 로고    scopus 로고
    • Towards practical Baeyer-Villigermonooxygenases: Design of cyclohexanone monooxygenase mutants with enhanced oxidative stability
    • Opperman, D.J.; Reetz, M.T. Towards practical Baeyer- Villigermonooxygenases: design of cyclohexanone monooxygenase mutants with enhanced oxidative stability. Chembiochem, 2010, 11, 2589-2596.
    • (2010) Chembiochem , vol.11 , pp. 2589-2596
    • Opperman, D.J.1    Reetz, M.T.2
  • 74
    • 78649806846 scopus 로고    scopus 로고
    • Structural, functional and chemical changes in Pseudozyma antarctica lipase B on exposure to hydrogen peroxide
    • Tornvall, U.; Hedstrom, M.; Schillen, K.; Hatti-Kaul, R. Structural, functional and chemical changes in Pseudozyma antarctica lipase B on exposure to hydrogen peroxide. Biochimie, 2010, 92, 1867-1875.
    • (2010) Biochimie , vol.92 , pp. 1867-1875
    • Tornvall, U.1    Hedstrom, M.2    Schillen, K.3    Hatti-Kaul, R.4
  • 77
    • 77955524656 scopus 로고    scopus 로고
    • Enhancement of hydrogen pero xide stability of a novel Anabaena sp DyP-type peroxidase by site-directed mutagenesis of methionine residues
    • Ogola, H.J.; Hashimoto, N.; Miyabe, S.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y. Enhancement of hydrogen pero xide stability of a novel Anabaena sp. DyP-type peroxidase by site-directed mutagenesis of methionine residues. Appl. Microbiol. Biotechnol., 2010, 87, 1727-1736.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1727-1736
    • Ogola, H.J.1    Hashimoto, N.2    Miyabe, S.3    Ashida, H.4    Ishikawa, T.5    Shibata, H.6    Sawa, Y.7
  • 78
    • 77953083038 scopus 로고    scopus 로고
    • Molecular framework of steroid/retinoid discrimination in 17betahydroxysteroid dehydrogenase type 1 and photoreceptor-associated retinol dehydrogenase
    • Haller, F.; Moman, E.; Hartmann, R.W.; Adamski, J.; Mindnich, R. Molecular framework of steroid/retinoid discrimination in 17betahydroxysteroid dehydrogenase type 1 and photoreceptor-associated retinol dehydrogenase. J. Mol. Biol., 2010, 399, 255-267.
    • (2010) J. Mol. Biol. , vol.399 , pp. 255-267
    • Haller, F.1    Moman, E.2    Hartmann, R.W.3    Adamski, J.4    Mindnich, R.5
  • 79
    • 12844253127 scopus 로고    scopus 로고
    • Structural and functional consequences of methionine oxidation in thrombomodulin
    • DOI 10.1016/j.bbapap.2004.09.007, PII S157096390400247X, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Wood, M.J.; Helena Prieto, J.; Komives, E.A. Structural and functional consequences of methionine oxidation in thrombomodulin. Biochim. Biophys. Acta, 2005, 1703, 141-147. (Pubitemid 40170437)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 141-147
    • Wood, M.J.1    Helena Prieto, J.2    Komives, E.A.3
  • 80
    • 79953649275 scopus 로고    scopus 로고
    • Myeloperoxidase-catalyzed oxidative inactivation of human kininogens: The impairment of kininprecursor and prekallikrein-binding functions
    • Kozik, A.; Golda, A.; Mak, P.; Suder, P.; Silberring, J.; Barbasz, A.; Rapala-Kozik, M. Myeloperoxidase-catalyzed oxidative inactivation of human kininogens: the impairment of kininprecursor and prekallikrein-binding functions. Biol. Chem., 2011, 392, 263-274.
    • (2011) Biol. Chem. , vol.392 , pp. 263-274
    • Kozik, A.1    Golda, A.2    Mak, P.3    Suder, P.4    Silberring, J.5    Barbasz, A.6    Rapala-Kozik, M.7
  • 81
    • 73649104748 scopus 로고    scopus 로고
    • Formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13: A new prothrombotic mechanism in diseases associated with oxidative stress
    • Lancellotti, S.; De Filippis, V.; Pozzi, N.; Peyvandi, F.; Palla, R.; Rocca, B.; Rutella, S.; Pitocco, D.; Mannucci, P.M.; De Cristofaro, R., Formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13: A new prothrombotic mechanism in diseases associated with oxidative stress. Free Radic. Biol. Med., 2010, 48, 446-456.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 446-456
    • Lancellotti, S.1    De Filippis, V.2    Pozzi, N.3    Peyvandi, F.4    Palla, R.5    Rocca, B.6    Rutella, S.7    Pitocco, D.8    Mannucci, P.M.9    De Cristofaro, R.10
  • 82
    • 77949362124 scopus 로고    scopus 로고
    • Myeloperoxidase: An oxidative pathway for generating dysfunctional high-density lipoprotein
    • Shao, B.; Oda, M.N.; Oram, J.F.; Heinecke, J.W. Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein. Chem. Res. Toxicol., 2010, 23, 447-454.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 447-454
    • Shao, B.1    Oda, M.N.2    Oram, J.F.3    Heinecke, J.W.4
  • 83
    • 78650528867 scopus 로고    scopus 로고
    • Stability of human growth hormone: Influence of methionine oxidation on thermal folding
    • Mulinacci, F.; Capelle, M.A.; Gurny, R.; Drake, A.F.; Arvinte, T. Stability of human growth hormone: influence of methionine oxidation on thermal folding. J. Pharm. Sci., 2011, 100, 451-463.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 451-463
    • Mulinacci, F.1    Capelle, M.A.2    Gurny, R.3    Drake, A.F.4    Arvinte, T.5
  • 85
    • 79952714479 scopus 로고    scopus 로고
    • Rational development of a strategy for modifying the aggregatibility of proteins
    • Tan, Z.; Shang, S.; Danishefsky, S.J. Rational development of a strategy for modifying the aggregatibility of proteins. Proc. Natl. Acad. Sci. USA, 2011, 108, 4297-4302.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4297-4302
    • Tan, Z.1    Shang, S.2    Danishefsky, S.J.3
  • 86
    • 78650718216 scopus 로고    scopus 로고
    • Strategy for identification and detection of multiple oxidative modifications within proteins applied on persulfate-oxidized hemoglobin and human serum albumin
    • Mortstedt, H.; Jeppsson, M.C.; Ferrari, G.; Jonsson, B.A.; Karedal, M.H.; Lindh, C.H. Strategy for identification and detection of multiple oxidative modifications within proteins applied on persulfate-oxidized hemoglobin and human serum albumin. Rapid Commun. Mass Spectrom., 2011, 25, 327-340.
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , pp. 327-340
    • Mortstedt, H.1    Jeppsson, M.C.2    Ferrari, G.3    Jonsson, B.A.4    Karedal, M.H.5    Lindh, C.H.6
  • 89
    • 79956303754 scopus 로고    scopus 로고
    • Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase
    • Mahawar, M.; Tran, V.; Sharp, J.S.; Maier, R.J. Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase. J. Biol. Chem., 2011, 286, 19159-19169.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19159-19169
    • Mahawar, M.1    Tran, V.2    Sharp, J.S.3    Maier, R.J.4
  • 91
    • 35748932403 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals
    • DOI 10.1042/BJ20070929
    • Kim, H.Y.; Gladyshev, V.N., Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem. J., 2007, 407, 321-329. (Pubitemid 350058466)
    • (2007) Biochemical Journal , vol.407 , Issue.3 , pp. 321-329
    • Kim, H.-Y.1    Gladyshev, V.N.2
  • 92
    • 77958198646 scopus 로고    scopus 로고
    • Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry
    • Pan, Y.; Brown, L.; Konermann, L. Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry. J. Am. Soc. Mass Spectrom., 2010, 21, 1947-1956.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1947-1956
    • Pan, Y.1    Brown, L.2    Konermann, L.3


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