메뉴 건너뛰기




Volumn 50, Issue 6, 2011, Pages 749-762

Factors influencing protein tyrosine nitration-structure-based predictive models

Author keywords

Free radicals; Hydropathic interactions; Oxidative stress; Tyrosine nitration; Tyrosyl radical

Indexed keywords

AMINO ACID; PROTEIN TYROSINE KINASE; RADICAL; SULFUR;

EID: 79951676058     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.12.016     Document Type: Article
Times cited : (42)

References (80)
  • 1
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • DOI 10.1016/S0006-291X(03)00814-3
    • H. Ischiropoulos Biological selectivity and functional aspects of protein tyrosine nitration Biochem. Biophys. Res. Commun. 305 2003 776 783 (Pubitemid 36581936)
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , Issue.3 , pp. 776-783
    • Ischiropoulos, H.1
  • 3
    • 0036229078 scopus 로고    scopus 로고
    • Role of nitric oxide in inflammatory conditions
    • DOI 10.1159/000054723
    • R.C. Blantz, and K. Munger Role of nitric oxide in inflammatory conditions Nephron 90 2002 373 378 (Pubitemid 34310099)
    • (2002) Nephron , vol.90 , Issue.4 , pp. 373-378
    • Blantz, R.C.1    Munger, K.2
  • 4
    • 73849130301 scopus 로고    scopus 로고
    • Nitric oxide synthase isoenzyme expression and activity in peripheral lung tissue of patients with chronic obstructive pulmonary disease
    • C. Brindicci, S.A. Kharitonov, M. Ito, M.W. Elliott, J.C. Hogg, P.J. Barnes, and K. Ito Nitric oxide synthase isoenzyme expression and activity in peripheral lung tissue of patients with chronic obstructive pulmonary disease Am. J. Respir. Crit. Care Med. 181 2010 21 30
    • (2010) Am. J. Respir. Crit. Care Med. , vol.181 , pp. 21-30
    • Brindicci, C.1    Kharitonov, S.A.2    Ito, M.3    Elliott, M.W.4    Hogg, J.C.5    Barnes, P.J.6    Ito, K.7
  • 8
    • 77949386273 scopus 로고    scopus 로고
    • 2+ channels on excitation-transcription coupling in colonic inflammation
    • 2+ channels on excitation-transcription coupling in colonic inflammation Br. J. Pharmacol. 159 2010 1226 1235
    • (2010) Br. J. Pharmacol. , vol.159 , pp. 1226-1235
    • Kang, M.1    Ross, G.R.2    Akbarali, H.I.3
  • 12
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • P. Pacher, J.S. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424 (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 13
    • 77953560003 scopus 로고    scopus 로고
    • Loss of stromal caveolin-1 leads to oxidative stress, mimics hypoxia and drives inflammation in the tumor microenvironment, conferring the "reverse Warburg effect": A transcriptional informatics analysis with validation
    • S. Pavlides, A. Tsirigos, I. Vera, N. Flomenberg, P.G. Frank, M.C. Casimiro, C. Wang, P. Fortina, S. Addya, R.G. Pestell, U.E. Martinez-Outschoorn, F. Sotgia, and M.P. Lisanti Loss of stromal caveolin-1 leads to oxidative stress, mimics hypoxia and drives inflammation in the tumor microenvironment, conferring the "reverse Warburg effect": a transcriptional informatics analysis with validation Cell Cycle 9 2010 2201 2219
    • (2010) Cell Cycle , vol.9 , pp. 2201-2219
    • Pavlides, S.1    Tsirigos, A.2    Vera, I.3    Flomenberg, N.4    Frank, P.G.5    Casimiro, M.C.6    Wang, C.7    Fortina, P.8    Addya, S.9    Pestell, R.G.10    Martinez-Outschoorn, U.E.11    Sotgia, F.12    Lisanti, M.P.13
  • 14
    • 66749102277 scopus 로고    scopus 로고
    • Sepiapterin decreases acute rejection and apoptosis in cardiac transplants independently of changes in nitric oxide and inducible nitric-oxide synthase dimerization
    • G.M. Pieper, I.A. Ionova, B.C. Cooley, R.Q. Migrino, A.K. Khanna, J. Whitsett, and J. Vasquez-Vivar Sepiapterin decreases acute rejection and apoptosis in cardiac transplants independently of changes in nitric oxide and inducible nitric-oxide synthase dimerization J. Pharmacol. Exp. Ther. 329 2009 890 899
    • (2009) J. Pharmacol. Exp. Ther. , vol.329 , pp. 890-899
    • Pieper, G.M.1    Ionova, I.A.2    Cooley, B.C.3    Migrino, R.Q.4    Khanna, A.K.5    Whitsett, J.6    Vasquez-Vivar, J.7
  • 16
    • 13444287877 scopus 로고    scopus 로고
    • Site-specific nitration and oxidative dityrosine bridging of the τ protein by peroxynitrite: Implications for Alzheimer's disease
    • DOI 10.1021/bi047982v
    • M.R. Reynolds, R.W. Berry, and L.I. Binder Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease Biochemistry 44 2005 1690 1700 (Pubitemid 40204410)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1690-1700
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 17
    • 34250854596 scopus 로고    scopus 로고
    • Nitration in neurodegeneration: Deciphering the 'hows' 'nYs'
    • DOI 10.1021/bi700430y
    • M.R. Reynolds, R.W. Berry, and L.I. Binder Nitration in neurodegeneration: deciphering the "Hows" "nYs" Biochemistry 46 2007 7325 7336 (Pubitemid 46986359)
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7325-7336
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 18
    • 76949089289 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in mouse models of Parkinson's disease revealed by transcriptomics and proteomics
    • D.J. Smith Mitochondrial dysfunction in mouse models of Parkinson's disease revealed by transcriptomics and proteomics J. Bioenerg. Biomembr. 41 2009 487 491
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 487-491
    • Smith, D.J.1
  • 19
    • 67149117913 scopus 로고    scopus 로고
    • Atherosclerosis: A link between lipid intake and protein tyrosine nitration
    • R.K. Upmacis Atherosclerosis: a link between lipid intake and protein tyrosine nitration Lipid Insights 2 2008 75 78
    • (2008) Lipid Insights , vol.2 , pp. 75-78
    • Upmacis, R.K.1
  • 20
    • 77949502858 scopus 로고    scopus 로고
    • Peroxynitrite-mediated oxidative modifications of complex II: Relevance in myocardial infarction
    • L. Zhang, C.L. Chen, P.T. Kang, V. Garg, K. Hu, K.B. Green-Church, and Y.R. Chen Peroxynitrite-mediated oxidative modifications of complex II: relevance in myocardial infarction Biochemistry 49 2010 2529 2539
    • (2010) Biochemistry , vol.49 , pp. 2529-2539
    • Zhang, L.1    Chen, C.L.2    Kang, P.T.3    Garg, V.4    Hu, K.5    Green-Church, K.B.6    Chen, Y.R.7
  • 22
    • 0037424429 scopus 로고    scopus 로고
    • Lack of tyrosine nitration by hypochlorous acid in the presence of physiological concentrations of nitrite: Implications for the role of nitryl chloride in tyrosine nitration in vivo
    • DOI 10.1074/jbc.M211086200
    • M. Whiteman, J.L. Siau, and B. Halliwell Lack of tyrosine nitration by hypochlorous acid in the presence of physiological concentrations of nitrite: implications for the role of nitryl chloride in tyrosine nitration in vivo J. Biol. Chem. 278 2003 8380 8384 (Pubitemid 36800587)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8380-8384
    • Whiteman, M.1    Siau, J.L.2    Halliwell, B.3
  • 26
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • DOI 10.1006/abbi.1998.0755
    • H. Ischiropoulos Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species Arch. Biochem. Biophys. 356 1998 1 11 (Pubitemid 28364347)
    • (1998) Archives of Biochemistry and Biophysics , vol.356 , Issue.1 , pp. 1-11
    • Ischiropoulos, H.1
  • 27
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • B.E. Kemp, and R.B. Pearson Protein kinase recognition sequence motifs Trends Biochem. Sci. 15 1990 342 346 (Pubitemid 20255495)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.9 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 31
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration-functional alteration or just a biomarker?
    • J.M. Souza, G. Peluffo, and R. Radi Protein tyrosine nitration-functional alteration or just a biomarker? Free Radic. Biol. Med. 45 2008 357 366
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 32
    • 23844555866 scopus 로고    scopus 로고
    • The highly conserved Glu149 and Tyr190 residues contribute to peroxynitrite-mediated nitrotyrosine formation and the catalytic activity of cytochrome P450 2B1
    • DOI 10.1021/tx050100o
    • H.L. Lin, H. Zhang, L. Waskell, and P.F. Hollenberg The highly conserved Glu149 and Tyr190 residues contribute to peroxynitrite-mediated nitrotyrosine formation and the catalytic activity of cytochrome P450 2B1 Chem. Res. Toxicol. 18 2005 1203 1210 (Pubitemid 41170244)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.8 , pp. 1203-1210
    • Lin, H.-L.1    Zhang, H.2    Waskell, L.3    Hollenberg, P.F.4
  • 33
    • 34249101633 scopus 로고    scopus 로고
    • Protein tyrosine nitration in hydrophilic and hydrophobic environments
    • DOI 10.1007/s00726-006-0425-8, Special Issue: Focus on Amino Acid and Protein Modification by Oxygen and Nitrogen Species
    • S. Bartesaghi, G. Ferrer-Sueta, G. Peluffo, V. Valez, H. Zhang, B. Kalyanaraman, and R. Radi Protein tyrosine nitration in hydrophilic and hydrophobic environments Amino Acids 32 2007 501 515 (Pubitemid 46790931)
    • (2007) Amino Acids , vol.32 , Issue.4 , pp. 501-515
    • Bartesaghi, S.1    Ferrer-Sueta, G.2    Peluffo, G.3    Valez, V.4    Zhang, H.5    Kalyanaraman, B.6    Radi, R.7
  • 34
    • 33744959547 scopus 로고    scopus 로고
    • Mechanistic studies of peroxynitrite-mediated tyrosine nitration in membranes using the hydrophobic probe N-t-BOC-L-tyrosine tert-butyl ester
    • DOI 10.1021/bi060363x
    • S. Bartesaghi, V. Valez, M. Trujillo, G. Peluffo, N. Romero, H. Zhang, B. Kalyanaraman, and R. Radi Mechanistic studies of peroxynitrite-mediated tyrosine nitration in membranes using the hydrophobic probe N-t-BOC-l-tyrosine tert-butyl ester Biochemistry 45 2006 6813 6825 (Pubitemid 43856667)
    • (2006) Biochemistry , vol.45 , Issue.22 , pp. 6813-6825
    • Bartesaghi, S.1    Valez, V.2    Trujillo, M.3    Peluffo, G.4    Romero, N.5    Zhang, H.6    Kalyanaraman, B.7    Radi, R.8
  • 35
    • 37249051057 scopus 로고    scopus 로고
    • Peroxynitrite inactivation of human cytochrome P450s 2B6 and 2E1: Heme modification and site-specific nitrotyrosine formation
    • DOI 10.1021/tx700220e
    • H.L. Lin, E. Myshkin, L. Waskell, and P.F. Hollenberg Peroxynitrite inactivation of human cytochrome P450s 2B6 and 2E1: heme modification and site-specific nitrotyrosine formation Chem. Res. Toxicol. 20 2007 1612 1622 (Pubitemid 350275606)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.11 , pp. 1612-1622
    • Lin, H.-L.1    Myshkin, E.2    Waskell, L.3    Hollenberg, P.F.4
  • 37
    • 0032556905 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
    • DOI 10.1038/34923
    • J.P. Eiserich, M. Hristova, C.E. Cross, A.D. Jones, B.A. Freeman, B. Halliwell, and A. van der Vliet Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils Nature 391 1998 393 397 (Pubitemid 28093514)
    • (1998) Nature , vol.391 , Issue.6665 , pp. 393-397
    • Eiserich, J.P.1    Hristova, M.2    Cross, C.E.3    Jones, A.D.4    Freeman, B.A.5    Halliwell, B.6    Van Der Vliet, A.7
  • 39
    • 20144370272 scopus 로고    scopus 로고
    • Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite
    • DOI 10.1021/bi0474620
    • C. Batthyany, J.M. Souza, R. Duran, A. Cassina, C. Cervenansky, and R. Radi Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite Biochemistry 44 2005 8038 8046 (Pubitemid 40776665)
    • (2005) Biochemistry , vol.44 , Issue.22 , pp. 8038-8046
    • Batthyany, C.1    Souza, J.M.2    Duran, R.3    Cassina, A.4    Cervenansky, C.5    Radi, R.6
  • 40
    • 21244457292 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry
    • DOI 10.1074/jbc.M501773200
    • J. Kanski, S.J. Hong, and C. Schöneich Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine- containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry J. Biol. Chem. 280 2005 24261 24266 (Pubitemid 40884916)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 24261-24266
    • Kanski, J.1    Hong, S.J.2    Schoneich, C.3
  • 41
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxide-dependent generation of reactive species in sickle cell disease: Actin tyrosine nitration induces defective cytoskeletal polymerization
    • DOI 10.1074/jbc.M208916200
    • M. Aslan, T.M. Ryan, T.M. Townes, L. Coward, M.C. Kirk, S. Barnes, C.B. Alexander, S.S. Rosenfeld, and B.A. Freeman Nitric oxide-dependent generation of reactive species in sickle cell disease: actin tyrosine induces defective cytoskeletal polymerization J. Biol. Chem. 278 2003 4194 4204 (Pubitemid 36801157)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 4194-4204
    • Aslan, M.1    Ryan, T.M.2    Townes, T.M.3    Coward, L.4    Kirk, M.C.5    Barnes, S.6    Alexander, C.B.7    Rosenfeld, S.S.8    Freeman, B.A.9
  • 43
    • 79951674410 scopus 로고    scopus 로고
    • Graves, P.R.; Yakovlev, V.A.; Mikkelsen, R.B. unpublished data
    • Graves, P.R.; Yakovlev, V.A.; Mikkelsen, R.B. unpublished data.
  • 44
    • 18844455826 scopus 로고    scopus 로고
    • Nitration of the tyrosyl radical in ribonucleotide reductase by nitrogen dioxide: A gamma radiolysis study
    • DOI 10.1016/j.freeradbiomed.2005.02.013, PII S0891584905000857
    • M. Lepoivre, C. Houee-Levin, K. Coeytaux, P. Decottignies, G. Auger, and G. Lemaire Nitration of the tyrosyl radical in ribonucleotide reductase by nitrogen dioxide: a γ radiolysis study Free Radic. Biol. Med. 38 2005 1511 1517 (Pubitemid 40693835)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.11 , pp. 1511-1517
    • Lepoivre, M.1    Houee-Levin, C.2    Coeytaux, K.3    Decottignies, P.4    Auger, G.5    Lemaire, G.6
  • 45
    • 77953894189 scopus 로고    scopus 로고
    • Nitration of the tumor suppressor protein p53 at tyrosine 327 promotes p53 oligomerization and activation
    • V.A. Yakovlev, A.S. Bayden, P.A. Graves, G.E. Kellogg, and R.B. Mikkelsen Nitration of the tumor suppressor protein p53 at tyrosine 327 promotes p53 oligomerization and activation Biochemistry 49 2010 5331 5339
    • (2010) Biochemistry , vol.49 , pp. 5331-5339
    • Yakovlev, V.A.1    Bayden, A.S.2    Graves, P.A.3    Kellogg, G.E.4    Mikkelsen, R.B.5
  • 46
    • 0032501998 scopus 로고    scopus 로고
    • Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues
    • DOI 10.1021/bi971894b
    • L.A. MacMillan-Crow, J.P. Crow, and J.A. Thompson Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues Biochemistry 37 1998 1613 1622 (Pubitemid 28093677)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1613-1622
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Thompson, J.A.3
  • 47
    • 0034712707 scopus 로고    scopus 로고
    • Peroxynitrite-mediated nitration of the stable free radical tyrosine residue of the ribonucleotide reductase small subunit
    • DOI 10.1021/bi992206m
    • O. Guittet, P. Decottignies, L. Serani, Y. Henry, P. Le Marechal, O. Laprevote, and M. Lepoivre Peroxynitrite-mediated nitration of the stable free radical tyrosine residue of the ribonucleotide reductase small subunit Biochemistry 39 2000 4640 4648 (Pubitemid 30225327)
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4640-4648
    • Guittet, O.1    Decottignies, P.2    Serani, L.3    Henry, Y.4    Le Marechal, P.5    Laprevote, O.6    Lepoivre, M.7
  • 48
    • 0019557179 scopus 로고
    • The role of tyrosine residues in the function of bacteriorhodopsin
    • H.-D. Lemke, and D. Oesterhelt The role of tyrosine residues in the function of bacteriorhodopsin Eur. J. Biochem. 115 1981 595 604
    • (1981) Eur. J. Biochem. , vol.115 , pp. 595-604
    • Lemke, H.-D.1    Oesterhelt, D.2
  • 49
    • 24644469955 scopus 로고    scopus 로고
    • Sites and mechanisms of aconitase inactivation by peroxynitrite: Modulation by citrate and glutathione
    • DOI 10.1021/bi0509393
    • D. Han, R. Canali, J. Garcia, R. Aguilera, T.K. Gallaher, and E. Cadenas Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione Biochemistry 44 2005 11986 11996 (Pubitemid 41285696)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 11986-11996
    • Han, D.1    Canali, R.2    Garcia, J.3    Aguilera, R.4    Gallaher, T.K.5    Cadenas, E.6
  • 50
    • 33644850478 scopus 로고    scopus 로고
    • Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite
    • DOI 10.1074/jbc.M509480200
    • Y. Ji, I. Neverova, J.E. Van Eyk, and B.M. Bennett Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite J. Biol. Chem. 281 2006 1986 1991 (Pubitemid 43845785)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1986-1991
    • Ji, Y.1    Neverova, I.2    Van Eyk, J.E.3    Bennett, B.M.4
  • 52
    • 79951672444 scopus 로고    scopus 로고
    • Available at http://www.tripos.com.
  • 53
    • 0031551573 scopus 로고    scopus 로고
    • Hydropathic analysis of the non-covalent interactions between molecular subunits of structurally characterized hemoglobins
    • DOI 10.1006/jmbi.1997.1249
    • D.J. Abraham, G.E. Kellogg, J.M. Holt, and G.K. Ackers Hydropathic analysis of the non-covalent interactions between molecular subunits of structurally characterized hemoglobins J. Mol. Biol. 272 1997 613 632 (Pubitemid 27429846)
    • (1997) Journal of Molecular Biology , vol.272 , Issue.4 , pp. 613-632
    • Abraham, D.J.1    Kellogg, G.E.2    Holt, J.M.3    Ackers, G.K.4
  • 54
    • 0037030649 scopus 로고    scopus 로고
    • Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water
    • DOI 10.1021/jm0200299
    • P. Cozzini, M. Fornabaio, A. Marabotti, D.J. Abraham, G.E. Kellogg, and A. Mozzarelli Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water J. Med. Chem. 45 2002 2469 2483 (Pubitemid 34595216)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.12 , pp. 2469-2483
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogg, G.E.5    Mozzarelli, A.6
  • 56
    • 4143131457 scopus 로고    scopus 로고
    • The Importance of being exhaustive: Optimization of bridging structural water molecules and water networks in models of biological systems
    • G.E. Kellogg, and D.L. Chen The Importance of being exhaustive: optimization of bridging structural water molecules and water networks in models of biological systems Chem. Biodivers. 1 2004 98 105
    • (2004) Chem. Biodivers. , vol.1 , pp. 98-105
    • Kellogg, G.E.1    Chen, D.L.2
  • 57
    • 36649012579 scopus 로고    scopus 로고
    • Complexity in modeling and understanding protonation states: Computational titration of HIV-1-protease-inhibitor complexes
    • DOI 10.1002/cbdv.200790210
    • A. Tripathi, M. Fornabaio, F. Spyrakis, A. Mozzarelli, P. Cozzini, and G.E. Kellogg Complexity in modeling and understanding protonation states: computational titration of HIV-1-protease-inhibitor complexes Chem. Biodivers. 4 2007 2564 2577 (Pubitemid 350193483)
    • (2007) Chemistry and Biodiversity , vol.4 , Issue.11 , pp. 2564-2577
    • Tripathia, A.1    Fomabaioa, M.2    Spjrakis, F.3    Mozzarelli, A.4    Cozzini, P.5    Kellogg, G.E.6
  • 58
    • 0141923634 scopus 로고    scopus 로고
    • Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 2. Computational titration and pH effects in molecular models of neuraminidase-inhibitor complexes
    • DOI 10.1021/jm0302593
    • M. Fornabaio, P. Cozzini, A. Mozzarelli, D.J. Abraham, and G.E. Kellogg Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 2. Computational titration and pH effects in molecular models of neuraminidase-inhibitor complexes J. Med. Chem. 46 2003 4487 4500 (Pubitemid 37238750)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.21 , pp. 4487-4500
    • Fornabaio, M.1    Cozzini, P.2    Mozzarelli, A.3    Abraham, D.J.4    Kellogg, G.E.5
  • 59
    • 69249222839 scopus 로고    scopus 로고
    • Web application for studying the free energy of binding and protonation states of protein-ligand complexes based on HINT
    • A.S. Bayden, M. Fornabaio, J.N. Scarsdale, and G.E. Kellogg Web application for studying the free energy of binding and protonation states of protein-ligand complexes based on HINT J. Comput.-Aided Mol. Des. 23 2009 621 632
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 621-632
    • Bayden, A.S.1    Fornabaio, M.2    Scarsdale, J.N.3    Kellogg, G.E.4
  • 62
    • 76049125210 scopus 로고    scopus 로고
    • Combination of ant colony optimization with various local search strategies: A novel method for variable selection in multivariate calibration and QSPR study
    • M. Shamsipur, V. Zare-Shahabadi, B. Hemmateenejad, and M. Akhond Combination of ant colony optimization with various local search strategies: a novel method for variable selection in multivariate calibration and QSPR study QSAR Comb. Sci. 28 2009 1263 1275
    • (2009) QSAR Comb. Sci. , vol.28 , pp. 1263-1275
    • Shamsipur, M.1    Zare-Shahabadi, V.2    Hemmateenejad, B.3    Akhond, M.4
  • 63
    • 0035227873 scopus 로고    scopus 로고
    • A Novel Method for Building Regression Tree Models for QSAR Based on Artificial Ant Colony Systems
    • DOI 10.1021/ci000336s
    • S. Izrailev, and D.K. Agrafiotis A novel method for building regression tree models for QSAR based on artificial ant colony systems J. Chem. Inf. Comput. Sci. 41 2001 176 180 (Pubitemid 33645687)
    • (2001) Journal of Chemical Information and Computer Sciences , vol.41 , Issue.1 , pp. 176-180
    • Izrailev, S.1    Agrafiotis, D.2
  • 67
    • 1942455335 scopus 로고    scopus 로고
    • Protein Control of Electron Transfer Rates via Polarization: Molecular Dynamics Studies of Rubredoxin
    • E.A. Dolana, R.B. Yelle, B.W. Beck, J.T. Fischer, and T. Ichiye Protein control of electron transfer rates via polarization: molecular dynamics studies of rubredoxin Biophys. J. 86 2004 2030 2036 (Pubitemid 38524395)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2030-2036
    • Dolan, E.A.1    Yelle, R.B.2    Beck, B.W.3    Fischer, J.T.4    Ichiye, T.5
  • 68
    • 0041322950 scopus 로고    scopus 로고
    • Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: Evidence for the participation of other residues
    • DOI 10.1046/j.1432-1033.2003.03741.x
    • M. Stuart-Audette, Y. Blouquit, M. Faraggi, C. Sicard-Roselli, C. Houee-Levin, and P. Jolles Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: evidence for the participation of other residues Eur. J. Biochem. 270 2003 3565 3571 (Pubitemid 37046737)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.17 , pp. 3565-3571
    • Stuart-Audette, M.1    Blouquit, Y.2    Faraggi, M.3    Sicard-Roselli, C.4    Houee-Levin, C.5    Jolles, P.6
  • 69
    • 0032032705 scopus 로고    scopus 로고
    • Intramolecular electron transfer in the dipeptide, histidyltyrosine: A pulse radiolysis study
    • DOI 10.1016/S0891-5849(97)00340-7, PII S0891584997003407
    • C. Tanner, S. Navaratnam, and B.J. Parsons Intramolecular electron transfer in the dipeptide histidyltyrosine: a pulse radiolysis study Free Radic. Biol. Med. 24 1998 671 678 (Pubitemid 28150486)
    • (1998) Free Radical Biology and Medicine , vol.24 , Issue.4 , pp. 671-678
    • Tanner, C.1    Navaratnam, S.2    Parsons, B.J.3
  • 73
    • 0347117585 scopus 로고    scopus 로고
    • Aspects, mechanism, and biological relevance of mitochondrial protein nitration sustained by mitochondrial nitric oxide synthase
    • S.L. Elfering, V.L. Haynes, N.J. Traaseth, A. Ettl, and C. Giulivi Aspects, mechanism, and biological relevance of mitochondrial protein nitration sustained by mitochondrial nitric oxide synthase Am. J. Physiol. Heart Circ. Physiol. 286 2004 H22 H29
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.286
    • Elfering, S.L.1    Haynes, V.L.2    Traaseth, N.J.3    Ettl, A.4    Giulivi, C.5
  • 74
    • 44349183748 scopus 로고    scopus 로고
    • Solvent-exposed residues located in the β-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach
    • DOI 10.1002/prot.21854
    • P. Mora, R.J. Carbajo, A. Pineda-Lucena, M.M. Sanchez Del Pino, and E. Perez-Paya Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-a structural and combinatorial approach Proteins 71 2008 1670 1685 (Pubitemid 351732926)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.4 , pp. 1670-1685
    • Mora, P.1    Carbajo, R.J.2    Pineda-Lucena, A.3    Sanchez Del Pino, M.M.4    Perez-Paya, E.5
  • 75
    • 0031951844 scopus 로고    scopus 로고
    • Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template
    • DOI 10.1107/S0907444997006550
    • P.R. Mittl, P. Chene, and M.G. Grutter Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template Acta Crystallogr. D 54 1998 86 89 (Pubitemid 28111121)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.1 , pp. 86-89
    • Mittl, P.R.E.1    Chene, P.2    Grutter, M.G.3
  • 76
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • P.D. Jeffrey, S. Gorina, and N.P. Pavletich Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms Science 267 1995 1498 1502
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 78
    • 64749111770 scopus 로고    scopus 로고
    • Activation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: Does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function?
    • V.S. Sharov, N.A. Galeva, E.S. Dremina, T.D. Williams, and C. Schöneich Activation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function? Arch. Biochem. Biophys. 484 2009 155 166
    • (2009) Arch. Biochem. Biophys. , vol.484 , pp. 155-166
    • Sharov, V.S.1    Galeva, N.A.2    Dremina, E.S.3    Williams, T.D.4    Schöneich, C.5
  • 79
    • 33646184227 scopus 로고    scopus 로고
    • Age-associated tyrosine nitration of rat skeletal muscle glycogen phosphorylase b: Characterization by HPLC-nanoelectrospray-tandem mass spectrometry
    • V.S. Sharov, N.A. Galeva, J. Kanski, T.D. Williams, and C. Schöneich Age-associated tyrosine nitration of rat skeletal muscle glycogen phosphorylase b: characterization by HPLC-nanoelectrospray-tandem mass spectrometry Exp. Gerontol. 41 2006 407 416
    • (2006) Exp. Gerontol. , vol.41 , pp. 407-416
    • Sharov, V.S.1    Galeva, N.A.2    Kanski, J.3    Williams, T.D.4    Schöneich, C.5
  • 80
    • 34548420662 scopus 로고    scopus 로고
    • Nitration of a Critical Tyrosine Residue in the Allosteric Inhibitor Site of Muscle Glycogen Phosphorylase Impairs its Catalytic Activity
    • DOI 10.1016/j.jmb.2007.07.011, PII S0022283607009382
    • J. Dairou, B. Pluvinage, J. Noiran, E. Petit, J. Vinh, I. Haddad, J. Mary, J.-M. Dupret, and F. Rodrigues-Lima Nitration of a critical tyrosine residue in the allosteric inhibitor site of muscle glycogen phosphorylase impairs its catalytic activity J. Mol. Biol. 372 2007 1009 1021 (Pubitemid 47368347)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.4 , pp. 1009-1021
    • Dairou, J.1    Pluvinage, B.2    Noiran, J.3    Petit, E.4    Vinh, J.5    Haddad, I.6    Mary, J.7    Dupret, J.-M.8    Rodrigues-Lima, F.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.