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Volumn 183, Issue , 2013, Pages 19-29

High pressure effects on allergen food proteins

Author keywords

Allergen protein; Food allergen; High pressure; IgE binding; Unfolding

Indexed keywords

ALLERGEN FOOD PROTEIN; ARA H2 PROTEIN; BOS D5 PROTEIN; DAU C1 PROTEIN; FOOD ALLERGEN; GAD M1 PROTEIN; GAL D2 PROTEIN; IMMUNOGLOBULIN E; MAL D1 PROTEIN; MAL D3 PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84886640366     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.06.009     Document Type: Article
Times cited : (52)

References (125)
  • 2
    • 0034944834 scopus 로고    scopus 로고
    • Effects of hydrostatic pressure on lipid and surfactant phases
    • DOI 10.1016/S1359-0294(01)00092-9, PII S1359029401000929
    • R. Winter Effects of hydrostatic pressure on lipid and surfactant phases Curr. Opin. Colloid Interface Sci. 6 2001 303 312 (Pubitemid 32621665)
    • (2001) Current Opinion in Colloid and Interface Science , vol.6 , Issue.3 , pp. 303-312
    • Winter, R.1
  • 4
    • 0036836450 scopus 로고    scopus 로고
    • Protein hydration water: Structure and thermodynamics
    • DOI 10.1016/S0167-7322(02)00100-9, PII S0167732202001009
    • J.C. Smith, F. Merzel, C.S. Verma, and S. Fischer Protein hydration water: structure and thermodynamics J. Mol. Liq. 101 2002 27 33 (Pubitemid 35039709)
    • (2002) Journal of Molecular Liquids , vol.101 , Issue.1-3 , pp. 27-33
    • Smith, J.C.1    Merzel, F.2    Verma, C.S.3    Fischer, S.4
  • 6
    • 33748743556 scopus 로고    scopus 로고
    • Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A
    • DOI 10.1074/jbc.M604216200
    • G. Schay, L. Smeller, A. Tsuneshige, T. Yonetani, and J. Fidy Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A J. Biol. Chem. 281 2006 25972 25983 (Pubitemid 44401803)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 25972-25983
    • Schay, G.1    Smeller, L.2    Tsuneshige, A.3    Yonetani, T.4    Fidy, J.5
  • 7
    • 0033596963 scopus 로고    scopus 로고
    • Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin
    • L. Smeller, P. Rubens, and K. Heremans Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin Biochemistry 38 1999 3816 3820
    • (1999) Biochemistry , vol.38 , pp. 3816-3820
    • Smeller, L.1    Rubens, P.2    Heremans, K.3
  • 9
    • 0033067697 scopus 로고    scopus 로고
    • High pressure fourier transform infrared spectroscopy of poly(dA)poly(dT), poly(dA) and poly(dT)
    • DOI 10.1016/S0301-4622(98)00234-8, PII S0301462298002348
    • M.C. Lin, P. Eid, P.T.T. Wong, and R.B. Macgregor High pressure Fourier transform infrared spectroscopy of poly(dA)poly(dT), poly(dA) and poly(dT) Biophys. Chem. 76 1999 87 94 (Pubitemid 29092785)
    • (1999) Biophysical Chemistry , vol.76 , Issue.2 , pp. 87-94
    • Lin, M.-C.1    Eid, P.2    Wong, P.T.T.3    MacGregor Jr., R.B.4
  • 10
    • 21644459337 scopus 로고    scopus 로고
    • Temperature-pressure configurational landscape of lipid bilayers and proteins
    • R. Winter, and W. Dzwolak Temperature-pressure configurational landscape of lipid bilayers and proteins Cell. Mol. Biol. 50 2004 397 417
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 397-417
    • Winter, R.1    Dzwolak, W.2
  • 11
    • 79951559073 scopus 로고    scopus 로고
    • Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: Results from a combined calorimetry, spectroscopy and microscopy study
    • S. Kapoor, A. Werkmueller, C. Denter, Y. Zhai, J. Markgraf, K. Weise, N. Opitz, and R. Winter Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: results from a combined calorimetry, spectroscopy and microscopy study Biochimica Et Biophysica Acta-Biomembranes 1808 2011 1187 1195
    • (2011) Biochimica et Biophysica Acta-Biomembranes , vol.1808 , pp. 1187-1195
    • Kapoor, S.1    Werkmueller, A.2    Denter, C.3    Zhai, Y.4    Markgraf, J.5    Weise, K.6    Opitz, N.7    Winter, R.8
  • 12
    • 79952372060 scopus 로고    scopus 로고
    • Phase behavior and kinetics of pressure-jump induced phase transitions of bicellar lipid mixtures
    • C. Jeworrek, S. Uelner, and R. Winter Phase behavior and kinetics of pressure-jump induced phase transitions of bicellar lipid mixtures Soft Matter 7 2011 2709 2719
    • (2011) Soft Matter , vol.7 , pp. 2709-2719
    • Jeworrek, C.1    Uelner, S.2    Winter, R.3
  • 14
    • 33847312741 scopus 로고    scopus 로고
    • Towards an understanding of the temperature/ pressure configurational and free-energy landscape of biomolecules
    • DOI 10.1515/JNETDY.2007.003
    • R. Winter, D. Lopes, S. Grudzielanek, and K. Vogtt Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules J. Non-Equilib. Thermodyn. 32 2007 41 97 (Pubitemid 46326288)
    • (2007) Journal of Non-Equilibrium Thermodynamics , vol.32 , Issue.1 , pp. 41-97
    • Lopes, D.1    Grudzielanek, S.2    Vogtt, K.3    Winter, R.4
  • 15
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • DOI 10.1016/S0968-0004(01)01949-1, PII S0968000401019491
    • J.L. Silva, D. Foguel, and C.A. Royer Pressure provides new insights into protein folding, dynamics and structure Trends Biochem. Sci. 26 2001 612 618 (Pubitemid 32925191)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 16
    • 0037171122 scopus 로고    scopus 로고
    • High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes
    • DOI 10.1016/S0167-4838(01)00331-4, PII S0167483801003314
    • C. Balny, P. Masson, and K. Heremans High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1595 2002 3 10 (Pubitemid 34442632)
    • (2002) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1595 , Issue.1-2 , pp. 3-10
    • Balny, C.1    Masson, P.2    Heremans, K.3
  • 19
    • 58049167342 scopus 로고    scopus 로고
    • Towards a quantitative understanding of protein hydration and volumetric properties
    • L. Mitra, J.-B. Rouget, B. Garcia-Moreno, C.A. Royer, and R. Winter Towards a quantitative understanding of protein hydration and volumetric properties Chem. Phys. Chem. 9 2008 2715 2721
    • (2008) Chem. Phys. Chem. , vol.9 , pp. 2715-2721
    • Mitra, L.1    Rouget, J.-B.2    Garcia-Moreno, B.3    Royer, C.A.4    Winter, R.5
  • 20
    • 23844547180 scopus 로고    scopus 로고
    • Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies
    • C.A. Royer Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies Braz. J. Med. Biol. Res. 38 2005 1167 1173 (Pubitemid 41167280)
    • (2005) Brazilian Journal of Medical and Biological Research , vol.38 , Issue.8 , pp. 1167-1173
    • Royer, C.A.1
  • 21
  • 22
    • 11144319408 scopus 로고    scopus 로고
    • Protein volume changes on cosolvent denaturation
    • DOI 10.1016/j.bpc.2004.10.002, PII S030146220400273X
    • P.E. Smith Protein volume changes on cosolvent denaturation Biophys. Chem. 113 2005 299 302 (Pubitemid 40037810)
    • (2005) Biophysical Chemistry , vol.113 , Issue.3 , pp. 299-302
    • Smith, P.E.1
  • 24
    • 38949207174 scopus 로고    scopus 로고
    • Effect of temperature, pressure, and cosolvents on structural and dynamic properties of the hydration shell of SNase: A molecular dynamics computer simulation study
    • DOI 10.1021/jp076440v
    • N. Smolin, and R. Winter Effect of temperature, pressure, and cosolvents on structural and dynamic properties of the hydration shell of SNase: a molecular dynamics computer simulation study J. Phys. Chem. B 112 2008 997 1006 (Pubitemid 351212542)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.3 , pp. 997-1006
    • Smolin, N.1    Winter, R.2
  • 25
    • 1642409882 scopus 로고    scopus 로고
    • Effects of Chaotropic and Kosmotropic Cosolvents on the Pressure-Induced Unfolding and Denaturation of Proteins: An FT-IR Study on Staphylococcal Nuclease
    • DOI 10.1021/bi036106z
    • H. Herberhold, C.A. Royer, and R. Winter Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease Biochemistry 43 2004 3336 3345 (Pubitemid 38391690)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3336-3345
    • Herberhold, H.1    Royer, C.A.2    Winter, R.3
  • 27
    • 0036220998 scopus 로고    scopus 로고
    • The enzyme horseradish peroxidase is less compressible at higher pressures
    • L. Smeller, and J. Fidy The enzyme horseradish peroxidase is less compressible at higher pressures Biophys. J. 82 2002 426 436 (Pubitemid 34289815)
    • (2002) Biophysical Journal , vol.82 , Issue.1 , pp. 426-436
    • Smeller, L.1    Fidy, J.2
  • 28
    • 33645982880 scopus 로고    scopus 로고
    • Refolding studies using pressure: The folding landscape of lysozyme in the pressure-temperature plane
    • L. Smeller, F. Meersman, and K. Heremans Refolding studies using pressure: the folding landscape of lysozyme in the pressure-temperature plane Biochim. Biophys. Acta, Proteins Proteomics 1764 2006 497 505
    • (2006) Biochim. Biophys. Acta, Proteins Proteomics , vol.1764 , pp. 497-505
    • Smeller, L.1    Meersman, F.2    Heremans, K.3
  • 30
    • 0344198173 scopus 로고    scopus 로고
    • Temperature-Induced Dissociation of Protein Aggregates: Accessing the Denatured State
    • DOI 10.1021/bi035623e
    • F. Meersman, and K. Heremans Temperature-induced dissociation of protein aggregates: accessing the denatured state Biochemistry 42 2003 14234 14241 (Pubitemid 37499420)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14234-14241
    • Meersman, F.1    Heremans, K.2
  • 31
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • F. Meersman, L. Smeller, and K. Heremans Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin Biophys. J. 82 2002 2635 2644 (Pubitemid 34441301)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2635-2644
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 33
    • 84860487961 scopus 로고    scopus 로고
    • Differences in the structural stability and cooperativity between monomeric variants of natural and de novo Cro proteins revealed by high-pressure Fourier transform infrared spectroscopy
    • H. Imamura, Y. Isogai, and M. Kato Differences in the structural stability and cooperativity between monomeric variants of natural and de novo Cro proteins revealed by high-pressure Fourier transform infrared spectroscopy Biochemistry 51 2012 3539 3546
    • (2012) Biochemistry , vol.51 , pp. 3539-3546
    • Imamura, H.1    Isogai, Y.2    Kato, M.3
  • 34
    • 33746780089 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin
    • DOI 10.1529/biophysj.106.085928
    • Y. Cordeiro, J. Kraineva, M.C. Suarez, A.G. Tempesta, J.W. Kelly, J.L. Silva, R. Winter, and D. Foguel Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin Biophys. J. 91 2006 957 967 (Pubitemid 44161928)
    • (2006) Biophysical Journal , vol.91 , Issue.3 , pp. 957-967
    • Cordeiro, Y.1    Kraineva, J.2    Suarez, M.C.3    Tempesta, A.G.4    Kelly, J.W.5    Silva, J.L.6    Winter, R.7    Foguel, D.8
  • 36
    • 0036296247 scopus 로고    scopus 로고
    • A rare protein fluorescence behavior where the emission is dominated by tyrosine: Case of the 33-kDa protein from spinach photosystem II
    • DOI 10.1016/S0006-291X(02)00247-4, PII S0006291X02002474
    • K.C. Ruan, J. Li, R.Q. Liang, C.H. Xu, Y. Yu, R. Lange, and C. Balny A rare protein fluorescence behavior where the emission is dominated by tyrosine: case of the 33-kDa protein from spinach photosystem II Biochem. Biophys. Res. Commun. 293 2002 593 597 (Pubitemid 34694250)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.1 , pp. 593-597
    • Ruan, K.1    Li, J.2    Liang, R.3    Xu, C.4    Yu, Y.5    Lange, R.6    Balny, C.7
  • 37
    • 42449141471 scopus 로고    scopus 로고
    • Volume and free energy of folding for troponin C C-domain: Linkage to ion binding and N-domain interaction
    • DOI 10.1021/bi702058t
    • C.B. Rocha, M.C. Suarez, A. Yu, L. Ballard, M.M. Sorenson, D. Foguel, and J.L. Silva Volume and free energy of folding for troponin CC-domain: linkage to ion binding and N-domain interaction Biochemistry 47 2008 5047 5058 (Pubitemid 351575011)
    • (2008) Biochemistry , vol.47 , Issue.17 , pp. 5047-5058
    • Rocha, C.B.1    Suarez, M.C.2    Yu, A.3    Ballard, L.4    Sorenson, M.M.5    Foguel, D.6    Silva, J.L.7
  • 38
    • 78650372029 scopus 로고    scopus 로고
    • REVIEW: High pressure NMR study of proteins - Seeking roots for function, evolution, disease and food applications
    • K. Akasaka REVIEW: high pressure NMR study of proteins - seeking roots for function, evolution, disease and food applications High Pressure Res. 30 2010 453 457
    • (2010) High Pressure Res. , vol.30 , pp. 453-457
    • Akasaka, K.1
  • 39
    • 79955975933 scopus 로고    scopus 로고
    • Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature
    • Y.O. Kamatari, L.J. Smith, C.M. Dobson, and K. Akasaka Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature Biophys. Chem. 156 2011 24 30
    • (2011) Biophys. Chem. , vol.156 , pp. 24-30
    • Kamatari, Y.O.1    Smith, L.J.2    Dobson, C.M.3    Akasaka, K.4
  • 41
    • 84857311961 scopus 로고    scopus 로고
    • A delicate interplay of structure, dynamics, and thermodynamics for function: A high pressure NMR study of outer surface protein A
    • R. Kitahara, A.K. Simorellis, K. Hata, A. Maeno, S. Yokoyama, S. Koide, and K. Akasaka A delicate interplay of structure, dynamics, and thermodynamics for function: a high pressure NMR study of outer surface protein A Biophys. J. 102 2012 916 926
    • (2012) Biophys. J. , vol.102 , pp. 916-926
    • Kitahara, R.1    Simorellis, A.K.2    Hata, K.3    Maeno, A.4    Yokoyama, S.5    Koide, S.6    Akasaka, K.7
  • 42
    • 58049184362 scopus 로고    scopus 로고
    • Effect of osmolytes on pressure-induced unfolding of proteins: A high-pressure SAXS study
    • C. Krywka, C. Sternemann, M. Paulus, M. Tolan, C. Royer, and R. Winter Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study Chem. Phys. Chem. 9 2008 2809 2815
    • (2008) Chem. Phys. Chem. , vol.9 , pp. 2809-2815
    • Krywka, C.1    Sternemann, C.2    Paulus, M.3    Tolan, M.4    Royer, C.5    Winter, R.6
  • 44
    • 84867743873 scopus 로고    scopus 로고
    • High-pressure macromolecular crystallography and NMR: Status, achievements and prospects
    • R. Fourme, E. Girard, and K. Akasaka High-pressure macromolecular crystallography and NMR: status, achievements and prospects Curr. Opin. Struct. Biol. 22 2012 636 642
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 636-642
    • Fourme, R.1    Girard, E.2    Akasaka, K.3
  • 46
    • 15244359626 scopus 로고    scopus 로고
    • The role of the 132-160 region in prion protein conformational transitions
    • DOI 10.1110/ps.04989405
    • J. Torrent, M.T. Alvarez-Martinez, J.P. Liautard, C. Balny, and R. Lange The role of the 132-160 region in prion protein conformational transitions Protein Sci. 14 2005 956 967 (Pubitemid 40389366)
    • (2005) Protein Science , vol.14 , Issue.4 , pp. 956-967
    • Torrent, J.1    Alvarez-Martinez, M.T.2    Liautard, J.-P.3    Balny, C.4    Lange, R.5
  • 47
    • 49249135136 scopus 로고    scopus 로고
    • Epidemiology of food allergy in Europe
    • T. Schafer Epidemiology of food allergy in Europe Allergologie 31 2008 255 263
    • (2008) Allergologie , vol.31 , pp. 255-263
    • Schafer, T.1
  • 50
  • 58
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • C. Radauer, M. Bublin, S. Wagner, A. Mari, and H. Breiteneder Allergens are distributed into few protein families and possess a restricted number of biochemical functions J. Allergy Clin. Immunol. 121 2008 847 852
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 847-852
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5
  • 63
    • 84886641370 scopus 로고    scopus 로고
    • Pressure-jump fluorescence and 15 N/1H 2-D NMR studies of the unfolding of the beta-barrel protein, P13MTCP1
    • R. Kitahara, C. Roumestand, H. Yamada, J.L. Saldana, K. Akasaka, and C.A. Royer Pressure-jump fluorescence and 15 N/1H 2-D NMR studies of the unfolding of the beta-barrel protein, P13MTCP1 Biophys. J. 82 2002 296
    • (2002) Biophys. J. , vol.82 , pp. 296
    • Kitahara, R.1    Roumestand, C.2    Yamada, H.3    Saldana, J.L.4    Akasaka, K.5    Royer, C.A.6
  • 65
    • 33645843335 scopus 로고    scopus 로고
    • Cross-reacting allergens at the molecular scaled a north-south comparison
    • M. Fernandez-Rivas Cross-reacting allergens at the molecular scaled a north-south comparison Rev. Fr. Allerg. Immunol. Clin. 46 2006 167 169
    • (2006) Rev. Fr. Allerg. Immunol. Clin. , vol.46 , pp. 167-169
    • Fernandez-Rivas, M.1
  • 66
    • 11344255717 scopus 로고    scopus 로고
    • Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: An in silico analysis
    • DOI 10.1016/j.jaci.2004.10.026, PII S009167490402682X
    • J.A. Jenkins, S. Griffiths-Jones, P.R. Shewry, H. Breiteneder, and E.N.C. Mills Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis J. Allergy Clin. Immunol. 115 2005 163 170 (Pubitemid 40075438)
    • (2005) Journal of Allergy and Clinical Immunology , vol.115 , Issue.1 , pp. 163-170
    • Jenkins, J.A.1    Griffiths-Jones, S.2    Shewry, P.R.3    Breiteneder, H.4    Mills, E.N.C.5
  • 67
    • 0031453279 scopus 로고    scopus 로고
    • Allergenic cross-reactivity, food allergy and pollen
    • DOI 10.1016/S1382-6689(97)10043-6, PII S1382668997100436
    • S. Vieths Allergenic cross-reactivity, food allergy and pollen Environ. Toxicol. Pharmacol. 4 1997 61 70 (Pubitemid 28055303)
    • (1997) Environmental Toxicology and Pharmacology , vol.4 , Issue.1-2 , pp. 61-70
    • Vieths, S.1
  • 68
    • 30044451860 scopus 로고    scopus 로고
    • Anaphylactic reaction to apple, banana and lychee: What is common between botanically disparate plant families?
    • DOI 10.1111/j.1365-4632.2005.02286.x
    • A. Saraswat, and B. Kumar Anaphylactic reaction to apple, banana and lychee: what is common between botanically disparate plant families? Int. J. Dermatol. 44 2005 996 998 (Pubitemid 43046115)
    • (2005) International Journal of Dermatology , vol.44 , Issue.12 , pp. 996-998
    • Saraswat, A.1    Kumar, B.2
  • 71
    • 79955658999 scopus 로고    scopus 로고
    • Pressure and temperature stability of the main apple allergen Mal d1
    • J. Somkuti, M. Houska, and L. Smeller Pressure and temperature stability of the main apple allergen Mal d1 Eur. Biophys. J. Biophys. Lett. 40 2011 143 151
    • (2011) Eur. Biophys. J. Biophys. Lett. , vol.40 , pp. 143-151
    • Somkuti, J.1    Houska, M.2    Smeller, L.3
  • 72
    • 34047137958 scopus 로고    scopus 로고
    • Specific immuno-modulation and therapy by means\\ of high pressure treated allergens
    • DOI 10.1080/08957950601082557, PII 776051985
    • R. Meyer-Pittroff, H. Behrendt, and J. Ring Specific immuno-modulation and therapy by means of high pressure treated allergens High Pressure Res. 27 2007 63 67 (Pubitemid 46514865)
    • (2007) High Pressure Research , vol.27 , Issue.1 , pp. 63-67
    • Meyer-Pittroff, R.1    Behrendt, H.2    Ring, J.3
  • 75
    • 33847043065 scopus 로고    scopus 로고
    • Decrease of the IgE-binding by Mal d 1, the major apple allergen, by means of polyphenol oxidase and peroxidase treatments
    • DOI 10.1016/j.foodchem.2006.07.029, PII S0308814606006169
    • A. Garcia, J.H. Wichers, and H.J. Wichers Decrease of the IgE-binding by Mal d 1, the major apple allergen, by means of polyphenol oxidase and peroxidase treatments Food Chem. 103 2007 94 100 (Pubitemid 46274077)
    • (2007) Food Chemistry , vol.103 , Issue.1 , pp. 94-100
    • Garcia, A.1    Wichers, J.H.2    Wichers, H.J.3
  • 77
    • 76149144804 scopus 로고    scopus 로고
    • IgE binding capacity of apple allergens preserved after high pressure treatment
    • A. Fernandez, P. Butz, and B. Tauscher IgE binding capacity of apple allergens preserved after high pressure treatment High Pressure Res. 29 2009 705 712
    • (2009) High Pressure Res. , vol.29 , pp. 705-712
    • Fernandez, A.1    Butz, P.2    Tauscher, B.3
  • 78
    • 72149089700 scopus 로고    scopus 로고
    • Diamond anvil cell, 50th birthday
    • W.A. Bassett Diamond anvil cell, 50th birthday High Pressure Res. 29 2009 CP5 CP186
    • (2009) High Pressure Res. , vol.29
    • Bassett, W.A.1
  • 82
    • 70349798882 scopus 로고    scopus 로고
    • Thermodynamic characterization of the PR-10 allergens Bet v 1, Api g 1 and Dau c 1 and pH-dependence of nApi g 1 and nDau c 1
    • M.A. Bollen, H.J. Wichers, J. Helsper, H.F.J. Savelkoul, and M. van Boekel Thermodynamic characterization of the PR-10 allergens Bet v 1, Api g 1 and Dau c 1 and pH-dependence of nApi g 1 and nDau c 1 Food Chem. 119 2010 241 248
    • (2010) Food Chem. , vol.119 , pp. 241-248
    • Bollen, M.A.1    Wichers, H.J.2    Helsper, J.3    Savelkoul, H.F.J.4    Van Boekel, M.5
  • 83
    • 0032491188 scopus 로고    scopus 로고
    • Structural basis of the tanford transition of bovine β-lactoglobulin
    • DOI 10.1021/bi981016t
    • B.Y. Qin, M.C. Bewley, L.K. Creamer, H.M. Baker, E.N. Baker, and G.B. Jameson Structural basis of the Tanford transition of bovine beta-lactoglobulin Biochemistry 37 1998 14014 14023 (Pubitemid 28471234)
    • (1998) Biochemistry , vol.37 , Issue.40 , pp. 14014-14023
    • Qin, B.Y.1    Bewley, M.C.2    Creamer, L.K.3    Baker, H.M.4    Baker, E.N.5    Jameson, G.B.6
  • 84
    • 0034825616 scopus 로고    scopus 로고
    • 1: Structural differences between genetic variants A and B and features of the Tanford transition
    • DOI 10.1046/j.1432-1327.2001.01918.x
    • K.M. Oliveira, V.L. Valente-Mesquita, M.M. Botelho, L. Sawyer, S.T. Ferreira, and I. Polikarpov Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition Eur. J. Biochem./FEBS 268 2001 477 483 (Pubitemid 32862681)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.2 , pp. 477-483
    • Oliveira, K.M.G.1    Valente-Mesquita, V.L.2    Botelho, M.M.3    Sawyer, L.4    Ferreira, S.T.5    Polikarpov, I.6
  • 85
    • 0032741871 scopus 로고    scopus 로고
    • Solution structure and dynamics of bovine β-lactoglobulin A
    • K. Kuwata, M. Hoshino, V. Forge, S. Era, C.A. Batt, and Y. Goto Solution structure and dynamics of bovine beta-lactoglobulin A Protein Sci. Publ. Protein Soc. 8 1999 2541 2545 (Pubitemid 29536426)
    • (1999) Protein Science , vol.8 , Issue.11 , pp. 2541-2545
    • Kuwata, K.1    Hoshino, M.2    Forge, V.3    Era, S.4    Batt, C.A.5    Goto, Y.6
  • 86
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: β-lactoglobulin: Binding properties, structure, and function
    • G. Kontopidis, C. Holt, and L. Sawyer Invited review: beta-lactoglobulin: binding properties, structure, and function J. Dairy Sci. 87 2004 785 796 (Pubitemid 44151704)
    • (2004) Journal of Dairy Science , vol.87 , Issue.4 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 87
    • 0033580649 scopus 로고    scopus 로고
    • Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering
    • G. Panick, R. Malessa, and R. Winter Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering Biochemistry 38 1999 6512 6519
    • (1999) Biochemistry , vol.38 , pp. 6512-6519
    • Panick, G.1    Malessa, R.2    Winter, R.3
  • 88
    • 0030058251 scopus 로고    scopus 로고
    • Effect of pressure on the deuterium exchange reaction of α-lactalbumin and β-lactoglobulin
    • DOI 10.1016/0141-8130(95)01053-X
    • N. Tanaka, and S. Kunugi Effect of pressure on the deuterium exchange reaction of alpha-lactalbumin and beta-lactoglobulin Int. J. Biol. Macromol. 18 1996 33 39 (Pubitemid 26070466)
    • (1996) International Journal of Biological Macromolecules , vol.18 , Issue.1-2 , pp. 33-39
    • Tanaka, N.1    Kunugi, S.2
  • 89
    • 34447341183 scopus 로고    scopus 로고
    • Unfolding and refolding of β-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis
    • DOI 10.1021/jf070170w
    • J. Belloque, R. Chicon, and R. Lopez-Fandino Unfolding and refolding of beta-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis J. Agric. Food Chem. 55 2007 5282 5288 (Pubitemid 47056088)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.13 , pp. 5282-5288
    • Belloque, J.1    Chicon, R.2    Lopez-Fandino, R.3
  • 90
    • 0035793220 scopus 로고    scopus 로고
    • High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin
    • DOI 10.1006/jmbi.2000.4350
    • K. Kuwata, H. Li, H. Yamada, C.A. Batt, Y. Goto, and K. Akasaka High pressure NMR reveals a variety of fluctuating conformers in beta-lactoglobulin J. Mol. Biol. 305 2001 1073 1083 (Pubitemid 33027744)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 1073-1083
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Batt, C.A.4    Goto, Y.5    Akasaka, K.6
  • 91
    • 36348936097 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin
    • DOI 10.1016/j.ifset.2007.05.004, PII S1466856407000719
    • M. Zeece, T. Huppertz, and A. Kelly Effect of high-pressure treatment on in-vitro digestibility of beta-lactoglobulin Innovative Food Sci. Emerg. Technol. 9 2008 62 69 (Pubitemid 350152013)
    • (2008) Innovative Food Science and Emerging Technologies , vol.9 , Issue.1 , pp. 62-69
    • Zeece, M.1    Huppertz, T.2    Kelly, A.3
  • 92
    • 0029010736 scopus 로고
    • Serum amyloid p-component prevents proteolysis of the amyloid fibrils of Alzheimer-disease and systemic amyloidosis
    • G.A. Tennent, L.B. Lovat, and M.B. Pepys Serum amyloid p-component prevents proteolysis of the amyloid fibrils of Alzheimer-disease and systemic amyloidosis Proc. Natl. Acad. Sci. U. S. A. 92 1995 4299 4303
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 93
    • 33646088595 scopus 로고    scopus 로고
    • Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties
    • F. Meersman, and C.M. Dobson Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties Biochim. Biophys. Acta, Proteins Proteomics 1764 2006 452 460
    • (2006) Biochim. Biophys. Acta, Proteins Proteomics , vol.1764 , pp. 452-460
    • Meersman, F.1    Dobson, C.M.2
  • 95
    • 46949094923 scopus 로고    scopus 로고
    • Hydrolysis under high hydrostatic pressure as a means to reduce the binding of β-lactoglobulin to immunoglobulin E from human sera
    • R. Chicon, J. Belloque, E. Alonso, P.J. Martin-Alvarez, and R. Lopez-Fandino Hydrolysis under high hydrostatic pressure as a means to reduce the binding of beta-lactoglobulin to immunoglobulin E from human sera J. Food Prot. 71 2008 1453 1459 (Pubitemid 351961738)
    • (2008) Journal of Food Protection , vol.71 , Issue.7 , pp. 1453-1459
    • Chicon, R.1    Belloque, J.2    Alonso, E.3    Martin-Alvarez, P.J.4    Lopez-Fandino, R.5
  • 96
    • 84856150284 scopus 로고    scopus 로고
    • In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of beta-lactoglobulin are immunologically inert
    • I. Lopez-Exposito, R. Chicon, J. Belloque, R. Lopez-Fandino, and M.C. Berin In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of beta-lactoglobulin are immunologically inert J. Dairy Sci. 95 2012 541 548
    • (2012) J. Dairy Sci. , vol.95 , pp. 541-548
    • Lopez-Exposito, I.1    Chicon, R.2    Belloque, J.3    Lopez-Fandino, R.4    Berin, M.C.5
  • 100
    • 34548238214 scopus 로고    scopus 로고
    • Peanut allergy: Emerging concepts and approaches for an apparent epidemic
    • DOI 10.1016/j.jaci.2007.07.015, PII S0091674907013887
    • S.H. Sicherer, and H.A. Sampson Peanut allergy: emerging concepts and approaches for an apparent epidemic J. Allergy Clin. Immunol. 120 2007 491 503 (Pubitemid 47320772)
    • (2007) Journal of Allergy and Clinical Immunology , vol.120 , Issue.3 , pp. 491-503
    • Sicherer, S.H.1    Sampson, H.A.2
  • 101
    • 0142245696 scopus 로고    scopus 로고
    • High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2
    • DOI 10.1016/S1046-5928(03)00190-6
    • K. Lehmann, S. Hoffmann, P. Neudecker, M. Suhr, W.M. Becker, and P. Rosch High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2 Protein Expr. Purif. 31 2003 250 259 (Pubitemid 37325573)
    • (2003) Protein Expression and Purification , vol.31 , Issue.2 , pp. 250-259
    • Lehmann, K.1    Hoffmann, S.2    Neudecker, P.3    Suhr, M.4    Becker, W.-M.5    Rosch, P.6
  • 103
    • 84867811699 scopus 로고    scopus 로고
    • A potential practical approach to reduce Ara h 6 allergenicity by gamma irradiation
    • C.P. Luo, C.Q. Hu, J.Y. Gao, X. Li, Z.H. Wu, A.S. Yang, and H.B. Chen A potential practical approach to reduce Ara h 6 allergenicity by gamma irradiation Food Chem. 136 2013 1141 1147
    • (2013) Food Chem. , vol.136 , pp. 1141-1147
    • Luo, C.P.1    Hu, C.Q.2    Gao, J.Y.3    Li, X.4    Wu, Z.H.5    Yang, A.S.6    Chen, H.B.7
  • 104
    • 33646249121 scopus 로고    scopus 로고
    • Structure and stability of 2S albumin-type peanut allergens: Implications for the severity of peanut allergic reactions
    • K. Lehmann, K. Schweimer, G. Reese, S. Randow, M. Suhr, W.M. Becker, S. Vieths, and P. Rosch Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions Biochem. J. 395 2006 463 472
    • (2006) Biochem. J. , vol.395 , pp. 463-472
    • Lehmann, K.1    Schweimer, K.2    Reese, G.3    Randow, S.4    Suhr, M.5    Becker, W.M.6    Vieths, S.7    Rosch, P.8
  • 105
    • 75149143075 scopus 로고    scopus 로고
    • Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2
    • J. Li, K. Shefcheck, J. Callahan, and C. Fenselau Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2 Protein Sci. Publ. Protein Soc. 19 2010 174 182
    • (2010) Protein Sci. Publ. Protein Soc. , vol.19 , pp. 174-182
    • Li, J.1    Shefcheck, K.2    Callahan, J.3    Fenselau, C.4
  • 106
    • 0000748473 scopus 로고
    • Pressure dependence of weak acid ionization in aqueous buffers
    • R.C. Neuman, W. Kauzmann, and A. Zipp Pressure dependence of weak acid ionization in aqueous buffers J. Phys. Chem. 77 1973 2687 2691
    • (1973) J. Phys. Chem. , vol.77 , pp. 2687-2691
    • Neuman, R.C.1    Kauzmann, W.2    Zipp, A.3
  • 107
    • 0000818472 scopus 로고
    • Reaction volume of protonic ionization for buffering agents - Prediction of pressure-dependence of pH and pOH
    • Y. Kitamura, and T. Itoh Reaction volume of protonic ionization for buffering agents - prediction of pressure-dependence of pH and pOH J. Solut. Chem. 16 1987 715 725
    • (1987) J. Solut. Chem. , vol.16 , pp. 715-725
    • Kitamura, Y.1    Itoh, T.2
  • 108
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • K. Arnold, L. Bordoli, J. Kopp, and T. Schwede The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 111
    • 77953561091 scopus 로고    scopus 로고
    • Important variations in parvalbumin content in common fish species: A factor possibly contributing to variable allergenicity
    • A. Kuehn, T. Scheuermann, C. Hilger, and F. Hentges Important variations in parvalbumin content in common fish species: a factor possibly contributing to variable allergenicity Int. Arch. Allergy Immunol. 153 2010 359 366
    • (2010) Int. Arch. Allergy Immunol. , vol.153 , pp. 359-366
    • Kuehn, A.1    Scheuermann, T.2    Hilger, C.3    Hentges, F.4
  • 112
    • 0020392253 scopus 로고
    • Correlation of parvalbumin concentration with relaxation speed in mammalian muscles
    • C.W. Heizmann, M.W. Berchtold, and A.M. Rowlerson Correlation of parvalbumin concentration with relaxation speed in mammalian muscles Proc. Natl. Acad. Sci.-Biol. 79 1982 7243 7247
    • (1982) Proc. Natl. Acad. Sci.-Biol. , vol.79 , pp. 7243-7247
    • Heizmann, C.W.1    Berchtold, M.W.2    Rowlerson, A.M.3
  • 114
    • 79551480505 scopus 로고    scopus 로고
    • Solution structures of chicken parvalbumin 3 in the Ca(2 +)-free and Ca(2 +)-bound states
    • M.T. Henzl, J.J. Tanner, and A. Tan Solution structures of chicken parvalbumin 3 in the Ca(2 +)-free and Ca(2 +)-bound states Proteins 79 2011 752 764
    • (2011) Proteins , vol.79 , pp. 752-764
    • Henzl, M.T.1    Tanner, J.J.2    Tan, A.3
  • 115
    • 0004844595 scopus 로고    scopus 로고
    • Purification, biochemical, and immunological characterisation of a major food allergen: Different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin
    • DOI 10.1136/gut.46.5.661
    • A. Bugajska-Schretter, M. Grote, L. Vangelista, P. Valent, W.R. Sperr, H. Rumpold, A. Pastore, R. Reichelt, R. Valenta, and S. Spitzauer Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin Gut 46 2000 661 669 (Pubitemid 30305784)
    • (2000) Gut , vol.46 , Issue.5 , pp. 661-669
    • Bugajska-Schretter, A.1    Grote, M.2    Vangelista, L.3    Valent, P.4    Sperr, W.R.5    Rumpold, H.6    Pastore, A.7    Reichelt, R.8    Valenta, R.9    Spitzauer, S.10
  • 116
    • 0033570025 scopus 로고    scopus 로고
    • Metal-ion affinity and specificity in EF-hand proteins: Coordination geometry and domain plasticity in parvalbumin
    • DOI 10.1016/S0969-2126(00)80060-X
    • M.S. Cates, M.B. Berry, E.L. Ho, Q. Li, J.D. Potter, and G.N. Phillips Jr. Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin Structure 7 1999 1269 1278 (Pubitemid 29482988)
    • (1999) Structure , vol.7 , Issue.10 , pp. 1269-1278
    • Cates, M.S.1    Berry, M.B.2    Ho, E.L.3    Li, Q.4    Potter, J.D.5    Phillips Jr., G.N.6
  • 118
    • 0032881610 scopus 로고    scopus 로고
    • Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core
    • J.P. Declercq, C. Evrard, V. Lamzin, and J. Parello Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core Protein Sci. Publ. Protein Soc. 8 1999 2194 2204 (Pubitemid 29489948)
    • (1999) Protein Science , vol.8 , Issue.10 , pp. 2194-2204
    • Declercq, J.-P.1    Evrard, C.2    Lamzin, V.3    Parello, J.4
  • 119
    • 0033979601 scopus 로고    scopus 로고
    • X-ray crystal structure and molecular dynamics simulations of silver hake parvalbumin (Isoform B)
    • R.C. Richardson, N.M. King, D.J. Harrington, H. Sun, W.E. Royer, and D.J. Nelson X-ray crystal structure and molecular dynamics simulations of silver hake parvalbumin (Isoform B) Protein Sci. Publ. Protein Soc. 9 2000 73 82 (Pubitemid 30070941)
    • (2000) Protein Science , vol.9 , Issue.1 , pp. 73-82
    • Richardson, R.C.1    King, N.M.2    Harrington, D.J.3    Sun, H.4    Royer, W.E.5    Nelson, D.J.6
  • 121
    • 77956540807 scopus 로고    scopus 로고
    • High-pressure treatment with silver carp (Hypophthalmichthys molitrix) protein and its allergic analysis
    • R. Liu, and W. Xue High-pressure treatment with silver carp (Hypophthalmichthys molitrix) protein and its allergic analysis High Pressure Res. 30 2010 438 442
    • (2010) High Pressure Res. , vol.30 , pp. 438-442
    • Liu, R.1    Xue, W.2
  • 122
    • 84871218974 scopus 로고    scopus 로고
    • Is high pressure treatment able to modify the allergenicity of the largemouth bass allergens?
    • C.-Y. Liu, S. Tao, R. Liu, F.-S. Chen, and W.-T. Xue Is high pressure treatment able to modify the allergenicity of the largemouth bass allergens? High Pressure Res. 32 2012 551 556
    • (2012) High Pressure Res. , vol.32 , pp. 551-556
    • Liu, C.-Y.1    Tao, S.2    Liu, R.3    Chen, F.-S.4    Xue, W.-T.5
  • 123
    • 84864480701 scopus 로고    scopus 로고
    • 2 + binding, and pressure-temperature phase diagram of cod parvalbumin: Gad m 1
    • 2 + binding, and pressure-temperature phase diagram of cod parvalbumin: Gad m 1 Biochemistry 51 2012 5903 5911
    • (2012) Biochemistry , vol.51 , pp. 5903-5911
    • Somkuti, J.1    Bublin, M.2    Breiteneder, H.3    Smeller, L.4
  • 124
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 125
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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