메뉴 건너뛰기




Volumn 45, Issue 14, 2008, Pages 3740-3747

Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes

Author keywords

Allergens; Linear epitopes; SDAP; Structural database

Indexed keywords

ALANINE; ALLERGEN; ASPARAGINE; EPITOPE; GLYCINE; IMMUNOGLOBULIN E; LYSINE; SERINE;

EID: 48149098909     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.05.026     Document Type: Article
Times cited : (61)

References (64)
  • 1
    • 33847199653 scopus 로고    scopus 로고
    • Assessment of allergen cross-reactivity
    • Aalberse R.C. Assessment of allergen cross-reactivity. Clin. Mol. Allergy 5 (2007) 2
    • (2007) Clin. Mol. Allergy , vol.5 , pp. 2
    • Aalberse, R.C.1
  • 2
    • 33746280250 scopus 로고    scopus 로고
    • In silico predictability of allergenicity: from amino acid sequence via 3-D structure to allergenicity
    • Aalberse R.C., and Stadler B.M. In silico predictability of allergenicity: from amino acid sequence via 3-D structure to allergenicity. Mol. Nutr. Food Res. 50 (2006) 625-627
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 625-627
    • Aalberse, R.C.1    Stadler, B.M.2
  • 4
    • 0242499979 scopus 로고    scopus 로고
    • Par j 1 and Par j 2, the major allergens from Parietaria judaica pollen, have similar immunoglobulin E epitopes
    • Asturias J.A., Gomez-Bayon N., Eseverri J.L., and Martinez A. Par j 1 and Par j 2, the major allergens from Parietaria judaica pollen, have similar immunoglobulin E epitopes. Clin. Exp. Allergy 33 (2003) 518-524
    • (2003) Clin. Exp. Allergy , vol.33 , pp. 518-524
    • Asturias, J.A.1    Gomez-Bayon, N.2    Eseverri, J.L.3    Martinez, A.4
  • 8
    • 22244464599 scopus 로고    scopus 로고
    • Plant food allergens-structural and functional aspects of allergenicity
    • Breiteneder H., and Mills E.N.C. Plant food allergens-structural and functional aspects of allergenicity. Biotechnol. Adv. 23 (2005) 395-399
    • (2005) Biotechnol. Adv. , vol.23 , pp. 395-399
    • Breiteneder, H.1    Mills, E.N.C.2
  • 11
    • 0034163776 scopus 로고    scopus 로고
    • Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies
    • Chow L.P., Liu S.L., Yu C.J., Liao H.K., Tsai J.J., and Tang T.K. Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies. Biochem. J. 346 Pt 2 (2000) 423-431
    • (2000) Biochem. J. , vol.346 PART 2 , pp. 423-431
    • Chow, L.P.1    Liu, S.L.2    Yu, C.J.3    Liao, H.K.4    Tsai, J.J.5    Tang, T.K.6
  • 12
    • 0042029616 scopus 로고    scopus 로고
    • Mutational analysis of major, sequential IgE-binding epitopes in alpha(s1)-casein, a major cow's milk allergen
    • Cocco R.R., Jarvinen K.M., Sampson H.A., and Beyer K. Mutational analysis of major, sequential IgE-binding epitopes in alpha(s1)-casein, a major cow's milk allergen. J. Allergy Clin. Immunol. 112 (2003) 433-437
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 433-437
    • Cocco, R.R.1    Jarvinen, K.M.2    Sampson, H.A.3    Beyer, K.4
  • 13
    • 13544259023 scopus 로고    scopus 로고
    • Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals a parallel beta-helical core
    • Czerwinski E.W., Midoro-Horiuti T., White M.A., Brooks E.G., and Goldblum R.M. Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals a parallel beta-helical core. J. Biol. Chem. 280 (2005) 3740-3746
    • (2005) J. Biol. Chem. , vol.280 , pp. 3740-3746
    • Czerwinski, E.W.1    Midoro-Horiuti, T.2    White, M.A.3    Brooks, E.G.4    Goldblum, R.M.5
  • 14
    • 14644435040 scopus 로고    scopus 로고
    • A genetic engineering strategy to eliminate peanut allergy
    • Dodo H., Konan K., and Viquez O. A genetic engineering strategy to eliminate peanut allergy. Curr. Allergy Asthma Rep. 5 (2005) 67-73
    • (2005) Curr. Allergy Asthma Rep. , vol.5 , pp. 67-73
    • Dodo, H.1    Konan, K.2    Viquez, O.3
  • 15
    • 0034843745 scopus 로고    scopus 로고
    • Easier threading through web-based comparisons and cross-validations
    • Douguet D., and Labesse G. Easier threading through web-based comparisons and cross-validations. Bioinformatics 17 (2001) 752-753
    • (2001) Bioinformatics , vol.17 , pp. 752-753
    • Douguet, D.1    Labesse, G.2
  • 17
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R., and Braun W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19 (1998) 319-333
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 19
    • 33746323640 scopus 로고    scopus 로고
    • Practical and predictive bioinformatics methods for the identification of potentially cross-reactive protein matches
    • Goodman R.E. Practical and predictive bioinformatics methods for the identification of potentially cross-reactive protein matches. Mol. Nutr. Food Res. 50 (2006) 655-660
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 655-660
    • Goodman, R.E.1
  • 20
    • 16244384649 scopus 로고    scopus 로고
    • Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition
    • Gustchina A., Li M., Wunschmann S., Chapman M.D., Pomes A., and Wlodawer A. Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition. J. Mol. Biol. 348 (2005) 433-444
    • (2005) J. Mol. Biol. , vol.348 , pp. 433-444
    • Gustchina, A.1    Li, M.2    Wunschmann, S.3    Chapman, M.D.4    Pomes, A.5    Wlodawer, A.6
  • 21
    • 0035576365 scopus 로고    scopus 로고
    • Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily
    • Henriksen A., King T.P., Mirza O., Monsalve R.I., Meno K., Ipsen H., Larsen J.N., Gajhede M., and Spangfort M.D. Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins 45 (2001) 438-448
    • (2001) Proteins , vol.45 , pp. 438-448
    • Henriksen, A.1    King, T.P.2    Mirza, O.3    Monsalve, R.I.4    Meno, K.5    Ipsen, H.6    Larsen, J.N.7    Gajhede, M.8    Spangfort, M.D.9
  • 22
    • 0036772523 scopus 로고    scopus 로고
    • Data mining of sequences and 3D structures of allergenic proteins
    • Ivanciuc O., Schein C.H., and Braun W. Data mining of sequences and 3D structures of allergenic proteins. Bioinformatics 18 (2002) 1358-1364
    • (2002) Bioinformatics , vol.18 , pp. 1358-1364
    • Ivanciuc, O.1    Schein, C.H.2    Braun, W.3
  • 23
    • 0042303843 scopus 로고    scopus 로고
    • Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-Food
    • Ivanciuc O., Mathura V., Midoro-Horiuti T., Braun W., Goldblum R.M., and Schein C.H. Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-Food. J. Agric. Food Chem. 51 (2003) 4830-4837
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 4830-4837
    • Ivanciuc, O.1    Mathura, V.2    Midoro-Horiuti, T.3    Braun, W.4    Goldblum, R.M.5    Schein, C.H.6
  • 24
    • 11344255717 scopus 로고    scopus 로고
    • Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis
    • Jenkins J.A., Griffiths-Jones S., Shewry P.R., Breiteneder H., and Mills E.N.C. 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
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 163-170
    • Jenkins, J.A.1    Griffiths-Jones, S.2    Shewry, P.R.3    Breiteneder, H.4    Mills, E.N.C.5
  • 25
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences
    • Jones D.T. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287 (1999) 797-815
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 26
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., and Sternberg M.J.E. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299 (2000) 499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 27
    • 0030292980 scopus 로고    scopus 로고
    • Immunochemical studies of stinging insect venom allergens
    • King T.P. Immunochemical studies of stinging insect venom allergens. Toxicon 34 (1996) 1455-1458
    • (1996) Toxicon , vol.34 , pp. 1455-1458
    • King, T.P.1
  • 28
    • 0001399408 scopus 로고    scopus 로고
    • Recombinant allergens with reduced allergenicity but retaining immunogenicity of the natural allergens: hybrids of yellow jacket and paper wasp venom allergen antigen 5s
    • King T.P., Jim S.Y., Monsalve R.I., Kagey-Sobotka A., Lichtenstein L.M., and Spangfort M.D. Recombinant allergens with reduced allergenicity but retaining immunogenicity of the natural allergens: hybrids of yellow jacket and paper wasp venom allergen antigen 5s. J. Immunol. 166 (2001) 6057-6065
    • (2001) J. Immunol. , vol.166 , pp. 6057-6065
    • King, T.P.1    Jim, S.Y.2    Monsalve, R.I.3    Kagey-Sobotka, A.4    Lichtenstein, L.M.5    Spangfort, M.D.6
  • 29
    • 0024032336 scopus 로고
    • Chain conformations of polycarbonate from abinitio calculations
    • Laskowski B.C., Yoon D.Y., McLean D., and Jaffe R.L. Chain conformations of polycarbonate from abinitio calculations. Macromolecules 21 (1988) 1629-1633
    • (1988) Macromolecules , vol.21 , pp. 1629-1633
    • Laskowski, B.C.1    Yoon, D.Y.2    McLean, D.3    Jaffe, R.L.4
  • 31
    • 10844244091 scopus 로고    scopus 로고
    • Structural and functional alterations in major peanut allergens caused by thermal processing
    • Maleki S.J., and Hurlburt B.K. Structural and functional alterations in major peanut allergens caused by thermal processing. J. AOAC Int. 87 (2004) 1475-1479
    • (2004) J. AOAC Int. , vol.87 , pp. 1475-1479
    • Maleki, S.J.1    Hurlburt, B.K.2
  • 33
    • 0029610793 scopus 로고
    • Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry
    • Mumenthaler C., and Braun W. Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry. J. Mol. Biol. 254 (1995) 465-480
    • (1995) J. Mol. Biol. , vol.254 , pp. 465-480
    • Mumenthaler, C.1    Braun, W.2
  • 34
    • 0028961335 scopus 로고
    • Scop-a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. Scop-a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 35
    • 34848854803 scopus 로고    scopus 로고
    • Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces
    • Negi S.S., and Braun W. Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces. J. Mol. Model. 13 (2007) 1157-1167
    • (2007) J. Mol. Model. , vol.13 , pp. 1157-1167
    • Negi, S.S.1    Braun, W.2
  • 36
    • 33845550595 scopus 로고
    • Energy parameters in polypeptides 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen-bond interactions for the naturally-occurring amino-acids
    • Nemethy G., Pottle M.S., and Scheraga H.A. Energy parameters in polypeptides 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen-bond interactions for the naturally-occurring amino-acids. J. Phys. Chem. 87 (1983) 1883-1887
    • (1983) J. Phys. Chem. , vol.87 , pp. 1883-1887
    • Nemethy, G.1    Pottle, M.S.2    Scheraga, H.A.3
  • 37
    • 33846611599 scopus 로고    scopus 로고
    • New perspectives for use of native and engineered recombinant food proteins in treatment of food allergy
    • Nowak-Wegzyn A. New perspectives for use of native and engineered recombinant food proteins in treatment of food allergy. Immunol. Allergy Clin. N. Am. 27 (2007) 105-127
    • (2007) Immunol. Allergy Clin. N. Am. , vol.27 , pp. 105-127
    • Nowak-Wegzyn, A.1
  • 38
    • 0036217249 scopus 로고    scopus 로고
    • Automated assignment and 3D structure calculations using combinations of 2D homonuclear and 3D heteronuclear NOESY spectra
    • Oezguen N., Adamian L., Xu Y., Rajarathnam K., and Braun W. Automated assignment and 3D structure calculations using combinations of 2D homonuclear and 3D heteronuclear NOESY spectra. J. Biomol. Nmr. 22 (2002) 249-263
    • (2002) J. Biomol. Nmr. , vol.22 , pp. 249-263
    • Oezguen, N.1    Adamian, L.2    Xu, Y.3    Rajarathnam, K.4    Braun, W.5
  • 41
  • 42
    • 0033064254 scopus 로고    scopus 로고
    • Food allergy. Part 1: immunopathogenesis and clinical disorders
    • Sampson H.A. Food allergy. Part 1: immunopathogenesis and clinical disorders. J. Allergy Clin. Immunol. 103 (1999) 717-728
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 717-728
    • Sampson, H.A.1
  • 43
    • 0032813419 scopus 로고    scopus 로고
    • Food allergy. Part 2: diagnosis and management
    • Sampson H.A. Food allergy. Part 2: diagnosis and management. J. Allergy Clin. Immunol. 103 (1999) 981-989
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 981-989
    • Sampson, H.A.1
  • 44
    • 11344294345 scopus 로고    scopus 로고
    • Food allergy: when mucosal immunity goes wrong
    • Sampson H.A. Food allergy: when mucosal immunity goes wrong. J. Allergy Clin. Immunol. 115 (2005) 139-141
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 139-141
    • Sampson, H.A.1
  • 46
    • 0024721519 scopus 로고
    • GEOM, a new tool for molecular modeling based on distance geometry calculations with NMR data
    • Sanner M., Widmer A., Senn H., and Braun W. GEOM, a new tool for molecular modeling based on distance geometry calculations with NMR data. J. Comp. Aided Mol. Des. 3 (1989) 195-210
    • (1989) J. Comp. Aided Mol. Des. , vol.3 , pp. 195-210
    • Sanner, M.1    Widmer, A.2    Senn, H.3    Braun, W.4
  • 47
    • 0025344281 scopus 로고
    • A program, FANTOM, for energy refinement of polypeptides and proteins using a Newton-Raphson Minimizer in the torsion angle space
    • Schaumann T., Braun W., and Wuthrich K. A program, FANTOM, for energy refinement of polypeptides and proteins using a Newton-Raphson Minimizer in the torsion angle space. Biopolymers 29 (1990) 679-694
    • (1990) Biopolymers , vol.29 , pp. 679-694
    • Schaumann, T.1    Braun, W.2    Wuthrich, K.3
  • 48
    • 0034956711 scopus 로고    scopus 로고
    • Aplysia attractin: biophysical characterization and modeling of a water-borne protein pheromone
    • Schein C.H., Nagle G.T., Page J.S., Sweedler J.V., Xu Y., Painter S.D., and Braun W. Aplysia attractin: biophysical characterization and modeling of a water-borne protein pheromone. Biophys. J. 81 (2001) 463-472
    • (2001) Biophys. J. , vol.81 , pp. 463-472
    • Schein, C.H.1    Nagle, G.T.2    Page, J.S.3    Sweedler, J.V.4    Xu, Y.5    Painter, S.D.6    Braun, W.7
  • 49
    • 27744566919 scopus 로고    scopus 로고
    • Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens
    • Schein C.H., Ivanciuc O., and Braun W. Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens. J. Agric. Food Chem. 53 (2005) 8752-8759
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8752-8759
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 50
    • 33846586517 scopus 로고    scopus 로고
    • Structural database of allergenic proteins (SDAP)
    • Maleki S.J., Burks A.W., and Helm R.M. (Eds), ASM Press, Washington, DC
    • Schein C.H., Ivanciuc O., and Braun W. Structural database of allergenic proteins (SDAP). In: Maleki S.J., Burks A.W., and Helm R.M. (Eds). Food Allergy (2006), ASM Press, Washington, DC 257-283
    • (2006) Food Allergy , pp. 257-283
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 51
    • 33744984790 scopus 로고    scopus 로고
    • NMR structure of the viral peptide linked to the genome (VPg) of poliovirus
    • Schein C.H., Oezguen N., Volk D.E., Garimella R., Paul A., and Braun W. NMR structure of the viral peptide linked to the genome (VPg) of poliovirus. Peptides 27 (2006) 1676-1684
    • (2006) Peptides , vol.27 , pp. 1676-1684
    • Schein, C.H.1    Oezguen, N.2    Volk, D.E.3    Garimella, R.4    Paul, A.5    Braun, W.6
  • 52
    • 33846631464 scopus 로고    scopus 로고
    • Bioinformatics approaches to classifying allergens and predicting cross-reactivity
    • Schein C.H., Ivanciuc O., and Braun W. Bioinformatics approaches to classifying allergens and predicting cross-reactivity. Immunol. Allergy Clin. N. Am. 27 (2007) 1-27
    • (2007) Immunol. Allergy Clin. N. Am. , vol.27 , pp. 1-27
    • Schein, C.H.1    Ivanciuc, O.2    Braun, W.3
  • 53
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., and Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310 (2001) 243-257
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 54
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11 (1998) 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 55
    • 0346995202 scopus 로고    scopus 로고
    • Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study
    • Sicherer S., Munoz-Furlong A., and Sampson H.A. Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J. Allergy Clin. Immunol. 112 (2003) 1203-1207
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 1203-1207
    • Sicherer, S.1    Munoz-Furlong, A.2    Sampson, H.A.3
  • 58
    • 47849104660 scopus 로고    scopus 로고
    • The big eight foods: clinical and epidemiological overview
    • Malecki S. (Ed), ASM Press, Washington, DC
    • Teuber S., Beyer K., Comstock S., and Wallowitz M. The big eight foods: clinical and epidemiological overview. In: Malecki S. (Ed). Food Allergy (2006), ASM Press, Washington, DC 49-79
    • (2006) Food Allergy , pp. 49-79
    • Teuber, S.1    Beyer, K.2    Comstock, S.3    Wallowitz, M.4
  • 59
    • 33846901166 scopus 로고    scopus 로고
    • Major mountain cedar allergen, Jun a 1, contains conformational as well as linear IgE epitopes
    • Varshney S., Goldblum R.M., Kearney C., Watanabe M., and Midoro-Horiuti T. Major mountain cedar allergen, Jun a 1, contains conformational as well as linear IgE epitopes. Mol. Immunol. 44 (2007) 2781-2785
    • (2007) Mol. Immunol. , vol.44 , pp. 2781-2785
    • Varshney, S.1    Goldblum, R.M.2    Kearney, C.3    Watanabe, M.4    Midoro-Horiuti, T.5
  • 60
    • 0037326618 scopus 로고    scopus 로고
    • Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1)
    • Wensing M., Knulst A.C., Piersma S., O'Kane F., Knol E.F., and Koppelman S.J. Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1). J. Allergy Clin. Immunol. 111 (2003) 420-424
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 420-424
    • Wensing, M.1    Knulst, A.C.2    Piersma, S.3    O'Kane, F.4    Knol, E.F.5    Koppelman, S.J.6
  • 61
    • 0002697439 scopus 로고    scopus 로고
    • Combined automated assignment of NMR spectra and calculation of three-dimensional protein structures
    • Krishna, and Berliner (Eds), Kluwer Academic/Plenum Publishers, New York
    • Xu Y., Schein C.H., and Braun W. Combined automated assignment of NMR spectra and calculation of three-dimensional protein structures. In: Krishna, and Berliner (Eds). Biological Magnetic Resonance: Structure Computation and Dynamics in Protein NMR vol. 17 (1999), Kluwer Academic/Plenum Publishers, New York 37-79
    • (1999) Biological Magnetic Resonance: Structure Computation and Dynamics in Protein NMR , vol.17 , pp. 37-79
    • Xu, Y.1    Schein, C.H.2    Braun, W.3
  • 62
    • 0032607423 scopus 로고    scopus 로고
    • Automated 2D NOESY assignment and structure calculation of crambin (S22/I25) with the self-correcting distance geometry based NOAH/DIAMOD programs
    • Xu Y., Wu J., Gorenstein D., and Braun W. Automated 2D NOESY assignment and structure calculation of crambin (S22/I25) with the self-correcting distance geometry based NOAH/DIAMOD programs. J. Mag. Res. 136 (1999) 76-85
    • (1999) J. Mag. Res. , vol.136 , pp. 76-85
    • Xu, Y.1    Wu, J.2    Gorenstein, D.3    Braun, W.4
  • 63
    • 0035744168 scopus 로고    scopus 로고
    • Automatic assignment of NOESY cross peaks and determination of the protein structure of a New World scorpion neurotoxin using NOAH/DIAMOD
    • Xu Y., Jablonsky M.J., Jackson P.L., Braun W., and Krishna N.R. Automatic assignment of NOESY cross peaks and determination of the protein structure of a New World scorpion neurotoxin using NOAH/DIAMOD. J. Mag. Res. 148 (2001) 35-46
    • (2001) J. Mag. Res. , vol.148 , pp. 35-46
    • Xu, Y.1    Jablonsky, M.J.2    Jackson, P.L.3    Braun, W.4    Krishna, N.R.5
  • 64
    • 0030586029 scopus 로고    scopus 로고
    • Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin
    • Yang X., and Moffat K. Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin. Structure 4 (1996) 837-852
    • (1996) Structure , vol.4 , pp. 837-852
    • Yang, X.1    Moffat, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.