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Volumn 46, Issue 16, 2009, Pages 3476-3487

Alternaria alternata TCTP, a novel cross-reactive ascomycete allergen

Author keywords

Allergy; Alternaria alternata; Ascomycete; Fungi; Mold; Recombinant protein; TCTP

Indexed keywords

ALLERGEN; COMPLEMENTARY DNA; IMMUNOGLOBULIN E; RECOMBINANT TRANSLATIONALLY CONTROLLED TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 70349445290     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.07.024     Document Type: Article
Times cited : (14)

References (95)
  • 1
    • 0034995912 scopus 로고    scopus 로고
    • Cross-reactivity of IgE antibodies to allergens
    • Aalberse R.C., Akkerdaas J., and van Ree R. Cross-reactivity of IgE antibodies to allergens. Allergy 56 (2001) 478-490
    • (2001) Allergy , vol.56 , pp. 478-490
    • Aalberse, R.C.1    Akkerdaas, J.2    van Ree, R.3
  • 4
    • 85032069466 scopus 로고    scopus 로고
    • A simple method for extraction of fungal genomic DNA
    • Al-Samarrai T.H., and Schmid J. A simple method for extraction of fungal genomic DNA. Lett. Appl. Microbiol. 30 (2000) 53-56
    • (2000) Lett. Appl. Microbiol. , vol.30 , pp. 53-56
    • Al-Samarrai, T.H.1    Schmid, J.2
  • 5
    • 8544232810 scopus 로고    scopus 로고
    • TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway
    • Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B., Amson R., and Telerman A. TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway. J. Biol. Chem. 279 (2004) 46104-46112
    • (2004) J. Biol. Chem. , vol.279 , pp. 46104-46112
    • Amzallag, N.1    Passer, B.J.2    Allanic, D.3    Segura, E.4    Thery, C.5    Goud, B.6    Amson, R.7    Telerman, A.8
  • 8
    • 0033627623 scopus 로고    scopus 로고
    • Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe
    • Baxter N.J., Thaw P., Higgins L.D., Sedelnikova S.E., Bramley A.L., Price C., Waltho J.P., and Craven C.J. Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe. J. Biomol. NMR 16 (2000) 83-84
    • (2000) J. Biomol. NMR , vol.16 , pp. 83-84
    • Baxter, N.J.1    Thaw, P.2    Higgins, L.D.3    Sedelnikova, S.E.4    Bramley, A.L.5    Price, C.6    Waltho, J.P.7    Craven, C.J.8
  • 10
    • 0034665666 scopus 로고    scopus 로고
    • Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line AML14-3D10
    • Bheekha-Escura R., MacGlashan D.W., Langdon J.M., and MacDonald S.M. Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line AML14-3D10. Blood 96 (2000) 2191-2198
    • (2000) Blood , vol.96 , pp. 2191-2198
    • Bheekha-Escura, R.1    MacGlashan, D.W.2    Langdon, J.M.3    MacDonald, S.M.4
  • 11
    • 0032568952 scopus 로고    scopus 로고
    • The Plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin
    • Bhisutthibhan J., Pan X.Q., Hossler P.A., Walker D.J., Yowell C.A., Carlton J., Dame J.B., and Meshnick S.R. The Plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin. J. Biol. Chem. 273 (1998) 16192-16198
    • (1998) J. Biol. Chem. , vol.273 , pp. 16192-16198
    • Bhisutthibhan, J.1    Pan, X.Q.2    Hossler, P.A.3    Walker, D.J.4    Yowell, C.A.5    Carlton, J.6    Dame, J.B.7    Meshnick, S.R.8
  • 12
    • 0034058643 scopus 로고    scopus 로고
    • Sensitivity to fungal allergens is a risk factor for life-threatening asthma
    • Black P.N., Udy A.A., and Brodie S.M. Sensitivity to fungal allergens is a risk factor for life-threatening asthma. Allergy 55 (2000) 501-504
    • (2000) Allergy , vol.55 , pp. 501-504
    • Black, P.N.1    Udy, A.A.2    Brodie, S.M.3
  • 13
    • 0347480218 scopus 로고    scopus 로고
    • The translationally controlled tumour protein (TCTP)
    • Bommer U.A., and Thiele B.J. The translationally controlled tumour protein (TCTP). Int. J. Biochem. Cell Biol. 36 (2004) 379-385
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 379-385
    • Bommer, U.A.1    Thiele, B.J.2
  • 14
    • 0028284722 scopus 로고
    • Immunotherapy in pollen and mould asthma
    • Bonifazi F. Immunotherapy in pollen and mould asthma. Monaldi Arch. Chest Dis. 49 (1994) 150-153
    • (1994) Monaldi Arch. Chest Dis. , vol.49 , pp. 150-153
    • Bonifazi, F.1
  • 15
    • 0034650344 scopus 로고    scopus 로고
    • Identification and transcription control of fission yeast genes repressed by an ammonium starvation growth arrest
    • Bonnet C., Perret E., Dumont X., Picard A., Caput D., and Lenaers G. Identification and transcription control of fission yeast genes repressed by an ammonium starvation growth arrest. Yeast 16 (2000) 23-33
    • (2000) Yeast , vol.16 , pp. 23-33
    • Bonnet, C.1    Perret, E.2    Dumont, X.3    Picard, A.4    Caput, D.5    Lenaers, G.6
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0036279145 scopus 로고    scopus 로고
    • The allergens of Cladosporium herbarum and Alternaria alternata
    • Breitenbach M., and Simon-Nobbe B. The allergens of Cladosporium herbarum and Alternaria alternata. Chem. Immunol. 81 (2002) 48-72
    • (2002) Chem. Immunol. , vol.81 , pp. 48-72
    • Breitenbach, M.1    Simon-Nobbe, B.2
  • 18
    • 0036793981 scopus 로고    scopus 로고
    • An update on pollen and fungal spore aerobiology
    • Burge H.A. An update on pollen and fungal spore aerobiology. J. Allergy Clin. Immunol. 110 (2002) 544-552
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 544-552
    • Burge, H.A.1
  • 24
    • 1042264217 scopus 로고    scopus 로고
    • Transition of recombinant allergens from bench to clinical application
    • Cromwell O., Suck R., Kahlert H., Nandy A., Weber B., and Fiebig H. Transition of recombinant allergens from bench to clinical application. Methods 32 (2004) 300-312
    • (2004) Methods , vol.32 , pp. 300-312
    • Cromwell, O.1    Suck, R.2    Kahlert, H.3    Nandy, A.4    Weber, B.5    Fiebig, H.6
  • 28
    • 36249030493 scopus 로고    scopus 로고
    • The environment and asthma in US inner cities
    • Eggleston P.A. The environment and asthma in US inner cities. Chest 132 (2007) 782S-788S
    • (2007) Chest , vol.132
    • Eggleston, P.A.1
  • 29
    • 1142297337 scopus 로고    scopus 로고
    • Manufacturing and standardizing fungal allergen products
    • Esch R.E. Manufacturing and standardizing fungal allergen products. J. Allergy Clin. Immunol. 113 (2004) 210-215
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 210-215
    • Esch, R.E.1
  • 30
    • 35448955158 scopus 로고    scopus 로고
    • Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR
    • Feng Y., Liu D., Yao H., and Wang J. Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR. Arch. Biochem. Biophys. 467 (2007) 48-57
    • (2007) Arch. Biochem. Biophys. , vol.467 , pp. 48-57
    • Feng, Y.1    Liu, D.2    Yao, H.3    Wang, J.4
  • 31
    • 3042817304 scopus 로고    scopus 로고
    • Customized antigens for desensitizing allergic patients
    • Ferreira F., Wallner M., and Thalhamer J. Customized antigens for desensitizing allergic patients. Adv. Immunol. 84 (2004) 79-129
    • (2004) Adv. Immunol. , vol.84 , pp. 79-129
    • Ferreira, F.1    Wallner, M.2    Thalhamer, J.3
  • 32
    • 0036674382 scopus 로고    scopus 로고
    • Immunological and structural analysis of IgE-mediated cross-reactivity between manganese superoxide dismutases
    • Fluckiger S., Scapozza L., Mayer C., Blaser K., Folkers G., and Crameri R. Immunological and structural analysis of IgE-mediated cross-reactivity between manganese superoxide dismutases. Int. Arch. Allergy Immunol. 128 (2002) 292-303
    • (2002) Int. Arch. Allergy Immunol. , vol.128 , pp. 292-303
    • Fluckiger, S.1    Scapozza, L.2    Mayer, C.3    Blaser, K.4    Folkers, G.5    Crameri, R.6
  • 33
    • 1142297340 scopus 로고    scopus 로고
    • Mold allergy: some progress made, more needed
    • Frew A.J. Mold allergy: some progress made, more needed. J. Allergy Clin. Immunol. 113 (2004) 216-218
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 216-218
    • Frew, A.J.1
  • 35
    • 0032892605 scopus 로고    scopus 로고
    • The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle
    • Gachet Y., Tournier S., Lee M., Lazaris-Karatzas A., Poulton T., and Bommer U.A. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J. Cell Sci. 112 Pt 8 (1999) 1257-1271
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 8 , pp. 1257-1271
    • Gachet, Y.1    Tournier, S.2    Lee, M.3    Lazaris-Karatzas, A.4    Poulton, T.5    Bommer, U.A.6
  • 36
    • 0034924493 scopus 로고    scopus 로고
    • SWISS-PROT: connecting biomolecular knowledge via a protein database
    • Gasteiger E., Jung E., and Bairoch A. SWISS-PROT: connecting biomolecular knowledge via a protein database. Curr. Issues Mol. Biol. 3 (2001) 47-55
    • (2001) Curr. Issues Mol. Biol. , vol.3 , pp. 47-55
    • Gasteiger, E.1    Jung, E.2    Bairoch, A.3
  • 37
    • 0023543405 scopus 로고
    • The prevalence of allergic skin test reactivity to eight common aeroallergens in the U.S. population: results from the second National Health and Nutrition Examination Survey
    • Gergen P.J., Turkeltaub P.C., and Kovar M.G. The prevalence of allergic skin test reactivity to eight common aeroallergens in the U.S. population: results from the second National Health and Nutrition Examination Survey. J. Allergy Clin. Immunol. 80 (1987) 669-679
    • (1987) J. Allergy Clin. Immunol. , vol.80 , pp. 669-679
    • Gergen, P.J.1    Turkeltaub, P.C.2    Kovar, M.G.3
  • 38
    • 0037197743 scopus 로고    scopus 로고
    • Molecular characterization of a calcium binding translationally controlled tumor protein homologue from the filarial parasites Brugia malayi and Wuchereria bancrofti
    • Gnanasekar M., Rao K.V., Chen L., Narayanan R.B., Geetha M., Scott A.L., Ramaswamy K., and Kaliraj P. Molecular characterization of a calcium binding translationally controlled tumor protein homologue from the filarial parasites Brugia malayi and Wuchereria bancrofti. Mol. Biochem. Parasitol. 121 (2002) 107-118
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 107-118
    • Gnanasekar, M.1    Rao, K.V.2    Chen, L.3    Narayanan, R.B.4    Geetha, M.5    Scott, A.L.6    Ramaswamy, K.7    Kaliraj, P.8
  • 42
    • 33847174115 scopus 로고    scopus 로고
    • Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase
    • Hsu Y.C., Chern J.J., Cai Y., Liu M., and Choi K.W. Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase. Nature 445 (2007) 785-788
    • (2007) Nature , vol.445 , pp. 785-788
    • Hsu, Y.C.1    Chern, J.J.2    Cai, Y.3    Liu, M.4    Choi, K.W.5
  • 44
    • 0343337581 scopus 로고    scopus 로고
    • Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor
    • Kang H.S., Lee M.J., Song H., Han S.H., Kim Y.M., Im J.Y., and Choi I. Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J. Immunol. 166 (2001) 6545-6554
    • (2001) J. Immunol. , vol.166 , pp. 6545-6554
    • Kang, H.S.1    Lee, M.J.2    Song, H.3    Han, S.H.4    Kim, Y.M.5    Im, J.Y.6    Choi, I.7
  • 45
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust R.B., Tozser J., Fox J.D., Anderson D.E., Cherry S., Copeland T.D., and Waugh D.S. Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng. 14 (2001) 993-1000
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 46
    • 0036038966 scopus 로고    scopus 로고
    • Evidence for the genetic control of immunoglobulin E reactivity to the allergens of Alternaria alternata
    • Karihaloo C., Tovey E.R., Mitakakis T.Z., Duffy D.L., and Britton W.J. Evidence for the genetic control of immunoglobulin E reactivity to the allergens of Alternaria alternata. Clin. Exp. Allergy 32 (2002) 1316-1322
    • (2002) Clin. Exp. Allergy , vol.32 , pp. 1316-1322
    • Karihaloo, C.1    Tovey, E.R.2    Mitakakis, T.Z.3    Duffy, D.L.4    Britton, W.J.5
  • 47
    • 0034016626 scopus 로고    scopus 로고
    • Fungal allergens and peptide epitopes
    • Kurup V.P., and Banerjee B. Fungal allergens and peptide epitopes. Peptides 21 (2000) 589-599
    • (2000) Peptides , vol.21 , pp. 589-599
    • Kurup, V.P.1    Banerjee, B.2
  • 50
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 51
    • 1842578213 scopus 로고    scopus 로고
    • Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta)
    • Langdon J.M., Vonakis B.M., and MacDonald S.M. Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta). Biochim. Biophys. Acta 1688 (2004) 232-236
    • (2004) Biochim. Biophys. Acta , vol.1688 , pp. 232-236
    • Langdon, J.M.1    Vonakis, B.M.2    MacDonald, S.M.3
  • 52
    • 33751104704 scopus 로고    scopus 로고
    • Improved method for predicting linear B-cell epitopes
    • Larsen J.E., Lund O., and Nielsen M. Improved method for predicting linear B-cell epitopes. Immunome Res. 2 (2006) 2
    • (2006) Immunome Res. , vol.2 , pp. 2
    • Larsen, J.E.1    Lund, O.2    Nielsen, M.3
  • 53
    • 41149096388 scopus 로고    scopus 로고
    • Interaction between fortilin and transforming growth factor-beta stimulated clone-22 (TSC-22) prevents apoptosis via the destabilization of TSC-22
    • Lee J.H., Rho S.B., Park S.Y., and Chun T. Interaction between fortilin and transforming growth factor-beta stimulated clone-22 (TSC-22) prevents apoptosis via the destabilization of TSC-22. FEBS Lett. 582 (2008) 1210-1218
    • (2008) FEBS Lett. , vol.582 , pp. 1210-1218
    • Lee, J.H.1    Rho, S.B.2    Park, S.Y.3    Chun, T.4
  • 54
    • 16244384614 scopus 로고    scopus 로고
    • Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP
    • Liu H., Peng H.W., Cheng Y.S., Yuan H.S., and Yang-Yen H.F. Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol. Cell. Biol. 25 (2005) 3117-3126
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3117-3126
    • Liu, H.1    Peng, H.W.2    Cheng, Y.S.3    Yuan, H.S.4    Yang-Yen, H.F.5
  • 56
    • 0030889878 scopus 로고    scopus 로고
    • Human recombinant histamine-releasing factor
    • MacDonald S.M. Human recombinant histamine-releasing factor. Int. Arch. Allergy Immunol. 113 (1997) 187-189
    • (1997) Int. Arch. Allergy Immunol. , vol.113 , pp. 187-189
    • MacDonald, S.M.1
  • 58
    • 0028982775 scopus 로고
    • Molecular identification of an IgE-dependent histamine-releasing factor
    • MacDonald S.M., Rafnar T., Langdon J., and Lichtenstein L.M. Molecular identification of an IgE-dependent histamine-releasing factor. Science 269 (1995) 688-690
    • (1995) Science , vol.269 , pp. 688-690
    • MacDonald, S.M.1    Rafnar, T.2    Langdon, J.3    Lichtenstein, L.M.4
  • 59
    • 0036034836 scopus 로고    scopus 로고
    • Association of the Src homology 2 domain-containing inositol 5′ phosphatase (SHIP) to releasability in human basophils
    • MacDonald S.M., and Vonakis B.M. Association of the Src homology 2 domain-containing inositol 5′ phosphatase (SHIP) to releasability in human basophils. Mol. Immunol. 38 (2002) 1323-1327
    • (2002) Mol. Immunol. , vol.38 , pp. 1323-1327
    • MacDonald, S.M.1    Vonakis, B.M.2
  • 60
    • 33847691514 scopus 로고    scopus 로고
    • Heat-inducible translationally controlled tumor protein of Trichinella pseudospiralis: cloning and regulation of gene expression
    • Mak C.H., Poon M.W., Lun H.M., Kwok P.Y., and Ko R.C. Heat-inducible translationally controlled tumor protein of Trichinella pseudospiralis: cloning and regulation of gene expression. Parasitol. Res. 100 (2007) 1105-1111
    • (2007) Parasitol. Res. , vol.100 , pp. 1105-1111
    • Mak, C.H.1    Poon, M.W.2    Lun, H.M.3    Kwok, P.Y.4    Ko, R.C.5
  • 61
    • 0026918994 scopus 로고
    • Immunotherapy for mold allergy
    • Malling H.J. Immunotherapy for mold allergy. Clin. Rev. Allergy 10 (1992) 237-251
    • (1992) Clin. Rev. Allergy , vol.10 , pp. 237-251
    • Malling, H.J.1
  • 62
    • 0033519237 scopus 로고    scopus 로고
    • Humoral and cell-mediated autoimmune reactions to human acidic ribosomal P2 protein in individuals sensitized to Aspergillus fumigatus P2 protein
    • Mayer C., Appenzeller U., Seelbach H., Achatz G., Oberkofler H., Breitenbach M., Blaser K., and Crameri R. Humoral and cell-mediated autoimmune reactions to human acidic ribosomal P2 protein in individuals sensitized to Aspergillus fumigatus P2 protein. J. Exp. Med. 189 (1999) 1507-1512
    • (1999) J. Exp. Med. , vol.189 , pp. 1507-1512
    • Mayer, C.1    Appenzeller, U.2    Seelbach, H.3    Achatz, G.4    Oberkofler, H.5    Breitenbach, M.6    Blaser, K.7    Crameri, R.8
  • 63
    • 0032984743 scopus 로고    scopus 로고
    • Is sensitization to Alternaria alternata a risk factor for severe asthma? A population-based study
    • Neukirch C., Henry C., Leynaert B., Liard R., Bousquet J., and Neukirch F. Is sensitization to Alternaria alternata a risk factor for severe asthma? A population-based study. J. Allergy Clin. Immunol. 103 (1999) 709-711
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 709-711
    • Neukirch, C.1    Henry, C.2    Leynaert, B.3    Liard, R.4    Bousquet, J.5    Neukirch, F.6
  • 67
    • 0037163041 scopus 로고    scopus 로고
    • Cloning and characterization of a calcium-binding, histamine-releasing protein from Schistosoma mansoni
    • Rao K.V., Chen L., Gnanasekar M., and Ramaswamy K. Cloning and characterization of a calcium-binding, histamine-releasing protein from Schistosoma mansoni. J. Biol. Chem. 277 (2002) 31207-31213
    • (2002) J. Biol. Chem. , vol.277 , pp. 31207-31213
    • Rao, K.V.1    Chen, L.2    Gnanasekar, M.3    Ramaswamy, K.4
  • 69
    • 0345491504 scopus 로고    scopus 로고
    • Asthma as a paradigm for autoimmune disease
    • Rottem M., and Shoenfeld Y. Asthma as a paradigm for autoimmune disease. Int. Arch. Allergy Immunol. 132 (2003) 210-214
    • (2003) Int. Arch. Allergy Immunol. , vol.132 , pp. 210-214
    • Rottem, M.1    Shoenfeld, Y.2
  • 71
    • 0034947620 scopus 로고    scopus 로고
    • A review of Alternaria alternata sensitivity
    • Sanchez H., and Bush R.K. A review of Alternaria alternata sensitivity. Rev. Iberoam. Micol. 18 (2001) 56-59
    • (2001) Rev. Iberoam. Micol. , vol.18 , pp. 56-59
    • Sanchez, H.1    Bush, R.K.2
  • 75
    • 0031178801 scopus 로고    scopus 로고
    • Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13 secretion by human basophils
    • Schroeder J.T., Lichtenstein L.M., and MacDonald S.M. Recombinant histamine-releasing factor enhances IgE-dependent IL-4 and IL-13 secretion by human basophils. J. Immunol. 159 (1997) 447-452
    • (1997) J. Immunol. , vol.159 , pp. 447-452
    • Schroeder, J.T.1    Lichtenstein, L.M.2    MacDonald, S.M.3
  • 76
    • 33645087131 scopus 로고    scopus 로고
    • Recombinant glutathione-S-transferase a major allergen from Alternaria alternata for clinical use in allergy patients
    • Shankar J., Singh B.P., Gaur S.N., and Arora N. Recombinant glutathione-S-transferase a major allergen from Alternaria alternata for clinical use in allergy patients. Mol. Immunol. 43 (2006) 1927-1932
    • (2006) Mol. Immunol. , vol.43 , pp. 1927-1932
    • Shankar, J.1    Singh, B.P.2    Gaur, S.N.3    Arora, N.4
  • 77
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield P., Garrard S., and Derewenda Z. Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expres. Purif. 15 (1999) 34-39
    • (1999) Protein Expres. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 82
    • 1142309497 scopus 로고    scopus 로고
    • Are indoor molds causing a new disease?
    • Terr A.I. Are indoor molds causing a new disease?. J. Allergy Clin. Immunol. 113 (2004) 221-226
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 221-226
    • Terr, A.I.1
  • 83
    • 45249105602 scopus 로고    scopus 로고
    • Purification of inclusion body-forming peptides and proteins in soluble form by fusion to Escherichia coli thermostable proteins
    • Thapa A., Shahnawaz M., Karki P., Raj Dahal G., Golam Sharoar M., Yub Shin S., Sup Lee J., Cho B., and Park I.S. Purification of inclusion body-forming peptides and proteins in soluble form by fusion to Escherichia coli thermostable proteins. Biotechniques 44 (2008) 787-796
    • (2008) Biotechniques , vol.44 , pp. 787-796
    • Thapa, A.1    Shahnawaz, M.2    Karki, P.3    Raj Dahal, G.4    Golam Sharoar, M.5    Yub Shin, S.6    Sup Lee, J.7    Cho, B.8    Park, I.S.9
  • 84
  • 88
    • 0036238086 scopus 로고    scopus 로고
    • Recombinant allergen-based concepts for diagnosis and therapy of type I allergy
    • Valenta R. Recombinant allergen-based concepts for diagnosis and therapy of type I allergy. Allergy 57 Suppl 71 (2002) 66-67
    • (2002) Allergy , vol.57 , Issue.SUPPL. 71 , pp. 66-67
    • Valenta, R.1
  • 90
    • 23444451601 scopus 로고    scopus 로고
    • Evolution and expression of translationally controlled tumour protein (TCTP) of fish
    • Venugopal T. Evolution and expression of translationally controlled tumour protein (TCTP) of fish. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 142 (2005) 8-17
    • (2005) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.142 , pp. 8-17
    • Venugopal, T.1
  • 92
    • 0033801599 scopus 로고    scopus 로고
    • A cnidarian homologue of translationally controlled tumor protein (P23/TCTP)
    • Yan L., Fei K., Bridge D., and Sarras Jr. M.P. A cnidarian homologue of translationally controlled tumor protein (P23/TCTP). Dev. Genes Evol. 210 (2000) 507-511
    • (2000) Dev. Genes Evol. , vol.210 , pp. 507-511
    • Yan, L.1    Fei, K.2    Bridge, D.3    Sarras Jr., M.P.4
  • 93
    • 23044467160 scopus 로고    scopus 로고
    • An N-terminal region of translationally controlled tumor protein is required for its antiapoptotic activity
    • Yang Y., Yang F., Xiong Z., Yan Y., Wang X., Nishino M., Mirkovic D., Nguyen J., Wang H., and Yang X.F. An N-terminal region of translationally controlled tumor protein is required for its antiapoptotic activity. Oncogene 24 (2005) 4778-4788
    • (2005) Oncogene , vol.24 , pp. 4778-4788
    • Yang, Y.1    Yang, F.2    Xiong, Z.3    Yan, Y.4    Wang, X.5    Nishino, M.6    Mirkovic, D.7    Nguyen, J.8    Wang, H.9    Yang, X.F.10
  • 94
    • 0036334279 scopus 로고    scopus 로고
    • Plk phosphorylation regulates the microtubule-stabilizing protein TCTP
    • Yarm F.R. Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. Mol. Cell. Biol. 22 (2002) 6209-6221
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6209-6221
    • Yarm, F.R.1
  • 95
    • 0037167308 scopus 로고    scopus 로고
    • Sensitisation to airborne moulds and severity of asthma: cross sectional study from European Community respiratory health survey
    • Zureik M., Neukirch C., Leynaert B., Liard R., Bousquet J., and Neukirch F. Sensitisation to airborne moulds and severity of asthma: cross sectional study from European Community respiratory health survey. BMJ 325 (2002) 411-414
    • (2002) BMJ , vol.325 , pp. 411-414
    • Zureik, M.1    Neukirch, C.2    Leynaert, B.3    Liard, R.4    Bousquet, J.5    Neukirch, F.6


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