메뉴 건너뛰기




Volumn 41, Issue 11, 2011, Pages 1157-1164

Peroxidase catalysed cross-linking of an intrinsically unstructured protein via dityrosine bonds in the oocyst wall of the apicomplexan parasite, Eimeria maxima

Author keywords

Apicomplexa; Coccidia; Dityrosine bonds; Eimeria; Intrinsically unstructured protein; Macrogamete; Oocyst

Indexed keywords

ARTHROMYCES PEROXIDASE; DITYROSINE; DOPA; HORSERADISH PEROXIDASE; MYELOPEROXIDASE; PEROXIDASE; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 80052297407     PISSN: 00207519     EISSN: 18790135     Source Type: Journal    
DOI: 10.1016/j.ijpara.2011.07.001     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0017182516 scopus 로고
    • Formation of dityrosine cross-links in proteins by oxidation of tyrosine
    • Aeschbach R., Amado R., Heukom H. Formation of dityrosine cross-links in proteins by oxidation of tyrosine. Biochim. Biophys. Acta 1976, 439:292-301.
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 292-301
    • Aeschbach, R.1    Amado, R.2    Heukom, H.3
  • 2
    • 21044454794 scopus 로고    scopus 로고
    • Aquaporins from pathogenic protozoan parasites: structure, function and potential for chemotherapy
    • Beitz E. Aquaporins from pathogenic protozoan parasites: structure, function and potential for chemotherapy. Biol. Cell 2005, 97:373-383.
    • (2005) Biol. Cell , vol.97 , pp. 373-383
    • Beitz, E.1
  • 4
    • 0036275533 scopus 로고    scopus 로고
    • Biochemical characterisation of the 56 and 82 kilodalton immunodominant gametocyte antigens from Eimeria maxima
    • Belli S.I., Lee M., Thebo P., Wallach M., Schwartsburd S., Smith N.C. Biochemical characterisation of the 56 and 82 kilodalton immunodominant gametocyte antigens from Eimeria maxima. Int. J. Parasitol. 2002, 32:805-816.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 805-816
    • Belli, S.I.1    Lee, M.2    Thebo, P.3    Wallach, M.4    Schwartsburd, S.5    Smith, N.C.6
  • 5
    • 4944226419 scopus 로고    scopus 로고
    • Characterisation of the antigenic and immunogenic properties of bacterially expressed, sexual stage antigens of the coccidian parasite, Eimeria maxima
    • Belli S.I., Mai K., Skene C.D., Gleeson M.T., Witcombe D.M., Katrib M., Finger A., Wallach M.G., Smith N.C. Characterisation of the antigenic and immunogenic properties of bacterially expressed, sexual stage antigens of the coccidian parasite, Eimeria maxima. Vaccine 2004, 22:4316-4325.
    • (2004) Vaccine , vol.22 , pp. 4316-4325
    • Belli, S.I.1    Mai, K.2    Skene, C.D.3    Gleeson, M.T.4    Witcombe, D.M.5    Katrib, M.6    Finger, A.7    Wallach, M.G.8    Smith, N.C.9
  • 7
    • 0038482167 scopus 로고    scopus 로고
    • Role of tyrosine-rich precursor glycoproteins and dityrosine- and 3,4-dihydroxyphenylalanine-mediated protein cross-linking in development of the oocyst wall in the coccidian parasite Eimeria maxima
    • Belli S.I., Wallach M.G., Luxford C., Davies M.J., Smith N.C. Role of tyrosine-rich precursor glycoproteins and dityrosine- and 3,4-dihydroxyphenylalanine-mediated protein cross-linking in development of the oocyst wall in the coccidian parasite Eimeria maxima. Eukaryot. Cell 2003, 2:456-464.
    • (2003) Eukaryot. Cell , vol.2 , pp. 456-464
    • Belli, S.I.1    Wallach, M.G.2    Luxford, C.3    Davies, M.J.4    Smith, N.C.5
  • 8
    • 0037137570 scopus 로고    scopus 로고
    • Functional genomics of gam56: characterisation of the role of a 56 kilodalton sexual stage antigen in oocyst wall formation in Eimeria maxima
    • Belli S.I., Witcombe D., Wallach M.G., Smith N.C. Functional genomics of gam56: characterisation of the role of a 56 kilodalton sexual stage antigen in oocyst wall formation in Eimeria maxima. Int. J. Parasitol. 2002, 32:1727-1737.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1727-1737
    • Belli, S.I.1    Witcombe, D.2    Wallach, M.G.3    Smith, N.C.4
  • 9
    • 27944488680 scopus 로고    scopus 로고
    • Accurate prediction of protein disordered regions by mining protein structure data
    • Cheng J., Sweredoski M., Baldi P. Accurate prediction of protein disordered regions by mining protein structure data. Data Mining Knowledge Discov 2005, 11:213-222.
    • (2005) Data Mining Knowledge Discov , vol.11 , pp. 213-222
    • Cheng, J.1    Sweredoski, M.2    Baldi, P.3
  • 10
    • 0037518468 scopus 로고    scopus 로고
    • Developmentally regulated biosynthesis of carbohydrate and storage polysaccharide during differentiation and tissue cyst formation in Toxoplasma gondii
    • Coppin A., Dzierszinski F., Legrand S., Mortuaire M., Ferguson D., Tomavo S. Developmentally regulated biosynthesis of carbohydrate and storage polysaccharide during differentiation and tissue cyst formation in Toxoplasma gondii. Biochimie 2003, 85:353-361.
    • (2003) Biochimie , vol.85 , pp. 353-361
    • Coppin, A.1    Dzierszinski, F.2    Legrand, S.3    Mortuaire, M.4    Ferguson, D.5    Tomavo, S.6
  • 11
    • 26844566629 scopus 로고    scopus 로고
    • Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment
    • Cortese M.S., Baird J.P., Uversky V.N., Dunker A.K. Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment. J. Proteome Res. 2005, 4:1610-1618.
    • (2005) J. Proteome Res. , vol.4 , pp. 1610-1618
    • Cortese, M.S.1    Baird, J.P.2    Uversky, V.N.3    Dunker, A.K.4
  • 12
    • 0027190626 scopus 로고
    • An interactive program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deleage G., Geourjon C. An interactive program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci. 1993, 2:197-199.
    • (1993) Comput. Appl. Biosci. , vol.2 , pp. 197-199
    • Deleage, G.1    Geourjon, C.2
  • 13
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z., Csizmok V., Tompa P., Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005, 21:3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 15
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson H.J., Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 2004, 104:3607-3662.
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3662
    • Dyson, H.J.1    Wright, P.E.2
  • 16
    • 20544463153 scopus 로고    scopus 로고
    • Structure and inter-domain interactions of domain II from the blood-stage malarial protein, apical membrane antigen 1
    • Feng Z.-P., Keizer D.W., Stevenson R.A., Yao S., Babon J.J., Murphy V.J., Anders R.F., Norton R.S. Structure and inter-domain interactions of domain II from the blood-stage malarial protein, apical membrane antigen 1. J. Mol. Biol. 2005, 350:641-656.
    • (2005) J. Mol. Biol. , vol.350 , pp. 641-656
    • Feng, Z.-P.1    Keizer, D.W.2    Stevenson, R.A.3    Yao, S.4    Babon, J.J.5    Murphy, V.J.6    Anders, R.F.7    Norton, R.S.8
  • 17
    • 33750711671 scopus 로고    scopus 로고
    • Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan proteomes
    • Feng Z.-P., Zhang X.-Z., Han P.-F., Arora N., Anders R.F., Norton R.S. Abundance of intrinsically unstructured proteins in P. falciparum and other apicomplexan proteomes. Mol. Biochem. Parasitol. 2006, 150:256-267.
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 256-267
    • Feng, Z.-P.1    Zhang, X.-Z.2    Han, P.-F.3    Arora, N.4    Anders, R.F.5    Norton, R.S.6
  • 18
    • 0141644173 scopus 로고    scopus 로고
    • The development of the macrogamete and oocyst wall in Eimeria maxima: immuno-light and electron microscopy
    • Ferguson D.J.P., Belli S.I., Smith N.C., Wallach M.G. The development of the macrogamete and oocyst wall in Eimeria maxima: immuno-light and electron microscopy. Int. J. Parasitol. 2003, 33:1329-1340.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1329-1340
    • Ferguson, D.J.P.1    Belli, S.I.2    Smith, N.C.3    Wallach, M.G.4
  • 19
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier J., Gibrat J.F., Robson B. GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 1996, 266:540-553.
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 20
    • 0029595442 scopus 로고
    • SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C., Deléage G. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Bioinformatics 1995, 11:681-684.
    • (1995) Bioinformatics , vol.11 , pp. 681-684
    • Geourjon, C.1    Deléage, G.2
  • 21
    • 1842607375 scopus 로고    scopus 로고
    • Amylopectin: a major component of the residual body in Cryptosporidium parvum oocysts
    • Harris H.R., Adrian M., Petry F. Amylopectin: a major component of the residual body in Cryptosporidium parvum oocysts. Parasitology 2004, 128:269-282.
    • (2004) Parasitology , vol.128 , pp. 269-282
    • Harris, H.R.1    Adrian, M.2    Petry, F.3
  • 23
    • 0028133032 scopus 로고
    • The role of dityrosine formation in the crosslinking of CUT-2, the product of a second cuticlin gene of Caenorhabditis elegans
    • Lassandro F., Sebastiano M., Zei F., Bazzicalupo P. The role of dityrosine formation in the crosslinking of CUT-2, the product of a second cuticlin gene of Caenorhabditis elegans. Mol. Biochem. Parasitol. 1994, 65:147-159.
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 147-159
    • Lassandro, F.1    Sebastiano, M.2    Zei, F.3    Bazzicalupo, P.4
  • 25
    • 0029919963 scopus 로고    scopus 로고
    • Dityrosine formation in calmodulin: cross-linking and polymerization catalysed by Arthromyces peroxidase
    • Malencik D.A., Anderson S.R. Dityrosine formation in calmodulin: cross-linking and polymerization catalysed by Arthromyces peroxidase. Biochemistry 1996, 35:4375-4386.
    • (1996) Biochemistry , vol.35 , pp. 4375-4386
    • Malencik, D.A.1    Anderson, S.R.2
  • 26
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 2000, 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 27
    • 33748079101 scopus 로고    scopus 로고
    • Comparative genomic and phylogenetic analyses of calcium ATPase and calcium-regulated proteins in the Apicomplexa
    • Nagamune K., Sibley L.D. Comparative genomic and phylogenetic analyses of calcium ATPase and calcium-regulated proteins in the Apicomplexa. Mol. Biol. Evol. 2006, 23:1613-1627.
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1613-1627
    • Nagamune, K.1    Sibley, L.D.2
  • 28
    • 0035088867 scopus 로고    scopus 로고
    • Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria
    • Nishiyama Y., Massey V., Takeda K., Kawasaki S., Sato J., Watanabe T., Niimura Y. Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria. J. Bacteriol. 2001, 183:2431-2438.
    • (2001) J. Bacteriol. , vol.183 , pp. 2431-2438
    • Nishiyama, Y.1    Massey, V.2    Takeda, K.3    Kawasaki, S.4    Sato, J.5    Watanabe, T.6    Niimura, Y.7
  • 30
    • 80052283667 scopus 로고    scopus 로고
    • APSSP2: a combination method for protein secondary structure prediction based on neural network and example based learning. CASP5 A-132.
    • Raghava, G.P.S., 2002. APSSP2: a combination method for protein secondary structure prediction based on neural network and example based learning. CASP5 A-132.
    • (2002)
    • Raghava, G.P.S.1
  • 32
    • 0014557219 scopus 로고
    • Amylopectin, the storage polysaccharide of the coccidia Eimeria brunetti and E. tenella
    • Ryley J.F., Bentley M., Manner D.J., Stark J.R. Amylopectin, the storage polysaccharide of the coccidia Eimeria brunetti and E. tenella. J. Parasitol. 1969, 55:839-845.
    • (1969) J. Parasitol. , vol.55 , pp. 839-845
    • Ryley, J.F.1    Bentley, M.2    Manner, D.J.3    Stark, J.R.4
  • 34
    • 0030628379 scopus 로고    scopus 로고
    • Eimeria spp. from the chicken: occurrence, identification and genetics
    • Shirley M.W. Eimeria spp. from the chicken: occurrence, identification and genetics. Acta Vet. Hun. 1997, 45:331-347.
    • (1997) Acta Vet. Hun. , vol.45 , pp. 331-347
    • Shirley, M.W.1
  • 36
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable α-synuclein polymers
    • Souza J.M., Giasson B.I., Chen Q., Lee V.M.-Y., Ischiropoulos H. Dityrosine cross-linking promotes formation of stable α-synuclein polymers. J. Biol. Chem. 2000, 275:18344-18349.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.-Y.4    Ischiropoulos, H.5
  • 37
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005, 579:3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 38
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky V.N. A protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 2003, 21:211-234.
    • (2003) J. Biomol. Struct. Dyn. , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 40
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 2004, 337:635-645.
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 41
    • 0036307786 scopus 로고    scopus 로고
    • Progress with parasite plastids
    • Wilson R.J.M. Progress with parasite plastids. J. Mol. Biol. 2002, 319:257-274.
    • (2002) J. Mol. Biol. , vol.319 , pp. 257-274
    • Wilson, R.J.M.1
  • 42
    • 20744437001 scopus 로고    scopus 로고
    • RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang Z.R., Thomson R., McNeil P., Esnouf R.M. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 2005, 21:3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 43
    • 42749096469 scopus 로고    scopus 로고
    • Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2
    • Zhang X., Perugini M.A., Yao S., Add C.G., Murphy V.J., Low A., Anders R.F., Norton R.S. Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. J. Mol. Biol. 2008, 379:105-121.
    • (2008) J. Mol. Biol. , vol.379 , pp. 105-121
    • Zhang, X.1    Perugini, M.A.2    Yao, S.3    Add, C.G.4    Murphy, V.J.5    Low, A.6    Anders, R.F.7    Norton, R.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.