메뉴 건너뛰기




Volumn 29, Issue 1, 2007, Pages 47-56

Expression of the recombinant protein disulphide isomerase of Teladorsagia circumcincta

Author keywords

IgA; Immunity; Protein disulphide isomerase; Sheep; Teladorsagia circumcincta

Indexed keywords

COMPLEMENTARY DNA; DISULFIDE ISOMERASE; IMMUNOGLOBULIN A; PARASITE ANTIGEN; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; RNA;

EID: 33845580817     PISSN: 01419838     EISSN: 13653024     Source Type: Journal    
DOI: 10.1111/j.1365-3024.2006.00922.x     Document Type: Article
Times cited : (6)

References (23)
  • 1
    • 33646170060 scopus 로고    scopus 로고
    • Gastrointestinal nematode infection in sheep - A review of the alternatives to anthelmintics in parasite control
    • Sayers G & Sweeney T. Gastrointestinal nematode infection in sheep - a review of the alternatives to anthelmintics in parasite control. Anim Health Res Rev 2005; 6: 159-171.
    • (2005) Anim Health Res Rev , vol.6 , pp. 159-171
    • Sayers, G.1    Sweeney, T.2
  • 3
    • 0036092424 scopus 로고    scopus 로고
    • The genetic control of IgA activity against Teladorsagia circumcincta and its association with parasite resistance in naturally infected sheep
    • Strain SA, Bishop SC, Henderson NG, et al. The genetic control of IgA activity against Teladorsagia circumcincta and its association with parasite resistance in naturally infected sheep. Parasitology 2002; 124: 545-552.
    • (2002) Parasitology , vol.124 , pp. 545-552
    • Strain, S.A.1    Bishop, S.C.2    Henderson, N.G.3
  • 5
    • 0027959156 scopus 로고
    • Protein disulphide-isomerase: Building bridges in protein folding
    • Freedman RB, Hirst TR & Tuite MF. Protein disulphide-isomerase: building bridges in protein folding. Trends Biochem Sci 1994; 19: 331-336.
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 6
    • 0033054307 scopus 로고    scopus 로고
    • The recognition of molecules from fourth-stage larvae of Ostertagia circumcincta by IgA from infected sheep
    • Strain SA & Stear MJ. The recognition of molecules from fourth-stage larvae of Ostertagia circumcincta by IgA from infected sheep. Parasite Immunol 1999; 21: 163-168.
    • (1999) Parasite Immunol , vol.21 , pp. 163-168
    • Strain, S.A.1    Stear, M.J.2
  • 8
    • 0034737591 scopus 로고    scopus 로고
    • A fast and convenient MALDI-MS based proteomic approach: Identification of components scaffolded by the actin cytoskeleton of activated human thrombocytes
    • Gevaert K, Eggermont L, Demol H & Vandekerckhove J. A fast and convenient MALDI-MS based proteomic approach: identification of components scaffolded by the actin cytoskeleton of activated human thrombocytes. J Biotechnol 2000; 78: 259-269.
    • (2000) J Biotechnol , vol.78 , pp. 259-269
    • Gevaert, K.1    Eggermont, L.2    Demol, H.3    Vandekerckhove, J.4
  • 9
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM & Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999; 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 10
    • 0035850233 scopus 로고    scopus 로고
    • Treatment versus non-treatment of helminth infections in cattle: Defining the threshold
    • Vercruysse J & Claerebout E. Treatment versus non-treatment of helminth infections in cattle: defining the threshold. Vet Parasitol 2001; 98: 195-214.
    • (2001) Vet Parasitol , vol.98 , pp. 195-214
    • Vercruysse, J.1    Claerebout, E.2
  • 11
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand AR, Cuozzo JW & Kaiser CA. Pathways for protein disulphide bond formation. Trends Cell Biol 2000; 10: 203-210.
    • (2000) Trends Cell Biol , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 12
    • 0037292401 scopus 로고    scopus 로고
    • Protein disulphide isomerase of Ostertagia ostertagi: An excretory-secretory product of L4 and adult worms?
    • Geldhof P, Vercauteren I, Knox D, et al. Protein disulphide isomerase of Ostertagia ostertagi: an excretory-secretory product of L4 and adult worms? Int J Parasitol 2003; 33: 129-136.
    • (2003) Int J Parasitol , vol.33 , pp. 129-136
    • Geldhof, P.1    Vercauteren, I.2    Knox, D.3
  • 13
    • 0036850222 scopus 로고    scopus 로고
    • Conserved regions of protein disulfide isomerase are targeted by natural IgA antibodies in humans
    • Meek B, Back JW, Klaren VNA, Speijer D & Peek R. Conserved regions of protein disulfide isomerase are targeted by natural IgA antibodies in humans. Int Immunol 2002; 11: 1291-1301.
    • (2002) Int Immunol , vol.11 , pp. 1291-1301
    • Meek, B.1    Back, J.W.2    Klaren, V.N.A.3    Speijer, D.4    Peek, R.5
  • 14
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S & Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987; 48: 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 15
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman JC, Ellis L, Blacher RW, Roth RA & Rutter WJ. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 1985; 317: 267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 16
    • 0031688779 scopus 로고    scopus 로고
    • A recombinant protein disulfide isomerase homologue from Ancylostoma caninum
    • Epe C, Kohlmetz C & Schnieder T. A recombinant protein disulfide isomerase homologue from Ancylostoma caninum. Parasitol Res 1998; 84: 763-766.
    • (1998) Parasitol Res , vol.84 , pp. 763-766
    • Epe, C.1    Kohlmetz, C.2    Schnieder, T.3
  • 17
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia ML & Lennarz WJ. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 1993; 74: 899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 18
    • 0028242359 scopus 로고
    • The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase
    • Puig A, Lyles MM, Noiva R & Gilbert HF. The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase. J Biol Chem 1994; 269: 19128-19135.
    • (1994) J Biol Chem , vol.269 , pp. 19128-19135
    • Puig, A.1    Lyles, M.M.2    Noiva, R.3    Gilbert, H.F.4
  • 19
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman RB, Klappa P & Ruddock LW. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO J 2002; 3: 136-140.
    • (2002) EMBO J , vol.3 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 20
    • 0014939566 scopus 로고
    • The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate
    • Gonzalez Porque P, Baldesten A & Reichard P. The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate. J Biol Chem 1970; 245: 2371-2374.
    • (1970) J Biol Chem , vol.245 , pp. 2371-2374
    • Gonzalez Porque, P.1    Baldesten, A.2    Reichard, P.3
  • 21
    • 0031034725 scopus 로고    scopus 로고
    • Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2
    • Yao Y, Zhou Y & Wang C. Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. EMBO J 1997; 16: 651-658.
    • (1997) EMBO J , vol.16 , pp. 651-658
    • Yao, Y.1    Zhou, Y.2    Wang, C.3
  • 22
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi T, Helaakoski T, Tasanen K, et al. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J 1987; 6: 643-649.
    • (1987) EMBO J , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3
  • 23
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau JR, Combs KA, Spinner SN & Joiner BJ. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 1990; 265: 9801-9807.
    • (1990) J Biol Chem , vol.265 , pp. 9801-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.