메뉴 건너뛰기




Volumn 99, Issue 2, 1999, Pages 301-306

Expression pattern and functional significance of a divergent nematode cyclophilin in Caenorhabditis elegans

Author keywords

Brugia malayi; Caenorhabditis elegans; Cyclophilin; CyclosporinA; Filariae; Peptidyl prolyl cis trans isomerase

Indexed keywords

CYCLOPHILIN; CYCLOSPORIN A; DRUG BINDING PROTEIN; PROLINE;

EID: 0032933154     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00044-4     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagens
    • Bachinger H.P. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagens. J. Biol. Chem. 262:1987;17144-17148.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17144-17148
    • Bachinger, H.P.1
  • 2
    • 0025968746 scopus 로고
    • CyclosporinA slows collagen triple-helix formation in vivo: Indirect evidence for a physiological role of peptidyl prolyl cis-trans isomerase
    • Steinmann B., Bruckner P., Superti-Furga A. CyclosporinA slows collagen triple-helix formation in vivo: indirect evidence for a physiological role of peptidyl prolyl cis-trans isomerase. J. Biol. Chem. 266:1991;1299-1303.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 3
    • 0025311245 scopus 로고
    • Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding
    • Kiefhaber T., Grunert H.P., Hahn U., Schmid F.X. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry. 29:1991;6475-6480.
    • (1991) Biochemistry , vol.29 , pp. 6475-6480
    • Kiefhaber, T.1    Grunert, H.P.2    Hahn, U.3    Schmid, F.X.4
  • 4
    • 0025916166 scopus 로고
    • CyclosporineA inhibits an initial step in folding of transferrin within the endoplasmic reticulum
    • Lodish H.F., Kong N. CyclosporineA inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J. Biol. Chem. 266:1991;14835-14838.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14835-14838
    • Lodish, H.F.1    Kong, N.2
  • 5
    • 0025995535 scopus 로고
    • The cyclophilin homolog NINAa is required in the secretory pathway
    • Colley N., Baker E., Stamnes M., Zuker C. The cyclophilin homolog NINAa is required in the secretory pathway. Cell. 67:1991;255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.1    Baker, E.2    Stamnes, M.3    Zuker, C.4
  • 6
    • 0027971782 scopus 로고
    • Functional association of cyclophilinA with HIV-1 virions
    • Thali M., Bukovsky A., Kondo E. Functional association of cyclophilinA with HIV-1 virions. Nature. 372:1994;363-365.
    • (1994) Nature , vol.372 , pp. 363-365
    • Thali, M.1    Bukovsky, A.2    Kondo, E.3
  • 7
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G., Wittmann-Liebold B., Lang K., Kiefhaber T., Schmid F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature. 337:1989;476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 8
    • 0029885634 scopus 로고    scopus 로고
    • Cloning and biochemical characterisation of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans
    • Page A.P., MacNiven K., Hengartner M.O. Cloning and biochemical characterisation of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans. Biochem. J. 317:1996;179-185.
    • (1996) Biochem. J. , vol.317 , pp. 179-185
    • Page, A.P.1    MacNiven, K.2    Hengartner, M.O.3
  • 9
    • 0029078606 scopus 로고
    • Parasite cyclophilins and antiparasite activity of cyclosporinA
    • Page A.P., Kumar S., Carlow C.K.S. Parasite cyclophilins and antiparasite activity of cyclosporinA. Parasitol. Today. 11:1995;385-388.
    • (1995) Parasitol. Today , vol.11 , pp. 385-388
    • Page, A.P.1    Kumar, S.2    Carlow, C.K.S.3
  • 10
    • 0029114309 scopus 로고
    • Molecular characterization of a cyclosporinA - insensitive cyclophilin from the parasitic nematode Brugia malayi
    • Page A.P., Landry D., Wilson G.G., Carlow C.K.S. Molecular characterization of a cyclosporinA - insensitive cyclophilin from the parasitic nematode Brugia malayi. Biochemistry. 34:1995;11545-11550.
    • (1995) Biochemistry , vol.34 , pp. 11545-11550
    • Page, A.P.1    Landry, D.2    Wilson, G.G.3    Carlow, C.K.S.4
  • 11
    • 0032030459 scopus 로고    scopus 로고
    • Highly conserved large molecular weight cyclophilin of filarial parasites
    • Hong X.Q., Ma D., Page A.P., Kumar S., Carlow C.K.S. Highly conserved large molecular weight cyclophilin of filarial parasites. Exp. Parasitol. 88:1998;246-251.
    • (1998) Exp. Parasitol. , vol.88 , pp. 246-251
    • Hong, X.Q.1    Ma, D.2    Page, A.P.3    Kumar, S.4    Carlow, C.K.S.5
  • 12
    • 0010726063 scopus 로고
    • CyclosporinA: Antiparasitic drug, modulator of the host-parasite relationship and immunosuppressant
    • Chappell L.H., Wastling J.L. CyclosporinA: antiparasitic drug, modulator of the host-parasite relationship and immunosuppressant. Parasitology. 105:1992;S25-S40.
    • (1992) Parasitology , vol.105
    • Chappell, L.H.1    Wastling, J.L.2
  • 13
    • 0032571575 scopus 로고    scopus 로고
    • The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi
    • Taylor P., Page A.P., Kontopidis G., Husi H., Walkinshaw M.D. The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi. FEBS Lett. 425:1998;361-366.
    • (1998) FEBS Lett. , vol.425 , pp. 361-366
    • Taylor, P.1    Page, A.P.2    Kontopidis, G.3    Husi, H.4    Walkinshaw, M.D.5
  • 14
    • 0031441989 scopus 로고    scopus 로고
    • Cyclophilin and protein disulfide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans
    • Page A.P. Cyclophilin and protein disulfide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans. DNA Cell. Biol. 16:1997;1335-1343.
    • (1997) DNA Cell. Biol. , vol.16 , pp. 1335-1343
    • Page, A.P.1
  • 15
    • 0030218143 scopus 로고    scopus 로고
    • The SR protein family: Pleiotropic functions in pre-mRNA splicing
    • Valcarcel J., Green M.R. The SR protein family: pleiotropic functions in pre-mRNA splicing. TIBS. 21:1996;296-301.
    • (1996) TIBS , vol.21 , pp. 296-301
    • Valcarcel, J.1    Green, M.R.2
  • 16
    • 0032531371 scopus 로고    scopus 로고
    • A divergent multi-domain cyclophilin is highly conserved between parasitic and free-living nematode species and is important in larval muscle development
    • Page A.P., Winter A.D. A divergent multi-domain cyclophilin is highly conserved between parasitic and free-living nematode species and is important in larval muscle development. Mol. Biochem. Parasitol. 95:1998;215-227.
    • (1998) Mol. Biochem. Parasitol. , vol.95 , pp. 215-227
    • Page, A.P.1    Winter, A.D.2
  • 17
    • 0030026910 scopus 로고    scopus 로고
    • Isolation and characterisation of four developmentally regulated cathepsin B-like cysteine protease genes from the nematode Caenorhabditis elegans
    • Larminie C.G.C., Johnstone I.L. Isolation and characterisation of four developmentally regulated cathepsin B-like cysteine protease genes from the nematode Caenorhabditis elegans. DNA Cell. Biol. 15:1996;75-82.
    • (1996) DNA Cell. Biol. , vol.15 , pp. 75-82
    • Larminie, C.G.C.1    Johnstone, I.L.2
  • 18
    • 0029898363 scopus 로고    scopus 로고
    • Temporal reiteration of a precise gene expression pattern during nematode development
    • Johnstone I.L., Barry J.D. Temporal reiteration of a precise gene expression pattern during nematode development. EMBO J. 15:1996;3633-3639.
    • (1996) EMBO J. , vol.15 , pp. 3633-3639
    • Johnstone, I.L.1    Barry, J.D.2
  • 19
    • 0024469811 scopus 로고
    • Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II
    • Bird D.M., Riddle D.L. Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II. Mol. Cell. Biol. 9:1989;4119-4130.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4119-4130
    • Bird, D.M.1    Riddle, D.L.2
  • 21
    • 0021770409 scopus 로고
    • Cloning of a yolk protein gene family from Caenorhabditis elegans
    • Blumenthal T., Squire M., Kirtland S. Cloning of a yolk protein gene family from Caenorhabditis elegans. J. Mol. Biol. 174:1984;1-18.
    • (1984) J. Mol. Biol. , vol.174 , pp. 1-18
    • Blumenthal, T.1    Squire, M.2    Kirtland, S.3
  • 22
    • 0027402124 scopus 로고
    • The gut esterase gene (ges-1) from the nematodes Caenorhabditis elegans and Caenorhabditis briggsae
    • Kennedy B.P., Aamodt E.J., Allen F.L., Chung M.A., Heschl M.F.P., McGhee J.D. The gut esterase gene (ges-1) from the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. J. Mol. Biol. 229:1993;890-908.
    • (1993) J. Mol. Biol. , vol.229 , pp. 890-908
    • Kennedy, B.P.1    Aamodt, E.J.2    Allen, F.L.3    Chung, M.A.4    Heschl, M.F.P.5    McGhee, J.D.6
  • 23
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A., Xu S., Montgomery M.K., Kostas S.A., Driver S.E., Mello C.C. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature. 391:1998;806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.