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Volumn 22, Issue 12, 2005, Pages 927-945

The cyclophilin repertoire of the fission yeast Schizosaccharomyces pombe

Author keywords

Cyclophilin; Peptidyl prolyl cis trans isomerase; Schizosaccharomyces pombe

Indexed keywords

CYCLOPHILIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; ISOMERASE; PROLINE DERIVATIVE; RNA;

EID: 25844497014     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/yea.1288     Document Type: Review
Times cited : (15)

References (185)
  • 1
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams MD. 2000. The genome sequence of Drosophila melanogaster. Science 287: 2185-2195.
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1
  • 2
    • 0028361571 scopus 로고
    • Characterization of surface binding sites for cyclophilin B on a human tumour T-cell line
    • Allain F, Denys A, Spik G. 1994. Characterization of surface binding sites for cyclophilin B on a human tumour T-cell line. J Biol Chem 269: 16537-16546.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16537-16546
    • Allain, F.1    Denys, A.2    Spik, G.3
  • 3
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 4
    • 0034811414 scopus 로고    scopus 로고
    • The fission yeast ortholog of the coregulator SKIP interacts with the small subunit of U2AF
    • Ambrozkova M, Puta F, Fukova K et al. 2001. The fission yeast ortholog of the coregulator SKIP interacts with the small subunit of U2AF. Biochem Biophys Res Commun 284: 1148-1154.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 1148-1154
    • Ambrozkova, M.1    Puta, F.2    Fukova, K.3
  • 5
    • 0036935208 scopus 로고    scopus 로고
    • A new family of cyclophilins with an RNA recognition motif that interact with members of the trx/MLL protein family in Drosophila and human cells
    • Anderson M, Fair K, Amero S et al. 2002. A new family of cyclophilins with an RNA recognition motif that interact with members of the trx/MLL protein family in Drosophila and human cells. Dev Genes Evol 212: 107-113.
    • (2002) Dev. Genes Evol. , vol.212 , pp. 107-113
    • Anderson, M.1    Fair, K.2    Amero, S.3
  • 6
    • 0036789573 scopus 로고    scopus 로고
    • Cyclophilin A peptidyl-prolyl isomerase activity promotes Zpr1 nuclear export
    • Ansari H, Greco G, Luban J. 2002. Cyclophilin A peptidyl-prolyl isomerase activity promotes Zpr1 nuclear export. Mol Cell Biol 22: 6993-7003.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6993-7003
    • Ansari, H.1    Greco, G.2    Luban, J.3
  • 7
    • 0242528876 scopus 로고    scopus 로고
    • Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase
    • Arevalo-Rodriguez M, Cardenas ME, Wu X, Hanes SD, Heitman J. 2000. Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J 19: 3739-3749.
    • (2000) EMBO J. , vol.19 , pp. 3739-3749
    • Arevalo-Rodriguez, M.1    Cardenas, M.E.2    Wu, X.3    Hanes, S.D.4    Heitman, J.5
  • 8
    • 13744256202 scopus 로고    scopus 로고
    • Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae
    • Arevalo-Rodriguez M, Heitman J. 2005. Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae. Eukaryot Cell 4: 17-29.
    • (2005) Eukaryot. Cell , vol.4 , pp. 17-29
    • Arevalo-Rodriguez, M.1    Heitman, J.2
  • 11
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, Kaiser RA, Purcell NH et al. 2005. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434: 658.
    • (2005) Nature , vol.434 , pp. 658
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 12
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a sTable complex in vivo with its protein target rhodopsin
    • Baker EK, Colley NJ, Zuker CS. 1994. The cyclophilin homolog NinaA functions as a chaperone, forming a sTable complex in vivo with its protein target rhodopsin. EMBO J 13: 4886-4895.
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 13
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso E, Fante L, Fowlkes J et al. 2005. Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J Biol Chem 280: 18558-18561.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3
  • 14
    • 0026552438 scopus 로고
    • Molecular mechanisms of immunosuppression
    • Baumann G, Zenke G, Wenger R et al. 1992. Molecular mechanisms of immunosuppression. J Autoimmun 5: 67-72.
    • (1992) J. Autoimmun. , vol.5 , pp. 67-72
    • Baumann, G.1    Zenke, G.2    Wenger, R.3
  • 15
    • 0035937462 scopus 로고    scopus 로고
    • Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40
    • Berardini TZ, Bollman K, Sun H, Peothig RS. 2001. Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40. Science 291: 2405-2407.
    • (2001) Science , vol.291 , pp. 2405-2407
    • Berardini, T.Z.1    Bollman, K.2    Sun, H.3    Peothig, R.S.4
  • 17
    • 0034284122 scopus 로고    scopus 로고
    • Recent changes to RasMol, recombining the variants
    • Bernstein H. 2000. Recent changes to RasMol, recombining the variants. Trends Biochem Sci 25: 453-455.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 453-455
    • Bernstein, H.1
  • 18
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo
    • Bharadwaj S, Ali A, Ovsenek N. 1999. Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo. Mol Cell Biol 19: 8033-8041.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 19
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney E, Kumar S, Krainer AR. 1993. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res 21: 5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 20
    • 0030844256 scopus 로고    scopus 로고
    • A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II
    • Bourquin J, Stagljar I, Meier P et al. 1997. A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II. Nucleic Acids Res 25: 2055-2061.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2055-2061
    • Bourquin, J.1    Stagljar, I.2    Meier, P.3
  • 21
    • 0027323876 scopus 로고
    • Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: Roles of calcineurin binding and cellular location
    • Bram RJ, Hung DT, Martin PK, Schreiber SL, Crabtree GR. 1993. Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location. Mol Cell Biol 13: 4760-4769.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4760-4769
    • Bram, R.J.1    Hung, D.T.2    Martin, P.K.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 22
  • 23
    • 0035930607 scopus 로고    scopus 로고
    • Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles
    • Brown CR, Cui D-Y, Hung GG-C, Chiang H-L. 2001. Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles. J Biol Chem 276: 48017-48026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48017-48026
    • Brown, C.R.1    Cui, D.-Y.2    Hung, G.G-.C.3    Chiang, H.-L.4
  • 24
    • 0242321995 scopus 로고    scopus 로고
    • Structural characterization of the HIV-1Vpr N-terminus: Evidence of cis/trans proline isomerism
    • Bruns K, Fossen T, Wray V et al. 2003. Structural characterization of the HIV-1Vpr N-terminus: evidence of cis/trans proline isomerism. J Biol Chem 278: 43188-43201.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43188-43201
    • Bruns, K.1    Fossen, T.2    Wray, V.3
  • 25
    • 0036644582 scopus 로고    scopus 로고
    • Cyclophilins: Unexpected messengers in intracellular communications
    • Bukrinsky MI. 2002. Cyclophilins: unexpected messengers in intracellular communications. Trends Immunol 23: 323-325.
    • (2002) Trends Immunol. , vol.23 , pp. 323-325
    • Bukrinsky, M.I.1
  • 26
    • 1542426641 scopus 로고    scopus 로고
    • AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis
    • Cande C, Vahsen N, Kouranti I et al. 2004. AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis. Oncogene 23: 1514-1521.
    • (2004) Oncogene , vol.23 , pp. 1514-1521
    • Cande, C.1    Vahsen, N.2    Kouranti, I.3
  • 27
    • 0028787622 scopus 로고
    • Only in the presence of Immunophilins can cyclosporine and FK506 disrupt in vivo binding of Calcineurin A to its autoinhibitory domain yet strengthen interaction between Calcineurin A and B subunits
    • Chaudhuri B, Stephan C. 1995. Only in the presence of Immunophilins can cyclosporine and FK506 disrupt in vivo binding of Calcineurin A to its autoinhibitory domain yet strengthen interaction between Calcineurin A and B subunits. Biochem Biophys Res Commun 215: 781-790.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 781-790
    • Chaudhuri, B.1    Stephan, C.2
  • 28
    • 12244267727 scopus 로고    scopus 로고
    • Global transcriptional responses of fission yeast to environmental stress
    • Chen D, Toone WM, Mata J et al. 2003. Global transcriptional responses of fission yeast to environmental stress. Mol Biol Cell 14: 214-229.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 214-229
    • Chen, D.1    Toone, W.M.2    Mata, J.3
  • 29
    • 0037144409 scopus 로고    scopus 로고
    • Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A
    • Clarke SJ, McStay GP, Halestrap, AP. 2002. Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A. J Biol Chem 277: 34793-34799.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34793-34799
    • Clarke, S.J.1    McStay, G.P.2    Halestrap, A.P.3
  • 30
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros MG, von Heijne G. 1994. TopPred II: an improved software for membrane protein structure predictions. CABIOS 10: 685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    von Heijne, G.2
  • 31
    • 0037322838 scopus 로고    scopus 로고
    • A novel and functional interaction between cyclophilin A and prolactin receptor
    • Clevenger CV. 2003. A novel and functional interaction between cyclophilin A and prolactin receptor. Endocrine 20: 83-90.
    • (2003) Endocrine , vol.20 , pp. 83-90
    • Clevenger, C.V.1
  • 32
    • 17644371362 scopus 로고    scopus 로고
    • Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin
    • Coaker G, Falick A, Staskawicz B. 2005. Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin. Science 308: 548-550.
    • (2005) Science , vol.308 , pp. 548-550
    • Coaker, G.1    Falick, A.2    Staskawicz, B.3
  • 33
    • 18644384463 scopus 로고    scopus 로고
    • Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine
    • Colgan J, Asmal M, Yu B, Luban J. 2005. Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine. J Immunol 174: 6030-6038.
    • (2005) J. Immunol. , vol.174 , pp. 6030-6038
    • Colgan, J.1    Asmal, M.2    Yu, B.3    Luban, J.4
  • 34
    • 0025995535 scopus 로고
    • The cyclophilin homolog NinaA is required in the secretory pathway
    • Colley NJ, Baker EY, Stamnes MA, Zuker CS. 1991. The cyclophilin homolog NinaA is required in the secretory pathway. Cell 67: 255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.Y.2    Stamnes, M.A.3    Zuker, C.S.4
  • 35
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • The C. elegans Genome Consortium
    • The C. elegans Genome Consortium. 1998. Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282: 2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 36
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. 1999. The mitochondrial permeability transition pore and its role in cell death. Biochem J 314: 233-249.
    • (1999) Biochem. J. , vol.314 , pp. 233-249
    • Crompton, M.1
  • 37
    • 0032568328 scopus 로고    scopus 로고
    • The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42
    • Dahl R, Wani B, Hayman MJ. 1998. The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42. Oncogene 16: 1579-1586.
    • (1998) Oncogene , vol.16 , pp. 1579-1586
    • Dahl, R.1    Wani, B.2    Hayman, M.J.3
  • 38
    • 13544267438 scopus 로고    scopus 로고
    • Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506
    • Davies TH, Ning YM, Sanchez ER. 2005. Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506. Biochemistry 44: 2030-2038.
    • (2005) Biochemistry , vol.44 , pp. 2030-2038
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 39
    • 0024339276 scopus 로고
    • Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix
    • Davis J, Boswell B, Bachinger H. 1989. Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix. J Biol Chem 264: 8956-8962.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8956-8962
    • Davis, J.1    Boswell, B.2    Bachinger, H.3
  • 40
    • 0035884167 scopus 로고    scopus 로고
    • Parameters affecting in vitro oxidation/folding or maurotoxin, a four-disulphide-bridged scorpion toxin
    • Di Luccio E, Azulay D-O, Regaya I et al. 2001. Parameters affecting in vitro oxidation/folding or maurotoxin, a four-disulphide-bridged scorpion toxin. Biochem J 358: 681-692.
    • (2001) Biochem. J. , vol.358 , pp. 681-692
    • Di Luccio, E.1    Azulay, D.-O.2    Regaya, I.3
  • 41
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski K, Muir S, Cardenas M, Heitman J. 1997. All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 94: 13093-13098.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 42
    • 0033166336 scopus 로고    scopus 로고
    • Evidence that cyclophilin-A protects cells against oxidative stress
    • Doyle V, Virji S, Crompton M. 1999. Evidence that cyclophilin-A protects cells against oxidative stress. Biochem J 341: 127-132.
    • (1999) Biochem. J. , vol.341 , pp. 127-132
    • Doyle, V.1    Virji, S.2    Crompton, M.3
  • 43
    • 2542463867 scopus 로고    scopus 로고
    • The human nuclear SR-cyp is a cell cycle-regulated cyclophilin
    • Dubourg B, Kamphausen T, Weiwad M et al. 2004. The human nuclear SR-cyp is a cell cycle-regulated cyclophilin. J Biol Chem 279: 22322-22330.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22322-22330
    • Dubourg, B.1    Kamphausen, T.2    Weiwad, M.3
  • 44
    • 0032563195 scopus 로고    scopus 로고
    • Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response
    • Duina AA, Kalton HM, Gaber RF. 1998. Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273: 18974-18978.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18974-18978
    • Duina, A.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 45
    • 20444404651 scopus 로고    scopus 로고
    • Synthetic lethality of retinoblastoma mutant cells in the Drosophila eye by mutation of a novel peptidyl-prolyl isomerase gene
    • Edgar KA, Belvin M, Parks AL et al. 2005. Synthetic lethality of retinoblastoma mutant cells in the Drosophila eye by mutation of a novel peptidyl-prolyl isomerase gene. Genetics: 170: 161-171.
    • (2005) Genetics , vol.170 , pp. 161-171
    • Edgar, K.A.1    Belvin, M.2    Parks, A.L.3
  • 46
    • 0028175752 scopus 로고
    • Cyclophilin residues that affect non-competitive inhibition of the protein serine phosphatase activity of calcineurin by the cyclophilin-cyclosporin A complex
    • Etzkorn F, Chang Z, Stolz L, Walsh C. 1994. Cyclophilin residues that affect non-competitive inhibition of the protein serine phosphatase activity of calcineurin by the cyclophilin-cyclosporin A complex. Biochemistry 33: 2380-2388.
    • (1994) Biochemistry , vol.33 , pp. 2380-2388
    • Etzkorn, F.1    Chang, Z.2    Stolz, L.3    Walsh, C.4
  • 47
    • 0142011068 scopus 로고    scopus 로고
    • A novel binding protein for a member of CyP40-type cyclophilins: Neurospora crassa CyPBP37, a growth and thiamine regulated protein homolog to yeast Thi4p
    • Faou P, Tropschug M. 2003. A novel binding protein for a member of CyP40-type cyclophilins: Neurospora crassa CyPBP37, a growth and thiamine regulated protein homolog to yeast Thi4p. J Mol Biol 333: 831-844.
    • (2003) J. Mol. Biol. , vol.333 , pp. 831-844
    • Faou, P.1    Tropschug, M.2
  • 48
    • 0021668676 scopus 로고
    • Determination of enzyme catalysis for cis-trans-isomerization of peptide-bonds using proline-containing peptides as substrates
    • Fischer G, Bang H, Mech C. 1984. Determination of enzyme catalysis for cis-trans-isomerization of peptide-bonds using proline-containing peptides as substrates. Biomed Biochim Acta 43: 1101-1111.
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 49
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans-isomerase are probably identical proteins
    • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. 1989. Cyclophilin and peptidyl-prolyl cis-trans-isomerase are probably identical proteins. Nature 337: 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
  • 51
    • 0036797844 scopus 로고    scopus 로고
    • Good fungi gone bad: The corruption of calcineurin
    • Fox DS, Heitman J. 2002. Good fungi gone bad: the corruption of calcineurin. BioEssays 24: 894-903.
    • (2002) BioEssays , vol.24 , pp. 894-903
    • Fox, D.S.1    Heitman, J.2
  • 52
    • 0028013517 scopus 로고
    • Calcineurin acts in synergy with I kappa B/MAD3, an inhibitor of NF-kappa B
    • Frantz B, Nordby EC, Bren G et al. 1994. Calcineurin acts in synergy with I kappa B/MAD3, an inhibitor of NF-kappa B. EMBO J 13: 861-870.
    • (1994) EMBO J. , vol.13 , pp. 861-870
    • Frantz, B.1    Nordby, E.C.2    Bren, G.3
  • 53
    • 0035941108 scopus 로고    scopus 로고
    • Crosstalk of prolyl isomerases, Pin1/ESS1, and cyclophilin A
    • Fujimori F, Gunji W, Kikuchi J et al. 2001. Crosstalk of prolyl isomerases, Pin1/ESS1, and cyclophilin A. Biochem Biophys Res Commun 289: 181-190.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 181-190
    • Fujimori, F.1    Gunji, W.2    Kikuchi, J.3
  • 54
    • 0027363385 scopus 로고
    • Peptidyl proline cis-trans-isomerases: Immunophilins
    • Galat A. 1993. Peptidyl proline cis-trans-isomerases: immunophilins. Eur J Biochem 216: 689-707.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 689-707
    • Galat, A.1
  • 55
    • 0033571184 scopus 로고    scopus 로고
    • Variations of sequences and amino acid compositions of proteins that sustain their biological functions: An analysis of the cyclophilin family of proteins
    • Galat A. 1999. Variations of sequences and amino acid compositions of proteins that sustain their biological functions: an analysis of the cyclophilin family of proteins. Arch Biochem Biophys 371: 149-162.
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 149-162
    • Galat, A.1
  • 56
    • 4043129511 scopus 로고    scopus 로고
    • Function-dependent clustering of orthologues and paralogues of cyclophilins
    • Galat A. 2004. Function-dependent clustering of orthologues and paralogues of cyclophilins. Proteins 56: 808-820.
    • (2004) Proteins , vol.56 , pp. 808-820
    • Galat, A.1
  • 58
    • 0029147007 scopus 로고
    • Specific interaction between cyclophilin and cyclic peptides
    • Gallo P, Saviano M, Rossi F et al. 1995. Specific interaction between cyclophilin and cyclic peptides. Biopolymers 36: 273-281.
    • (1995) Biopolymers , vol.36 , pp. 273-281
    • Gallo, P.1    Saviano, M.2    Rossi, F.3
  • 59
    • 0030045688 scopus 로고    scopus 로고
    • Effects of cyclolinopeptide A on T lymphocyte activation and peptidyl prolyl isomerase activity
    • Gaymes TJ, Carrett NJ, Patel N, Kay JE, Siemion IZ. 1996. Effects of cyclolinopeptide A on T lymphocyte activation and peptidyl prolyl isomerase activity. Biochem Soc Trans 24: 90S.
    • (1996) Biochem. Soc. Trans. , vol.24
    • Gaymes, T.J.1    Carrett, N.J.2    Patel, N.3    Kay, J.E.4    Siemion, I.Z.5
  • 60
    • 0030775874 scopus 로고    scopus 로고
    • Cyclolinopeptide A (CLA) mediates its immunosuppressive activity through cyclophilin-dependent calcineurin inactivation
    • Gaymes TJ, Cebrat M, Siemion IZ, Kay JE. 1997. Cyclolinopeptide A (CLA) mediates its immunosuppressive activity through cyclophilin-dependent calcineurin inactivation. FEBS Lett 418: 224-227.
    • (1997) FEBS Lett. , vol.418 , pp. 224-227
    • Gaymes, T.J.1    Cebrat, M.2    Siemion, I.Z.3    Kay, J.E.4
  • 63
    • 0035003608 scopus 로고    scopus 로고
    • Hsp90 chaparone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1
    • Goes FS, Martin J. 2001. Hsp90 chaparone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1. Eur J Biochem 268: 2281-2289.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2281-2289
    • Goes, F.S.1    Martin, J.2
  • 65
    • 0029876890 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerase of Bacillus subtilis: Residues involved in cyclosporin A affinity and catalytic efficiency
    • Gothel SF, Herrler M, Marahiel MA. 1996. Peptidyl-prolyl cis-trans isomerase of Bacillus subtilis: residues involved in cyclosporin A affinity and catalytic efficiency. Biochemistry 35: 3636-3640.
    • (1996) Biochemistry , vol.35 , pp. 3636-3640
    • Gothel, S.F.1    Herrler, M.2    Marahiel, M.A.3
  • 68
    • 0026012156 scopus 로고
    • FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae
    • Heitman J, Movva N, Hiestand P, Hall M. 1991. FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 88: 1948-1952.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1948-1952
    • Heitman, J.1    Movva, N.2    Hiestand, P.3    Hall, M.4
  • 69
    • 0027715374 scopus 로고
    • Proline isomerases in microorganisms small eukaryotes
    • Hemenway C, Heitman J. 1993. Proline isomerases in microorganisms and small eukaryotes. Ann NY Acad Sci 696: 38-46.
    • (1993) Ann. NY Acad. Sci. , vol.696 , pp. 38-46
    • Hemenway, C.1    Heitman, J.2
  • 70
    • 0029557842 scopus 로고
    • Protein import into the nucleus: An integrated view
    • Hicks GR, Raikhel NV. 1995. Protein import into the nucleus: an integrated view. Ann Rev Cell Dev Biol 11: 155-188.
    • (1995) Ann. Rev. Cell Dev. Biol. , vol.11 , pp. 155-188
    • Hicks, G.R.1    Raikhel, N.V.2
  • 72
    • 0028922905 scopus 로고
    • Expression of human cyclophilin-40 and the effect of the His141 → Trp mutation on catalysis and cyclosporin A binding
    • Hoffmann K, Kakalis LT, Anderson KS, Armitage IM, Handschumacher RE. 1995. Expression of human cyclophilin-40 and the effect of the His141 → Trp mutation on catalysis and cyclosporin A binding. Eur J Biochem 229: 188-193.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 188-193
    • Hoffmann, K.1    Kakalis, L.T.2    Anderson, K.S.3    Armitage, I.M.4    Handschumacher, R.E.5
  • 73
    • 0036740693 scopus 로고    scopus 로고
    • The chaparone activity of protein disulfite isomerase is affected by cyclophilin B and cyclosporin A in vitro
    • Horibe T, Yosho C, Okada S et al. 2002. The chaparone activity of protein disulfite isomerase is affected by cyclophilin B and cyclosporin A in vitro. J Biochem (Tokyo) 132: 401-407.
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 401-407
    • Horibe, T.1    Yosho, C.2    Okada, S.3
  • 74
    • 0031440025 scopus 로고    scopus 로고
    • A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs
    • Horowitz DS, Kobayashi R, Krainer AR. 1997. A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. RNA 3: 1374-1387.
    • (1997) RNA , vol.3 , pp. 1374-1387
    • Horowitz, D.S.1    Kobayashi, R.2    Krainer, A.R.3
  • 75
    • 0031027009 scopus 로고    scopus 로고
    • A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor
    • Horowitz DS, Krainer AR. 1997. A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor. Genes Dev 11: 139-151.
    • (1997) Genes Dev. , vol.11 , pp. 139-151
    • Horowitz, D.S.1    Krainer, A.R.2
  • 77
    • 0030332781 scopus 로고    scopus 로고
    • A probabilistic classification system for predicting the cellular localization sites of proteins
    • Horton P, Nakai K. 1996. A probabilistic classification system for predicting the cellular localization sites of proteins. Proc Int Conf Intell Syst Mol Biol 4: 109-115.
    • (1996) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.4 , pp. 109-115
    • Horton, P.1    Nakai, K.2
  • 78
    • 0030624540 scopus 로고    scopus 로고
    • Better prediction of protein cellular localization sites with the k nearest neighbors classifier
    • Horton P, Nakai K. 1997. Better prediction of protein cellular localization sites with the k nearest neighbors classifier. Proc Int Conf Intell Syst Mol Biol 5: 147-152.
    • (1997) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.5 , pp. 147-152
    • Horton, P.1    Nakai, K.2
  • 79
    • 0037020272 scopus 로고    scopus 로고
    • Phosphorylation dependent interaction of the asialoglycoprotein receptor with molecular chaperones
    • Huang T, Deng H, Wolkoff AW, Stockert RJ. 2002. Phosphorylation dependent interaction of the asialoglycoprotein receptor with molecular chaperones. J Biol Chem 227: 37798-37803.
    • (2002) J. Biol. Chem. , vol.227 , pp. 37798-37803
    • Huang, T.1    Deng, H.2    Wolkoff, A.W.3    Stockert, R.J.4
  • 80
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • Huh WK, Falvo JV, Gerke LC et al. 2003. Global analysis of protein localization in budding yeast. Nature 425: 686-691.
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1    Falvo, J.V.2    Gerke, L.C.3
  • 81
    • 0037178118 scopus 로고    scopus 로고
    • The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin
    • Hur S, Bruice TC. 2002. The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin. J Am Chem Soc 124: 7303-7313.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7303-7313
    • Hur, S.1    Bruice, T.C.2
  • 82
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiativ
    • The Arabidopsis Genome Initiativ. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408: 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 83
    • 0033736147 scopus 로고    scopus 로고
    • Immunophillins: Switched on protein binding domains
    • Ivery M. 2000. Immunophillins: switched on protein binding domains. Med Res Rev 20: 452-484.
    • (2000) Med. Res. Rev. , vol.20 , pp. 452-484
    • Ivery, M.1
  • 84
    • 0034721931 scopus 로고    scopus 로고
    • Cyclophilin A is a secreted growth factor induced by oxidative stress
    • Jin Z-G, Melaragno MG, Liao D-F et al. 2000. Cyclophilin A is a secreted growth factor induced by oxidative stress. Circ Res 87: 789-796.
    • (2000) Circ. Res. , vol.87 , pp. 789-796
    • Jin, Z.-G.1    Melaragno, M.G.2    Liao, D.-F.3
  • 85
    • 20444479819 scopus 로고    scopus 로고
    • Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6 A resolution
    • Kallen J, Sedrani R, Zenke G, Wagner J. 2005. Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6 A resolution. J Biol Chem 280: 21965-21971.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21965-21971
    • Kallen, J.1    Sedrani, R.2    Zenke, G.3    Wagner, J.4
  • 86
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen J, Spitzfaden C, Zurini MG et al. 1991. Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353: 276-279.
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.3
  • 87
    • 0026042453 scopus 로고
    • Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution
    • Ke H, Zydowsky L, Liu J, Walsh C. 1991. Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution. Proc Natl Acad Sci USA 88: 9483-9487.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9483-9487
    • Ke, H.1    Zydowsky, L.2    Liu, J.3    Walsh, C.4
  • 88
    • 0028928739 scopus 로고
    • A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin
    • Kern G, Kern D, Schmid FX, Fischer G. 1995. A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin. J Biol Chem 270: 740-745.
    • (1995) J. Biol. Chem. , vol.270 , pp. 740-745
    • Kern, G.1    Kern, D.2    Schmid, F.X.3    Fischer, G.4
  • 89
    • 0029085091 scopus 로고
    • Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation
    • Klappa P, Freedman RB, Zimmermann R. 1995. Protein disulphide isomerase and a lumenal cyclophilin-type peptidyl prolyl cis-trans isomerase are in transient contact with secretory proteins during late stages of translocation. Eur J Biochem 232: 755-764.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 755-764
    • Klappa, P.1    Freedman, R.B.2    Zimmermann, R.3
  • 90
    • 0026092585 scopus 로고
    • Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein
    • Koltin Y, Faucette L, Bergsma DJ et al. 1991. Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein. Mol Cell Biol 11: 1718-1723.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 1718-1723
    • Koltin, Y.1    Faucette, L.2    Bergsma, D.J.3
  • 91
    • 0030825790 scopus 로고    scopus 로고
    • Residues in the WD repeats of Tup1 required for interaction with alpha2
    • Komachi K, Johnson A. 1997. Residues in the WD repeats of Tup1 required for interaction with alpha2. Mol Cell Biol 17: 6023-6028.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6023-6028
    • Komachi, K.1    Johnson, A.2
  • 92
    • 0035723860 scopus 로고    scopus 로고
    • KIN241: A gene involved in cell morphogenesis in Paramecium tetraurelia reveals a novel protein family of cyclophilin-RNA interacting proteins (CRIPs) conserved from fission yeast to man
    • Krzywicka A, Beisson J, Keller A-M et al. 2001. KIN241: a gene involved in cell morphogenesis in Paramecium tetraurelia reveals a novel protein family of cyclophilin-RNA interacting proteins (CRIPs) conserved from fission yeast to man. Mol Microbiol 42: 257-267.
    • (2001) Mol. Microbiol. , vol.42 , pp. 257-267
    • Krzywicka, A.1    Beisson, J.2    Keller, A.-M.3
  • 93
    • 0028675509 scopus 로고
    • Molecular taxonomy of the yeasts
    • Kurtzman CP. 1994. Molecular taxonomy of the yeasts. Yeast 10: 1727-1740.
    • (1994) Yeast , vol.10 , pp. 1727-1740
    • Kurtzman, C.P.1
  • 94
    • 0032747257 scopus 로고    scopus 로고
    • Intracellular distribution of a cytoplasmic progesterone receptor mutant and of immunophilins cyclophilin 40 and FKBP59: Effects of cyclosporine A, of various metabolic inhibitors and of several culture conditions
    • Lebeau M, Jung-Testas I, Baulieu E. 1999. Intracellular distribution of a cytoplasmic progesterone receptor mutant and of immunophilins cyclophilin 40 and FKBP59: effects of cyclosporine A, of various metabolic inhibitors and of several culture conditions. J Steroid Biochem Mol Biol 70: 219-228.
    • (1999) J. Steroid Biochem. Mol. Biol. , vol.70 , pp. 219-228
    • Lebeau, M.1    Jung-Testas, I.2    Baulieu, E.3
  • 95
    • 0035839494 scopus 로고    scopus 로고
    • Cyclophilin A binds to peroxiredoxins and activates their peroxidase activity
    • Lee S-P, Hwang Y-S, Kim Y-J et al. 2001. Cyclophilin A binds to peroxiredoxins and activates their peroxidase activity. J Biol Chem 276: 29826-29832.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29826-29832
    • Lee, S.-P.1    Hwang, Y.-S.2    Kim, Y.-J.3
  • 96
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • Lin D-T, Lechleiter JD. 2002. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J Biol Chem 277: 31134-31141.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31134-31141
    • Lin, D.-T.1    Lechleiter, J.D.2
  • 97
    • 0025755354 scopus 로고
    • Human and Escherichia coli cyclophilins: Sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue
    • Liu J, Chen CM, Walsh CT. 1991. Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry 30: 2306-2310.
    • (1991) Biochemistry , vol.30 , pp. 2306-2310
    • Liu, J.1    Chen, C.M.2    Walsh, C.T.3
  • 98
    • 0036087630 scopus 로고    scopus 로고
    • CDD: A database of conserved domain alignments with links to domain three-dimensional structure
    • Marchler-Bauer A, Panchenko AR, Shoemaker BA et al. 2002. CDD: a database of conserved domain alignments with links to domain three-dimensional structure. Nucleic Acids Res 30: 281-283.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 281-283
    • Marchler-Bauer, A.1    Panchenko, A.R.2    Shoemaker, B.A.3
  • 99
    • 0035072679 scopus 로고    scopus 로고
    • Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock
    • Mark PJ, Ward BK, Kumar P et al. 2001. Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock. Cell Stress Chap 6: 59-70.
    • (2001) Cell Stress Chap. , vol.6 , pp. 59-70
    • Mark, P.J.1    Ward, B.K.2    Kumar, P.3
  • 100
    • 0036470051 scopus 로고    scopus 로고
    • Protein Explorer: Easy yet powerful macromolecular visualization
    • Martz E. 2002. Protein Explorer: easy yet powerful macromolecular visualization. Trends Biochem Sci 27: 107-109.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 107-109
    • Martz, E.1
  • 101
    • 0036729529 scopus 로고    scopus 로고
    • The transcriptional program of meiosis and sporulation in fission yeast
    • Mata J, Lyne R, Burns G, Bahler J. 2002. The transcriptional program of meiosis and sporulation in fission yeast. Nat Genet 32: 143-147.
    • (2002) Nat. Genet. , vol.32 , pp. 143-147
    • Mata, J.1    Lyne, R.2    Burns, G.3    Bahler, J.4
  • 102
    • 0034602390 scopus 로고    scopus 로고
    • Cpr6 and Cpr7, two closely related HSP90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties
    • Mayr C, Richter K, Lilie H, Bucher J. 2000. Cpr6 and Cpr7, two closely related HSP90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J Biol Chem 275: 34140-34146.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34140-34146
    • Mayr, C.1    Richter, K.2    Lilie, H.3    Bucher, J.4
  • 103
    • 0032771330 scopus 로고    scopus 로고
    • Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing
    • McDonald WH, Ohi R, Smelkova N, Frendewey D, Gould KL. 1999. Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing. Mol Cell Biol 19: 5352-5362.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5352-5362
    • McDonald, W.H.1    Ohi, R.2    Smelkova, N.3    Frendewey, D.4    Gould, K.L.5
  • 104
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood Y-K, Chung KT, Hendershot LM. 2002. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.-K.2    Chung, K.T.3    Hendershot, L.M.4
  • 105
    • 0028242351 scopus 로고
    • A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin
    • Montague JW, Gaido ML, Frye C, Cidlowski JA. 1994. A calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin. J Biol Chem 269: 18877-18880.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18877-18880
    • Montague, J.W.1    Gaido, M.L.2    Frye, C.3    Cidlowski, J.A.4
  • 106
    • 0030972976 scopus 로고    scopus 로고
    • Native recombinant cyclophilins A, B and C degrade DNA independently of peptidyl-prolyl cis/trans-isomerase activity
    • Montague JW, Hughes FM Jr, Cidlowski JA. 1997. Native recombinant cyclophilins A, B and C degrade DNA independently of peptidyl-prolyl cis/trans-isomerase activity. J Biol Chem 272: 6677-6684.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6677-6684
    • Montague, J.W.1    Hughes Jr., F.M.2    Cidlowski, J.A.3
  • 107
    • 0032478732 scopus 로고    scopus 로고
    • Matrin CYP, an SR-rich cyclophilin that associates with the nuclear matrix and splicing factors
    • Mortillaro MJ, Berezney R. 1998. Matrin CYP, an SR-rich cyclophilin that associates with the nuclear matrix and splicing factors. J Biol Chem 273: 8183-8192.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8183-8192
    • Mortillaro, M.J.1    Berezney, R.2
  • 108
    • 0034667981 scopus 로고    scopus 로고
    • Possible involvement of cyclophilin B and caspase-activated deoxyribonuclease in the induction of chromosomal DNA degradation in TCR-stimulated thymocytes
    • Nagata T, Kishi H, Lui Q et al. 2000. Possible involvement of cyclophilin B and caspase-activated deoxyribonuclease in the induction of chromosomal DNA degradation in TCR-stimulated thymocytes. J Immunol 165: 4281-4289.
    • (2000) J. Immunol. , vol.165 , pp. 4281-4289
    • Nagata, T.1    Kishi, H.2    Lui, Q.3
  • 109
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T et al. 2005. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434: 652.
    • (2005) Nature , vol.434 , pp. 652
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3
  • 110
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. 1994. The ancient regulatory-protein family of WD-repeat proteins. Nature 371: 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 111
    • 2542417703 scopus 로고    scopus 로고
    • RS cyclophilins: Identification of an NK-TR1-related cyclophilin
    • Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK. 1996. RS cyclophilins: identification of an NK-TR1-related cyclophilin. Gene 180: 151-155.
    • (1996) Gene , vol.180 , pp. 151-155
    • Nestel, F.P.1    Colwill, K.2    Harper, S.3    Pawson, T.4    Anderson, S.K.5
  • 112
    • 22244476202 scopus 로고    scopus 로고
    • Role of cyclophilin B in activation of interferon regulatory factor-3
    • Obata Y, Yamamoto K, Miyazaki M et al. 2005. Role of cyclophilin B in activation of interferon regulatory factor-3. J Biol Chem 280: 18355-18360.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18355-18360
    • Obata, Y.1    Yamamoto, K.2    Miyazaki, M.3
  • 113
    • 0036118353 scopus 로고    scopus 로고
    • Proteomics analysis reveals sTable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs
    • Ohi MD, Link AJ, Ren L et al. 2002. Proteomics analysis reveals sTable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. Mol Cell Biol 22: 2011-2024.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2011-2024
    • Ohi, M.D.1    Link, A.J.2    Ren, L.3
  • 114
    • 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 AP, Winter AD. 1998. 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: 215-217.
    • (1998) Mol. Biochem. Parasitol. , vol.95 , pp. 215-217
    • Page, A.P.1    Winter, A.D.2
  • 115
    • 25844449075 scopus 로고    scopus 로고
    • The Identification, Cloning and Characterization of the Cyclophilin Repertoire of the Fission Yeast Schizosaccharomyces pombe
    • Doctoral Thesis, University of Sussex, Brighton, UK
    • Pemberton TJ. 2004. The Identification, Cloning and Characterization of the Cyclophilin Repertoire of the Fission Yeast Schizosaccharomyces pombe. Doctoral Thesis, University of Sussex, Brighton, UK.
    • (2004)
    • Pemberton, T.J.1
  • 116
    • 0345303672 scopus 로고    scopus 로고
    • Cyclophilin sensitivity to sanglifehrin A can be correlated to the same specific tryptophan residue as cyclosporin A
    • Pemberton TJ, Kay JE. 2003. Cyclophilin sensitivity to sanglifehrin A can be correlated to the same specific tryptophan residue as cyclosporin A. FEBS Lett 555: 335-340.
    • (2003) FEBS Lett. , vol.555 , pp. 335-340
    • Pemberton, T.J.1    Kay, J.E.2
  • 117
    • 24944532876 scopus 로고    scopus 로고
    • Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe
    • (in press)
    • Pemberton TJ, Kay JE. 2005. Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe. Comp Funct Genom (in press).
    • (2005) Comp. Funct. Genom.
    • Pemberton, T.J.1    Kay, J.E.2
  • 118
    • 0345668478 scopus 로고    scopus 로고
    • Cloning and characterization of Schizosaccharomyces pombe cyclophilin 3: A cyclosporin A-insensitive orthologue of human USA-CyP
    • Pemberton TJ, Rulten SL, Kay JE. 2003. Cloning and characterization of Schizosaccharomyces pombe cyclophilin 3: a cyclosporin A-insensitive orthologue of human USA-CyP. J Chrom B 786: 81-91.
    • (2003) J. Chrom. B , vol.786 , pp. 81-91
    • Pemberton, T.J.1    Rulten, S.L.2    Kay, J.E.3
  • 119
    • 0035890135 scopus 로고    scopus 로고
    • The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program
    • Pijnappel WWMP, Schaft D, Roguev A et al. 2001. The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program. Genes Dev 15: 2991-3004.
    • (2001) Genes Dev. , vol.15 , pp. 2991-3004
    • Pijnappel, W.W.M.P.1    Schaft, D.2    Roguev, A.3
  • 120
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • Pirkl F, Buchner J. 2001. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J Mol Biol 308: 795-806.
    • (2001) J. Mol. Biol. , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 121
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophillin chaperones
    • Pratt WB, Toft DO. 1997. Steroid receptor interactions with heat shock protein and immunophillin chaperones. Endocr Rev 18: 306-360.
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 122
    • 0028227015 scopus 로고
    • Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A
    • Price ER, Jin MJ, Lim D et al. 1994. Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A. Proc Natl Acad Sci USA 91: 3931-3935.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3931-3935
    • Price, E.R.1    Jin, M.J.2    Lim, D.3
  • 123
    • 0026013566 scopus 로고
    • Human cyclophilin B: A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • Price ER, Zydowsky LD, Jin MJ et al. 1991. Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc Natl Acad Sci USA 88: 1903-1907.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1903-1907
    • Price, E.R.1    Zydowsky, L.D.2    Jin, M.J.3
  • 124
    • 0035375052 scopus 로고    scopus 로고
    • Interaction of the ring-finger related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes
    • Pringa E, Martinez-Noel G, Muller U, Harbers K. 2001. Interaction of the ring-finger related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. J Biol Chem 276: 19617-19623.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19617-19623
    • Pringa, E.1    Martinez-Noel, G.2    Muller, U.3    Harbers, K.4
  • 125
    • 0033081968 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
    • Prodromou C, Siligardi G, O'Brien R et al. 1999. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18: 754-762.
    • (1999) EMBO J. , vol.18 , pp. 754-762
    • Prodromou, C.1    Siligardi, G.2    O'Brien, R.3
  • 126
    • 0035932951 scopus 로고    scopus 로고
    • CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A
    • Pushkarsky T, Zybarth G, Dubrovsky L et al. 2001. CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A. Proc Natl Acad Sci USA 98: 6360-6365.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6360-6365
    • Pushkarsky, T.1    Zybarth, G.2    Dubrovsky, L.3
  • 127
    • 23044470285 scopus 로고    scopus 로고
    • Cell surface expression of CD147/emmprin is regulated by cyclophilin 60
    • Pushkarsky T, Yurchenko V, Vanpouille C et al. 2005. Cell surface expression of CD147/emmprin is regulated by cyclophilin 60. J Biol Chem 280: 27866-27871.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27866-27871
    • Pushkarsky, T.1    Yurchenko, V.2    Vanpouille, C.3
  • 128
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
    • Ratajczak T, Carrello A, Mark P et al. 1993. The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59). J Biol Chem 268: 13187-13192.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.3
  • 129
    • 0035019855 scopus 로고    scopus 로고
    • A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding
    • Reader JS, Van Nuland NAJ, Thompson GS et al. 2001. A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding. Protein Sci 10: 1216-1224.
    • (2001) Protein Sci. , vol.10 , pp. 1216-1224
    • Reader, J.S.1    Van Nuland, N.A.J.2    Thompson, G.S.3
  • 130
    • 0034677984 scopus 로고    scopus 로고
    • Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin
    • Reidt U, Reuter K, Achsel T et al. 2000. Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. J Biol Chem 275: 7439-7442.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7439-7442
    • Reidt, U.1    Reuter, K.2    Achsel, T.3
  • 131
    • 0037823485 scopus 로고    scopus 로고
    • Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide
    • Reidt U, Wahl MC, Fasshauer D et al. 2003. Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol 331: 45-56.
    • (2003) J. Mol. Biol. , vol.331 , pp. 45-56
    • Reidt, U.1    Wahl, M.C.2    Fasshauer, D.3
  • 132
  • 133
    • 3543042493 scopus 로고    scopus 로고
    • Periodic gene expression program of the fission yeast cell cycle
    • Rustici G, Mata J, Kivinen K et al. 2004. Periodic gene expression program of the fission yeast cell cycle. Nat Genet 36: 809-817.
    • (2004) Nat. Genet. , vol.36 , pp. 809-817
    • Rustici, G.1    Mata, J.2    Kivinen, K.3
  • 134
    • 0033669609 scopus 로고    scopus 로고
    • Role of cyclophilins in somatolactogenic action
    • Rycyzyn MA, Clevenger CV. 2000. Role of cyclophilins in somatolactogenic action. Ann NY Acad Sci 917: 514-521.
    • (2000) Ann. NY Acad. Sci. , vol.917 , pp. 514-521
    • Rycyzyn, M.A.1    Clevenger, C.V.2
  • 135
    • 0037076393 scopus 로고    scopus 로고
    • The intracellular prolactin/cyclophilin B complex as a transcriptional inducer
    • Rycyzyn MA, Clevenger CV. 2002. The intracellular prolactin/cyclophilin B complex as a transcriptional inducer. Proc Natl Acad Sci USA 99: 6790-6795.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6790-6795
    • Rycyzyn, M.A.1    Clevenger, C.V.2
  • 136
    • 2542509071 scopus 로고    scopus 로고
    • Immunophilins, heat shock proteins, and glucocorticoid receptor actions in vivo
    • Sanchez E, Ning Y-M. 1996. Immunophilins, heat shock proteins, and glucocorticoid receptor actions in vivo. Comp Methods Enzymol 9: 188-200.
    • (1996) Comp. Methods Enzymol. , vol.9 , pp. 188-200
    • Sanchez, E.1    Ning, Y.-M.2
  • 137
  • 138
    • 0035917897 scopus 로고    scopus 로고
    • Receptor accessory folding helper enzymes: The functional role of peptidyl prolyl cis/trans isomerases
    • Schiene-Fischer C, Yu C. 2001. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Lett 495: 1-6.
    • (2001) FEBS Lett. , vol.495 , pp. 1-6
    • Schiene-Fischer, C.1    Yu, C.2
  • 139
    • 0024707288 scopus 로고
    • Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein)
    • Schneuwly S, Shortridge RD, Larrivee DC et al. 1989. Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein). Proc Natl Acad Sci USA 86: 5390-5394.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5390-5394
    • Schneuwly, S.1    Shortridge, R.D.2    Larrivee, D.C.3
  • 140
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporine A and FK506
    • Schreiber SL, Crabtree GR. 1992. The mechanism of action of cyclosporine A and FK506. Immunol Today 13: 136-142.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 141
    • 0030766182 scopus 로고    scopus 로고
    • TWo modes of activation of the permeability transition pore: The role of mitochondrial cyclophilin
    • Scorrano L, Nicolli A, Basso E, Petronilli V, Bernardi P. 1997. TWo modes of activation of the permeability transition pore: the role of mitochondrial cyclophilin. Mol Cell Biochem 174: 181-184.
    • (1997) Mol. Cell Biochem. , vol.174 , pp. 181-184
    • Scorrano, L.1    Nicolli, A.2    Basso, E.3    Petronilli, V.4    Bernardi, P.5
  • 142
    • 0037414302 scopus 로고    scopus 로고
    • Sanglifehrin-cyclophilin interaction: Degradation work, synthetic macrocyclic analogues, X-ray crystal structure, and binding data
    • Sedrani R, Kallen J, Cabrejas LMM et al. 2003. Sanglifehrin-cyclophilin interaction: degradation work, synthetic macrocyclic analogues, X-ray crystal structure, and binding data. J Am Chem Soc 125: 3849-3859.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3849-3859
    • Sedrani, R.1    Kallen, J.2    Cabrejas, L.M.M.3
  • 143
    • 0024959573 scopus 로고
    • The NinaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein
    • Shieh BH, Stamnes MA, Seavello S et al. 1989. The NinaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein. Nature 338: 67-70.
    • (1989) Nature , vol.338 , pp. 67-70
    • Shieh, B.H.1    Stamnes, M.A.2    Seavello, S.3
  • 144
    • 0035980253 scopus 로고    scopus 로고
    • Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe
    • Skruzny M, Ambrozkova M, Fukova K et al. 2001. Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe. Biochim Biophys Acta 1521: 146-151.
    • (2001) Biochim. Biophys. Acta , vol.1521 , pp. 146-151
    • Skruzny, M.1    Ambrozkova, M.2    Fukova, K.3
  • 145
    • 0025907054 scopus 로고
    • The cyclophilin homolog NinaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
    • Stamnes MA, Shieh BH, Chuman L, Harris GL, Zuker CS. 1991. The cyclophilin homolog NinaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins. Cell 65: 219-227.
    • (1991) Cell , vol.65 , pp. 219-227
    • Stamnes, M.A.1    Shieh, B.H.2    Chuman, L.3    Harris, G.L.4    Zuker, C.S.5
  • 146
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase
    • Steinmann B, Bruckner P, Superti-Furga A. 1991. Cyclosporin A slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase. J Biol Chem 266: 1299-1303.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 147
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G, Rucknagel K, Nierhaus K et al. 1995. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948.
    • (1995) EMBO J. , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rucknagel, K.2    Nierhaus, K.3
  • 148
    • 0029962123 scopus 로고    scopus 로고
    • An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity
    • Stoller G, Tradler T, Rucknagel KP, Rahfeld J-U, Fischer G. 1996. An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis /trans isomerase activity. FEBS Lett 384: 117-122.
    • (1996) FEBS Lett. , vol.384 , pp. 117-122
    • Stoller, G.1    Tradler, T.2    Rucknagel, K.P.3    Rahfeld, J.-U.4    Fischer, G.5
  • 149
    • 0032736595 scopus 로고    scopus 로고
    • Cyclosporin A attenuates acute mitochondrial dysfunction following traumatic brain injury
    • Sullivan PG, Thompson MB, Scheff SW. 1999. Cyclosporin A attenuates acute mitochondrial dysfunction following traumatic brain injury. Exp Neurol 160: 226-234.
    • (1999) Exp. Neurol. , vol.160 , pp. 226-234
    • Sullivan, P.G.1    Thompson, M.B.2    Scheff, S.W.3
  • 151
    • 0037087504 scopus 로고    scopus 로고
    • Cell-cycle-dependent localization of U1p1, a Schizosaccharomyces pombe Pmt3 (SUMO)-specific protease
    • Taylor DL, Ho JCY, Oliver A, Watts FZ. 2002. Cell-cycle-dependent localization of U1p1, a Schizosaccharomyces pombe Pmt3 (SUMO)-specific protease. J Cell Sci 115: 1113-1122.
    • (2002) J. Cell Sci. , vol.115 , pp. 1113-1122
    • Taylor, D.L.1    Ho, J.C.Y.2    Oliver, A.3    Watts, F.Z.4
  • 152
    • 0034980394 scopus 로고    scopus 로고
    • TWo structures of cyclophilin 40: Folding and fidelity in the Tpr domains
    • Taylor P, Dornan J, Carrello A et al. 2001. TWo structures of cyclophilin 40: folding and fidelity in the Tpr domains. Struct Fold Des 9: 431-435.
    • (2001) Struct. Fold. Des. , vol.9 , pp. 431-435
    • Taylor, P.1    Dornan, J.2    Carrello, A.3
  • 153
    • 0031916381 scopus 로고    scopus 로고
    • The 20 kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins
    • Teigelkamp S, Achsel T, Mundt C et al. 1998. The 20 kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. RNA 4: 127-141.
    • (1998) RNA , vol.4 , pp. 127-141
    • Teigelkamp, S.1    Achsel, T.2    Mundt, C.3
  • 154
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. 1997. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 24: 4876-4882.
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 156
    • 0024844391 scopus 로고
    • Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae
    • Tropschug M, Barthelmess IB, Neupert W. 1989. Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae. Nature 342: 953-955.
    • (1989) Nature , vol.342 , pp. 953-955
    • Tropschug, M.1    Barthelmess, I.B.2    Neupert, W.3
  • 157
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter JC. 2001. The sequence of the human genome. Science 291: 1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 158
    • 0026716643 scopus 로고
    • Membrane protein structure prediction: Hydrophobicity analysis and the 'positive inside' rule
    • von Heijne G. 1992. Membrane protein structure prediction: hydrophobicity analysis and the 'positive inside' rule. J Mol Biol 225: 487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 159
    • 0036088518 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by the nonimmunosuppressive cyclosporin derviative NIM811
    • Waldmeier PC, Feldtrauer J-J, Qian T, Lemasters JJ. 2002. Inhibition of the mitochondrial permeability transition by the nonimmunosuppressive cyclosporin derviative NIM811. Mol Pharm 62: 22-29.
    • (2002) Mol. Pharm. , vol.62 , pp. 22-29
    • Waldmeier, P.C.1    Feldtrauer, J.-J.2    Qian, T.3    Lemasters, J.J.4
  • 160
    • 0026629246 scopus 로고
    • Cyclosporin A, the cyclophilin class of peptidylprolyl isomerases, and blockade of T cell signal transduction
    • Walsh CT, Zydowsky LD, McKeon FD. 1992. Cyclosporin A, the cyclophilin class of peptidylprolyl isomerases, and blockade of T cell signal transduction. J Biol Chem 267: 13115-13118.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13115-13118
    • Walsh, C.T.1    Zydowsky, L.D.2    McKeon, F.D.3
  • 161
    • 0030020702 scopus 로고    scopus 로고
    • Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c
    • Wang BB, Hayenga KJ, Payan DG, Fisher JM. 1996. Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c. Biochem J 314: 313-319.
    • (1996) Biochem. J. , vol.314 , pp. 313-319
    • Wang, B.B.1    Hayenga, K.J.2    Payan, D.G.3    Fisher, J.M.4
  • 162
    • 18644385343 scopus 로고    scopus 로고
    • A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90
    • Ward BK, Allan RK, Mok D et al. 2002. A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90. J Biol Chem 277: 40799-40809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40799-40809
    • Ward, B.K.1    Allan, R.K.2    Mok, D.3
  • 163
    • 0034744315 scopus 로고    scopus 로고
    • Allelic loss of cyclophilin 40, an estrogen receptor-associated immunophilin, in breast carcinomas
    • Ward BK, Kumar P, Turbett GR et al. 2001. Allelic loss of cyclophilin 40, an estrogen receptor-associated immunophilin, in breast carcinomas. J Cancer Res Clin Oncol 127: 109-115.
    • (2001) J. Cancer Res. Clin. Oncol. , vol.127 , pp. 109-115
    • Ward, B.K.1    Kumar, P.2    Turbett, G.R.3
  • 164
    • 0033490140 scopus 로고    scopus 로고
    • Expression of the estrogen receptor-associated immunophilins, cyclophilin 40 and FKBP52, in breast cancer
    • Ward BK, Mark PJ, Ingram DM, Minchin RF, Ratajczak T. 1999. Expression of the estrogen receptor-associated immunophilins, cyclophilin 40 and FKBP52, in breast cancer. Breast Cancer Res Treatm 58: 267-280.
    • (1999) Breast Cancer Res. Treatm. , vol.58 , pp. 267-280
    • Ward, B.K.1    Mark, P.J.2    Ingram, D.M.3    Minchin, R.F.4    Ratajczak, T.5
  • 165
    • 0030919428 scopus 로고    scopus 로고
    • Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation
    • Warth R, Briand PA, Picard D. 1997. Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Biol Chem 378: 381-391.
    • (1997) Biol. Chem. , vol.378 , pp. 381-391
    • Warth, R.1    Briand, P.A.2    Picard, D.3
  • 166
    • 0033015180 scopus 로고    scopus 로고
    • A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock
    • Weighardt F, Cobianchi F, Cartegni L et al. 1999. A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. J Cell Sci 112: 1465-1476.
    • (1999) J. Cell Sci. , vol.112 , pp. 1465-1476
    • Weighardt, F.1    Cobianchi, F.2    Cartegni, L.3
  • 167
    • 0030046813 scopus 로고    scopus 로고
    • A multicopy suppressor of a cell cycle defect in Sz. pombe encodes a heat shock inducible 40 kDa cyclophilin-like protein
    • Weisman R, Creanor J, Fantes P. 1996. A multicopy suppressor of a cell cycle defect in Sz. pombe encodes a heat shock inducible 40 kDa cyclophilin-like protein. EMBO J 15: 447-456.
    • (1996) EMBO J. , vol.15 , pp. 447-456
    • Weisman, R.1    Creanor, J.2    Fantes, P.3
  • 169
    • 0036304715 scopus 로고    scopus 로고
    • Website review: How to get the best from fission yeast genome data
    • Wood V, Bahler J. 2002. Website review: how to get the best from fission yeast genome data. Comp Funct Genom 3: 282-288.
    • (2002) Comp. Funct. Genom. , vol.3 , pp. 282-288
    • Wood, V.1    Bahler, J.2
  • 170
    • 0037148758 scopus 로고    scopus 로고
    • The genome sequence of Schizosaccharomyces pombe
    • Wood V, Gwilliam R, Rajandream MA et al. 2002. The genome sequence of Schizosaccharomyces pombe. Nature 415: 871-880.
    • (2002) Nature , vol.415 , pp. 871-880
    • Wood, V.1    Gwilliam, R.2    Rajandream, M.A.3
  • 171
    • 0034679626 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery
    • Wu X, Wilcox CB, Devasahayam G et al. 2000. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J 19: 3727-3738.
    • (2000) EMBO J. , vol.19 , pp. 3727-3738
    • Wu, X.1    Wilcox, C.B.2    Devasahayam, G.3
  • 172
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe MB, Schutkowski M, Shen M et al. 1997. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278: 1957-1960.
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1    Schutkowski, M.2    Shen, M.3
  • 173
    • 0036207028 scopus 로고    scopus 로고
    • The model unicellular eukaryote, Schizosaccharomyces pombe
    • Yanagida M. 2002. The model unicellular eukaryote, Schizosaccharomyces pombe. Gen Biol 3: 1-4.
    • (2002) Gen. Biol. , vol.3 , pp. 1-4
    • Yanagida, M.1
  • 174
    • 0030218962 scopus 로고    scopus 로고
    • The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene
    • Yokoi H, Shimizu Y, Anazawa H et al. 1996. The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene. Genomics 35: 448-455.
    • (1996) Genomics , vol.35 , pp. 448-455
    • Yokoi, H.1    Shimizu, Y.2    Anazawa, H.3
  • 175
    • 0032541163 scopus 로고    scopus 로고
    • Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of Hsp90
    • Young JC, Obermann WMJ, Hartl FU. 1998. Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of Hsp90. J Biol Chem 273: 18007-18010.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18007-18010
    • Young, J.C.1    Obermann, W.M.J.2    Hartl, F.U.3
  • 177
    • 20444453672 scopus 로고    scopus 로고
    • Regulation of CD147 cell surface expression: Involvement of the proline residue in the CD147 transmembrane domain
    • Yurchenko V, Pushkarsky T, Li J-H et al. 2005. Regulation of CD147 cell surface expression: involvement of the proline residue in the CD147 transmembrane domain. J Biol Chem 280: 17013-17019.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17013-17019
    • Yurchenko, V.1    Pushkarsky, T.2    Li, J.-H.3
  • 178
    • 0037151109 scopus 로고    scopus 로고
    • Active-site residues of cyclophilin A are crucial for its signalling activity via CD147
    • Yurchenko V, Zybarth G, O'Connor M et al. 2002. Active-site residues of cyclophilin A are crucial for its signalling activity via CD147. J Biol Chem 277: 22959-22969.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22959-22969
    • Yurchenko, V.1    Zybarth, G.2    O'Connor, M.3
  • 179
    • 0035877122 scopus 로고    scopus 로고
    • Sanglifehrin A, a novel cyclophilin-binding compound showing immunosuppressive activity with a new mechanism of action
    • Zenke G, Strittmatter U, Fuchs S et al. 2001. Sanglifehrin A, a novel cyclophilin-binding compound showing immunosuppressive activity with a new mechanism of action. J Immunol 16: 7165-7171.
    • (2001) J. Immunol. , vol.16 , pp. 7165-7171
    • Zenke, G.1    Strittmatter, U.2    Fuchs, S.3
  • 180
    • 0037470139 scopus 로고    scopus 로고
    • Nascent lipidated apolipoprotein is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaparones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B
    • Zhang J, Herscovitz H. 2003. Nascent lipidated apolipoprotein is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaparones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B. J Biol Chem 278: 7459-7468.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7459-7468
    • Zhang, J.1    Herscovitz, H.2
  • 182
    • 0035941234 scopus 로고    scopus 로고
    • Inhibition of cell cycle progression by the novel cyclophilin ligand sanglifehrin A is mediated through the NFκB-dependent activation of p53
    • Zhang L-H, Youn H-D, Liu JO. 2001. Inhibition of cell cycle progression by the novel cyclophilin ligand sanglifehrin A is mediated through the NFκB-dependent activation of p53. J Biol Chem 276: 43534-43540.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43534-43540
    • Zhang, L.-H.1    Youn, H.-D.2    Liu, J.O.3
  • 183
    • 25844483987 scopus 로고    scopus 로고
    • Insight into conversion of substrate to inhibitor
    • (unpublished data)
    • Zhao Y, Chen Y, Schutkowski M, Fischer G, Ke H. 1999. Insight into conversion of substrate to inhibitor (unpublished data).
    • (1999)
    • Zhao, Y.1    Chen, Y.2    Schutkowski, M.3    Fischer, G.4    Ke, H.5
  • 184
    • 0031568329 scopus 로고    scopus 로고
    • Cyclophilin A complexed with a fragment of HIV-1 gag protein: Insights into HIV-1 infectious activity
    • Zhao Y, Chen Y, Schutkowski M, Fischer G, Ke HM. 1997. Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity. Structure 5: 139-146.
    • (1997) Structure , vol.5 , pp. 139-146
    • Zhao, Y.1    Chen, Y.2    Schutkowski, M.3    Fischer, G.4    Ke, H.M.5
  • 185
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky LD, Etzkorn FA, Chang HY et al. 1992. Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci 1: 1092-1099.
    • (1992) Protein Sci. , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3


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