메뉴 건너뛰기




Volumn 55, Issue 3, 1999, Pages 423-436

Peptidyl-prolyl cis-trams isomerases, a superfamily of ubiquitous folding catalysts

Author keywords

Cyclophilins; FKBPs; Immunosuppression; Parvulins; Peptidyl prolyl cis trans isomerases; Protein folding

Indexed keywords

CALCIUM ION; CHAPERONE; CYCLOPHILIN; CYCLOSPORIN A; FK 506 BINDING PROTEIN; GAG PROTEIN; HEAT SHOCK PROTEIN 90; IMMUNOSUPPRESSIVE AGENT; PARVULIN; PROLINE DERIVATIVE; PROTEIN DISULFIDE ISOMERASE; RAPAMYCIN; STEROID RECEPTOR; TACROLIMUS; UNCLASSIFIED DRUG;

EID: 0032926319     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050299     Document Type: Review
Times cited : (556)

References (96)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C. B. (1973) Principles that govern the folding of protein chains. Science 181: 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0025195732 scopus 로고
    • Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions
    • Kiefhaber T., Quaas R., Hahn U. and Schmid F. X. (1990) Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry 29: 3061-3070
    • (1990) Biochemistry , vol.29 , pp. 3061-3070
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 3
    • 0021668676 scopus 로고
    • Determination of enzymatic catalysis for the cis-trans isomerization of peptide binding in proline containing peptides
    • Fischer G., Bang H. and Mech H. (1984) Determination of enzymatic catalysis for the cis-trans isomerization of peptide binding in proline containing peptides. Biomed. Biochim. Acta 43: 1101-1111
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, H.3
  • 4
    • 0024955297 scopus 로고
    • Pharmacology of cyclopsorin (Sandimmune). Pharmacological properties in vivo
    • Borel J. F. (1989) Pharmacology of cyclopsorin (Sandimmune). Pharmacological properties in vivo. Pharmacol. Rev. 41: 259-371
    • (1989) Pharmacol. Rev. , vol.41 , pp. 259-371
    • Borel, J.F.1
  • 6
    • 0023317629 scopus 로고
    • Complementary DNA for human T-cell cyclophilin
    • Haendler B., Hofer-Warbinek R. and Hofer E. (1987) Complementary DNA for human T-cell cyclophilin. EMBO J. 6: 947-950
    • (1987) EMBO J. , vol.6 , pp. 947-950
    • Haendler, B.1    Hofer-Warbinek, R.2    Hofer, 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. and Schmid F. W. (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.W.5
  • 8
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein
    • Takahashi N., Hayano T. and Suzuki M. (1989) Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein. Nature 337: 473-475
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 9
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding M. W., Galat A., Ueling S. L. and Schreiber S. (1989) A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature 341: 758-760
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Ueling, S.L.3    Schreiber, S.4
  • 10
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Sikierka J. J., Hung S. H. Y., Poe M., C.S. L. and Sigal N. H.(1989) A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 341: 755
    • (1989) Nature , vol.341 , pp. 755
    • Sikierka, J.J.1    Hung, S.H.Y.2    Poe, M.C.S.L.3    Sigal, N.H.4
  • 11
    • 0023245677 scopus 로고
    • FK506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics
    • Kino T., Hatanaka H., Hashimoto M., Nishiyama M., Goto T., Okuhara M. et al. (1987) FK506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics. J. Antibiotics 40: 1249-1255
    • (1987) J. Antibiotics , vol.40 , pp. 1249-1255
    • Kino, T.1    Hatanaka, H.2    Hashimoto, M.3    Nishiyama, M.4    Goto, T.5    Okuhara, M.6
  • 12
    • 0016713286 scopus 로고
    • Rapamycin (AY-22989), a new antifungal antibiotic. II. Fermentation, isolation and characterization
    • Sehgal S. N., Baker H. and Vezina C. (1975) Rapamycin (AY-22989), a new antifungal antibiotic. II. Fermentation, isolation and characterization. J. Antibiotics 28: 727-732
    • (1975) J. Antibiotics , vol.28 , pp. 727-732
    • Sehgal, S.N.1    Baker, H.2    Vezina, C.3
  • 13
    • 0025061678 scopus 로고
    • Molecular cloning and overexpression of the human K506-binding protein, FKBP
    • Standaert R. F., Galat A., Verdine G. L. and Schreiber S. L.(1990) Molecular cloning and overexpression of the human K506-binding protein, FKBP. Nature 346: 671-674
    • (1990) Nature , vol.346 , pp. 671-674
    • Standaert, R.F.1    Galat, A.2    Verdine, G.L.3    Schreiber, S.L.4
  • 14
    • 0028124244 scopus 로고
    • Conformation of the existence of a third family among peptidyl-prolyl cis-trans isomerases: Amino acid sequence and recombinant production of parvulin
    • Rahfeld J. U., Rücknagel K. P., Scheibert B., Ludwig B., Hacker J., Mann K. et al. (1994) Conformation of the existence of a third family among peptidyl-prolyl cis-trans isomerases: amino acid sequence and recombinant production of parvulin. FEBS Lett. 352: 180-184
    • (1994) FEBS Lett. , vol.352 , pp. 180-184
    • Rahfeld, J.U.1    Rücknagel, K.P.2    Scheibert, B.3    Ludwig, B.4    Hacker, J.5    Mann, K.6
  • 15
    • 4243863892 scopus 로고
    • A new family of peptidyl-prolyl isomerases: Evidence for general protein folding catalysts
    • Rudd K. E., Sofia H. J., Koonin E. V., Plunket G., Lazar S. and Rouviere P. E. (1995) A new family of peptidyl-prolyl isomerases: evidence for general protein folding catalysts. EMBO J. 14: 5494-5505
    • (1995) EMBO J. , vol.14 , pp. 5494-5505
    • Rudd, K.E.1    Sofia, H.J.2    Koonin, E.V.3    Plunket, G.4    Lazar, S.5    Rouviere, P.E.6
  • 16
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis-trans isomerase from Escherichia coli
    • Rahfeld J. U., Schierhorn A., Mann K. and Fischer G. (1994) A novel peptidyl-prolyl cis-trans isomerase from Escherichia coli. FEBS Lett. 343: 65-69
    • (1994) FEBS Lett. , vol.343 , pp. 65-69
    • Rahfeld, J.U.1    Schierhorn, A.2    Mann, K.3    Fischer, G.4
  • 17
    • 0032574832 scopus 로고    scopus 로고
    • Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone
    • Henning L., Christner C., Kipping M., Scheiben B., Rücknagel K., Grabley S. et al. (1998) Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. Biochemistry 37: 5953-5960
    • (1998) Biochemistry , vol.37 , pp. 5953-5960
    • Henning, L.1    Christner, C.2    Kipping, M.3    Scheiben, B.4    Rücknagel, K.5    Grabley, S.6
  • 18
    • 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 C.-M. and Walsh C. T. (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
  • 20
    • 0026499393 scopus 로고
    • Immunofluorescent localization and immunochemicakl determination of cyclophilin-A with specific rabbit antisera
    • Sarris A. H., Harding M. W., Jiang T.-R., Aftab D. and Handschuhmacher R. E. (1992) Immunofluorescent localization and immunochemicakl determination of cyclophilin-A with specific rabbit antisera. Transplantation 54: 904-910
    • (1992) Transplantation , vol.54 , pp. 904-910
    • Sarris, A.H.1    Harding, M.W.2    Jiang, T.-R.3    Aftab, D.4    Handschuhmacher, R.E.5
  • 21
    • 0026077983 scopus 로고
    • Molecular cloning and regional distribution of rat brain cyclophilin
    • Lad R. P., Smith M. A. and Hilt D. C. (1992) Molecular cloning and regional distribution of rat brain cyclophilin. Mol. Brain Res. 9: 239-244
    • (1992) Mol. Brain Res. , vol.9 , pp. 239-244
    • Lad, R.P.1    Smith, M.A.2    Hilt, D.C.3
  • 22
    • 0026013566 scopus 로고
    • Human cyclophilin B. A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • Price E. R., Zydowsky L. D., Jin M. J., Baker C. H., McKeon F. D. and Walsh C. T. (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    Baker, C.H.4    McKeon, F.D.5    Walsh, C.T.6
  • 23
    • 0026527418 scopus 로고
    • s-cyclophilin is retained intracellularly via the unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin
    • Arber S., Krause K.-H. and Caroni P. (1992) s-Cyclophilin is retained intracellularly via the unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J. Cell. Biol. 116: 113-125
    • (1992) J. Cell. Biol. , vol.116 , pp. 113-125
    • Arber, S.1    Krause, K.-H.2    Caroni, P.3
  • 24
    • 0025831980 scopus 로고
    • Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA
    • Friedman J. and Weissman I. (1991) Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: one in the presence and one in the absence of CsA. Cell 66: 799-866
    • (1991) Cell , vol.66 , pp. 799-866
    • Friedman, J.1    Weissman, I.2
  • 25
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., Farmer J. D., Lane W. S., Friedman J., Weissman I. and Schreiber S. L. (1991) Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66: 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 26
    • 0029750182 scopus 로고    scopus 로고
    • Identification of two CyP-40-like cyclophilins in Sacharomyces cerevisiae, one of which is required for normal cell growth
    • Duina A. A., Marsh J. A. and Gaber R. F. (1996) Identification of two CyP-40-like cyclophilins in Sacharomyces cerevisiae, one of which is required for normal cell growth. Yeast 12: 943-952
    • (1996) Yeast , vol.12 , pp. 943-952
    • Duina, A.A.1    Marsh, J.A.2    Gaber, R.F.3
  • 27
    • 0029807530 scopus 로고    scopus 로고
    • A cyclophilin function in Hsp90-dependent signal transduction
    • Duina A. A., Chang H.-C. J., March J. A., Lindquist S. and Gaber R. F. (1996) A cyclophilin function in Hsp90-dependent signal transduction. Science 274: 1713-1715
    • (1996) Science , vol.274 , pp. 1713-1715
    • Duina, A.A.1    Chang, H.-C.J.2    March, J.A.3    Lindquist, S.4    Gaber, R.F.5
  • 28
    • 0030050335 scopus 로고    scopus 로고
    • Cyclophilin 40 (CyP-40), mapping of its hsp 90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding
    • Ratajczak T. and Carrello A. (1996) Cyclophilin 40 (CyP-40), mapping of its hsp 90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding. J. Biol. Chem. 271: 2961-2965
    • (1996) J. Biol. Chem. , vol.271 , pp. 2961-2965
    • Ratajczak, T.1    Carrello, A.2
  • 29
    • 0031916381 scopus 로고    scopus 로고
    • The 20kD 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., Göthel S. F., Cronshagen U., Lane W. S. et al. (1998) The 20kD 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    Göthel, S.F.4    Cronshagen, U.5    Lane, W.S.6
  • 30
    • 0030815912 scopus 로고    scopus 로고
    • Fit for life? Evolution of chaperones and folding catalysts parallels the development of complex organisms
    • Pahl A., Brune K. and Bang H. (1997) Fit for life? Evolution of chaperones and folding catalysts parallels the development of complex organisms. Cell Stress Chaperones 2: 78-86
    • (1997) Cell Stress Chaperones , vol.2 , pp. 78-86
    • Pahl, A.1    Brune, K.2    Bang, H.3
  • 31
    • 0041172666 scopus 로고    scopus 로고
    • Cylophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions
    • Göthel S. F., Scholz C., Schmid F. X. and Marahiel M. A. (1998) Cylophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. Biochemistry 37: 13392-13399
    • (1998) Biochemistry , vol.37 , pp. 13392-13399
    • Göthel, S.F.1    Scholz, C.2    Schmid, F.X.3    Marahiel, M.A.4
  • 32
    • 0026619463 scopus 로고
    • Similarities and differences between human cyclophilin A and other β-barrel structures. Structural refinement at 1.63 Å resolution
    • Ke H. (1992) Similarities and differences between human cyclophilin A and other β-barrel structures. Structural refinement at 1.63 Å resolution. J. Mol. Biol. 228: 539-550
    • (1992) J. Mol. Biol. , vol.228 , pp. 539-550
    • Ke, H.1
  • 33
    • 0027201734 scopus 로고
    • Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli
    • Clubb R. T., Thanabal V., Fejzo J., Ferguson S. B., Zydowsky L., Baker C. H. et al. (1993) Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli. Biochemistry 32: 6391-6401
    • (1993) Biochemistry , vol.32 , pp. 6391-6401
    • Clubb, R.T.1    Thanabal, V.2    Fejzo, J.3    Ferguson, S.B.4    Zydowsky, L.5    Baker, C.H.6
  • 34
    • 0028326431 scopus 로고
    • Three-dimensional solution structure of Escherichia coli periplasmatic cyclophilin
    • Clubb R. T., Ferguson S. B., Walsh C. T. and Wagner G. (1994) Three-dimensional solution structure of Escherichia coli periplasmatic cyclophilin. Biochemistry 33: 2761-2772
    • (1994) Biochemistry , vol.33 , pp. 2761-2772
    • Clubb, R.T.1    Ferguson, S.B.2    Walsh, C.T.3    Wagner, G.4
  • 35
    • 0026532431 scopus 로고
    • The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A
    • Kallen J. and Walkinshaw M. D. (1992) The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A. FEBS Lett. 300: 286-290
    • (1992) FEBS Lett. , vol.300 , pp. 286-290
    • Kallen, J.1    Walkinshaw, M.D.2
  • 37
    • 0025923446 scopus 로고
    • A single Trp121 to Ala121 mutation in human cyclophilin alters cyclophilin affinity and peptidyl-prolyl cis-trans isomerase activity
    • Bossard M. J., Koser P. L., Brandt M., Bergsma D. J. and Levy M. A. (1991) A single Trp121 to Ala121 mutation in human cyclophilin alters cyclophilin affinity and peptidyl-prolyl cis-trans isomerase activity. Biochem. Biophys. Res. Commun. 176: 1142-1148
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1142-1148
    • Bossard, M.J.1    Koser, P.L.2    Brandt, M.3    Bergsma, D.J.4    Levy, M.A.5
  • 38
    • 0043224256 scopus 로고    scopus 로고
    • Engineering cyclophilin into a proline-specific endopeptidase
    • Quéméneur E., Moutiez M., Charbonnier J.-B. and Ménez A. (1998) Engineering cyclophilin into a proline-specific endopeptidase. Nature 391: 301-304
    • (1998) Nature , vol.391 , pp. 301-304
    • Quéméneur, E.1    Moutiez, M.2    Charbonnier, J.-B.3    Ménez, A.4
  • 39
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble T. R., Vajados F. F., Sanghee Y., Worthlake D. K., Houseweart M., Sundquist W. I. et al. (1996) Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87: 1285-1294
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajados, F.F.2    Sanghee, Y.3    Worthlake, D.K.4    Houseweart, M.5    Sundquist, W.I.6
  • 40
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 gag protein binds to cyclophilin A and B
    • Luban J., Bossolt K. L., Franke E. K., Kalpana G. V. and Goff S. P. (1993) Human immunodeficiency virus type 1 gag protein binds to cyclophilin A and B. Cell 73: 1067-1078
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 41
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke E. K., Yuan H. E. H. and Luban J. (1994) Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372: 359-362
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 42
    • 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. and Ke H. (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.5
  • 43
    • 0025647885 scopus 로고
    • Two distinct signal transmission pathways are inhibited in T-lymphocytes by complexes formed between an immunophilin and either FK506 or rapamycin
    • Bierer B. E., Mattila P. S., Standaert R. F., Herzenberg L. A., Burakoff S. J., Crabtree G. et al. (1990) Two distinct signal transmission pathways are inhibited in T-lymphocytes by complexes formed between an immunophilin and either FK506 or rapamycin. Proc. Natl. Acad. Sci. USA 87: 9231-9235
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9231-9235
    • Bierer, B.E.1    Mattila, P.S.2    Standaert, R.F.3    Herzenberg, L.A.4    Burakoff, S.J.5    Crabtree, G.6
  • 44
    • 0029816659 scopus 로고    scopus 로고
    • Cellular functions of immunophilins
    • Marks A. R. (1996) Cellular functions of immunophilins. Physiol. Rev. 76: 631-649
    • (1996) Physiol. Rev. , vol.76 , pp. 631-649
    • Marks, A.R.1
  • 46
    • 0028785482 scopus 로고
    • A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor
    • Lam E., Martin M. M., Timerman A. P., Sabers C., Fleischer S., Lukas T. et al. (1995) A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. J. Biol. Chem. 270: 26511-26522
    • (1995) J. Biol. Chem. , vol.270 , pp. 26511-26522
    • Lam, E.1    Martin, M.M.2    Timerman, A.P.3    Sabers, C.4    Fleischer, S.5    Lukas, T.6
  • 47
    • 0032576689 scopus 로고    scopus 로고
    • Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12
    • Shou W., Aghdasi B., Armstrong D. L., Guo Q., Bao S., Charng M.-J. et al. (1998) Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12. Nature 391: 489-492
    • (1998) Nature , vol.391 , pp. 489-492
    • Shou, W.1    Aghdasi, B.2    Armstrong, D.L.3    Guo, Q.4    Bao, S.5    Charng, M.-J.6
  • 49
    • 0026511332 scopus 로고
    • Mip protein of Legionella pneumophila exhibits peptidyl-prolyl cis/trans isomerase PPIase activity
    • Fischer G., Bang H., Ludwig B., Mann K. and Jacker J. (1992) Mip protein of Legionella pneumophila exhibits peptidyl-prolyl cis/trans isomerase PPIase activity. Mol. Microbiol. 6: 1375-1383
    • (1992) Mol. Microbiol. , vol.6 , pp. 1375-1383
    • Fischer, G.1    Bang, H.2    Ludwig, B.3    Mann, K.4    Jacker, J.5
  • 50
    • 0028846924 scopus 로고
    • Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells
    • Wintermeyer E., Ludwig B., Steinert M., Schmidt B., Fischer G. and Hacker J. (1995) Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infect. Immun. 63: 4576-4583
    • (1995) Infect. Immun. , vol.63 , pp. 4576-4583
    • Wintermeyer, E.1    Ludwig, B.2    Steinert, M.3    Schmidt, B.4    Fischer, G.5    Hacker, J.6
  • 51
    • 0028123018 scopus 로고
    • Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains; Its gene is transcriptionally coupled to the FKBP-12 gene
    • Pahl A. and Keller U. (1994) Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains; its gene is transcriptionally coupled to the FKBP-12 gene. EMBO J. 13: 3472-3480
    • (1994) EMBO J. , vol.13 , pp. 3472-3480
    • Pahl, A.1    Keller, U.2
  • 52
    • 0026495863 scopus 로고
    • Expression and characterization of human FKBP52, an immunophilin that associates with the 90 kDa heat shock protein and is a component of steroid receptor complexes
    • Peattie D. A., Handing M. W., Fleming M. A., DeCenzo M. T., Lippke J. A., Livington D. J. et al. (1992) Expression and characterization of human FKBP52, an immunophilin that associates with the 90 kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA 89: 10974-10978
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Handing, M.W.2    Fleming, M.A.3    Decenzo, M.T.4    Lippke, J.A.5    Livington, D.J.6
  • 53
    • 0030849456 scopus 로고    scopus 로고
    • FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisae
    • Alarcón C. M. and Heitman J. (1997) FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisae. Mol. Cell. Biol. 17: 5968-5975
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5968-5975
    • Alarcón, C.M.1    Heitman, J.2
  • 54
    • 0029064061 scopus 로고
    • Escherichia coli and other species if the Enterobacteriacae encode a protein similar to the family of Mip-like FK506-binding proteins
    • Home S. M. and Young K. D. (1995) Escherichia coli and other species if the Enterobacteriacae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch. Microbiol 163: 357-365
    • (1995) Arch. Microbiol , vol.163 , pp. 357-365
    • Home, S.M.1    Young, K.D.2
  • 55
    • 0027934203 scopus 로고
    • An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif
    • Wülfing C., Lombardero J. and Plückthun A. (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269: 2895-2901
    • (1994) J. Biol. Chem. , vol.269 , pp. 2895-2901
    • Wülfing, C.1    Lombardero, J.2    Plückthun, A.3
  • 56
    • 0028789790 scopus 로고
    • Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family
    • Callebaut I. and Mornon J.-P. (1995) Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. FEBS Lett. 374: 211-215
    • (1995) FEBS Lett. , vol.374 , pp. 211-215
    • Callebaut, I.1    Mornon, J.-P.2
  • 57
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G., Rücknagel K. P., Nierhaus K. H., Schmid F. X., Fischer G. and Rahfeld J.-U. (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    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.-U.6
  • 58
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506. Immunol
    • Schreiber S. L. and Crabtree G. R. (1992) The mechanism of action of cyclosporin A and FK506. Immunol. Today 13: 136-142
    • (1992) Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 59
    • 0028928611 scopus 로고
    • The chemistry of signai transduction
    • Clardy J. (1995) The chemistry of signai transduction. Proc. Natl. Acad. Sci. USA 92: 56-61
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 56-61
    • Clardy, J.1
  • 60
    • 0025826966 scopus 로고
    • Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
    • Michnick S. W., Rosen M. K., Wandless T. J., Karplus M. and Schreiber S. L. (1991) Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science 252: 836-839
    • (1991) Science , vol.252 , pp. 836-839
    • Michnick, S.W.1    Rosen, M.K.2    Wandless, T.J.3    Karplus, M.4    Schreiber, S.L.5
  • 62
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne G. D., Standaert R. F., Karplus P. A., Schreiber S. L. and Clardy J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229: 105-124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 63
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar S. W. and Kolter R. (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178: 1770-1773
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 64
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakis D., Betton J.-M. and Raina S. (1996) New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21: 871-884
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakis, D.1    Betton, J.-M.2    Raina, S.3
  • 65
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D. and Raina S. (1997) Protein folding in the bacterial periplasm. J. Bacteriol. 179: 2465-2471
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 66
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière P. E. and Gross C. A. (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10: 3170-3182
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouvière, P.E.1    Gross, C.A.2
  • 67
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue C. and Raina S. (1998) A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 17: 3968-3980
    • (1998) EMBO J. , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 68
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essentiell for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
    • Kontinen V. P. and Sarvas M. (1993) The PrsA lipoprotein is essentiell for protein secretion in Bacillus subtilis and sets a limit for high-level secretion. Mol. Microbiol. 8: 727-737
    • (1993) Mol. Microbiol. , vol.8 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 69
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl cis-trans isomerase essential for regulation of mitosis
    • Lu K. P., Hanes S. D. and Hunter T. (1996) A human peptidyl-prolyl cis-trans isomerase essential for regulation of mitosis. Nature 380: 544-547
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 70
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., Lu K. P., Hunter T. and Noel J. P. (1997) Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89: 875-886
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 71
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe M. B., Schutkowski M., Shen M., Zhou X. Z., Stukenberg P. T., Rahfeld J.-U. et al. (1997) Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278: 1947-1960
    • (1997) Science , vol.278 , pp. 1947-1960
    • Yaffe, M.B.1    Schutkowski, M.2    Shen, M.3    Zhou, X.Z.4    Stukenberg, P.T.5    Rahfeld, J.-U.6
  • 72
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and PIx1
    • Crenshaw D. G., Yang J., Means A. R. and Kornbluth S. (1998) The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and PIx1. EMBO J. 17: 1315-1327
    • (1998) EMBO J. , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 73
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
    • Shen M., Stukenberg P. T., Kirschner M. W. and Lu K. P. (1998) The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev 12: 706-720
    • (1998) Genes Dev , vol.12 , pp. 706-720
    • Shen, M.1    Stukenberg, P.T.2    Kirschner, M.W.3    Lu, K.P.4
  • 74
    • 0000294801 scopus 로고
    • Über peptidyl-prolyl-cis/trans-isomerasen und ihre effektoren
    • Fischer G. (1994) Über Peptidyl-Prolyl-cis/trans-Isomerasen und ihre Effektoren. Angew. Chem. 106: 1479-1501
    • (1994) Angew. Chem. , vol.106 , pp. 1479-1501
    • Fischer, G.1
  • 75
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl-prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron J. L., Kuzmic P., Kishore V., Bonilla-Colon E. and Rich D. H. (1991) Determination of kinetic constants for peptidyl-prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30: 6127-6134
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Bonilla-Colon, E.4    Rich, D.H.5
  • 76
    • 0026651050 scopus 로고
    • Lithium chloride pertubation of cis-trans peptide bonds equilibria - Effects on conformational equilibria in cyclosporin A and on time dependent inhibition of cyclophilin
    • Kofron J. L., Kuzmic P., Kishore V., Gemmecker G., Fesik S. W. and Rich D. H. (1992) Lithium chloride pertubation of cis-trans peptide bonds equilibria - effects on conformational equilibria in cyclosporin A and on time dependent inhibition of cyclophilin. J. Am. Chem. Soc. 114: 2670-2675
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2670-2675
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Gemmecker, G.4    Fesik, S.W.5    Rich, D.H.6
  • 77
    • 0028877264 scopus 로고
    • Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy
    • Kern D., Kern G., Scherer G., Fischer G. and Drakenberg T. (1995) Kinetic analysis of cyclophilin-catalyzed prolyl cis/ trans isomerization by dynamic NMR spectroscopy. Biochemistry 34: 13594-13602
    • (1995) Biochemistry , vol.34 , pp. 13594-13602
    • Kern, D.1    Kern, G.2    Scherer, G.3    Fischer, G.4    Drakenberg, T.5
  • 78
    • 0031572824 scopus 로고    scopus 로고
    • A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates
    • Janowski B., Wollner S., Schutkowski M. and Fischer G. (1997) A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates. Anal. Biochem. 252: 299-307
    • (1997) Anal. Biochem. , vol.252 , pp. 299-307
    • Janowski, B.1    Wollner, S.2    Schutkowski, M.3    Fischer, G.4
  • 79
    • 0020473605 scopus 로고
    • Specific protein nucleic acid recognition in ribonuclease T1-2′-guanylic acid complex
    • Heinemann U. and Saenger W. (1982) Specific protein nucleic acid recognition in ribonuclease T1-2′-guanylic acid complex. Nature 299: 27-31
    • (1982) Nature , vol.299 , pp. 27-31
    • Heinemann, U.1    Saenger, W.2
  • 80
    • 0025311245 scopus 로고
    • Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding
    • Kiefhaber T., Gruner H.-P., Hahn U. and Schmid F. X. (1990) Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry 29: 6475-6480
    • (1990) Biochemistry , vol.29 , pp. 6475-6480
    • Kiefhaber, T.1    Gruner, H.-P.2    Hahn, U.3    Schmid, F.X.4
  • 81
    • 0027952952 scopus 로고
    • Characterization of folding intermediates using prolyl isomerase
    • Veeraraghavan S. and Nall B. T. (1994) Characterization of folding intermediates using prolyl isomerase. Biochemistry 33: 687-692
    • (1994) Biochemistry , vol.33 , pp. 687-692
    • Veeraraghavan, S.1    Nall, B.T.2
  • 82
    • 0031029046 scopus 로고    scopus 로고
    • Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
    • Scholz C., Stoller G., Zarnt T., Fischer G. and Schmid F. X. (1997) Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16: 54-58
    • (1997) EMBO J. , vol.16 , pp. 54-58
    • Scholz, C.1    Stoller, G.2    Zarnt, T.3    Fischer, G.4    Schmid, F.X.5
  • 84
    • 0031554922 scopus 로고    scopus 로고
    • Modular structure of the trigger factor required for high activity in protein folding
    • Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F. X. and Fischer G. (1997) Modular structure of the trigger factor required for high activity in protein folding. J. Mol. Biol. 271: 827-837
    • (1997) J. Mol. Biol. , vol.271 , pp. 827-837
    • Zarnt, T.1    Tradler, T.2    Stoller, G.3    Scholz, C.4    Schmid, F.X.5    Fischer, G.6
  • 85
    • 0032478521 scopus 로고    scopus 로고
    • Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues
    • Scholz O, Mücke M., Rape M., Pecht A., Pahl A., Bang H. et al. (1998) Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues. J. Mol. Biol. 277: 723-732
    • (1998) J. Mol. Biol. , vol.277 , pp. 723-732
    • Scholz, O.1    Mücke, M.2    Rape, M.3    Pecht, A.4    Pahl, A.5    Bang, H.6
  • 86
    • 0023387587 scopus 로고
    • Trigger factor: A soluble protein that folds pro-OmpA into a membrane-assembly-competent form
    • Crooke E. and Wickner W. (1987) Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc. Natl. Acad. Sci. USA 84: 5216-5220
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5216-5220
    • Crooke, E.1    Wickner, W.2
  • 87
    • 0024295389 scopus 로고
    • ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
    • Crooke E., Guthrie B., Lecker S., Lill R. and Wickner W. (1988) ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle. Cell 54: 1003-1011
    • (1988) Cell , vol.54 , pp. 1003-1011
    • Crooke, E.1    Guthrie, B.2    Lecker, S.3    Lill, R.4    Wickner, W.5
  • 88
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the Chaperones GroEL and GroES
    • Kandror O., Busconi L., Sherman M. and Goldberg A. L.(1994) Rapid degradation of an abnormal protein in Escherichia coli involves the Chaperones GroEL and GroES. J. Biol. Chem. 269: 23575-23582
    • (1994) J. Biol. Chem. , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 89
    • 0028849206 scopus 로고
    • Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes its binding of GroEL to unfolded proteins
    • Kandror O., Sherman M., Rhode M. and Goldberg A. L.(1995) Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes its binding of GroEL to unfolded proteins. EMBO J. 14: 6021-6027
    • (1995) EMBO J. , vol.14 , pp. 6021-6027
    • Kandror, O.1    Sherman, M.2    Rhode, M.3    Goldberg, A.L.4
  • 90
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chain
    • Hesterkamp T., Hauser S., Lutcke H. and Bukau B. (1996) Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chain. Proc. Natl. Acad. Sci. USA 93: 4437-4441
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lutcke, H.3    Bukau, B.4
  • 92
    • 0025907054 scopus 로고
    • The cyclophilin homolog ninaA is a tissue specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsin
    • Stamnes M. A., Shieh B. H., Chuman L., Harris G. L. and Zuker C. S. (1991) The cyclophilin homolog ninaA is a tissue specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsin. 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
  • 93
    • 0028809455 scopus 로고
    • Characterization of an Escherichia coli rotA mutant, affected in periplasmatic peptidyl-prolyl cis/trans isomerase
    • Kleerebezem M., Heutink M. and Tommassen J. (1995) Characterization of an Escherichia coli rotA mutant, affected in periplasmatic peptidyl-prolyl cis/trans isomerase. Mol. Microbiol. 18: 313-320
    • (1995) Mol. Microbiol. , vol.18 , pp. 313-320
    • Kleerebezem, M.1    Heutink, M.2    Tommassen, J.3
  • 94
    • 0027959745 scopus 로고
    • A gene of Acinetobacter calcoaceticus BD413 encodes a periplasmatic peptidyl-prolyl cis trans isomerase of the cyclophilin sub-class that is not essential for growth
    • Kok R. G., Christoffels V. M., Vosman B. and Hellingwerf K. J. (1994) A gene of Acinetobacter calcoaceticus BD413 encodes a periplasmatic peptidyl-prolyl cis trans isomerase of the cyclophilin sub-class that is not essential for growth. Biochim. Biophys. Acta 1219: 601-606
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 601-606
    • Kok, R.G.1    Christoffels, V.M.2    Vosman, B.3    Hellingwerf, K.J.4
  • 96
    • 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. and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.