메뉴 건너뛰기




Volumn 63, Issue 24, 2006, Pages 2889-2900

Immunophilins: For the love of proteins

Author keywords

Chaperone; Cyclophilin (Cyp); Dual family immunophilin; FK506 binding protein (FK506); Immunophilin; PPIase; Protein folding; TPR domain; Trigger factor

Indexed keywords

CHAPERONE; CYCLOPHILIN; FK 506 BINDING PROTEIN; IMMUNOPHILIN; ISOMERASE;

EID: 33846059755     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-006-6215-3     Document Type: Review
Times cited : (183)

References (104)
  • 1
    • 0141707715 scopus 로고    scopus 로고
    • Peptidylprolyl cis/trans isomerases (immunophilins): Biological diversity - targets - functions
    • Galat, A. (2003) Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity - targets - functions. Curr. Top. Med. Chem. 3, 1315-1347.
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 1315-1347
    • Galat, A.1
  • 2
    • 0027339327 scopus 로고
    • NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs
    • McCaffrey, P. G., Perrino, B. A., Soderling, T. R. and Rao, A. (1993) NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs. J. Biol. Chem. 268, 3747-3752.
    • (1993) J. Biol. Chem , vol.268 , pp. 3747-3752
    • McCaffrey, P.G.1    Perrino, B.A.2    Soderling, T.R.3    Rao, A.4
  • 4
    • 14844363721 scopus 로고    scopus 로고
    • Signaling by target of rapamycin proteins in cell growth control
    • Inoki, K., Ouyang, H., Li, Y. and Guan, K. L. (2005) Signaling by target of rapamycin proteins in cell growth control. Microbiol. Mol. Biol. Rev. 69, 79-100.
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 79-100
    • Inoki, K.1    Ouyang, H.2    Li, Y.3    Guan, K.L.4
  • 5
    • 21644458647 scopus 로고    scopus 로고
    • A novel class of dual-family immunophilins
    • Adams, B., Musiyenko, A., Kumar, R. and Barik, S. (2005) A novel class of dual-family immunophilins. J. Biol. Chem. 280, 24308-24314.
    • (2005) J. Biol. Chem , vol.280 , pp. 24308-24314
    • Adams, B.1    Musiyenko, A.2    Kumar, R.3    Barik, S.4
  • 6
  • 7
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • Schmid, F. X. (1993) Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22, 123-142.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 8
    • 0023236959 scopus 로고
    • Catalysis of protein folding by prolyl isomerase
    • Lang, K., Schmid, F. X. and Fischer, G. (1987) Catalysis of protein folding by prolyl isomerase. Nature 329, 268-270.
    • (1987) Nature , vol.329 , pp. 268-270
    • Lang, K.1    Schmid, F.X.2    Fischer, G.3
  • 9
  • 10
    • 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. X. (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
  • 11
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T. and Suzuki, M. (1989) Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 12
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bachinger, H. P. (1987) The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 262, 17144-17148.
    • (1987) J. Biol. Chem , vol.262 , pp. 17144-17148
    • Bachinger, H.P.1
  • 13
    • 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. M., Boswell, B. A. and Bachinger, H. P. (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.M.1    Boswell, B.A.2    Bachinger, H.P.3
  • 14
    • 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. and 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
  • 15
    • 0031580205 scopus 로고    scopus 로고
    • The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2
    • Tan, Y. J., Oliveberg, M., Otzen, D. E. and Fersht, A. R. (1997) The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. J. Mol. Biol. 269, 611-622.
    • (1997) J. Mol. Biol , vol.269 , pp. 611-622
    • Tan, Y.J.1    Oliveberg, M.2    Otzen, D.E.3    Fersht, A.R.4
  • 16
    • 0028928739 scopus 로고
    • A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin
    • Kern, G., Kern, D., Schmid, F. X. and 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
  • 17
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard, P. O., Bergenhem, N., Jonsson, B. H., Svensson, M. and Carlsson, U. (1992) Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258, 466-468.
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.O.1    Bergenhem, N.2    Jonsson, B.H.3    Svensson, M.4    Carlsson, U.5
  • 18
    • 0025195733 scopus 로고
    • Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
    • Kiefhaber, T., Quaas, R., Hahn, U. and Schmid, F. X. (1990) Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29, 3053-3061.
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 19
    • 0026619463 scopus 로고
    • Similarities and differences between human cyclophilin A and other beta barrel structures. Structural refinement at 1.63 Å resolution
    • Ke, H. (1992) Similarities and differences between human cyclophilin A and other beta 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
  • 21
    • 0029784483 scopus 로고    scopus 로고
    • Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence
    • Ansai, T., Dupuy, L. C., Barik, S. (1996) Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence. J. Biol. Chem. 271, 24401-24407.
    • (1996) J. Biol. Chem , vol.271 , pp. 24401-24407
    • Ansai, T.1    Dupuy, L.C.2    Barik, S.3
  • 22
    • 0027369888 scopus 로고
    • Expression and biochemical properties of a protein serine/threonine phosphatase encoded by bacteriophage lambda
    • Barik, S. (1993) Expression and biochemical properties of a protein serine/threonine phosphatase encoded by bacteriophage lambda. Proc. Natl. Acad. Sci. USA 90, 10633-10637.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10633-10637
    • Barik, S.1
  • 23
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution
    • Das, A. K., Helps, N. R., Cohen, P. T., Barford, D. (1996) Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution. EMBO J. 15, 6798-6809.
    • (1996) EMBO J , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 24
    • 0033551778 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5
    • Sinclair, C., Borchers, C., Parker, C., Tomer, K., Charbonneau, H. and Rossie, S. (1999) The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5. J. Biol. Chem. 274, 23666-23672.
    • (1999) J. Biol. Chem , vol.274 , pp. 23666-23672
    • Sinclair, C.1    Borchers, C.2    Parker, C.3    Tomer, K.4    Charbonneau, H.5    Rossie, S.6
  • 26
    • 22244464562 scopus 로고    scopus 로고
    • The cyclophilins
    • Wang, P. and Heitman, J. (2005) The cyclophilins. Genome Biol. 6, 226.
    • (2005) Genome Biol , vol.6 , pp. 226
    • Wang, P.1    Heitman, J.2
  • 27
    • 2942593899 scopus 로고    scopus 로고
    • 3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
    • Wu, B., Li, P., Liu, Y., Lou, Z., Ding, Y., Shu, C., Ye, S., Bartlam, M., Shen, B. and Rao, Z. (2004) 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex. Proc. Natl. Acad. Sci. USA 101, 8348-8353.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8348-8353
    • Wu, B.1    Li, P.2    Liu, Y.3    Lou, Z.4    Ding, Y.5    Shu, C.6    Ye, S.7    Bartlam, M.8    Shen, B.9    Rao, Z.10
  • 28
    • 0345144024 scopus 로고    scopus 로고
    • Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes
    • Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F. and Clardy, J. (2003) Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA100, 868-873.
    • (2003) Proc. Natl. Acad. Sci , vol.USA100 , pp. 868-873
    • Sinars, C.R.1    Cheung-Flynn, J.2    Rimerman, R.A.3    Scammell, J.G.4    Smith, D.F.5    Clardy, J.6
  • 29
    • 0035813134 scopus 로고    scopus 로고
    • Localization of the chaperone domain of FKBP52
    • Pirkl, F., Fischer, E., Modrow, S., Buchner, J. (2001) Localization of the chaperone domain of FKBP52. J. Biol. Chem. 276, 37034-37041..
    • (2001) J. Biol. Chem , vol.276 , pp. 37034-37041
    • Pirkl, F.1    Fischer, E.2    Modrow, S.3    Buchner, J.4
  • 30
    • 12344264071 scopus 로고    scopus 로고
    • A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities
    • Monaghan, P. and Bell, A. (2005) A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities. Mol. Biochem. Parasitol. 139, 185-195.
    • (2005) Mol. Biochem. Parasitol , vol.139 , pp. 185-195
    • Monaghan, P.1    Bell, A.2
  • 31
    • 17844396246 scopus 로고    scopus 로고
    • The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity
    • Kumar, R., Adams, B., Musiyenko, A., Shulyayeva, O. and Barik, S. (2005) The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. Mol. Biochem. Parasitol. 141, 163-173.
    • (2005) Mol. Biochem. Parasitol , vol.141 , pp. 163-173
    • Kumar, R.1    Adams, B.2    Musiyenko, A.3    Shulyayeva, O.4    Barik, S.5
  • 32
    • 0032230312 scopus 로고    scopus 로고
    • Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes
    • Barent, R. L., Nair, S. C., Carr, D. C., Ruan, Y., Rimerman, R. A., Fulton, J., Zhang, Y. and Smith, D. F. (1998) Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes. Mol. Endocrinol. 12, 342-354.
    • (1998) Mol. Endocrinol , vol.12 , pp. 342-354
    • Barent, R.L.1    Nair, S.C.2    Carr, D.C.3    Ruan, Y.4    Rimerman, R.A.5    Fulton, J.6    Zhang, Y.7    Smith, D.F.8
  • 33
    • 4644318581 scopus 로고    scopus 로고
    • Davies, T. H. and Sanchez, E. R. (2005) FKBP52. Int. J. Biochem. Cell Biol. 37, 42-47.
    • Davies, T. H. and Sanchez, E. R. (2005) FKBP52. Int. J. Biochem. Cell Biol. 37, 42-47.
  • 34
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans- isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • Ramm, K. and Pluckthun, A. (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans- isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J. Biol. Chem. 275, 17106-17113.
    • (2000) J. Biol. Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Pluckthun, A.2
  • 35
    • 0035816225 scopus 로고    scopus 로고
    • High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA
    • Ramm, K. and Pluckthun, A. (2001) High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J. Mol. Biol. 310, 485-498.
    • (2001) J. Mol. Biol , vol.310 , pp. 485-498
    • Ramm, K.1    Pluckthun, A.2
  • 36
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F. A., Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. (2004) Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335, 595-608.
    • (2004) J. Mol. Biol , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Vulliez-le Normand, B.3    Kahn, R.4    Betton, J.M.5    Bentley, G.A.6
  • 37
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R., Vajdos, F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I. and Hill, C. P. (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    Vajdos, F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 38
    • 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
  • 39
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel, S. F. and Marahiel, M. A. (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell. Mol. Life Sci. 55, 423-436.
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 40
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
    • Fischer, G. and Aumuller, T. (2003) Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 148, 105-150.
    • (2003) Rev. Physiol. Biochem. Pharmacol , vol.148 , pp. 105-150
    • Fischer, G.1    Aumuller, T.2
  • 41
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C, Toft, D. O. and Morimoto, R. I. (1996) Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 42
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose, S., Weikl, T., Bugl, H. and Buchner, J. (1996) Chaperone function of Hsp90-associated proteins. Science 274, 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 43
    • 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. and Buchner, 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    Buchner, J.4
  • 44
    • 29344457166 scopus 로고    scopus 로고
    • Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters
    • Weiergraber, O. H., Eckhoff, A. and Granzin, J. (2006) Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters. FEBS Lett. 580, 251-255.
    • (2006) FEBS Lett , vol.580 , pp. 251-255
    • Weiergraber, O.H.1    Eckhoff, A.2    Granzin, J.3
  • 45
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rucknagel, 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    Rucknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 46
    • 0345802691 scopus 로고    scopus 로고
    • Trigger factor-assisted folding of bovine carbonic anhydrase II
    • Liu, C. P. and Zhou, J. M. (2004) Trigger factor-assisted folding of bovine carbonic anhydrase II. Biochem. Biophys. Res. Commun. 313, 509-515.
    • (2004) Biochem. Biophys. Res. Commun , vol.313 , pp. 509-515
    • Liu, C.P.1    Zhou, J.M.2
  • 47
    • 1842639447 scopus 로고    scopus 로고
    • Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
    • Kramer, G., Patzelt, H., Rauch, T., Kurz, T. A., Vorderwulbecke, S., Bukau, B. and Deuerling, E. (2004) Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J. Biol. Chem. 279, 14165-14170.
    • (2004) J. Biol. Chem , vol.279 , pp. 14165-14170
    • Kramer, G.1    Patzelt, H.2    Rauch, T.3    Kurz, T.A.4    Vorderwulbecke, S.5    Bukau, B.6    Deuerling, E.7
  • 48
    • 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
  • 49
    • 33646578837 scopus 로고    scopus 로고
    • The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains
    • Mok, D., Allan, R. K., Carrello, A., Wangoo, K., Walkinshaw, M. D., Ratajczak, T. (2006) The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. FEBS Lett. 580, 2761-2768.
    • (2006) FEBS Lett , vol.580 , pp. 2761-2768
    • Mok, D.1    Allan, R.K.2    Carrello, A.3    Wangoo, K.4    Walkinshaw, M.D.5    Ratajczak, T.6
  • 50
    • 2442704477 scopus 로고    scopus 로고
    • Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004
    • Maruyama, T., Suzuki, R. and Furutani, M. (2004) Archaeal peptidyl prolyl cis-trans isomerases (PPIases) update 2004. Front. Biosci. 9, 1680-1720.
    • (2004) Front. Biosci , vol.9 , pp. 1680-1720
    • Maruyama, T.1    Suzuki, R.2    Furutani, M.3
  • 51
    • 0037033042 scopus 로고    scopus 로고
    • A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function
    • Chakraborty, A., Das, I., Datta, R., Sen, B., Bhattacharyya, D., Mandal, C. and Datta, A. K. (2002) A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function. J. Biol. Chem. 277, 47451-47460.
    • (2002) J. Biol. Chem , vol.277 , pp. 47451-47460
    • Chakraborty, A.1    Das, I.2    Datta, R.3    Sen, B.4    Bhattacharyya, D.5    Mandal, C.6    Datta, A.K.7
  • 52
    • 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
  • 53
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice, S. S., Hunstad, D. A., Harper, J. R., Duguay, A. R., Pinkner, J. S., Bann, J., Frieden, C., Silhavy, T. J. and Hultgren, S. J. (2005) Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 187, 7680-7686.
    • (2005) J. Bacteriol , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5    Bann, J.6    Frieden, C.7    Silhavy, T.J.8    Hultgren, S.J.9
  • 54
    • 0041172666 scopus 로고    scopus 로고
    • Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions
    • Gothel, S. F., Scholz, C., Schmid, F. X. and Marahiel, M. A. (1998) Cyclophilin 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
    • Gothel, S.F.1    Scholz, C.2    Schmid, F.X.3    Marahiel, M.A.4
  • 55
    • 0027949996 scopus 로고
    • Prolyl isomerase requirement for the expression of functional homooligomeric ligand-gated ion channels
    • Helekar, S. A., Char, D., Neff, S. and Patrick, J. (1994) Prolyl isomerase requirement for the expression of functional homooligomeric ligand-gated ion channels. Neuron 12, 179-189.
    • (1994) Neuron , vol.12 , pp. 179-189
    • Helekar, S.A.1    Char, D.2    Neff, S.3    Patrick, J.4
  • 56
    • 0036789573 scopus 로고    scopus 로고
    • Cyclophilin A peptidyl-prolyl isomerase activity promotes Zprl nuclear export
    • Ansari, H., Greco, G. and Luban, J. (2002) Cyclophilin A peptidyl-prolyl isomerase activity promotes Zprl nuclear export. Mol. Cell. Biol. 22, 6971-6978.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6971-6978
    • Ansari, H.1    Greco, G.2    Luban, J.3
  • 57
    • 1942533443 scopus 로고    scopus 로고
    • Cyclophilin A as a novel biphasic mediator of endothelial activation and dysfunction
    • Kim, S. H., Lessner, S. M., Sakurai, Y. and Galis, Z. S. (2004) Cyclophilin A as a novel biphasic mediator of endothelial activation and dysfunction. Am. J. Pathol. 164, 1567-1574.
    • (2004) Am. J. Pathol , vol.164 , pp. 1567-1574
    • Kim, S.H.1    Lessner, S.M.2    Sakurai, Y.3    Galis, Z.S.4
  • 58
    • 0026554163 scopus 로고
    • Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide- activated macrophages
    • Sherry, B., Yarlett, N., Strupp, A. and Cerami, A. (1992) Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide- activated macrophages. Proc. Natl. Acad. Sci. USA 89, 3511-3515.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3511-3515
    • Sherry, B.1    Yarlett, N.2    Strupp, A.3    Cerami, A.4
  • 59
    • 23444434115 scopus 로고    scopus 로고
    • Cyclophilins in rheumatoid arthritis-stepping into an undiscovered country?
    • Pap, T. (2005) Cyclophilins in rheumatoid arthritis-stepping into an undiscovered country? Clin. Immunol. 116, 199-201.
    • (2005) Clin. Immunol , vol.116 , pp. 199-201
    • Pap, T.1
  • 60
    • 4143074548 scopus 로고    scopus 로고
    • Colgan, J., Asmal, M., Neagu, M., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A. and Luban, J. (2004) Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk. Immunity 21, 189-201.
    • Colgan, J., Asmal, M., Neagu, M., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A. and Luban, J. (2004) Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk. Immunity 21, 189-201.
  • 61
    • 0037076393 scopus 로고    scopus 로고
    • The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer
    • Rycyzyn, M. A. and Clevenger, C. V. (2002) The intranuclear 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
  • 62
    • 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., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T. and Tsujimoto, Y. (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434, 652-658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 65
    • 33645064275 scopus 로고    scopus 로고
    • Dealing with the family: CD147 interactions with cyclophilins
    • Yurchenko, V., Constant, S. and Bukrinsky, M. (2006) Dealing with the family: CD147 interactions with cyclophilins. Immunology 117, 301-309.
    • (2006) Immunology , vol.117 , pp. 301-309
    • Yurchenko, V.1    Constant, S.2    Bukrinsky, M.3
  • 67
    • 0035932951 scopus 로고    scopus 로고
    • Pushkarsky, T., Zybarth, G., Dubrovsky, L., Yurchenko, V., Tang, H., Guo, H., Toole, B., Sherry, B. and Bukrinsky, M. (2001) CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin, A. Proc. Natl. Acad. Sci. USA 98, 6360-6365.
    • Pushkarsky, T., Zybarth, G., Dubrovsky, L., Yurchenko, V., Tang, H., Guo, H., Toole, B., Sherry, B. and Bukrinsky, M. (2001) CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin, A. Proc. Natl. Acad. Sci. USA 98, 6360-6365.
  • 69
    • 0141707713 scopus 로고    scopus 로고
    • Immunophilin chaperones in steroid receptor signalling
    • Ratajczak, T., Ward, B. K. and Minchin, R. F. (2003) Immunophilin chaperones in steroid receptor signalling. Curr. Top. Med. Chem. 3, 1348-1357.
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 1348-1357
    • Ratajczak, T.1    Ward, B.K.2    Minchin, R.F.3
  • 71
    • 13544267438 scopus 로고    scopus 로고
    • Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506
    • Davies, T. H., Ning, Y. M. and Sanchez, E. R. (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
  • 72
    • 33644747306 scopus 로고    scopus 로고
    • Analysis of calstabin2 (FKBP12.6)-ryanodine receptor interactions: Rescue of heart failure by calstabin2 in mice
    • Huang, F., Shan, J., Reiken, S., Wehrens, X. H. and Marks, A. R. (2006) Analysis of calstabin2 (FKBP12.6)-ryanodine receptor interactions: rescue of heart failure by calstabin2 in mice. Proc. Natl. Acad. Sci. USA 103, 3456-3461.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3456-3461
    • Huang, F.1    Shan, J.2    Reiken, S.3    Wehrens, X.H.4    Marks, A.R.5
  • 73
    • 0033712280 scopus 로고    scopus 로고
    • Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding
    • Denny, W. B., Valentine, D. L., Reynolds, P. D., Smith, D. F. and Scammell, J. G. (2000) Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding. Endocrinology 141, 4107-4113.
    • (2000) Endocrinology , vol.141 , pp. 4107-4113
    • Denny, W.B.1    Valentine, D.L.2    Reynolds, P.D.3    Smith, D.F.4    Scammell, J.G.5
  • 74
    • 22144494187 scopus 로고    scopus 로고
    • Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activity
    • Denny, W. B., Prapapanich, V., Smith, D. F. and Scammell, J. G. (2005) Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activity. Endocrinology 146, 3194-3201.
    • (2005) Endocrinology , vol.146 , pp. 3194-3201
    • Denny, W.B.1    Prapapanich, V.2    Smith, D.F.3    Scammell, J.G.4
  • 75
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies, T. H., Ning, Y. M. and Sanchez, E. R. (2002) A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. J. Biol. Chem. 277, 4597-4600.
    • (2002) J. Biol. Chem , vol.277 , pp. 4597-4600
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 76
    • 14244262261 scopus 로고    scopus 로고
    • FK506- binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • Wochnik, G. M., Ruegg, J., Abel, G. A., Schmidt, U., Holsboer, F. and Rein, T. (2005) FK506- binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280, 4609-4616.
    • (2005) J. Biol. Chem , vol.280 , pp. 4609-4616
    • Wochnik, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holsboer, F.5    Rein, T.6
  • 80
    • 33846050261 scopus 로고    scopus 로고
    • Yang, Z., Wolf, I., Chen, H., Periyasamy, S., Yucel, S., Chen, Z., Yong, W., Shi, S., Sanchez, E. R. and Shou, W. (in press) FKBP52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform. Mol. Endocrinol.
    • Yang, Z., Wolf, I., Chen, H., Periyasamy, S., Yucel, S., Chen, Z., Yong, W., Shi, S., Sanchez, E. R. and Shou, W. (in press) FKBP52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform. Mol. Endocrinol.
  • 81
    • 0037418243 scopus 로고    scopus 로고
    • The FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesis
    • Krummrei, U., Baulieu, E. E. and Chambraud, B. (2003) The FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesis. Proc. Natl. Acad. Sci. USA100, 2444-2449.
    • (2003) Proc. Natl. Acad. Sci , vol.USA100 , pp. 2444-2449
    • Krummrei, U.1    Baulieu, E.E.2    Chambraud, B.3
  • 82
    • 19344375177 scopus 로고    scopus 로고
    • Plant immunophilins: Functional versatility beyond protein maturation
    • Romano, P., Gray, J., Horton, P. and Luan, S. (2005) Plant immunophilins: functional versatility beyond protein maturation. New Phytol. 166, 753-769.
    • (2005) New Phytol , vol.166 , pp. 753-769
    • Romano, P.1    Gray, J.2    Horton, P.3    Luan, S.4
  • 83
    • 0141818987 scopus 로고    scopus 로고
    • Immunophilins in nervous system degeneration and regeneration
    • Avramut, M. and Achim, C. L. (2003) Immunophilins in nervous system degeneration and regeneration. Curr. Top. Med. Chem. 3, 1376-1282.
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 1376-1282
    • Avramut, M.1    Achim, C.L.2
  • 84
    • 0141595912 scopus 로고    scopus 로고
    • Neuroimmunophilin ligands: The development of novel neuroregenerative/neuroprotective compounds
    • Gold, B. G. and Villafranca, J. E. (2003) Neuroimmunophilin ligands: the development of novel neuroregenerative/neuroprotective compounds. Curr. Top. Med. Chem. 3, 1368-1375.
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 1368-1375
    • Gold, B.G.1    Villafranca, J.E.2
  • 86
    • 0032168133 scopus 로고    scopus 로고
    • A novel human gene FKBP6 is deleted in Williams syndrome
    • Meng, X., Lu, X., Morris, C. A. and Keating, M. T. (1998) A novel human gene FKBP6 is deleted in Williams syndrome. Genomics 52, 130-137.
    • (1998) Genomics , vol.52 , pp. 130-137
    • Meng, X.1    Lu, X.2    Morris, C.A.3    Keating, M.T.4
  • 87
    • 16444386224 scopus 로고    scopus 로고
    • Autosomal dominant inheritance of Williams-Beuren syndrome in a father and son with haploinsufficiency for FKBP6
    • Metcalfe, K., Simeonov, E., Beckett, W., Donnai, D. and Tassabehji, M. (2005) Autosomal dominant inheritance of Williams-Beuren syndrome in a father and son with haploinsufficiency for FKBP6. Clin. Dysmorphol. 14, 61-65.
    • (2005) Clin. Dysmorphol , vol.14 , pp. 61-65
    • Metcalfe, K.1    Simeonov, E.2    Beckett, W.3    Donnai, D.4    Tassabehji, M.5
  • 90
    • 20244377844 scopus 로고    scopus 로고
    • Role for the nuclear factor kappa B pathway in transforming growth factor-beta1 production in idiopathic myelofibrosis: Possible relationship with FK506 binding protein 51 overexpression
    • Komura, E., Tonetti, C., Penard-Lacronique, V., Chagraoui, H., Lacout, C., Lecouedic, J. P., Rameau, P., Debili, N., Vainchenker, W. and Giraudier, S. (2005) Role for the nuclear factor kappa B pathway in transforming growth factor-beta1 production in idiopathic myelofibrosis: possible relationship with FK506 binding protein 51 overexpression. Cancer Res. 65, 3281-3289.
    • (2005) Cancer Res , vol.65 , pp. 3281-3289
    • Komura, E.1    Tonetti, C.2    Penard-Lacronique, V.3    Chagraoui, H.4    Lacout, C.5    Lecouedic, J.P.6    Rameau, P.7    Debili, N.8    Vainchenker, W.9    Giraudier, S.10
  • 91
    • 18744391391 scopus 로고    scopus 로고
    • Plunder and stowaways: Incorporation of cellular proteins by enveloped viruses
    • Cantin, R., Methot, S. and Tremblay, M. J. (2005) Plunder and stowaways: incorporation of cellular proteins by enveloped viruses. J. Virol. 79, 6577-6587.
    • (2005) J. Virol , vol.79 , pp. 6577-6587
    • Cantin, R.1    Methot, S.2    Tremblay, M.J.3
  • 93
    • 20744449661 scopus 로고    scopus 로고
    • 1.88 A crystal structure of the C domain of hCyP33: A novel domain of peptidyl-prolyl cis-trans isomerase
    • Wang, T., Yun, C. H., Gu, S. Y., Chang, W. R. and Liang, D. C. (2005) 1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase. Biochem. Biophys. Res. Commun. 333, 845-849.
    • (2005) Biochem. Biophys. Res. Commun , vol.333 , pp. 845-849
    • Wang, T.1    Yun, C.H.2    Gu, S.Y.3    Chang, W.R.4    Liang, D.C.5
  • 94
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E. K., Yuan, H. E. 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.2    Luban, J.3
  • 96
    • 8644286696 scopus 로고    scopus 로고
    • Target cell cyclophilin A modulates human immunodeficiency virus type 1 infectivity
    • Sokolskaja, E., Sayah, D. M. and Luban, J. (2004) Target cell cyclophilin A modulates human immunodeficiency virus type 1 infectivity. J. Virol. 78, 12800-12808.
    • (2004) J. Virol , vol.78 , pp. 12800-12808
    • Sokolskaja, E.1    Sayah, D.M.2    Luban, J.3
  • 98
    • 28944453311 scopus 로고    scopus 로고
    • Peptidyl prolyl cis/trans-isomerases: Comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates
    • Golbik, R., Yu, C., Weyher-Stingl, E., Huber, R., Moroder, L., Budisa, N. and Schiene-Fischer, C. (2005) Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates. Biochemistry 44, 16026-16034.
    • (2005) Biochemistry , vol.44 , pp. 16026-16034
    • Golbik, R.1    Yu, C.2    Weyher-Stingl, E.3    Huber, R.4    Moroder, L.5    Budisa, N.6    Schiene-Fischer, C.7
  • 99
    • 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
  • 100
    • 0033856956 scopus 로고    scopus 로고
    • Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics
    • Sich, C., Improta, S., Cowley, D. J., Guenet, C., Merly, J. P., Teufel, M. and Saudek, V. (2000) Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics. Eur. J. Biochem. 267, 5342-5355.
    • (2000) Eur. J. Biochem , vol.267 , pp. 5342-5355
    • Sich, C.1    Improta, S.2    Cowley, D.J.3    Guenet, C.4    Merly, J.P.5    Teufel, M.6    Saudek, V.7
  • 101
    • 0028091462 scopus 로고
    • The molecular replacement solution and X-ray refinement to 2.8 Å of a decameric complex of human cyclophilin A with the immunosuppressive drug cyclosporin, A
    • Pflugl, G. M., Kallen, J., Jansonius, J. N. and Walkinshaw, M. D. (1994) The molecular replacement solution and X-ray refinement to 2.8 Å of a decameric complex of human cyclophilin A with the immunosuppressive drug cyclosporin, A. J. Mol. Biol. 244, 385-409.
    • (1994) J. Mol. Biol , vol.244 , pp. 385-409
    • Pflugl, G.M.1    Kallen, J.2    Jansonius, J.N.3    Walkinshaw, M.D.4
  • 102
    • 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
  • 103
    • 0029982651 scopus 로고    scopus 로고
    • Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization
    • Zhao, Y. and Ke, H. (1996) Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry 35, 7356-7361.
    • (1996) Biochemistry , vol.35 , pp. 7356-7361
    • Zhao, Y.1    Ke, H.2
  • 104
    • 0038780573 scopus 로고    scopus 로고
    • Howard, B. R., Vajdos, F. F., Li, S., Sundquist, W. I. and Hill, C. P. (2003) Structural insights into the catalytic mechanism of cyclophilin, A. Nat. Struct. Biol. 10, 475-481.
    • Howard, B. R., Vajdos, F. F., Li, S., Sundquist, W. I. and Hill, C. P. (2003) Structural insights into the catalytic mechanism of cyclophilin, A. Nat. Struct. Biol. 10, 475-481.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.