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Volumn 70, Issue 18, 2013, Pages 3243-3275

Functional diversity and pharmacological profiles of the FKBPs and their complexes with small natural ligands

Author keywords

FK506; FKBP; PPIase; Rapamycin; Sirolimus; Tacrolimus

Indexed keywords

ANTIBIOTIC AGENT; ASCOMYCIN; EVEROLIMUS; FK 506 BINDING PROTEIN; IMMUNOSUPPRESSIVE AGENT; PIMECROLIMUS; PROTEIN FKBP12; PROTEIN VARIANT; RAPAMYCIN; RIDAFOROLIMUS; TACROLIMUS; TEMSIROLIMUS; UNCLASSIFIED DRUG; ZOTAROLIMUS;

EID: 84883448191     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1206-z     Document Type: Review
Times cited : (34)

References (278)
  • 2
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK-506 is a cis-trans peptidyl-prolyl isomerase
    • Harding MW, Galat A, Uehling DE, Schreiber SL (1989) A receptor for the immunosuppressant FK-506 is a cis-trans peptidyl-prolyl isomerase. Nature 341:761-763
    • (1989) Nature , vol.341 , pp. 761-763
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 3
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekerka JJ, Hung SHY, Poe M, Lin SC, Sigal NH (1989) A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 341:755-757
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekerka, J.J.1    Hung, S.H.Y.2    Poe, M.3    Lin, S.C.4    Sigal, N.H.5
  • 4
    • 2342529037 scopus 로고    scopus 로고
    • A note on clustering the functionally related paralogues and orthologues of proteins: A case of the FK506-binding proteins (FKBPs)
    • 1:CAS:528:DC%2BD2cXjvVGisb8%3D
    • Galat A (2004) A note on clustering the functionally related paralogues and orthologues of proteins: a case of the FK506-binding proteins (FKBPs). Comp Biol Chem 28:129-140
    • (2004) Comp Biol Chem , vol.28 , pp. 129-140
    • Galat, A.1
  • 5
    • 0023245677 scopus 로고
    • FK505, A novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics
    • 1:CAS:528:DyaL2sXmt1ylurc%3D
    • Kino T, Hatanaka H, Hashimoto M, Nishiyama M, Goto T, Okuhara M, Kohsaka M, Aoki H, Imanaka H (1987) FK505, A novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics. J Antibiot (Tokyo) 40:1249-1255
    • (1987) J Antibiot (Tokyo) , vol.40 , pp. 1249-1255
    • Kino, T.1    Hatanaka, H.2    Hashimoto, M.3    Nishiyama, M.4    Goto, T.5    Okuhara, M.6    Kohsaka, M.7    Aoki, H.8    Imanaka, H.9
  • 6
    • 0016713286 scopus 로고
    • Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization
    • 1:CAS:528:DyaE28Xis1eqsg%3D%3D
    • Sehgal SN, Baker H, Vezina C (1975) Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization. J Antibiot (Tokyo) 28:727-732
    • (1975) J Antibiot (Tokyo) , vol.28 , pp. 727-732
    • Sehgal, S.N.1    Baker, H.2    Vezina, C.3
  • 7
    • 0021164348 scopus 로고
    • Activity of rapamycin (AY-22,989) against transplanted tumors
    • 1:CAS:528:DyaL2cXmt1ahsLo%3D
    • Eng CP, Sehgal SN, Vezina C (1984) Activity of rapamycin (AY-22,989) against transplanted tumors. J Antibiot (Tokyo) 37:1231-1237
    • (1984) J Antibiot (Tokyo) , vol.37 , pp. 1231-1237
    • Eng, C.P.1    Sehgal, S.N.2    Vezina, C.3
  • 8
    • 0023708531 scopus 로고
    • FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. I. Taxonomy of the producing strain
    • 1:CAS:528:DyaL1MXhs12qs7o%3D
    • Hatanaka H, Iwami M, Kino T, Goto T, Okuhara M (1988) FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. I. Taxonomy of the producing strain. J Antibiot (Tokyo) 41:1586-1591
    • (1988) J Antibiot (Tokyo) , vol.41 , pp. 1586-1591
    • Hatanaka, H.1    Iwami, M.2    Kino, T.3    Goto, T.4    Okuhara, M.5
  • 9
    • 0023691846 scopus 로고
    • FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. II. Fermentation, isolation and physico-chemical and biological characteristics
    • 1:CAS:528:DyaL1MXhsVOntr4%3D
    • Hatanaka H, Kino T, Miyata S, Inamura N, Kuroda A, Goto T, Tanaka H, Okuhara M (1988) FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. II. Fermentation, isolation and physico-chemical and biological characteristics. J Antibiot (Tokyo) 41:1592-1601
    • (1988) J Antibiot (Tokyo) , vol.41 , pp. 1592-1601
    • Hatanaka, H.1    Kino, T.2    Miyata, S.3    Inamura, N.4    Kuroda, A.5    Goto, T.6    Tanaka, H.7    Okuhara, M.8
  • 10
    • 34548076410 scopus 로고    scopus 로고
    • In vitro metabolic study of temsirolimus: Preparation, isolation, and identification of the metabolites
    • 17540708 1:CAS:528:DC%2BD2sXpslKqsrg%3D
    • Cai P, Tsao R, Ruppen ME (2007) In vitro metabolic study of temsirolimus: preparation, isolation, and identification of the metabolites. Drug Metab Dispos 35:1554-1563
    • (2007) Drug Metab Dispos , vol.35 , pp. 1554-1563
    • Cai, P.1    Tsao, R.2    Ruppen, M.E.3
  • 11
    • 0038688097 scopus 로고    scopus 로고
    • Phase i and pharmacokinetic study of CCI-779, a novel cytostatic cell-cycle inhibitor, in combination with 5-fluorouracil and leucovorin in patients with advanced solid tumors
    • 12796032 1:STN:280:DC%2BD3s3mvFGmtg%3D%3D
    • Punt CJ, Boni J, Bruntsch U, Peters M, Thielert C (2003) Phase I and pharmacokinetic study of CCI-779, a novel cytostatic cell-cycle inhibitor, in combination with 5-fluorouracil and leucovorin in patients with advanced solid tumors. Ann Oncol 14:931-937
    • (2003) Ann Oncol , vol.14 , pp. 931-937
    • Punt, C.J.1    Boni, J.2    Bruntsch, U.3    Peters, M.4    Thielert, C.5
  • 13
    • 70349240297 scopus 로고    scopus 로고
    • Structural identification and characterization of potential degradants of zotarolimus on zotarolimus-coated drug-eluting stents
    • 19581067 1:CAS:528:DC%2BD1MXhtF2ht7fM
    • Chen Q, Zielinski D, Chen J, Nowak S, Zhou CC (2009) Structural identification and characterization of potential degradants of zotarolimus on zotarolimus-coated drug-eluting stents. J Pharm Biomed Anal 50:778-786
    • (2009) J Pharm Biomed Anal , vol.50 , pp. 778-786
    • Chen, Q.1    Zielinski, D.2    Chen, J.3    Nowak, S.4    Zhou, C.C.5
  • 14
    • 79955428464 scopus 로고    scopus 로고
    • Isolation and structure of homotemsirolimuses A, B, and C
    • 21438579 1:CAS:528:DC%2BC3MXjvVSitr0%3D
    • Kong F, Zhu T, Yu K, Pagano TG, Desai P, Radebaugh G, Fawzi M (2011) Isolation and structure of homotemsirolimuses A, B, and C. J Nat Prod 74:547-553
    • (2011) J Nat Prod , vol.74 , pp. 547-553
    • Kong, F.1    Zhu, T.2    Yu, K.3    Pagano, T.G.4    Desai, P.5    Radebaugh, G.6    Fawzi, M.7
  • 16
    • 80051668635 scopus 로고    scopus 로고
    • Targeting FKBP isoforms with small-molecule ligands
    • 21803654 1:CAS:528:DC%2BC3MXhtVaitr%2FM
    • Blackburn EA, Walkinshaw MD (2011) Targeting FKBP isoforms with small-molecule ligands. Curr Opin Pharmacol 11:365-371
    • (2011) Curr Opin Pharmacol , vol.11 , pp. 365-371
    • Blackburn, E.A.1    Walkinshaw, M.D.2
  • 17
    • 0028180772 scopus 로고
    • 15N NMR relaxation studies of the FK506 binding protein: Dynamic effects of ligand binding and implications for calcineurin recognition
    • 7512379 1:CAS:528:DyaK2cXitlyls70%3D
    • 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry 33:4093-4100
    • (1994) Biochemistry , vol.33 , pp. 4093-4100
    • Cheng, J.W.1    Lepre, C.A.2    Moore, J.M.3
  • 19
    • 0141748498 scopus 로고    scopus 로고
    • Energetic and structural analysis of the role of tryptophan 59 in FKBP12
    • 12600203 1:CAS:528:DC%2BD3sXptVSjtw%3D%3D
    • Fulton KF, Jackson SE, Buckle AM (2003) Energetic and structural analysis of the role of tryptophan 59 in FKBP12. Biochemistry 42:2364-2372
    • (2003) Biochemistry , vol.42 , pp. 2364-2372
    • Fulton, K.F.1    Jackson, S.E.2    Buckle, A.M.3
  • 20
    • 0027483193 scopus 로고
    • Chlamydia trachomatis Mip-like protein has peptidyl-prolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection
    • 7682281 1:CAS:528:DyaK3sXitlWns7c%3D
    • Lundemose AG, Kay JE, Pearce JH (1993) Chlamydia trachomatis Mip-like protein has peptidyl-prolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection. Mol Microbiol 7:777-783
    • (1993) Mol Microbiol , vol.7 , pp. 777-783
    • Lundemose, A.G.1    Kay, J.E.2    Pearce, J.H.3
  • 23
    • 44349186241 scopus 로고    scopus 로고
    • Functional drift of sequence attributes in the FK506-binding proteins (FKBPs)
    • 18412331 1:CAS:528:DC%2BD1cXks1Ontbk%3D
    • Galat A (2008) Functional drift of sequence attributes in the FK506-binding proteins (FKBPs). J Chem Inf Model 48:1118-1130
    • (2008) J Chem Inf Model , vol.48 , pp. 1118-1130
    • Galat, A.1
  • 32
    • 0242365676 scopus 로고    scopus 로고
    • Genome-scale approaches to resolving incongruence in molecular phylogenies
    • 14574403 1:CAS:528:DC%2BD3sXotlWqsbc%3D
    • Rokas A, Williams BL, King N, Carroll SB (2003) Genome-scale approaches to resolving incongruence in molecular phylogenies. Nature 425:798-804
    • (2003) Nature , vol.425 , pp. 798-804
    • Rokas, A.1    Williams, B.L.2    King, N.3    Carroll, S.B.4
  • 34
    • 0033869659 scopus 로고    scopus 로고
    • Sequence diversification of the FK506-binding proteins in several different genomes
    • 10931176 1:CAS:528:DC%2BD3cXmtVeisbg%3D
    • Galat A (2000) Sequence diversification of the FK506-binding proteins in several different genomes. Eur J Biochem 267:4945-4959
    • (2000) Eur J Biochem , vol.267 , pp. 4945-4959
    • Galat, A.1
  • 35
    • 77957357258 scopus 로고    scopus 로고
    • Molecular aspects of cyclophilins mediating therapeutic actions of their ligands
    • 20602248 1:CAS:528:DC%2BC3cXhtFOrtbzI
    • Galat A, Bua J (2010) Molecular aspects of cyclophilins mediating therapeutic actions of their ligands. Cell Mol Life Sci 67:3467-3488
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3467-3488
    • Galat, A.1    Bua, J.2
  • 36
    • 33751082083 scopus 로고    scopus 로고
    • Structural comparison of oxidized and reduced FKBP13 from Arabidopsis thaliana
    • 17029235 1:CAS:528:DC%2BD28Xht1eisLrL
    • Gopalan G, He Z, Battaile KP, Luan S, Swaminathan K (2006) Structural comparison of oxidized and reduced FKBP13 from Arabidopsis thaliana. Proteins 65:789-795
    • (2006) Proteins , vol.65 , pp. 789-795
    • Gopalan, G.1    He, Z.2    Battaile, K.P.3    Luan, S.4    Swaminathan, K.5
  • 37
    • 33750603228 scopus 로고    scopus 로고
    • Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires
    • 16995943
    • Pemberton TJ (2006) Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires. BMC Genomics 7:244
    • (2006) BMC Genomics , vol.7 , pp. 244
    • Pemberton, T.J.1
  • 38
    • 34447281117 scopus 로고    scopus 로고
    • Cloning, expression and characterization of FKB-6, the sole large TPR-containing immunophilin from C. elegans
    • 17610845 1:CAS:528:DC%2BD2sXnslSqsLc%3D
    • Richardson JM, Dornan J, Opamawutthikul M, Bruce S, Page AP, Walkinshaw MD (2007) Cloning, expression and characterization of FKB-6, the sole large TPR-containing immunophilin from C. elegans. Biochem Biophys Res Commun 360:566-572
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 566-572
    • Richardson, J.M.1    Dornan, J.2    Opamawutthikul, M.3    Bruce, S.4    Page, A.P.5    Walkinshaw, M.D.6
  • 40
    • 1442286922 scopus 로고    scopus 로고
    • A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing
    • 14981505 1:CAS:528:DC%2BD2cXhsFajtL0%3D
    • Kuzuhara T, Horikoshi M (2004) A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing. Nat Struct Mol Biol 11:275-283
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 275-283
    • Kuzuhara, T.1    Horikoshi, M.2
  • 41
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • 16959570 1:CAS:528:DC%2BD28XpvVKitbY%3D
    • Nelson CJ, Santos-Rosa H, Kouzarides T (2006) Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126:905-916
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 42
    • 70349298295 scopus 로고    scopus 로고
    • Fpr3 and Zip3 ensure that initiation of meiotic recombination precedes chromosome synapsis in budding yeast
    • 19765989 1:CAS:528:DC%2BD1MXhtF2iu7fL
    • Macqueen AJ, Roeder GS (2009) Fpr3 and Zip3 ensure that initiation of meiotic recombination precedes chromosome synapsis in budding yeast. Curr Biol 19:1519-1526
    • (2009) Curr Biol , vol.19 , pp. 1519-1526
    • Macqueen, A.J.1    Roeder, G.S.2
  • 43
    • 25144520389 scopus 로고    scopus 로고
    • The FK506 binding protein Fpr3 counteracts protein phosphatase 1 to maintain meiotic recombination checkpoint activity
    • 16179256 1:CAS:528:DC%2BD2MXhtVOrurnE
    • Hochwagen A, Tham WH, Brar GA, Amon A (2005) The FK506 binding protein Fpr3 counteracts protein phosphatase 1 to maintain meiotic recombination checkpoint activity. Cell 122:861-873
    • (2005) Cell , vol.122 , pp. 861-873
    • Hochwagen, A.1    Tham, W.H.2    Brar, G.A.3    Amon, A.4
  • 44
    • 63049132799 scopus 로고    scopus 로고
    • The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress
    • 18946088 1:CAS:528:DC%2BD1MXht1Sktbk%3D
    • Padmanabhan N, Fichtner L, Dickmanns A, Ficner R, Schulz JB, Braus GH (2009) The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress. Mol Biol Cell 20:68-77
    • (2009) Mol Biol Cell , vol.20 , pp. 68-77
    • Padmanabhan, N.1    Fichtner, L.2    Dickmanns, A.3    Ficner, R.4    Schulz, J.B.5    Braus, G.H.6
  • 46
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • 3656427 1:CAS:528:DyaL2sXlt12gur0%3D
    • Cornette JL, Cease KB, Margalit H, Spouge JL, Berzofsky JA, DeLisi C (1987) Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J Mol Biol 195:659-685
    • (1987) J Mol Biol , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    Delisi, C.6
  • 47
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • 15497498 1:CAS:528:DC%2BD2cXntVGqtrs%3D
    • Smith DF (2004) Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 9:109-121
    • (2004) Cell Stress Chaperones , vol.9 , pp. 109-121
    • Smith, D.F.1
  • 48
    • 68149099512 scopus 로고    scopus 로고
    • On transversal hydrophobicity of some proteins and their modules
    • 19569645 1:CAS:528:DC%2BD1MXnvFWkurc%3D
    • Galat A (2009) On transversal hydrophobicity of some proteins and their modules. J Chem Inf Model 49:1821-1830
    • (2009) J Chem Inf Model , vol.49 , pp. 1821-1830
    • Galat, A.1
  • 49
    • 33748796612 scopus 로고    scopus 로고
    • Involvement of some large immunophilins and their ligands in the protection and regeneration of neurons: A hypothetical mode of action
    • 16996313 1:CAS:528:DC%2BD28XhtVSisr%2FF
    • Galat A (2006) Involvement of some large immunophilins and their ligands in the protection and regeneration of neurons: a hypothetical mode of action. Comput Biol Chem 30:348-359
    • (2006) Comput Biol Chem , vol.30 , pp. 348-359
    • Galat, A.1
  • 50
    • 4544271500 scopus 로고    scopus 로고
    • Association of immunophilins with mammalian TRPC channels
    • 15199065 1:CAS:528:DC%2BD2cXmvFenu74%3D
    • Sinkins WG, Goel M, Estacion M, Schilling WP (2004) Association of immunophilins with mammalian TRPC channels. J Biol Chem 279:34521-34529
    • (2004) J Biol Chem , vol.279 , pp. 34521-34529
    • Sinkins, W.G.1    Goel, M.2    Estacion, M.3    Schilling, W.P.4
  • 52
    • 0034980394 scopus 로고    scopus 로고
    • Two structures of cyclophilin 40: Folding and fidelity of the TPR domains
    • 11377203 1:CAS:528:DC%2BD3MXjslCisb8%3D
    • Taylor P, Dornan J, Carrello A, Minchin RF, Ratajczak T, Walkinshaw MD (2001) Two structures of cyclophilin 40: folding and fidelity of the TPR domains. Structure 9:431-438
    • (2001) Structure , vol.9 , pp. 431-438
    • Taylor, P.1    Dornan, J.2    Carrello, A.3    Minchin, R.F.4    Ratajczak, T.5    Walkinshaw, M.D.6
  • 53
    • 33751035450 scopus 로고    scopus 로고
    • Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plant ABC transporters
    • 17045295 1:CAS:528:DC%2BD28Xht1ersb7I
    • Granzin J, Eckhoff A, Weiergraber OH (2006) Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters. J Mol Biol 364:799-809
    • (2006) J Mol Biol , vol.364 , pp. 799-809
    • Granzin, J.1    Eckhoff, A.2    Weiergraber, O.H.3
  • 54
    • 34250787537 scopus 로고    scopus 로고
    • Anchoring the 26S proteasome to the organellar membrane by FKBP38
    • 17573772 1:CAS:528:DC%2BD2sXmvF2qsro%3D
    • Nakagawa T, Shirane M, Iemura SI, Natsuame T, Nakayama KI (2007) Anchoring the 26S proteasome to the organellar membrane by FKBP38. Genes Cells 12:709-719
    • (2007) Genes Cells , vol.12 , pp. 709-719
    • Nakagawa, T.1    Shirane, M.2    Iemura, S.I.3    Natsuame, T.4    Nakayama, K.I.5
  • 55
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • 7678431
    • van Duyne GD, Standaert RF, Karplus PA, Schreiber SLS, 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.S.4    Clardy, J.5
  • 58
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • 8662507 1:CAS:528:DyaK28Xkt1Crs7k%3D
    • Choi J, Chen J, Schreiber SL, Clardy J (1996) Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science 273:239-242
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 59
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type i TGFβ receptor in complex with FKBP12
    • 10025408 1:CAS:528:DyaK1MXht1eqs7Y%3D
    • Huse M, Chen YG, Massagué J, Kuriyan J (1999) Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12. Cell 96:425-436
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massagué, J.3    Kuriyan, J.4
  • 60
    • 0034796457 scopus 로고    scopus 로고
    • The TGFβ receptor activation process: An inhibitor- to substrate-binding switch
    • 11583628 1:CAS:528:DC%2BD3MXnslGmt7w%3D
    • Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massagué J (2001) The TGFβ receptor activation process: an inhibitor- to substrate-binding switch. Mol Cell 8:671-682
    • (2001) Mol Cell , vol.8 , pp. 671-682
    • Huse, M.1    Muir, T.W.2    Xu, L.3    Chen, Y.G.4    Kuriyan, J.5    Massagué, J.6
  • 61
    • 2942593899 scopus 로고    scopus 로고
    • 3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
    • 15159550 1:CAS:528:DC%2BD2cXkvFOmsLg%3D
    • Wu B, Li R, Liu Y, Lou Z, Ding Y, Shu C, Ye S, Bartlam M, Shen B, 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, R.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
  • 62
    • 0345144024 scopus 로고    scopus 로고
    • Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complex
    • 12538866 1:CAS:528:DC%2BD3sXhtF2gs74%3D
    • Sinars C, Cheung-Flynn J, Rimerman RA, Scammell JG, Smith DF, Clardy J (2003) Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complex. Proc Natl Acad Sci USA 100:868-873
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 868-873
    • Sinars, C.1    Cheung-Flynn, J.2    Rimerman, R.A.3    Scammell, J.G.4    Smith, D.F.5    Clardy, J.6
  • 63
    • 79957986223 scopus 로고    scopus 로고
    • Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90
    • 21636895 1:CAS:528:DC%2BC3MXmvFyrsLg%3D
    • Bracher A, Kozany C, Thost AK, Hausch F (2011) Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90. Acta Crystallogr D Biol Crystallogr 67:549-559
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 549-559
    • Bracher, A.1    Kozany, C.2    Thost, A.K.3    Hausch, F.4
  • 65
    • 80054722795 scopus 로고    scopus 로고
    • Common structural traits for cystine knot domain of the TGFβ superfamily of proteins and three-fingered ectodomain of their cellular receptors
    • 21369710 1:CAS:528:DC%2BC3MXht1eis77N
    • Galat A (2011) Common structural traits for cystine knot domain of the TGFβ superfamily of proteins and three-fingered ectodomain of their cellular receptors. Cell Mol Life Sci 68:3437-3451
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3437-3451
    • Galat, A.1
  • 66
    • 0025035782 scopus 로고
    • Substrate specificity for the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics
    • 1:CAS:528:DyaK3cXkvFersbk%3D
    • Albers MW, Walsh CT, Schreiber SL (1990) Substrate specificity for the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics. J Org Chem 55:4984-4986
    • (1990) J Org Chem , vol.55 , pp. 4984-4986
    • Albers, M.W.1    Walsh, C.T.2    Schreiber, S.L.3
  • 67
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • 9371805 1:CAS:528:DyaK2sXnvFamsbw%3D
    • 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
  • 68
    • 0035028813 scopus 로고    scopus 로고
    • Protein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells
    • 11313484 1:CAS:528:DC%2BD3MXjtF2jtrY%3D
    • Fair K, Anderson M, Bulanova E, Mi H, Tropschug M, Diaz MO (2001) Protein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells. Mol Cell Biol 21:3589-3597
    • (2001) Mol Cell Biol , vol.21 , pp. 3589-3597
    • Fair, K.1    Anderson, M.2    Bulanova, E.3    Mi, H.4    Tropschug, M.5    Diaz, M.O.6
  • 69
    • 77953912031 scopus 로고    scopus 로고
    • Pro Isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression
    • 20541251 1:CAS:528:DC%2BC3cXovFartbY%3D
    • Wang Z, Song J, Milne TA, Wang GG, Li H, Allis CD, Patel DJ (2010) Pro Isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell 141:1183-1194
    • (2010) Cell , vol.141 , pp. 1183-1194
    • Wang, Z.1    Song, J.2    Milne, T.A.3    Wang, G.G.4    Li, H.5    Allis, C.D.6    Patel, D.J.7
  • 70
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • 18641628 1:CAS:528:DC%2BD1cXoslClsb8%3D
    • Goodey NM, Benkovic SJ (2008) Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 4:474-482
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 71
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • 18075577 1:CAS:528:DC%2BD2sXhsVaqtr%2FP
    • Kuriyan J, Eisenberg D (2007) The origin of protein interactions and allostery in colocalization. Nature 450:983-990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 72
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • 1715244 1:CAS:528:DyaK3MXlsV2qu7w%3D
    • Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL (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
  • 73
    • 0026748870 scopus 로고
    • Cyclosporin A, FK506, and rapamycin: Pharmacologic probes of lymphocyte signal transduction
    • 1:CAS:528:DyaK38XktVSju78%3D
    • Sigal NH, Dumont F (1992) Cyclosporin A, FK506, and rapamycin: pharmacologic probes of lymphocyte signal transduction. Ann Rev Immunol 10:519-560
    • (1992) Ann Rev Immunol , vol.10 , pp. 519-560
    • Sigal, N.H.1    Dumont, F.2
  • 74
    • 0026503434 scopus 로고
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A
    • 1373887 1:CAS:528:DyaK38Xkt1SisLo%3D
    • Fruman DA, Klee CB, Bierer BE, Burakoff SJ (1992) Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A. Proc Natl Acad Sci USA 89:3686-3690
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3686-3690
    • Fruman, D.A.1    Klee, C.B.2    Bierer, B.E.3    Burakoff, S.J.4
  • 76
    • 34247573902 scopus 로고    scopus 로고
    • Graft-versus-host disease
    • 17438575 1:CAS:528:DC%2BD2sXksFeksrY%3D
    • Shlomchik WD (2007) Graft-versus-host disease. Nat Rev Immunol 7:340-352
    • (2007) Nat Rev Immunol , vol.7 , pp. 340-352
    • Shlomchik, W.D.1
  • 77
    • 28444486367 scopus 로고    scopus 로고
    • Stem cell niche: Structure and function
    • 16212509 1:CAS:528:DC%2BD2MXhtlektbvE
    • Li L, Xie T (2005) Stem cell niche: structure and function. Annu Rev Cell Dev Biol 21:605-631
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 605-631
    • Li, L.1    Xie, T.2
  • 78
    • 0344441706 scopus 로고    scopus 로고
    • Structure of NFAT bound to DNA as a monomer
    • 14643663 1:CAS:528:DC%2BD3sXptF2qurY%3D
    • Stroud JC, Chen L (2003) Structure of NFAT bound to DNA as a monomer. J Mol Biol 334:1009-1022
    • (2003) J Mol Biol , vol.334 , pp. 1009-1022
    • Stroud, J.C.1    Chen, L.2
  • 79
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • 1715094 1:CAS:528:DyaK3MXlsl2hsr8%3D
    • Heitman J, Movva NR, Hall MN (1991) Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 253:905-909
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 81
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • 7518356 1:CAS:528:DyaK2cXlvFOhu7Y%3D
    • Sabatini DM, Erdjument-Bromage H, Lui M, Tempst P, Snyder SH (1994) RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78:35-43
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 83
    • 0026092585 scopus 로고
    • Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl-prolyl cis-trans isomerase related to human FK506-binding protein
    • 1996117 1:CAS:528:DyaK3MXltlWkt7c%3D
    • Koltin Y, Faucette L, Bergsma DJ, Levy MA, Cafferkey R, Koser PL, Johnson RK, Livi GP (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    Levy, M.A.4    Cafferkey, R.5    Koser, P.L.6    Johnson, R.K.7    Livi, G.P.8
  • 84
    • 0027382875 scopus 로고
    • Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity
    • 8413204 1:CAS:528:DyaK2cXksFCgsQ%3D%3D
    • Cafferkey R, Young PR, McLaughlin MM, Bergsma DJ, Koltin Y, Sathe GM, Faucette L, Eng WK, Johnson RK, Livi GP (1993) Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity. Mol Cell Biol 13:6012-6023
    • (1993) Mol Cell Biol , vol.13 , pp. 6012-6023
    • Cafferkey, R.1    Young, P.R.2    McLaughlin, M.M.3    Bergsma, D.J.4    Koltin, Y.5    Sathe, G.M.6    Faucette, L.7    Eng, W.K.8    Johnson, R.K.9    Livi, G.P.10
  • 85
    • 0031596416 scopus 로고    scopus 로고
    • Rapamycin induces the Go program of transcriptional repression in yeast by interfering with the TOR signaling pathway
    • Zagaroza D, Ghavidel A, Heitman J, Schultz MC (1998) Rapamycin induces the Go program of transcriptional repression in yeast by interfering with the TOR signaling pathway. Mol Cell Biol 18:4463-4470
    • (1998) Mol Cell Biol , vol.18 , pp. 4463-4470
    • Zagaroza, D.1    Ghavidel, A.2    Heitman, J.3    Schultz, M.C.4
  • 87
    • 0031028176 scopus 로고    scopus 로고
    • The immunosuppressant FK506 and its nonimmunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein
    • 8980772 1:CAS:528:DyaK2sXhsVWisQ%3D%3D
    • Odom A, Del Poeta M, Perfect J, Heitman J (1997) The immunosuppressant FK506 and its nonimmunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein. Antimicrob Agents Chemother 41:156-161
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 156-161
    • Odom, A.1    Del Poeta, M.2    Perfect, J.3    Heitman, J.4
  • 88
    • 73749087279 scopus 로고    scopus 로고
    • Elucidating the Candida albicans calcineurin signaling cascade controlling stress response and virulence
    • 19755168 1:CAS:528:DC%2BC3cXnsFWqtg%3D%3D
    • Reedy JL, Filler SG, Heitman J (2010) Elucidating the Candida albicans calcineurin signaling cascade controlling stress response and virulence. Fungal Genet Biol 47:107-116
    • (2010) Fungal Genet Biol , vol.47 , pp. 107-116
    • Reedy, J.L.1    Filler, S.G.2    Heitman, J.3
  • 89
    • 34249673350 scopus 로고    scopus 로고
    • NFAT signaling and the invention of vertebrates
    • 17493814 1:CAS:528:DC%2BD2sXmtVOms7w%3D
    • Wu H, Peisley A, Graef IA, Crabtree GR (2007) NFAT signaling and the invention of vertebrates. Trends Cell Biol 17:251-260
    • (2007) Trends Cell Biol , vol.17 , pp. 251-260
    • Wu, H.1    Peisley, A.2    Graef, I.A.3    Crabtree, G.R.4
  • 90
    • 79961154489 scopus 로고    scopus 로고
    • Genome-wide screening for genes associated with FK506 sensitivity in fission yeast
    • 21850271 1:CAS:528:DC%2BC3MXhtFajtL7M
    • Ma Y, Jiang W, Liu Q, Ryuko S, Kuno T (2011) Genome-wide screening for genes associated with FK506 sensitivity in fission yeast. PLoS One 6:e23422
    • (2011) PLoS One , vol.6 , pp. 23422
    • Ma, Y.1    Jiang, W.2    Liu, Q.3    Ryuko, S.4    Kuno, T.5
  • 91
    • 15544376264 scopus 로고    scopus 로고
    • Regulation of leucine uptake by tor1+ in Schizosaccharomyces pombe is sensitive to rapamycin
    • 15466417 1:CAS:528:DC%2BD2MXjtVOmtbw%3D
    • Weisman R, Roitburg I, Nahari T, Kupiec M (2005) Regulation of leucine uptake by tor1+ in Schizosaccharomyces pombe is sensitive to rapamycin. Genetics 169:539-550
    • (2005) Genetics , vol.169 , pp. 539-550
    • Weisman, R.1    Roitburg, I.2    Nahari, T.3    Kupiec, M.4
  • 92
    • 0042823564 scopus 로고    scopus 로고
    • The fission yeast TOR proteins and the rapamycin response: An unexpected tale
    • 14560953 1:CAS:528:DC%2BD3sXpt1Sktbc%3D
    • Weisman R (2004) The fission yeast TOR proteins and the rapamycin response: an unexpected tale. Curr Top Microbiol Immunol 279:85-95
    • (2004) Curr Top Microbiol Immunol , vol.279 , pp. 85-95
    • Weisman, R.1
  • 95
    • 9444266459 scopus 로고    scopus 로고
    • Altered excitation-contraction coupling with skeletal muscle specific FKBP12 deficiency
    • 15289441 1:CAS:528:DC%2BD2cXotFGiur4%3D
    • Tang W, Ingalls CP, Durham WJ, Snider J, Reid MB, Wu G, Matzuk MM, Hamilton SL (2004) Altered excitation-contraction coupling with skeletal muscle specific FKBP12 deficiency. FASEB J 18:1597-1599
    • (2004) FASEB J , vol.18 , pp. 1597-1599
    • Tang, W.1    Ingalls, C.P.2    Durham, W.J.3    Snider, J.4    Reid, M.B.5    Wu, G.6    Matzuk, M.M.7    Hamilton, S.L.8
  • 96
    • 76149123239 scopus 로고    scopus 로고
    • FKBP12.6-knockout mice display hyperinsulinemia and resistance to high-fat diet-induced hyperglycemia
    • 19805579 1:CAS:528:DC%2BC3cXhs1Ghur8%3D
    • Chen Z, Li Z, Wei B, Yin W, Xu T, Kotlikoff MI, Ji G (2010) FKBP12.6-knockout mice display hyperinsulinemia and resistance to high-fat diet-induced hyperglycemia. FASEB J 24:357-363
    • (2010) FASEB J , vol.24 , pp. 357-363
    • Chen, Z.1    Li, Z.2    Wei, B.3    Yin, W.4    Xu, T.5    Kotlikoff, M.I.6    Ji, G.7
  • 98
    • 84856693079 scopus 로고    scopus 로고
    • Inhibition of CaMKII phosphorylation of RyR2 prevents induction of atrial fibrillation in FKBP12.6 knockout mice
    • 22158709 1:CAS:528:DC%2BC38XhsVertL4%3D
    • Li N, Wang T, Wang W, Cutler MJ, Wang Q, Voigt N, Rosenbaum DS, Dobrev D, Wehrens XH (2012) Inhibition of CaMKII phosphorylation of RyR2 prevents induction of atrial fibrillation in FKBP12.6 knockout mice. Circ Res 110:465-470
    • (2012) Circ Res , vol.110 , pp. 465-470
    • Li, N.1    Wang, T.2    Wang, W.3    Cutler, M.J.4    Wang, Q.5    Voigt, N.6    Rosenbaum, D.S.7    Dobrev, D.8    Wehrens, X.H.9
  • 99
    • 0028108801 scopus 로고
    • Specific interaction of type i receptors of the TGFβ family with the immunophilin FKBP12
    • 7518616 1:CAS:528:DyaK2cXlt1Kjtrw%3D
    • Wang T, Donahoe PK, Zervos AS (1994) Specific interaction of type I receptors of the TGFβ family with the immunophilin FKBP12. Science 265:674-676
    • (1994) Science , vol.265 , pp. 674-676
    • Wang, T.1    Donahoe, P.K.2    Zervos, A.S.3
  • 100
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGFβ receptor inhibition by FKBP12
    • 9233797 1:CAS:528:DyaK2sXkslShur8%3D
    • Chen YG, Liu F, Massagué J (1997) Mechanism of TGFβ receptor inhibition by FKBP12. EMBO J 16:3866-3876
    • (1997) EMBO J , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massagué, J.3
  • 101
    • 77957735242 scopus 로고    scopus 로고
    • The dawn of developmental signaling in the metazoa
    • 19903747 1:CAS:528:DC%2BC38Xht1KksL7F
    • Richards GS, Degnan BM (2009) The dawn of developmental signaling in the metazoa. Cold Spring Harb Symp Quant Biol 74:81-90
    • (2009) Cold Spring Harb Symp Quant Biol , vol.74 , pp. 81-90
    • Richards, G.S.1    Degnan, B.M.2
  • 103
    • 53149099360 scopus 로고    scopus 로고
    • Molecular mechanisms of TGFβ receptor-triggered signaling cascades rapidly induced by the calcineurin inhibitors cyclosporin A and FK506
    • Akool el-S, Doller A, Babelova A, Tsalastra W, Moreth K, Schaefer L, Pfeilschifter J, Eberhardt W (2008) Molecular mechanisms of TGFβ receptor-triggered signaling cascades rapidly induced by the calcineurin inhibitors cyclosporin A and FK506. J Immunol 181:2831-2845
    • (2008) J Immunol , vol.181 , pp. 2831-2845
    • El-S, A.1    Doller, A.2    Babelova, A.3    Tsalastra, W.4    Moreth, K.5    Schaefer, L.6    Pfeilschifter, J.7    Eberhardt, W.8
  • 105
    • 0036904895 scopus 로고    scopus 로고
    • Genetic analysis of the mammalian transforming growth factor-β superfamily
    • 12466190 1:CAS:528:DC%2BD38XpvVSntLc%3D
    • Chang H, Brown CW, Matzuk MM (2002) Genetic analysis of the mammalian transforming growth factor-β superfamily. Endocr Rev 23:787-823
    • (2002) Endocr Rev , vol.23 , pp. 787-823
    • Chang, H.1    Brown, C.W.2    Matzuk, M.M.3
  • 106
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: From dissemination to organ-specific colonization
    • 19308067 1:CAS:528:DC%2BD1MXjsFSrsr4%3D
    • Nguyen DX, Bos PD, Massagué J (2009) Metastasis: from dissemination to organ-specific colonization. Nat Rev Cancer 9:274-284
    • (2009) Nat Rev Cancer , vol.9 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 107
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • 20961976 1:CAS:528:DC%2BC3cXhsFagtrbM
    • Lanner JT, Georgiou DK, Joshi AD, Hamilton SL (2010) Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harb Perspect Biol 2:a003996
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. 003996
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 108
    • 0030784252 scopus 로고    scopus 로고
    • FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain
    • 9346894 1:CAS:528:DyaK2sXnt12mu7Y%3D
    • Cameron AM, Nucifora FC Jr, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH (1997) FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain. J Biol Chem 272:27582-27588
    • (1997) J Biol Chem , vol.272 , pp. 27582-27588
    • Cameron, A.M.1    Nucifora, Jr.F.C.2    Fung, E.T.3    Livingston, D.J.4    Aldape, R.A.5    Ross, C.A.6    Snyder, S.H.7
  • 109
  • 110
    • 0027434403 scopus 로고
    • On the localization of FKBP25 in T-lymphocytes
    • 8422914
    • Rivière S, Ménez A, Galat A (1993) On the localization of FKBP25 in T-lymphocytes. FEBS Lett 315:247-251
    • (1993) FEBS Lett , vol.315 , pp. 247-251
    • Rivière, S.1    Ménez, A.2    Galat, A.3
  • 111
    • 0027296619 scopus 로고
    • The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin
    • 7689229 1:CAS:528:DyaK3sXlslKjtr8%3D
    • Jin YJ, Burakoff SJ (1993) The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin. Proc Natl Acad Sci USA 90:7769-7773
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7769-7773
    • Jin, Y.J.1    Burakoff, S.J.2
  • 112
    • 0034254789 scopus 로고    scopus 로고
    • Mammalian FKBP25 and its associated proteins
    • 10900128 1:CAS:528:DC%2BD3cXkvVKlurY%3D
    • Leclercq M, Vinci F, Galat A (2000) Mammalian FKBP25 and its associated proteins. Arch Biochem Biophys 380:20-28
    • (2000) Arch Biochem Biophys , vol.380 , pp. 20-28
    • Leclercq, M.1    Vinci, F.2    Galat, A.3
  • 113
    • 0035801704 scopus 로고    scopus 로고
    • The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor, YY1
    • 11532945 1:CAS:528:DC%2BD3MXnt1CmtLk%3D
    • Yang WM, Yao YL, Seto E (2001) The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor, YY1. EMBO J 20:4814-4825
    • (2001) EMBO J , vol.20 , pp. 4814-4825
    • Yang, W.M.1    Yao, Y.L.2    Seto, E.3
  • 114
    • 0142211208 scopus 로고    scopus 로고
    • The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity
    • 12920132 1:CAS:528:DC%2BD3sXot1als7k%3D
    • Yao YL, Yang WM (2003) The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity. J Biol Chem 278:42560-42568
    • (2003) J Biol Chem , vol.278 , pp. 42560-42568
    • Yao, Y.L.1    Yang, W.M.2
  • 116
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • 14654843 1:CAS:528:DC%2BD3sXpsVejtrg%3D
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M (2003) Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426:570-574
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 119
    • 23744483154 scopus 로고    scopus 로고
    • Multiple myeloma oncogene 1 (MUM1)/interferon regulatory factor 4 (IRF4) upregulates monokine induced by interferon-gamma (MIG) gene expression in B-cell malignancy
    • 15959530 1:CAS:528:DC%2BD2MXmtlSjsL4%3D
    • Uranishi M, Iida S, Sanda T, Ishida T, Tajima E, Ito M, Komatsu H, Inagaki H, Ueda R (2005) Multiple myeloma oncogene 1 (MUM1)/interferon regulatory factor 4 (IRF4) upregulates monokine induced by interferon-gamma (MIG) gene expression in B-cell malignancy. Leukemia 19:1471-1478
    • (2005) Leukemia , vol.19 , pp. 1471-1478
    • Uranishi, M.1    Iida, S.2    Sanda, T.3    Ishida, T.4    Tajima, E.5    Ito, M.6    Komatsu, H.7    Inagaki, H.8    Ueda, R.9
  • 120
    • 34250364576 scopus 로고    scopus 로고
    • Loss of secretory pathway FK506-binding proteins results in cold-sensitive lethality and associate extracellular matrix defects in the nematode Caenorhabditis elegans
    • 17339317 1:CAS:528:DC%2BD2sXksVSitL8%3D
    • Winter AD, Eschenlauer SC, McCormack G, Page AP (2007) Loss of secretory pathway FK506-binding proteins results in cold-sensitive lethality and associate extracellular matrix defects in the nematode Caenorhabditis elegans. J Biol Chem 282:12813-12821
    • (2007) J Biol Chem , vol.282 , pp. 12813-12821
    • Winter, A.D.1    Eschenlauer, S.C.2    McCormack, G.3    Page, A.P.4
  • 121
    • 84863315705 scopus 로고    scopus 로고
    • The Caenorhabditis elegans parvulin gene subfamily and their expression under cold or heat stress along with the fkb subfamily
    • 22683625 1:CAS:528:DC%2BC38XptlWqsbc%3D
    • Fasseas MK, Dimou M, Katinakis P (2012) The Caenorhabditis elegans parvulin gene subfamily and their expression under cold or heat stress along with the fkb subfamily. Biochem Biophys Res Commun 423:520-525
    • (2012) Biochem Biophys Res Commun , vol.423 , pp. 520-525
    • Fasseas, M.K.1    Dimou, M.2    Katinakis, P.3
  • 123
    • 33846444710 scopus 로고    scopus 로고
    • The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity
    • 17223077 1:CAS:528:DC%2BD2sXhtVClt7c%3D
    • Wang Y, Han R, Wu D, Li J, Chen C, Ma H, Mi H (2007) The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity. Biochem Biophys Res Commun 354:315-320
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 315-320
    • Wang, Y.1    Han, R.2    Wu, D.3    Li, J.4    Chen, C.5    Ma, H.6    Mi, H.7
  • 125
    • 0035980771 scopus 로고    scopus 로고
    • Identification and genetic mapping of the mouse Fkbp9 gene encoding a new member of FK506-binding protein family
    • 11710534 1:CAS:528:DC%2BD3MXot12mtLk%3D
    • Jo D, Lyu MS, Cho EG, Park D, Kozak CA, Kim MG (2001) Identification and genetic mapping of the mouse Fkbp9 gene encoding a new member of FK506-binding protein family. Mol Cells 12:272-275
    • (2001) Mol Cells , vol.12 , pp. 272-275
    • Jo, D.1    Lyu, M.S.2    Cho, E.G.3    Park, D.4    Kozak, C.A.5    Kim, M.G.6
  • 126
    • 0036267502 scopus 로고    scopus 로고
    • Genomic organization of mouse and human 65-kDa FK506-binding protein genes and evolution of the FKBP multigene family
    • 12036304 1:CAS:528:DC%2BD38XktVegsrg%3D
    • Patterson CE, Gao J, Rooney AP, Davis EC (2002) Genomic organization of mouse and human 65-kDa FK506-binding protein genes and evolution of the FKBP multigene family. Genomics 79:881-889
    • (2002) Genomics , vol.79 , pp. 881-889
    • Patterson, C.E.1    Gao, J.2    Rooney, A.P.3    Davis, E.C.4
  • 127
    • 57649134970 scopus 로고    scopus 로고
    • The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens
    • 18786928 1:CAS:528:DC%2BD1cXhtlCjsb3M
    • Ishikawa Y, Vranka J, Wirz J, Nagata K, Bachinger HP (2008) The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J Biol Chem 283:31584-31590
    • (2008) J Biol Chem , vol.283 , pp. 31584-31590
    • Ishikawa, Y.1    Vranka, J.2    Wirz, J.3    Nagata, K.4    Bachinger, H.P.5
  • 128
    • 29144462565 scopus 로고    scopus 로고
    • Developmental regulation and coordinate reexpression of FKBP65 with extracellular matrix proteins after lung injury suggest a specialized function for this endoplasmic reticulum immunophilin
    • 16333983 1:CAS:528:DC%2BD2MXhtlWgsr7N
    • Patterson CE, Abrams WR, Wolter NE, Rosenbloom J, Davis EC (2005) Developmental regulation and coordinate reexpression of FKBP65 with extracellular matrix proteins after lung injury suggest a specialized function for this endoplasmic reticulum immunophilin. Cell Stress Chaperones 10:285-295
    • (2005) Cell Stress Chaperones , vol.10 , pp. 285-295
    • Patterson, C.E.1    Abrams, W.R.2    Wolter, N.E.3    Rosenbloom, J.4    Davis, E.C.5
  • 129
    • 77956781051 scopus 로고    scopus 로고
    • Crystal structure of the three FK506 binding protein domains of wheat FKBP73: Evidence for a unique wFK73-2 domain
    • 20306145 1:CAS:528:DC%2BC3cXntlCkuro%3D
    • Unger T, Dym O, Albeck S, Jacobovitch Y, Bernehim R, Marom D, Pisanty O, Breiman A (2010) Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73-2 domain. J Struct Funct Genomics 11:113-123
    • (2010) J Struct Funct Genomics , vol.11 , pp. 113-123
    • Unger, T.1    Dym, O.2    Albeck, S.3    Jacobovitch, Y.4    Bernehim, R.5    Marom, D.6    Pisanty, O.7    Breiman, A.8
  • 133
    • 0032168133 scopus 로고    scopus 로고
    • A novel human gene FKBP6 is deleted in Williams syndrome
    • 9782077 1:CAS:528:DyaK1cXmvFCisrY%3D
    • Meng X, Lu X, Morris CA, Keating MT (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
  • 134
    • 46349094871 scopus 로고    scopus 로고
    • Affected homologous chromosome pairing and phosphorylation of testis specific histone, H2AX, in male meiosis under FKBP6 deficiency
    • 18408354
    • Noguchi J, Ozawa M, Nakai M, Somfai T, Kikuchi K, Kaneko H, Kunieda T (2008) Affected homologous chromosome pairing and phosphorylation of testis specific histone, H2AX, in male meiosis under FKBP6 deficiency. J Reprod Dev 54:203-207
    • (2008) J Reprod Dev , vol.54 , pp. 203-207
    • Noguchi, J.1    Ozawa, M.2    Nakai, M.3    Somfai, T.4    Kikuchi, K.5    Kaneko, H.6    Kunieda, T.7
  • 135
    • 0037227946 scopus 로고    scopus 로고
    • Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis
    • 12510191 1:CAS:528:DC%2BD3sXivFCh
    • Shirane M, Nakayama KI (2003) Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat Cell Biol 5:28-37
    • (2003) Nat Cell Biol , vol.5 , pp. 28-37
    • Shirane, M.1    Nakayama, K.I.2
  • 136
    • 80051666034 scopus 로고    scopus 로고
    • FKBP38-Bcl-2 interaction: A novel link to chemoresistance
    • 21571591 1:CAS:528:DC%2BC3MXhtVaitr7E
    • Choi BH, Yoon HS (2011) FKBP38-Bcl-2 interaction: a novel link to chemoresistance. Curr Opin Pharmacol 11:354-359
    • (2011) Curr Opin Pharmacol , vol.11 , pp. 354-359
    • Choi, B.H.1    Yoon, H.S.2
  • 137
    • 2542555722 scopus 로고    scopus 로고
    • FKBP8 is a negative regulator of mouse sonic hedgehog signalling in neural tissues
    • 15105374 1:CAS:528:DC%2BD2cXksFGju70%3D
    • Bulgakov OV, Eggenschwiler JT, Hong DH, Anderson KV, Li T (2004) FKBP8 is a negative regulator of mouse sonic hedgehog signalling in neural tissues. Development 131:2149-2159
    • (2004) Development , vol.131 , pp. 2149-2159
    • Bulgakov, O.V.1    Eggenschwiler, J.T.2    Hong, D.H.3    Anderson, K.V.4    Li, T.5
  • 138
    • 0043068043 scopus 로고    scopus 로고
    • Cell size regulation by the human TSC tumor suppressor proteins depends on PI3K and FKBP38
    • 12894220 1:CAS:528:DC%2BD3sXlvVKns78%3D
    • Rosner M, Hofer K, Kubista M, Hengstschlager M (2003) Cell size regulation by the human TSC tumor suppressor proteins depends on PI3K and FKBP38. Oncogene 22:4786-4798
    • (2003) Oncogene , vol.22 , pp. 4786-4798
    • Rosner, M.1    Hofer, K.2    Kubista, M.3    Hengstschlager, M.4
  • 140
    • 22144494187 scopus 로고    scopus 로고
    • Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activity
    • 15802496 1:CAS:528:DC%2BD2MXlslGht7w%3D
    • Denny WB, Prapapanich V, Smith DF, Scammell JG (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
  • 142
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain
    • 7526392 1:CAS:528:DyaK2cXmvF2ju7g%3D
    • Radanyi C, Chambraud B, Baulieu E-E (1994) The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proc Natl Acad Sci USA 91:11197-11201
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu, E.-E.3
  • 145
    • 34548485298 scopus 로고    scopus 로고
    • The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation
    • 17435176 1:CAS:528:DC%2BD2sXhtVehu77L
    • Chambraud B, Belabes H, Fontaine-Lenoir V, Fellous A, Baulieu EE (2007) The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation. FASEB J 21:2787-2797
    • (2007) FASEB J , vol.21 , pp. 2787-2797
    • Chambraud, B.1    Belabes, H.2    Fontaine-Lenoir, V.3    Fellous, A.4    Baulieu, E.E.5
  • 146
    • 84860341993 scopus 로고    scopus 로고
    • Galectin-1 markedly reduces the incidence of resorptions in mice missing immunophilin FKBP52
    • 22416080 1:CAS:528:DC%2BC38XmsVKmsr4%3D
    • Hirota Y, Burnum KE, Acar N, Rabinovich GA, Daikoku T, Dey SK (2012) Galectin-1 markedly reduces the incidence of resorptions in mice missing immunophilin FKBP52. Endocrinology 153:2486-2493
    • (2012) Endocrinology , vol.153 , pp. 2486-2493
    • Hirota, Y.1    Burnum, K.E.2    Acar, N.3    Rabinovich, G.A.4    Daikoku, T.5    Dey, S.K.6
  • 150
    • 77956234689 scopus 로고    scopus 로고
    • Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis
    • 20605780 1:CAS:528:DC%2BC3cXhtVOnsLzL
    • Chen H, Yong W, Hinds TD, Yang Z, Zhou Y, Sanchez ER, Shou W (2010) Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis. J Biol Chem 285:27776-27784
    • (2010) J Biol Chem , vol.285 , pp. 27776-27784
    • Chen, H.1    Yong, W.2    Hinds, T.D.3    Yang, Z.4    Zhou, Y.5    Sanchez, E.R.6    Shou, W.7
  • 152
    • 34447122476 scopus 로고    scopus 로고
    • FKBP52 deficiency-conferred uterine progesterone resistance is genetic background and pregnancy stage specific
    • 17571166 1:CAS:528:DC%2BD2sXnvVagurc%3D
    • Tranguch S, Wang H, Daikoku T, Xie H, Smith DF, Dey SK (2007) FKBP52 deficiency-conferred uterine progesterone resistance is genetic background and pregnancy stage specific. J Clin Invest 117:1824-1834
    • (2007) J Clin Invest , vol.117 , pp. 1824-1834
    • Tranguch, S.1    Wang, H.2    Daikoku, T.3    Xie, H.4    Smith, D.F.5    Dey, S.K.6
  • 153
    • 59849098177 scopus 로고    scopus 로고
    • Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity
    • 19073255 1:CAS:528:DC%2BD1MXitVyisro%3D
    • Wolf IM, Periyasamy S, Hinds T Jr, Yong W, Shou W, Sanchez ER (2009) Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity. J Steroid Biochem Mol Biol 113:36-45
    • (2009) J Steroid Biochem Mol Biol , vol.113 , pp. 36-45
    • Wolf, I.M.1    Periyasamy, S.2    Hinds, Jr.T.3    Yong, W.4    Shou, W.5    Sanchez, E.R.6
  • 154
    • 0032509519 scopus 로고    scopus 로고
    • Characterization of the Ah receptor-associated protein, ARA9
    • 9837941 1:CAS:528:DyaK1MXpsA%3D%3D
    • Carver LA, LaPress JJ, Jain S, Dunham EE, Bradfield CA (1998) Characterization of the Ah receptor-associated protein, ARA9. J Biol Chem 273:33580-33587
    • (1998) J Biol Chem , vol.273 , pp. 33580-33587
    • Carver, L.A.1    Lapress, J.J.2    Jain, S.3    Dunham, E.E.4    Bradfield, C.A.5
  • 156
    • 67649920749 scopus 로고    scopus 로고
    • Growth factors, matrices, and forces combine and control stem cells
    • 19556500 1:CAS:528:DC%2BD1MXnsFOmtbo%3D
    • Discher DE, Mooney DJ, Zandstra PW (2009) Growth factors, matrices, and forces combine and control stem cells. Science 324:1673-1677
    • (2009) Science , vol.324 , pp. 1673-1677
    • Discher, D.E.1    Mooney, D.J.2    Zandstra, P.W.3
  • 157
    • 84857321023 scopus 로고    scopus 로고
    • Telomeres and cancer: From crisis to stability to crisis to stability
    • 22341437 1:CAS:528:DC%2BC38XjtFSjsb0%3D
    • Campbell PJ (2012) Telomeres and cancer: from crisis to stability to crisis to stability. Cell 148:633-635
    • (2012) Cell , vol.148 , pp. 633-635
    • Campbell, P.J.1
  • 158
    • 84855881402 scopus 로고    scopus 로고
    • Exploiting the cancer genome: Strategies for the discovery and clinical development of targeted molecular therapeutics
    • 22235862 1:CAS:528:DC%2BC38XjsV2ntLg%3D
    • Yap TA, Workman P (2012) Exploiting the cancer genome: strategies for the discovery and clinical development of targeted molecular therapeutics. Annu Rev Pharmacol Toxicol 52:549-573
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 549-573
    • Yap, T.A.1    Workman, P.2
  • 164
    • 77952125059 scopus 로고    scopus 로고
    • The ulcerative colitis marker protein WAFL interacts with accessory proteins in endocytosis
    • 20376207 1:CAS:528:DC%2BC3cXltFWitLs%3D
    • Pan YF, Viklund IM, Tsai HH, Pettersson S, Maruyama IN (2010) The ulcerative colitis marker protein WAFL interacts with accessory proteins in endocytosis. Int J Biol Sci 6:163-171
    • (2010) Int J Biol Sci , vol.6 , pp. 163-171
    • Pan, Y.F.1    Viklund, I.M.2    Tsai, H.H.3    Pettersson, S.4    Maruyama, I.N.5
  • 165
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • 17142228 1:CAS:528:DC%2BD2sXivFKmtQ%3D%3D
    • Berman HM, Henrick K, Nakamura H, Markley JL (2007) The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res 35:D301-D303
    • (2007) Nucleic Acids Res , vol.35
    • Berman, H.M.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 166
    • 0033034203 scopus 로고    scopus 로고
    • Immunophilin FK506-binding protein 52 (not FK506-binding protein 12) mediates the neurotrophic action of FK506
    • 10336507 1:CAS:528:DyaK1MXjtlGgu7Y%3D
    • Gold BG, Densmore V, Shou W, Matzuk MM, Gordon HS (1999) Immunophilin FK506-binding protein 52 (not FK506-binding protein 12) mediates the neurotrophic action of FK506. J Pharmacol Exp Ther 289:1202-1210
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 1202-1210
    • Gold, B.G.1    Densmore, V.2    Shou, W.3    Matzuk, M.M.4    Gordon, H.S.5
  • 167
    • 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
    • 7687744 1:CAS:528:DyaK3sXlsl2itrc%3D
    • 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
  • 168
    • 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
    • 1652374 1:CAS:528:DyaK3MXlvFOqtL4%3D
    • Friedman J, 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 66:799-806
    • (1991) Cell , vol.66 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 170
    • 0027469775 scopus 로고
    • FKBP12-FK506 complex inhibits phosphatase activity of two mammalian isoforms of calcineurin irrespective of their substrates or activation mechanisms
    • 7683641 1:CAS:528:DyaK3sXit1Giurs%3D
    • Mukai H, Kuno T, Chang CD, Lane B, Luly JR, Tanaka C (1993) FKBP12-FK506 complex inhibits phosphatase activity of two mammalian isoforms of calcineurin irrespective of their substrates or activation mechanisms. J Biochem 113:292-298
    • (1993) J Biochem , vol.113 , pp. 292-298
    • Mukai, H.1    Kuno, T.2    Chang, C.D.3    Lane, B.4    Luly, J.R.5    Tanaka, C.6
  • 171
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin
    • 12357034 1:CAS:528:DC%2BD38XotVKms7c%3D
    • Jin L, Harrison SC (2002) Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci USA 99:13522-13526
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 172
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • 12218175 1:CAS:528:DC%2BD38XntlCltbk%3D
    • Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H (2002) Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci USA 99:12037-12042
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12037-12042
    • Huai, Q.1    Kim, H.Y.2    Liu, Y.3    Zhao, Y.4    Mondragon, A.5    Liu, J.O.6    Ke, H.7
  • 173
    • 0030444584 scopus 로고    scopus 로고
    • Calcineurin-immunosuppressor complexes
    • 8994877 1:CAS:528:DyaK2sXhtlGmuw%3D%3D
    • Stoddard BL, Flick KE (1996) Calcineurin-immunosuppressor complexes. Curr Opin Struct Biol 6:770-775
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 770-775
    • Stoddard, B.L.1    Flick, K.E.2
  • 174
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • 11015619 1:CAS:528:DC%2BD3cXnsVKisLk%3D
    • Rusnak F, Mertz P (2000) Calcineurin: form and function. Physiol Rev 80:1483-1521
    • (2000) Physiol Rev , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 175
    • 78751549570 scopus 로고    scopus 로고
    • Regulatory mechanisms of calcineurin phosphatase activity
    • 21110798 1:CAS:528:DC%2BC3MXkvVWrtLo%3D
    • Musson RE, Smit NP (2011) Regulatory mechanisms of calcineurin phosphatase activity. Curr Med Chem 18:301-315
    • (2011) Curr Med Chem , vol.18 , pp. 301-315
    • Musson, R.E.1    Smit, N.P.2
  • 176
    • 0029030652 scopus 로고
    • FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition
    • 7542743 1:CAS:528:DyaK2MXntVGitb0%3D
    • Baughman G, Wiederrecht GJ, Campbell NF, Martin MM, Bourgeois S (1995) FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition. Mol Cell Biol 15:4395-4402
    • (1995) Mol Cell Biol , vol.15 , pp. 4395-4402
    • Baughman, G.1    Wiederrecht, G.J.2    Campbell, N.F.3    Martin, M.M.4    Bourgeois, S.5
  • 177
    • 33845961032 scopus 로고    scopus 로고
    • Comparative analysis of calcineurin inhibition by complexes of immunosuppressive drugs with human FK506 binding proteins
    • 17176100 1:CAS:528:DC%2BD28XhtlChurvE
    • Weiwad M, Edlich F, Kilka S, Erdmann F, Jarczowski F, Dorn M, Moutty MC, Fischer G (2006) Comparative analysis of calcineurin inhibition by complexes of immunosuppressive drugs with human FK506 binding proteins. Biochemistry 45:15776-15784
    • (2006) Biochemistry , vol.45 , pp. 15776-15784
    • Weiwad, M.1    Edlich, F.2    Kilka, S.3    Erdmann, F.4    Jarczowski, F.5    Dorn, M.6    Moutty, M.C.7    Fischer, G.8
  • 178
    • 0028597938 scopus 로고
    • Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands
    • 7529175 1:CAS:528:DyaK2MXivFKgtLk%3D
    • Cardenas ME, Hemenway C, Muir RS, Ye R, Fiorentino D, Heitman J (1994) Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. EMBO J 13:5944-5957
    • (1994) EMBO J , vol.13 , pp. 5944-5957
    • Cardenas, M.E.1    Hemenway, C.2    Muir, R.S.3    Ye, R.4    Fiorentino, D.5    Heitman, J.6
  • 179
    • 0032849010 scopus 로고    scopus 로고
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A
    • 10497131 1:CAS:528:DyaK1MXmt12jtLY%3D
    • Aramburu J, Yaffe MB, Lopez-Rodriguez C, Cantley LC, Hogan PG, Rao A (1999) Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A. Science 285:2129-2133
    • (1999) Science , vol.285 , pp. 2129-2133
    • Aramburu, J.1    Yaffe, M.B.2    Lopez-Rodriguez, C.3    Cantley, L.C.4    Hogan, P.G.5    Rao, A.6
  • 180
    • 0034691195 scopus 로고    scopus 로고
    • A second calcineurin binding site on the NFAT regulatory domain
    • 10860980 1:CAS:528:DC%2BD3cXksVKit7w%3D
    • Park S, Uesugi M, Verdine GL (2000) A second calcineurin binding site on the NFAT regulatory domain. Proc Natl Acad Sci USA 97:7130-7135
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7130-7135
    • Park, S.1    Uesugi, M.2    Verdine, G.L.3
  • 181
    • 34248666084 scopus 로고    scopus 로고
    • Structure of calcineurin in complex with PVIVIT peptide: Portrait of a low-affinity signalling interaction
    • 17498738 1:CAS:528:DC%2BD2sXlvVyltLs%3D
    • Li H, Zhang L, Rao A, Harrison SC, Hogan PG (2007) Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction. J Mol Biol 369:1296-1306
    • (2007) J Mol Biol , vol.369 , pp. 1296-1306
    • Li, H.1    Zhang, L.2    Rao, A.3    Harrison, S.C.4    Hogan, P.G.5
  • 183
    • 34247868090 scopus 로고    scopus 로고
    • Structure of the calcineurin-NFAT complex: Defining a T cell activation switch using solution NMR and crystal coordinates
    • 17502104 1:CAS:528:DC%2BD2sXlt1aitbo%3D
    • Takeuchi K, Roehrl MH, Sun ZY, Wagner G (2007) Structure of the calcineurin-NFAT complex: defining a T cell activation switch using solution NMR and crystal coordinates. Structure 15:587-597
    • (2007) Structure , vol.15 , pp. 587-597
    • Takeuchi, K.1    Roehrl, M.H.2    Sun, Z.Y.3    Wagner, G.4
  • 184
    • 11144347825 scopus 로고    scopus 로고
    • Discovery of small-molecule inhibitors of the NFAT-calcineurin interaction by competitive high-throughput fluorescence polarization screening
    • 15610001 1:CAS:528:DC%2BD2cXhtVaisrzL
    • Roehrl MH, Wang JY, Wagner G (2004) Discovery of small-molecule inhibitors of the NFAT-calcineurin interaction by competitive high-throughput fluorescence polarization screening. Biochemistry 43:16067-16075
    • (2004) Biochemistry , vol.43 , pp. 16067-16075
    • Roehrl, M.H.1    Wang, J.Y.2    Wagner, G.3
  • 185
    • 2442714017 scopus 로고    scopus 로고
    • Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules
    • 15131267 1:CAS:528:DC%2BD2cXktlOlt7c%3D
    • Roehrl MH, Kang S, Aramburu J, Wagner G, Rao A, Hogan PG (2004) Selective inhibition of calcineurin-NFAT signaling by blocking protein-protein interaction with small organic molecules. Proc Natl Acad Sci USA 101:7554-7559
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7554-7559
    • Roehrl, M.H.1    Kang, S.2    Aramburu, J.3    Wagner, G.4    Rao, A.5    Hogan, P.G.6
  • 189
    • 0037312507 scopus 로고    scopus 로고
    • Tor signalling in bugs, brain and brawn
    • 12563289 1:CAS:528:DC%2BD3sXnsFaqug%3D%3D
    • Jacinto E, Hall MN (2003) Tor signalling in bugs, brain and brawn. Nat Rev Mol Cell Biol 4:117-126
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 191
    • 9244229490 scopus 로고    scopus 로고
    • CDNA cloning and gene mapping of a candidate human cell cycle checkpoint protein
    • 8610130 1:CAS:528:DyaK28XitVCitrk%3D
    • Cimprich KA, Shin TB, Keith CT, Schreiber SL (1996) cDNA cloning and gene mapping of a candidate human cell cycle checkpoint protein. Proc Natl Acad Sci USA 93:2850-2855
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2850-2855
    • Cimprich, K.A.1    Shin, T.B.2    Keith, C.T.3    Schreiber, S.L.4
  • 192
    • 13044309479 scopus 로고    scopus 로고
    • Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 Å resolution
    • 10089303 1:STN:280:DyaK1M7ptV2lsg%3D%3D
    • Liang J, Choi J, Clardy J (1999) Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 Å resolution. Acta Crystallogr D Biol Crystallogr 55(Pt 4):736-744
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 4 , pp. 736-744
    • Liang, J.1    Choi, J.2    Clardy, J.3
  • 193
    • 0030054923 scopus 로고    scopus 로고
    • X-ray crystal structure of 28-o-methylrapamycin complexed with FKBP12: Is the cyclohexyl moiety part of the effector domain of rapamycin?
    • 1:CAS:528:DyaK28Xjtlygurc%3D
    • Kallen J, Sedrani R, Cottens S (1996) X-ray crystal structure of 28-o-methylrapamycin complexed with FKBP12: is the cyclohexyl moiety part of the effector domain of rapamycin? J Am Chem Soc 118:5857-5861
    • (1996) J Am Chem Soc , vol.118 , pp. 5857-5861
    • Kallen, J.1    Sedrani, R.2    Cottens, S.3
  • 194
    • 0031657020 scopus 로고    scopus 로고
    • Chemical modification of rapamycin: The discovery of SDZ RAD
    • 9723437 1:CAS:528:DyaK1cXlvV2itb8%3D
    • Sedrani R, Cottens S, Kallen J, Schuler W (1998) Chemical modification of rapamycin: the discovery of SDZ RAD. Transplant Proc 30:2192-2194
    • (1998) Transplant Proc , vol.30 , pp. 2192-2194
    • Sedrani, R.1    Cottens, S.2    Kallen, J.3    Schuler, W.4
  • 195
    • 65349190615 scopus 로고    scopus 로고
    • Recent advances in the chemistry, biosynthesis and pharmacology of rapamycin analogs
    • 19387497 1:CAS:528:DC%2BD1MXkvValsrY%3D
    • Graziani EI (2009) Recent advances in the chemistry, biosynthesis and pharmacology of rapamycin analogs. Nat Prod Rep 26:602-609
    • (2009) Nat Prod Rep , vol.26 , pp. 602-609
    • Graziani, E.I.1
  • 198
    • 42349113247 scopus 로고    scopus 로고
    • A new pharmacologic action of CCI-779 involves FKBP12-independent inhibition of mTOR kinase activity and profound repression of global protein synthesis
    • 18413763 1:CAS:528:DC%2BD1cXks1Giu7c%3D
    • Shor B, Zhang WG, Toral-Barza L, Lucas J, Abraham RT, Gibbons JJ, Yu K (2008) A new pharmacologic action of CCI-779 involves FKBP12-independent inhibition of mTOR kinase activity and profound repression of global protein synthesis. Cancer Res 68:2934-2943
    • (2008) Cancer Res , vol.68 , pp. 2934-2943
    • Shor, B.1    Zhang, W.G.2    Toral-Barza, L.3    Lucas, J.4    Abraham, R.T.5    Gibbons, J.J.6    Yu, K.7
  • 199
    • 80052820448 scopus 로고    scopus 로고
    • North Central Cancer Treatment Group Phase i trial N057K of everolimus (RAD001) and temozolomide in combination with radiation therapy in patients with newly diagnosed glioblastoma multiforme
    • 20864273 1:CAS:528:DC%2BC3MXhtFShtb%2FL
    • Sarkaria JN, Galanis E, Wu W, Peller PJ, Giannini C, Brown PD, Uhm JH, McGraw S, Jaeckle KA, Buckner JC (2011) North Central Cancer Treatment Group Phase I trial N057K of everolimus (RAD001) and temozolomide in combination with radiation therapy in patients with newly diagnosed glioblastoma multiforme. Int J Radiat Oncol Biol Phys 81:468-475
    • (2011) Int J Radiat Oncol Biol Phys , vol.81 , pp. 468-475
    • Sarkaria, J.N.1    Galanis, E.2    Wu, W.3    Peller, P.J.4    Giannini, C.5    Brown, P.D.6    Uhm, J.H.7    McGraw, S.8    Jaeckle, K.A.9    Buckner, J.C.10
  • 200
    • 0035928843 scopus 로고    scopus 로고
    • Bench to bedside: The development of rapamycin and its application to stent restenosis
    • 11514367 1:CAS:528:DC%2BD3MXmvFKmsrk%3D
    • Marx SO, Marks AR (2001) Bench to bedside: the development of rapamycin and its application to stent restenosis. Circulation 104:852-855
    • (2001) Circulation , vol.104 , pp. 852-855
    • Marx, S.O.1    Marks, A.R.2
  • 204
    • 79551610758 scopus 로고    scopus 로고
    • Cardiotoxicity of kinase inhibitors: The prediction and translation of preclinical models to clinical outcomes
    • 21283106 1:CAS:528:DC%2BC3MXhtlektrg%3D
    • Force T, Kolaja KL (2011) Cardiotoxicity of kinase inhibitors: the prediction and translation of preclinical models to clinical outcomes. Nat Rev Drug Discov 10:111-126
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 111-126
    • Force, T.1    Kolaja, K.L.2
  • 206
    • 69949151386 scopus 로고    scopus 로고
    • Factors underlying sensitivity of cancers to small-molecule kinase inhibitors
    • 19629074 1:CAS:528:DC%2BD1MXovFylur4%3D
    • Janne PA, Gray N, Settleman J (2009) Factors underlying sensitivity of cancers to small-molecule kinase inhibitors. Nat Rev Drug Discov 8:709-723
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 709-723
    • Janne, P.A.1    Gray, N.2    Settleman, J.3
  • 207
    • 11144311139 scopus 로고    scopus 로고
    • Lessons from natural molecules
    • 15602548 1:CAS:528:DC%2BD2cXhtVOht7jP
    • Clardy J, Walsh C (2004) Lessons from natural molecules. Nature 432:829-837
    • (2004) Nature , vol.432 , pp. 829-837
    • Clardy, J.1    Walsh, C.2
  • 209
    • 0028202076 scopus 로고
    • Immunosuppressant FK506 promotes neurite outgrowth in cultures of PC12 cells and sensory ganglia
    • 7512727 1:CAS:528:DyaK2cXjtFGnsL0%3D
    • Lyons WE, George EB, Dawson TM, Steiner JP, Snyder SH (1994) Immunosuppressant FK506 promotes neurite outgrowth in cultures of PC12 cells and sensory ganglia. Proc Natl Acad Sci USA 91:3191-3195
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3191-3195
    • Lyons, W.E.1    George, E.B.2    Dawson, T.M.3    Steiner, J.P.4    Snyder, S.H.5
  • 210
    • 4344694987 scopus 로고    scopus 로고
    • Neuroimmunophilins: A novel drug therapy for the reversal of neurodegenerative disease?
    • 15450348 1:CAS:528:DC%2BD2cXmvFelsro%3D
    • Poulter MO, Payne KB, Steiner JP (2004) Neuroimmunophilins: a novel drug therapy for the reversal of neurodegenerative disease? Neuroscience 128:1-6
    • (2004) Neuroscience , vol.128 , pp. 1-6
    • Poulter, M.O.1    Payne, K.B.2    Steiner, J.P.3
  • 211
    • 20444368456 scopus 로고    scopus 로고
    • A crevice adjoining the ribosome tunnel: Hints for cotranslational folding
    • 15943964 1:CAS:528:DC%2BD2MXltFSqur8%3D
    • Amit M, Berisio R, Baram D, Harms J, Bashan A, Yonath A (2005) A crevice adjoining the ribosome tunnel: hints for cotranslational folding. FEBS Lett 579:3207-3213
    • (2005) FEBS Lett , vol.579 , pp. 3207-3213
    • Amit, M.1    Berisio, R.2    Baram, D.3    Harms, J.4    Bashan, A.5    Yonath, A.6
  • 212
    • 40049095697 scopus 로고    scopus 로고
    • Topical tacrolimus and pimecrolimus in the treatment of cutaneous lupus erythematosus: An evidence-based evaluation
    • 18157526 1:CAS:528:DC%2BD1cXisFCmsbg%3D
    • Tzellos TG, Kouvelas D (2008) Topical tacrolimus and pimecrolimus in the treatment of cutaneous lupus erythematosus: an evidence-based evaluation. Eur J Clin Pharmacol 64:337-341
    • (2008) Eur J Clin Pharmacol , vol.64 , pp. 337-341
    • Tzellos, T.G.1    Kouvelas, D.2
  • 213
    • 50049084618 scopus 로고    scopus 로고
    • Binding of pimecrolimus and tacrolimus to skin and plasma proteins: Implications for systemic exposure after topical application
    • 18524871 1:CAS:528:DC%2BD1cXhtVGqsrvN
    • Weiss HM, Fresneau M, Moenius T, Stuetz A, Billich A (2008) Binding of pimecrolimus and tacrolimus to skin and plasma proteins: implications for systemic exposure after topical application. Drug Metab Dispos 36:1812-1818
    • (2008) Drug Metab Dispos , vol.36 , pp. 1812-1818
    • Weiss, H.M.1    Fresneau, M.2    Moenius, T.3    Stuetz, A.4    Billich, A.5
  • 214
    • 58149165185 scopus 로고    scopus 로고
    • Topical calcineurin inhibitors in cutaneous lupus erythematosus
    • 18797893
    • Sàrdy M, Ruzicka T, Kuhn A (2009) Topical calcineurin inhibitors in cutaneous lupus erythematosus. Arch Dermatol Res 301:93-98
    • (2009) Arch Dermatol Res , vol.301 , pp. 93-98
    • Sàrdy, M.1    Ruzicka, T.2    Kuhn, A.3
  • 215
  • 216
    • 38049169557 scopus 로고    scopus 로고
    • Efficacy of sirolimus in treating tuberous sclerosis and lymphangioleiomyomatosis
    • 18184966 1:CAS:528:DC%2BD1cXltFaltQ%3D%3D
    • Paul E, Thiele E (2008) Efficacy of sirolimus in treating tuberous sclerosis and lymphangioleiomyomatosis. N Engl J Med 358:190-192
    • (2008) N Engl J Med , vol.358 , pp. 190-192
    • Paul, E.1    Thiele, E.2
  • 217
    • 33644689608 scopus 로고    scopus 로고
    • Molecular activity of sirolimus and its possible application in tuberous sclerosis treatment
    • 16329102 1:CAS:528:DC%2BD28XislOksL0%3D
    • Jozwiak J, Jozwiak S, Oldak M (2006) Molecular activity of sirolimus and its possible application in tuberous sclerosis treatment. Med Res Rev 26:160-180
    • (2006) Med Res Rev , vol.26 , pp. 160-180
    • Jozwiak, J.1    Jozwiak, S.2    Oldak, M.3
  • 218
    • 40749154421 scopus 로고    scopus 로고
    • Neointimal expression of rapamycin receptor FK506-binding protein FKBP12: Postinjury animal and human in-stent restenosis tissue characteristics
    • 17962721 1:CAS:528:DC%2BD1cXit1Wjsrg%3D
    • Bauriedel G, Jabs A, Kraemer S, Nickenig G, Skowasch D (2008) Neointimal expression of rapamycin receptor FK506-binding protein FKBP12: postinjury animal and human in-stent restenosis tissue characteristics. J Vasc Res 45:173-178
    • (2008) J Vasc Res , vol.45 , pp. 173-178
    • Bauriedel, G.1    Jabs, A.2    Kraemer, S.3    Nickenig, G.4    Skowasch, D.5
  • 220
    • 79953889736 scopus 로고    scopus 로고
    • Everolimus for the treatment of advanced renal cell carcinoma
    • 21470068 1:CAS:528:DC%2BC3MXksVertbw%3D
    • Amato R (2011) Everolimus for the treatment of advanced renal cell carcinoma. Expert Opin Pharmacother 12:1143-1155
    • (2011) Expert Opin Pharmacother , vol.12 , pp. 1143-1155
    • Amato, R.1
  • 222
    • 80054791210 scopus 로고    scopus 로고
    • Multimodal biomarker investigation on efficacy and mechanism of action for the mammalian target of rapamycin inhibitor, temsirolimus, in a preclinical mammary carcinoma OncoMouse model: A translational medicine study in support for early clinical development
    • 21835932 1:CAS:528:DC%2BC3MXhsFehtb3N
    • Wang X, Zhan Y, Zhao L, Alvarez J, Chaudhary I, Zhou BB, Abraham RT, Feuerstein GZ (2011) Multimodal biomarker investigation on efficacy and mechanism of action for the mammalian target of rapamycin inhibitor, temsirolimus, in a preclinical mammary carcinoma OncoMouse model: a translational medicine study in support for early clinical development. J Pharmacol Exp Ther 339:421-429
    • (2011) J Pharmacol Exp Ther , vol.339 , pp. 421-429
    • Wang, X.1    Zhan, Y.2    Zhao, L.3    Alvarez, J.4    Chaudhary, I.5    Zhou, B.B.6    Abraham, R.T.7    Feuerstein, G.Z.8
  • 224
    • 0035102687 scopus 로고    scopus 로고
    • New immunosuppressive drugs in heart transplantation
    • 11806772
    • Costanzo MR (2001) New immunosuppressive drugs in heart transplantation. Curr Control Trials Cardiovasc Med 2:45-55
    • (2001) Curr Control Trials Cardiovasc Med , vol.2 , pp. 45-55
    • Costanzo, M.R.1
  • 226
    • 54049089162 scopus 로고    scopus 로고
    • FK1706, a novel non-immunosuppressive immunophilin ligand, modifies the course of painful diabetic neuropathy
    • 18760290 1:CAS:528:DC%2BD1cXhtlShurvJ
    • Yamazaki S, Yamaji T, Murai N, Yamamoto H, Price RD, Matsuoka N, Mutoh S (2008) FK1706, a novel non-immunosuppressive immunophilin ligand, modifies the course of painful diabetic neuropathy. Neuropharmacology 55:1226-1230
    • (2008) Neuropharmacology , vol.55 , pp. 1226-1230
    • Yamazaki, S.1    Yamaji, T.2    Murai, N.3    Yamamoto, H.4    Price, R.D.5    Matsuoka, N.6    Mutoh, S.7
  • 227
    • 61449150347 scopus 로고    scopus 로고
    • Everolimus and sirolimus antagonize tacrolimus based calcineurin inhibition via competition for FK-binding protein 12
    • 19154728
    • van Rossum HH, Romijn FP, Smit NP, de Fijter JW, van Pelt J (2009) Everolimus and sirolimus antagonize tacrolimus based calcineurin inhibition via competition for FK-binding protein 12. Biochem Pharmacol 77:1206-1212
    • (2009) Biochem Pharmacol , vol.77 , pp. 1206-1212
    • Van Rossum, H.H.1    Romijn, F.P.2    Smit, N.P.3    De Fijter, J.W.4    Van Pelt, J.5
  • 228
    • 74849131091 scopus 로고    scopus 로고
    • Targeting mTOR globally in cancer: Thinking beyond rapamycin
    • 19901542 1:CAS:528:DC%2BC3cXotlWrtL4%3D
    • Shor B, Gibbons JJ, Abraham RT, Yu K (2009) Targeting mTOR globally in cancer: thinking beyond rapamycin. Cell Cycle 8:3831-3837
    • (2009) Cell Cycle , vol.8 , pp. 3831-3837
    • Shor, B.1    Gibbons, J.J.2    Abraham, R.T.3    Yu, K.4
  • 230
    • 77649210115 scopus 로고    scopus 로고
    • Nocardiopsins: New FKBP12-binding macrolide polyketides from an Australian marine-derived actinomycete, Nocardiopsis sp.
    • 20112311 1:CAS:528:DC%2BC3cXivFejsr0%3D
    • Raju R, Piggott AM, Conte M, Tnimov Z, Alexandrov K, Capon RJ (2010) Nocardiopsins: new FKBP12-binding macrolide polyketides from an Australian marine-derived actinomycete, Nocardiopsis sp. Chemistry 16:3194-3200
    • (2010) Chemistry , vol.16 , pp. 3194-3200
    • Raju, R.1    Piggott, A.M.2    Conte, M.3    Tnimov, Z.4    Alexandrov, K.5    Capon, R.J.6
  • 231
    • 76249099055 scopus 로고    scopus 로고
    • The novel calcineurin inhibitor CN585 has potent immunosuppressive properties in stimulated human T cells
    • 19923214 1:CAS:528:DC%2BC3cXjsVSksQ%3D%3D
    • Erdmann F, Weiwad M, Kilka S, Karanik M, Patzel M, Baumgrass R, Liebscher J, Fischer G (2010) The novel calcineurin inhibitor CN585 has potent immunosuppressive properties in stimulated human T cells. J Biol Chem 285:1888-1898
    • (2010) J Biol Chem , vol.285 , pp. 1888-1898
    • Erdmann, F.1    Weiwad, M.2    Kilka, S.3    Karanik, M.4    Patzel, M.5    Baumgrass, R.6    Liebscher, J.7    Fischer, G.8
  • 232
    • 84861030752 scopus 로고    scopus 로고
    • Evaluation of synthetic FK506 analogs as ligands for the FK506-binding proteins 51 and 52
    • 22455444 1:CAS:528:DC%2BC38XkvVWls74%3D
    • Gopalakrishnan R, Kozany C, Gaali S, Kress C, Hoogeland B, Bracher A, Hausch F (2012) Evaluation of synthetic FK506 analogs as ligands for the FK506-binding proteins 51 and 52. J Med Chem 55:4114-4122
    • (2012) J Med Chem , vol.55 , pp. 4114-4122
    • Gopalakrishnan, R.1    Kozany, C.2    Gaali, S.3    Kress, C.4    Hoogeland, B.5    Bracher, A.6    Hausch, F.7
  • 233
    • 84861071782 scopus 로고    scopus 로고
    • Exploration of pipecolate sulfonamides as binders of the FK506-binding proteins 51 and 52
    • 22455398 1:CAS:528:DC%2BC38XkvVWmtbw%3D
    • Gopalakrishnan R, Kozany C, Wang Y, Schneider S, Hoogeland B, Bracher A, Hausch F (2012) Exploration of pipecolate sulfonamides as binders of the FK506-binding proteins 51 and 52. J Med Chem 55:4123-4131
    • (2012) J Med Chem , vol.55 , pp. 4123-4131
    • Gopalakrishnan, R.1    Kozany, C.2    Wang, Y.3    Schneider, S.4    Hoogeland, B.5    Bracher, A.6    Hausch, F.7
  • 234
    • 72849149270 scopus 로고    scopus 로고
    • Novel inhibitors of the calcineurin/NFATc hub - Alternatives to CsA and FK506?
    • 19860902
    • Sieber M, Baumgrass R (2009) Novel inhibitors of the calcineurin/NFATc hub - alternatives to CsA and FK506? Cell Commun Signal 7:25
    • (2009) Cell Commun Signal , vol.7 , pp. 25
    • Sieber, M.1    Baumgrass, R.2
  • 239
    • 17144427728 scopus 로고    scopus 로고
    • Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors
    • 15833867 1:CAS:528:DC%2BD2MXjt1yrs78%3D
    • Takeuchi H, Kondo Y, Fujiwara K, Kanzawa T, Aoki H, Mills GB, Kondo S (2005) Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors. Cancer Res 65:3336-3346
    • (2005) Cancer Res , vol.65 , pp. 3336-3346
    • Takeuchi, H.1    Kondo, Y.2    Fujiwara, K.3    Kanzawa, T.4    Aoki, H.5    Mills, G.B.6    Kondo, S.7
  • 240
    • 84860872990 scopus 로고    scopus 로고
    • The role of mammalian target of rapamycin (mTOR) in the regulation of pancreatic β-cell mass: Implications in the development of type-2 diabetes
    • 22068611 1:CAS:528:DC%2BC38XksFajsLs%3D
    • Xie J, Herbert TP (2012) The role of mammalian target of rapamycin (mTOR) in the regulation of pancreatic β-cell mass: implications in the development of type-2 diabetes. Cell Mol Life Sci 69:1289-1304
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1289-1304
    • Xie, J.1    Herbert, T.P.2
  • 241
    • 84872464549 scopus 로고    scopus 로고
    • Therapeutic implications of targeting the PI3Kinase/AKT/mTOR signaling module in melanoma therapy
    • 22485197 1:CAS:528:DC%2BC38Xks1Kjtb8%3D
    • Jazirehi AR, Wenn PB, Damavand M (2012) Therapeutic implications of targeting the PI3Kinase/AKT/mTOR signaling module in melanoma therapy. Am J Cancer Res 2:178-191
    • (2012) Am J Cancer Res , vol.2 , pp. 178-191
    • Jazirehi, A.R.1    Wenn, P.B.2    Damavand, M.3
  • 243
    • 84857675728 scopus 로고    scopus 로고
    • The mTOR signalling pathway in human cancer
    • 22408430 1:CAS:528:DC%2BC38XivVKhtro%3D
    • Populo H, Lopes JM, Soares P (2012) The mTOR signalling pathway in human cancer. Int J Mol Sci 13:1886-1918
    • (2012) Int J Mol Sci , vol.13 , pp. 1886-1918
    • Populo, H.1    Lopes, J.M.2    Soares, P.3
  • 244
    • 84859416603 scopus 로고    scopus 로고
    • Novel therapies for metastatic renal cell carcinoma: Efforts to expand beyond the VEGF/mTOR signaling paradigm
    • 22351744 1:CAS:528:DC%2BC38XjtlKjtbg%3D
    • Pal SK, Williams S, Josephson DY, Carmichael C, Vogelzang NJ, Quinn DI (2012) Novel therapies for metastatic renal cell carcinoma: efforts to expand beyond the VEGF/mTOR signaling paradigm. Mol Cancer Ther 11:526-537
    • (2012) Mol Cancer Ther , vol.11 , pp. 526-537
    • Pal, S.K.1    Williams, S.2    Josephson, D.Y.3    Carmichael, C.4    Vogelzang, N.J.5    Quinn, D.I.6
  • 245
    • 84862260392 scopus 로고    scopus 로고
    • InTERTesting association between telomerase, mTOR and phytochemicals
    • 10.1017/erm.2012.1 22455872 1:CAS:528:DC%2BC38XhsVegtbnM
    • Sundin T, Hentosh P (2012) InTERTesting association between telomerase, mTOR and phytochemicals. Expert Rev Mol Med 14:e8. doi: 10.1017/erm.2012.1
    • (2012) Expert Rev Mol Med , vol.14 , pp. 8
    • Sundin, T.1    Hentosh, P.2
  • 246
    • 80054890748 scopus 로고    scopus 로고
    • Direct inhibition of calcineurin by caffeoyl phenylethanoid glycosides from Teucrium chamaedrys and Nepeta cataria
    • 21843624 1:CAS:528:DC%2BC3MXhtlOksbfM
    • Prescott TA, Veitch NC, Simmonds MS (2011) Direct inhibition of calcineurin by caffeoyl phenylethanoid glycosides from Teucrium chamaedrys and Nepeta cataria. J Ethnopharmacol 137:1306-1310
    • (2011) J Ethnopharmacol , vol.137 , pp. 1306-1310
    • Prescott, T.A.1    Veitch, N.C.2    Simmonds, M.S.3
  • 247
    • 79951787452 scopus 로고    scopus 로고
    • Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB
    • 21331044 1:CAS:528:DC%2BC3MXitVCksr0%3D
    • Mair W, Morantte I, Rodrigues AP, Manning G, Montminy M, Shaw RJ, Dillin A (2011) Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB. Nature 470:404-408
    • (2011) Nature , vol.470 , pp. 404-408
    • Mair, W.1    Morantte, I.2    Rodrigues, A.P.3    Manning, G.4    Montminy, M.5    Shaw, R.J.6    Dillin, A.7
  • 248
    • 84874530824 scopus 로고    scopus 로고
    • Calcineurin inhibitors and immunosuppression - A tale of two isoforms
    • 22805659
    • Williams CR, Gooch JL (2012) Calcineurin inhibitors and immunosuppression - a tale of two isoforms. Expert Rev Mol Med 14:e14
    • (2012) Expert Rev Mol Med , vol.14 , pp. 14
    • Williams, C.R.1    Gooch, J.L.2
  • 250
    • 77951176737 scopus 로고    scopus 로고
    • Extending healthy life span - From yeast to humans
    • 20395504 1:CAS:528:DC%2BC3cXks1Snsro%3D
    • Fontana L, Partridge L, Longo VD (2010) Extending healthy life span - from yeast to humans. Science 328:321-326
    • (2010) Science , vol.328 , pp. 321-326
    • Fontana, L.1    Partridge, L.2    Longo, V.D.3
  • 251
    • 80655140442 scopus 로고    scopus 로고
    • Progeria, rapamycin and normal aging: Recent breakthrough
    • 1:CAS:528:DC%2BC3MXhtF2ns7zE
    • Blagosklonny MV (2011) Progeria, rapamycin and normal aging: recent breakthrough. Aging (Albany NY) 3:685-691
    • (2011) Aging (Albany NY) , vol.3 , pp. 685-691
    • Blagosklonny, M.V.1
  • 252
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • 16453012 1:CAS:528:DC%2BD28Xhslelt78%3D
    • Cully M, You H, Levine AJ, Mak TW (2006) Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis. Nat Rev Cancer 6:184-192
    • (2006) Nat Rev Cancer , vol.6 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 253
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • 21157483 1:CAS:528:DC%2BC3cXhsFGqsbnK
    • Zoncu R, Efeyan A, Sabatini DM (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 12:21-35
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 254
    • 33750366826 scopus 로고    scopus 로고
    • Sirolimus accelerates senescence of endothelial progenitor cells through telomerase inactivation
    • 16455087 1:CAS:528:DC%2BD28XhtFCjsL3P
    • Imanishi T, Kobayashi K, Kuki S, Takahashi C, Akasaka T (2006) Sirolimus accelerates senescence of endothelial progenitor cells through telomerase inactivation. Atherosclerosis 189:288-296
    • (2006) Atherosclerosis , vol.189 , pp. 288-296
    • Imanishi, T.1    Kobayashi, K.2    Kuki, S.3    Takahashi, C.4    Akasaka, T.5
  • 257
    • 79951555130 scopus 로고    scopus 로고
    • Telomeres, aging, and plants: From weeds to Methuselah - A mini-review
    • 20375491 1:CAS:528:DC%2BC3MXhs1SnsLo%3D
    • Watson JM, Riha K (2011) Telomeres, aging, and plants: from weeds to Methuselah - a mini-review. Gerontology 57:129-136
    • (2011) Gerontology , vol.57 , pp. 129-136
    • Watson, J.M.1    Riha, K.2
  • 258
    • 79951577837 scopus 로고    scopus 로고
    • Aging and TOR: Interwoven in the fabric of life
    • 20960025 1:CAS:528:DC%2BC3MXhtFKrsrg%3D
    • Sharp ZD (2011) Aging and TOR: interwoven in the fabric of life. Cell Mol Life Sci 68:587-597
    • (2011) Cell Mol Life Sci , vol.68 , pp. 587-597
    • Sharp, Z.D.1
  • 259
    • 73849101809 scopus 로고    scopus 로고
    • Key factors in mTOR regulation
    • 19823764 1:CAS:528:DC%2BC3cXis1ejtg%3D%3D
    • Bai X, Jiang Y (2010) Key factors in mTOR regulation. Cell Mol Life Sci 67:239-253
    • (2010) Cell Mol Life Sci , vol.67 , pp. 239-253
    • Bai, X.1    Jiang, Y.2
  • 260
    • 84856675492 scopus 로고    scopus 로고
    • [18F]GSK2126458, the first radiosynthesis of new potential PET agents for imaging of PI3K and mTOR in cancers
    • 22297110 1:CAS:528:DC%2BC38XhslCgsbo%3D
    • [18F]GSK2126458, the first radiosynthesis of new potential PET agents for imaging of PI3K and mTOR in cancers. Bioorg Med Chem Lett 22:1569-1574
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 1569-1574
    • Wang, M.1    Gao, M.2    Miller, K.D.3    Sledge, G.W.4    Zheng, Q.H.5
  • 261
    • 33847391264 scopus 로고    scopus 로고
    • Acute sirolimus pulmonary toxicity in an infant heart transplant recipient: Case report and literature review
    • 17346635
    • Das BB, Shoemaker L, Subramanian S, Johnsrude C, Recto M, Austin EH (2007) Acute sirolimus pulmonary toxicity in an infant heart transplant recipient: case report and literature review. J Heart Lung Transplant 26:296-298
    • (2007) J Heart Lung Transplant , vol.26 , pp. 296-298
    • Das, B.B.1    Shoemaker, L.2    Subramanian, S.3    Johnsrude, C.4    Recto, M.5    Austin, E.H.6
  • 262
    • 48849092136 scopus 로고    scopus 로고
    • Pharmacodynamic monitoring of calcineurin phosphatase activity in transplant patients treated with calcineurin inhibitors
    • 18574318 1:CAS:528:DC%2BD1cXhtVSis73P
    • Yano I (2008) Pharmacodynamic monitoring of calcineurin phosphatase activity in transplant patients treated with calcineurin inhibitors. Drug Metab Pharmacokinet 23:150-157
    • (2008) Drug Metab Pharmacokinet , vol.23 , pp. 150-157
    • Yano, I.1
  • 263
    • 65549166679 scopus 로고    scopus 로고
    • Calcineurin inhibitor nephrotoxicity
    • 19218475 1:CAS:528:DC%2BD1MXjslagurc%3D
    • Naesens M, Kuypers DR, Sarwal M (2009) Calcineurin inhibitor nephrotoxicity. Clin J Am Soc Nephrol 4:481-508
    • (2009) Clin J Am Soc Nephrol , vol.4 , pp. 481-508
    • Naesens, M.1    Kuypers, D.R.2    Sarwal, M.3
  • 264
    • 81855173480 scopus 로고    scopus 로고
    • Sirolimus in solid organ transplantation: Current therapies and new frontiers
    • 22091684 1:CAS:528:DC%2BC3MXhsVymt7rN
    • Veroux M, Tallarita T, Corona D, D'Assoro A, Gurrieri C, Veroux P (2011) Sirolimus in solid organ transplantation: current therapies and new frontiers. Immunotherapy 3:1487-1497
    • (2011) Immunotherapy , vol.3 , pp. 1487-1497
    • Veroux, M.1    Tallarita, T.2    Corona, D.3    D'Assoro, A.4    Gurrieri, C.5    Veroux, P.6
  • 265
    • 80051802715 scopus 로고    scopus 로고
    • Pharmacodynamic disparities in tacrolimus-treated patients developing cytomegalus virus viremia
    • 21743376 1:CAS:528:DC%2BC3MXovF2hsr0%3D
    • Sommerer C, Zeier M, Czock D, Schnitzler P, Meuer S, Giese T (2011) Pharmacodynamic disparities in tacrolimus-treated patients developing cytomegalus virus viremia. Ther Drug Monit 33:373-379
    • (2011) Ther Drug Monit , vol.33 , pp. 373-379
    • Sommerer, C.1    Zeier, M.2    Czock, D.3    Schnitzler, P.4    Meuer, S.5    Giese, T.6
  • 267
    • 79960761944 scopus 로고    scopus 로고
    • An emerging role for TOR signaling in mammalian tissue and stem cell physiology
    • 21791526 1:CAS:528:DC%2BC3MXht1OmtrrN
    • Russell RC, Fang C, Guan KL (2011) An emerging role for TOR signaling in mammalian tissue and stem cell physiology. Development 138:3343-3356
    • (2011) Development , vol.138 , pp. 3343-3356
    • Russell, R.C.1    Fang, C.2    Guan, K.L.3
  • 271
    • 48449086316 scopus 로고    scopus 로고
    • TGF-β: A master of all T cell trades
    • 18692464 1:CAS:528:DC%2BD1cXhtVSis77N
    • Li MO, Flavell RA (2008) TGF-β: a master of all T cell trades. Cell 134:392-404
    • (2008) Cell , vol.134 , pp. 392-404
    • Li, M.O.1    Flavell, R.A.2
  • 273
    • 79954990980 scopus 로고    scopus 로고
    • Immunosuppressor FK506 increases endoglin and activin receptor-like kinase 1 expression and modulates transforming growth factor-β1 signaling in endothelial cells
    • 21310938 1:CAS:528:DC%2BC3MXls1Olt7c%3D
    • Albinana V, Sanz-Rodriguez F, Recio-Poveda L, Bernabeu C, Botella LM (2011) Immunosuppressor FK506 increases endoglin and activin receptor-like kinase 1 expression and modulates transforming growth factor-β1 signaling in endothelial cells. Mol Pharmacol 79:833-843
    • (2011) Mol Pharmacol , vol.79 , pp. 833-843
    • Albinana, V.1    Sanz-Rodriguez, F.2    Recio-Poveda, L.3    Bernabeu, C.4    Botella, L.M.5
  • 275
    • 34249874875 scopus 로고    scopus 로고
    • Screening of immunophilin ligands by quantitative analysis of neurofilament expression and neurite outgrowth in cultured neurons and cells
    • 17490751 1:CAS:528:DC%2BD2sXmtlSntrg%3D
    • Liu D, McIlvain HB, Fennell M, Dunlop J, Wood A, Zaleska MM, Graziani EI, Pong K (2007) Screening of immunophilin ligands by quantitative analysis of neurofilament expression and neurite outgrowth in cultured neurons and cells. J Neurosci Methods 163:310-320
    • (2007) J Neurosci Methods , vol.163 , pp. 310-320
    • Liu, D.1    McIlvain, H.B.2    Fennell, M.3    Dunlop, J.4    Wood, A.5    Zaleska, M.M.6    Graziani, E.I.7    Pong, K.8
  • 277
    • 70349786859 scopus 로고    scopus 로고
    • Enhancement of nerve regeneration and recovery by immunosuppressive agents
    • 19682647 1:CAS:528:DC%2BD1MXht1WlurvF
    • Kuffler DP (2009) Enhancement of nerve regeneration and recovery by immunosuppressive agents. Int Rev Neurobiol 87:347-862
    • (2009) Int Rev Neurobiol , vol.87 , pp. 347-862
    • Kuffler, D.P.1
  • 278
    • 80052911048 scopus 로고    scopus 로고
    • The role of immunophilin ligands in nerve regeneration
    • 21916598 1:CAS:528:DC%2BC3MXhtFOju7rP
    • Toll EC, Seifalian AM, Birchall MA (2011) The role of immunophilin ligands in nerve regeneration. Regen Med 6:635-652
    • (2011) Regen Med , vol.6 , pp. 635-652
    • Toll, E.C.1    Seifalian, A.M.2    Birchall, M.A.3


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