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Volumn 56, Issue 3, 2013, Pages 1041-1051

The precise chemical-physical nature of the pharmacore in FK506 binding protein inhibition: ElteX, a new class of nanomolar FKBP12 ligands

Author keywords

[No Author keywords available]

Indexed keywords

ELTEX; FK 506 BINDING PROTEIN; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 84873896713     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm3015052     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 80051668635 scopus 로고    scopus 로고
    • Targeting FKBP isoforms with small-molecule ligands
    • Blackburn, E. A.; Walkinshaw, M. D. Targeting FKBP isoforms with small-molecule ligands Curr. Opin. Pharmacol. 2011, 11, 365-371
    • (2011) Curr. Opin. Pharmacol. , vol.11 , pp. 365-371
    • Blackburn, E.A.1    Walkinshaw, M.D.2
  • 2
    • 82255169261 scopus 로고    scopus 로고
    • Role of FK506 binding proteins in neurodegenerative disorders
    • Chattopadhaya, S.; Harikishore, A.; Yoon, H. S. Role of FK506 binding proteins in neurodegenerative disorders Curr. Med. Chem. 2011, 18, 5380-5397
    • (2011) Curr. Med. Chem. , vol.18 , pp. 5380-5397
    • Chattopadhaya, S.1    Harikishore, A.2    Yoon, H.S.3
  • 3
    • 44349186241 scopus 로고    scopus 로고
    • Functional drift of sequence attributes in the FK506-binding proteins (FKBPs)
    • Galat, A. Functional drift of sequence attributes in the FK506-binding proteins (FKBPs) J. Chem. Inf. Model. 2008, 48, 1118-1130
    • (2008) J. Chem. Inf. Model. , vol.48 , pp. 1118-1130
    • Galat, A.1
  • 5
    • 0033736147 scopus 로고    scopus 로고
    • Immunophilins: Switched on protein binding domains?
    • Ivery, M. Immunophilins: switched on protein binding domains? Med. Res. Rev. 2000, 20, 452-484
    • (2000) Med. Res. Rev. , vol.20 , pp. 452-484
    • Ivery, M.1
  • 7
    • 0026575583 scopus 로고
    • Natural-products as probes of cellular function - Studies of immunophilins
    • Rosen, M. K.; Schreiber, S. L. Natural-products as probes of cellular function-studies of immunophilins Angew. Chem., Int. Ed. Engl. 1992, 31, 384-400
    • (1992) Angew. Chem., Int. Ed. Engl. , vol.31 , pp. 384-400
    • Rosen, M.K.1    Schreiber, S.L.2
  • 8
    • 0028848524 scopus 로고
    • Crystal-structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger, C. R. Crystal-structures of human calcineurin and the human FKBP12-FK506-calcineurin complex Nature 1995, 378, 641-644
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1
  • 9
    • 13044309479 scopus 로고    scopus 로고
    • Refined structure of the FKBP12-Rapamycin-FRB ternary complex at 2.2 A resolution
    • Liang, J.; Cho, i. J.; Clardy, J. Refined structure of the FKBP12-Rapamycin-FRB ternary complex at 2.2 A resolution Acta Crystallogr., Sect. D: Biol. Crystallogr. 1999, 55, 736-744
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.55 , pp. 736-744
    • Liang, J.1    Cho, I.J.2    Clardy, J.3
  • 10
    • 16844385435 scopus 로고    scopus 로고
    • Characterization of the FKBP.rapamycin.FRB ternary complex
    • Banaszynski, L.; C.W., L.; Wandless, T. Characterization of the FKBP.rapamycin.FRB ternary complex J. Am. Chem. Soc. 2004, 127, 4715-4721
    • (2004) J. Am. Chem. Soc. , vol.127 , pp. 4715-4721
    • Banaszynski, L.1    C, W.L.2    Wandless, T.3
  • 11
    • 84861157343 scopus 로고    scopus 로고
    • Mammalian target of rapamycin integrates diverse inputs to guide the outcome of antigen recognition in T cells
    • Waickman, A. T.; Powell, J. D. Mammalian target of rapamycin integrates diverse inputs to guide the outcome of antigen recognition in T cells J. Immunol. 2012, 188, 4721-4729
    • (2012) J. Immunol. , vol.188 , pp. 4721-4729
    • Waickman, A.T.1    Powell, J.D.2
  • 12
    • 57149093203 scopus 로고    scopus 로고
    • FKBP family proteins: Immunophilins with versatile biological functions
    • Kang, C.; Hong, Y.; Dhe-Paganon, S.; Yoon, H. FKBP family proteins: immunophilins with versatile biological functions Neurosignals 2008, 16, 318-325
    • (2008) Neurosignals , vol.16 , pp. 318-325
    • Kang, C.1    Hong, Y.2    Dhe-Paganon, S.3    Yoon, H.4
  • 14
    • 33749324414 scopus 로고    scopus 로고
    • The intracellular domain of amyloid precursor protein interacts with FKBP12
    • Liu, F.; Liu, P.; Shao, H.; Kung, F. The intracellular domain of amyloid precursor protein interacts with FKBP12 Biochem. Biophys. Res. Commun. 2006, 350, 472-477
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 472-477
    • Liu, F.1    Liu, P.2    Shao, H.3    Kung, F.4
  • 16
    • 77949264184 scopus 로고    scopus 로고
    • Rapamycin inhibits relapsing experimental autoimmune encephalomyelitis by both effector and regulatory T cells modulation
    • Esposito, M.; Ruffini, F.; Bellone, M.; Gagliani, N.; Battaglia, M.; Martino, G.; Furlan, R. Rapamycin inhibits relapsing experimental autoimmune encephalomyelitis by both effector and regulatory T cells modulation J. Neuroimmunol. 2010, 220, 52-63
    • (2010) J. Neuroimmunol. , vol.220 , pp. 52-63
    • Esposito, M.1    Ruffini, F.2    Bellone, M.3    Gagliani, N.4    Battaglia, M.5    Martino, G.6    Furlan, R.7
  • 17
    • 84856959528 scopus 로고    scopus 로고
    • Rapamycin reduces clinical signs and neuropathic pain in a chronic model of experimental autoimmune encephalomyelitis
    • Lisi, L.; Navarra, P.; Cirocchi, R.; Sharp, A.; Stigliano, E.; Feinstein, D. L.; Dello Russo, C. Rapamycin reduces clinical signs and neuropathic pain in a chronic model of experimental autoimmune encephalomyelitis J. Neuroimmunol. 2012, 243, 43-51
    • (2012) J. Neuroimmunol. , vol.243 , pp. 43-51
    • Lisi, L.1    Navarra, P.2    Cirocchi, R.3    Sharp, A.4    Stigliano, E.5    Feinstein, D.L.6    Dello Russo, C.7
  • 18
    • 84856512814 scopus 로고    scopus 로고
    • Differential mTOR and ERK pathway utilization by effector CD4 T cells suggests combinatorial drug therapy of arthritis
    • Lin, J. T.; Stein, E. A.; Wong, M. T.; Kalpathy, K. J.; Su, L. L.; Utz, P. J.; Robinson, W. H.; Fathnnan, C. G. Differential mTOR and ERK pathway utilization by effector CD4 T cells suggests combinatorial drug therapy of arthritis Clin. Immunol. 2012, 142, 127-138
    • (2012) Clin. Immunol. , vol.142 , pp. 127-138
    • Lin, J.T.1    Stein, E.A.2    Wong, M.T.3    Kalpathy, K.J.4    Su, L.L.5    Utz, P.J.6    Robinson, W.H.7    Fathnnan, C.G.8
  • 19
    • 0037052635 scopus 로고    scopus 로고
    • Early decrease of the immunophilin FKBP 52 in the spinal cord of a transgenic model for amyotrophic lateral sclerosis
    • Manabe, Y.; Warita, H.; Murakami, T.; Shiote, M.; Hayashi, T.; Omori, N.; Nagano, I.; Shoji, M.; Abe, K. Early decrease of the immunophilin FKBP 52 in the spinal cord of a transgenic model for amyotrophic lateral sclerosis Brain Res. 2002, 935, 124-128
    • (2002) Brain Res. , vol.935 , pp. 124-128
    • Manabe, Y.1    Warita, H.2    Murakami, T.3    Shiote, M.4    Hayashi, T.5    Omori, N.6    Nagano, I.7    Shoji, M.8    Abe, K.9
  • 20
    • 80155142474 scopus 로고    scopus 로고
    • Rapamycin passes the torch: A new generation of mTOR inhibitors
    • Benjamin, D.; Colombi, M.; Moroni, C.; Hall, M. N. Rapamycin passes the torch: a new generation of mTOR inhibitors Nature 2011, 10, 868-880
    • (2011) Nature , vol.10 , pp. 868-880
    • Benjamin, D.1    Colombi, M.2    Moroni, C.3    Hall, M.N.4
  • 21
    • 33645832333 scopus 로고    scopus 로고
    • The aggregation of alpha-synuclein is stimulated by FK506 binding proteins as shown by fluorescence correlation spectroscopy
    • Gerard, M.; Debyser, Z.; Desender, L.; Kahle, P. J.; Baert, J.; Baekelandt, V.; Engelborghs, Y. The aggregation of alpha-synuclein is stimulated by FK506 binding proteins as shown by fluorescence correlation spectroscopy FASEB J 2006, 20, 524-526
    • (2006) FASEB J , vol.20 , pp. 524-526
    • Gerard, M.1    Debyser, Z.2    Desender, L.3    Kahle, P.J.4    Baert, J.5    Baekelandt, V.6    Engelborghs, Y.7
  • 22
    • 42449147105 scopus 로고    scopus 로고
    • Fragment-Based Synthesis and SAR of Modified FKBP Ligands: Influence of Different Linking on Binding Affinity
    • Roehrig, C. H.; Loch, C.; Guan, J.-Y.; Siegal, G.; Overhand, M. Fragment-Based Synthesis and SAR of Modified FKBP Ligands: Influence of Different Linking on Binding Affinity Chem. Med. Chem. 2007, 2, 1054-1070
    • (2007) Chem. Med. Chem. , vol.2 , pp. 1054-1070
    • Roehrig, C.H.1    Loch, C.2    Guan, J.-Y.3    Siegal, G.4    Overhand, M.5
  • 23
    • 79956069862 scopus 로고    scopus 로고
    • Intraligand hydrophobic interactions rationalize drug affinities for peptidyl-prolyl cis-trans isomerase protein
    • Bizzarri, M.; Marsili, S.; Procacci, P. Intraligand hydrophobic interactions rationalize drug affinities for peptidyl-prolyl cis-trans isomerase protein J. Phys. Chem. B 2011, 115, 6193-6201
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6193-6201
    • Bizzarri, M.1    Marsili, S.2    Procacci, P.3
  • 27
    • 0025955186 scopus 로고
    • Atomic structure of the rapamycin human immunophilin FKBP-12 complex
    • Van-Duyne, G.; Standaert, R. F.; Schreiber, S. L.; Clardy, J. Atomic structure of the rapamycin human immunophilin FKBP-12 complex J. Am. Chem. Soc. 1991, 113, 7433-7434
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7433-7434
    • Van-Duyne, G.1    Standaert, R.F.2    Schreiber, S.L.3    Clardy, J.4
  • 28
    • 44449107714 scopus 로고    scopus 로고
    • Crystal structure of the FK506 binding domain of Plasmodium falciparum FKBP35 in complex with FK506
    • Kotaka, M.; Ye, H.; Alag, R.; Hu, G.; Bozdech, Z.; Preiser, P.; Yoon, H.; Lescar, J. Crystal structure of the FK506 binding domain of Plasmodium falciparum FKBP35 in complex with FK506 Biochemistry 2008, 47, 5951-5961
    • (2008) Biochemistry , vol.47 , pp. 5951-5961
    • Kotaka, M.1    Ye, H.2    Alag, R.3    Hu, G.4    Bozdech, Z.5    Preiser, P.6    Yoon, H.7    Lescar, J.8
  • 29
    • 77955098310 scopus 로고    scopus 로고
    • NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35
    • Alag, R.; Qureshi, I.; Bharatham, N.; Shin, J.; Lescar, J.; Yoon, H. S. NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35 Protein Sci. 2010, 19, 1577-1586
    • (2010) Protein Sci. , vol.19 , pp. 1577-1586
    • Alag, R.1    Qureshi, I.2    Bharatham, N.3    Shin, J.4    Lescar, J.5    Yoon, H.S.6
  • 31
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C.; Laskowski, R. A.; Thornton, J. M. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions Protein Eng. 1995, 8, 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 34
    • 0026649497 scopus 로고
    • PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism
    • Park, S. T.; Aldape, R. A.; OlgaFuter; DeCenzo, M. T.; Livingston, D. J. PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism J. Biol. Chem. 1992, 267, 3316-3324
    • (1992) J. Biol. Chem. , vol.267 , pp. 3316-3324
    • Park, S.T.1    Aldape, R.A.2    Olgafuter3    Decenzo, M.T.4    Livingston, D.J.5
  • 35
    • 0037157317 scopus 로고    scopus 로고
    • On the Hamiltonian replica exchange method for efficient sampling of biomolecular systems: Application to protein structure prediction
    • Fukunishi, H.; Watanabe, O.; Takada, S. On the Hamiltonian replica exchange method for efficient sampling of biomolecular systems: Application to protein structure prediction J. Chem. Phys. 2002, 116, 9058-9067
    • (2002) J. Chem. Phys. , vol.116 , pp. 9058-9067
    • Fukunishi, H.1    Watanabe, O.2    Takada, S.3
  • 36
    • 77953056324 scopus 로고    scopus 로고
    • ORAC: A molecular dynamics simulation program to explore free energy surfaces in biomolecular systems at the atomistic level
    • Marsili, S.; Signorini, G. F.; Chelli, R.; Marchi, M.; Procacci, P. ORAC: A molecular dynamics simulation program to explore free energy surfaces in biomolecular systems at the atomistic level J. Comput. Chem. 2010, 31, 1106-11161
    • (2010) J. Comput. Chem. , vol.31 , pp. 1106-11161
    • Marsili, S.1    Signorini, G.F.2    Chelli, R.3    Marchi, M.4    Procacci, P.5
  • 37
    • 25444481354 scopus 로고    scopus 로고
    • Replica exchange with solute tempering: A method for sampling biological systems in explicit water
    • Liu, P.; Kim, B.; Friesner, R. A.; Berne, B. J. Replica exchange with solute tempering: A method for sampling biological systems in explicit water Proc. Acad. Sci. 2005, 102, 13749-13754
    • (2005) Proc. Acad. Sci. , vol.102 , pp. 13749-13754
    • Liu, P.1    Kim, B.2    Friesner, R.A.3    Berne, B.J.4
  • 39
    • 33751157732 scopus 로고
    • Ab initio calculation of vibrational absorption and circular dichroism spectra using density functional force fields
    • Stephens, P. J.; Devlin, F. J.; Chablowski, C. F.; Frisch, M. Ab initio calculation of vibrational absorption and circular dichroism spectra using density functional force fields J. Phys. Chem. 1994, 98, 11623-11627
    • (1994) J. Phys. Chem. , vol.98 , pp. 11623-11627
    • Stephens, P.J.1    Devlin, F.J.2    Chablowski, C.F.3    Frisch, M.4
  • 40
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • Singh, U. C.; Kollman, P. A. An approach to computing electrostatic charges for molecules J. Comput. Chem. 1984, 5, 129-145
    • (1984) J. Comput. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 41
    • 0032729435 scopus 로고    scopus 로고
    • Exploring expression data: Identification and analysis of coexpressed genes
    • Heyer, L. J.; Kruglyak, S.; Yooseph, S. Exploring expression data: identification and analysis of coexpressed genes Genome Res. 1999, 9, 1106-1115
    • (1999) Genome Res. , vol.9 , pp. 1106-1115
    • Heyer, L.J.1    Kruglyak, S.2    Yooseph, S.3
  • 42
    • 84861088407 scopus 로고    scopus 로고
    • Conformational landscape of N-glycosylated peptides detecting autoantibodies in multiple sclerosis, revealed by hamiltonian replica exchange
    • Guardiani, C.; Signorini, G. F.; Livi, R.; Papini, A. M.; Procacci, P. Conformational landscape of N-glycosylated peptides detecting autoantibodies in multiple sclerosis, revealed by hamiltonian replica exchange J. Phys. Chem. B 2012, 116, 5458-5467
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5458-5467
    • Guardiani, C.1    Signorini, G.F.2    Livi, R.3    Papini, A.M.4    Procacci, P.5
  • 43
    • 33845550192 scopus 로고
    • Asymmetric carbon-carbon bond formation via β- allyldiisopinocampheylborane. Simple synthesis of secondary homoallylic alcohols with excellent enantiomeric purities
    • Brown, H. C.; Jadhavl, K. J. Asymmetric carbon-carbon bond formation via β-allyldiisopinocampheylborane. Simple synthesis of secondary homoallylic alcohols with excellent enantiomeric purities J. Am. Chem. Soc. 1983, 105, 2092-2093
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2092-2093
    • Brown, H.C.1    Jadhavl, K.J.2
  • 45
    • 79956069862 scopus 로고    scopus 로고
    • The conformations of sb3 diastereoisomers in water were obtained using the trajectory data of a previous work
    • The conformations of sb3 diastereoisomers in water were obtained using the trajectory data of a previous work: Bizzarri, M. J. Phys. Chem. B 2011, 115, 6193-6201
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6193-6201
    • Bizzarri, M.1
  • 46
    • 0001019593 scopus 로고
    • i relative to FK506 were taken from
    • i relative to FK506 were taken from Holt, D. A. J. Am. Chem. Soc. 1993, 115, 9925-9938
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9925-9938
    • Holt, D.A.1
  • 47
    • 0001142212 scopus 로고
    • i relative to FK506 were taken from
    • i relative to FK506 were taken from Armistead, D. M. Acta Crystallogr. 1995, D51, 522-529
    • (1995) Acta Crystallogr. , vol.51 , pp. 522-529
    • Armistead, D.M.1
  • 48
    • 84873907553 scopus 로고    scopus 로고
    • Gnuplot 4.4, An Interative Plotting Program.
    • Williams, T.; Kelley, C. Gnuplot 4.4, An Interative Plotting Program. 2011; http://sourceforge.net/projects/gnuplot.
    • (2011)
    • Williams, T.1    Kelley, C.2
  • 49
    • 84962360214 scopus 로고    scopus 로고
    • Thermodynamics of stacking in proteins
    • Procacci, P. Thermodynamics of stacking in proteins Annu. Rep. Progr. Chem. Sect. C 2011, 107, 242-262
    • (2011) Annu. Rep. Progr. Chem. Sect. C , vol.107 , pp. 242-262
    • Procacci, P.1
  • 50
    • 78049348054 scopus 로고    scopus 로고
    • Molecular binding: Under water's influence
    • Hummer, G. Molecular binding: Under water's influence Nature Chem. 2010, 2, 906-906
    • (2010) Nature Chem. , vol.2 , pp. 906-906
    • Hummer, G.1
  • 51
    • 33645741621 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerase inhibitors
    • Wand, X.; Etzkorn, F. Peptidyl-prolyl isomerase inhibitors Biopolymers 2006, 84, 125-146
    • (2006) Biopolymers , vol.84 , pp. 125-146
    • Wand, X.1    Etzkorn, F.2
  • 52
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding, M.; Galat, A.; Uehling, D.; Schreiber, S. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase Nature 1989, 341, 758-760
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.1    Galat, A.2    Uehling, D.3    Schreiber, S.4
  • 53
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK 506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka, J.; Hung, S.; Poe, M.; Lin, C.; Sigal, N. A cytosolic binding protein for the immunosuppressant FK 506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin Nature 1989, 341, 755-757
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.1    Hung, S.2    Poe, M.3    Lin, C.4    Sigal, N.5
  • 54
    • 0027742843 scopus 로고
    • A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)
    • Fischer, S.; Michnick, S.; Karplus, M. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP) Biochemistry 1993, 32, 13830-13837
    • (1993) Biochemistry , vol.32 , pp. 13830-13837
    • Fischer, S.1    Michnick, S.2    Karplus, M.3
  • 56
    • 43949134176 scopus 로고    scopus 로고
    • Antibiotic association with phospholipid nanoassemblies: A comparison between Langmuir-Blodgett films and supported lipid bilayers
    • Morandi, S.; Puggelli, M.; Caminati, G. Antibiotic association with phospholipid nanoassemblies: A comparison between Langmuir-Blodgett films and supported lipid bilayers Colloids Surf., A 2008, 321, 125-130
    • (2008) Colloids Surf., A , vol.321 , pp. 125-130
    • Morandi, S.1    Puggelli, M.2    Caminati, G.3
  • 57
    • 84873918586 scopus 로고    scopus 로고
    • Interactions of lysozyme with phospholipid vesicles: Effects of vesicle biophysical features on protein misfolding and aggregation
    • Al-Kayal, T.; Russo, E.; Pieri, L.; Caminati, G.; Berti, D.; Bucciantini, M.; Stefani, M.; Baglioni, P. Interactions of lysozyme with phospholipid vesicles: effects of vesicle biophysical features on protein misfolding and aggregation Soft Matter 2012, 8, 9115-9126
    • (2012) Soft Matter , vol.8 , pp. 9115-9126
    • Al-Kayal, T.1    Russo, E.2    Pieri, L.3    Caminati, G.4    Berti, D.5    Bucciantini, M.6    Stefani, M.7    Baglioni, P.8


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