메뉴 건너뛰기




Volumn 21, Issue 11, 2007, Pages 2787-2797

The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation

Author keywords

Cytoskeleton; FK506 binding protein; Microtubule dynamics; Neurite differentiation

Indexed keywords

FK 52 BINDING PROTEIN; IMMUNOPHILIN; SMALL INTERFERING RNA; TUBULIN; UNCLASSIFIED DRUG;

EID: 34548485298     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.06-7667com     Document Type: Article
Times cited : (83)

References (56)
  • 1
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S. L. (1991) Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251, 283-287
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 2
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J. D., Jr., Lane, W. S., Friedman, J., Weissman, I., and Schreiber, S. L. (1991) Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 3
    • 0025035368 scopus 로고
    • Complementary DNA encoding the human T-cell FK506 binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin
    • Maki, N., Sekiguchi, F., Nishimaki, J., Miwa, K., Hayano, T., Takahashi, N., and Susuki, M. (1990) Complementary DNA encoding the human T-cell FK506 binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin. Proc. Natl. Acad. Sci. U. S. A. 87, 5440-5443
    • (1990) Proc. Natl. Acad. Sci. U. S. A , vol.87 , pp. 5440-5443
    • Maki, N.1    Sekiguchi, F.2    Nishimaki, J.3    Miwa, K.4    Hayano, T.5    Takahashi, N.6    Susuki, M.7
  • 4
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Göthel, S. F., and Marahiel, M. A. (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol. Life Sci. 55, 423-436
    • (1999) Cell Mol. Life Sci , vol.55 , pp. 423-436
    • Göthel, S.F.1    Marahiel, M.A.2
  • 6
    • 0028900536 scopus 로고
    • Immunophilins and the nervous system
    • Snyder, S. H., and Sabatini, D. M. (1995) Immunophilins and the nervous system. Nature Med. 1, 32-37
    • (1995) Nature Med , vol.1 , pp. 32-37
    • Snyder, S.H.1    Sabatini, D.M.2
  • 7
    • 0035525574 scopus 로고    scopus 로고
    • FKBP ligands as novel therapeutics for neurological disorders
    • Christner, C., Herdegen, T., and Fischer, G. (2001) FKBP ligands as novel therapeutics for neurological disorders. Mini. Rev. Med. Chem. 1, 377-397
    • (2001) Mini. Rev. Med. Chem , vol.1 , pp. 377-397
    • Christner, C.1    Herdegen, T.2    Fischer, G.3
  • 8
    • 23644461186 scopus 로고    scopus 로고
    • Neuroprotection and promoting neurological recovery following peripheral nerve and spinal cord lesions
    • Sosa, I., Reyes, O., and Kuffler, D. P. (2005) Neuroprotection and promoting neurological recovery following peripheral nerve and spinal cord lesions. Exp. Neurol. 195, 7-15
    • (2005) Exp. Neurol , vol.195 , pp. 7-15
    • Sosa, I.1    Reyes, O.2    Kuffler, D.P.3
  • 9
    • 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)
    • Galat, A. (2004) A note on clustering the functionally-related paralogues and orthologues of proteins: a case of the FK506-binding proteins (FKBPs). Comput. Biol. Chem. 28, 129-140
    • (2004) Comput. Biol. Chem , vol.28 , pp. 129-140
    • Galat, A.1
  • 11
    • 0026495863 scopus 로고
    • Expression and characterisation of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes
    • Peattie, D. A., Harding, M. W., Fleming, M. A., DeCenzo, M. T., Lippke, J. A., Livingston, D. J., and Benasutti, M. (1992) Expression and characterisation of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. U. S. A. 89, 10974-10978
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Harding, M.W.2    Fleming, M.A.3    DeCenzo, M.T.4    Lippke, J.A.5    Livingston, D.J.6    Benasutti, M.7
  • 12
    • 4644318581 scopus 로고    scopus 로고
    • Davies, T. H., and Sanchez, E. R. (2005) FKBP52. Int. J. Biochem. Cell Biol. 37, 42-47
    • Davies, T. H., and Sanchez, E. R. (2005) FKBP52. Int. J. Biochem. Cell Biol. 37, 42-47
  • 13
    • 2942593899 scopus 로고    scopus 로고
    • 3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex
    • Wu, B., Li, P., Liu, Y., Lou, Z., Ding, Y., Shu, C., Ye, S., Bartlam, M., Shen, B., and Rao, Z. (2004) 3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex. Proc. Natl. Acad. Sci. U. S. A. 101, 8348-8353
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 8348-8353
    • Wu, B.1    Li, P.2    Liu, Y.3    Lou, Z.4    Ding, Y.5    Shu, C.6    Ye, S.7    Bartlam, M.8    Shen, B.9    Rao, Z.10
  • 17
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by tetratricopetide repeat domain
    • Radanyi, C., Chambraud, B., and Baulieu, E. E. (1994) The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by tetratricopetide repeat domain. Proc. Natl. Acad. Sci. U. S. A. 91, 11197-11201
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu, E.E.3
  • 18
    • 0022918191 scopus 로고
    • A 59-Kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors
    • Tai, P. K., Maeda, Y., Nakao, K., Wakim, N. G., Duhring, J. L., and Faber, L. E. (1986) A 59-Kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors. Biochemistry 25, 5269-5275
    • (1986) Biochemistry , vol.25 , pp. 5269-5275
    • Tai, P.K.1    Maeda, Y.2    Nakao, K.3    Wakim, N.G.4    Duhring, J.L.5    Faber, L.E.6
  • 19
    • 0025337581 scopus 로고
    • The Non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein
    • Renoir, J. M., Radanyi, C., Faber, L. E., and Baulieu, E. E. (1990) The Non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein. J. Biol. Chem. 265, 10740-10745
    • (1990) J. Biol. Chem , vol.265 , pp. 10740-10745
    • Renoir, J.M.1    Radanyi, C.2    Faber, L.E.3    Baulieu, E.E.4
  • 20
    • 0026730719 scopus 로고
    • Rabbit FKBP59-heat shock protein binding immunophilin (HBI) is a calmodulin binding protein
    • Massol, N., Lebau, M. C., Renoir, J. M., Faber, L. E., and Baulieu, E. E. (1992) Rabbit FKBP59-heat shock protein binding immunophilin (HBI) is a calmodulin binding protein. Biochem. Biophys. Res. Commun. 187, 1330-1335
    • (1992) Biochem. Biophys. Res. Commun , vol.187 , pp. 1330-1335
    • Massol, N.1    Lebau, M.C.2    Renoir, J.M.3    Faber, L.E.4    Baulieu, E.E.5
  • 22
    • 14244262261 scopus 로고    scopus 로고
    • FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • Wochnick, G. M., Ruegg, J., Abel, G. A., Schmidt, U., Holboer, F., and Rein, T. (2005) FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280, 4609-46016
    • (2005) J. Biol. Chem , vol.280 , pp. 4609-46016
    • Wochnick, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holboer, F.5    Rein, T.6
  • 23
    • 0028596331 scopus 로고
    • The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same non random regions within the nucleus as the steroid receptor
    • Czar, M. J., Owens-Grillo, J. K., Yem, A. W., Leach, K. L., Deibel, M. R., Welsh, M. J., and Pratt, W. B. (1994) The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same non random regions within the nucleus as the steroid receptor. Mol. Endocrinol. 8, 1731-1741
    • (1994) Mol. Endocrinol , vol.8 , pp. 1731-1741
    • Czar, M.J.1    Owens-Grillo, J.K.2    Yem, A.W.3    Leach, K.L.4    Deibel, M.R.5    Welsh, M.J.6    Pratt, W.B.7
  • 24
    • 0029013233 scopus 로고
    • The 59 kDa FK506-binding protein, a 90kDa heat shock protein binding immunophilin (FKBP59-HBI), is associated with the nucleus, the cytoskeleton and mitotic apparatus
    • Perrot-Applanat, M., Cibert, C., Géraud, G., Renoir, J. M., and Baulieu, E. E. (1995) The 59 kDa FK506-binding protein, a 90kDa heat shock protein binding immunophilin (FKBP59-HBI), is associated with the nucleus, the cytoskeleton and mitotic apparatus. J. Cell Sci. 108, 2037-2051
    • (1995) J. Cell Sci , vol.108 , pp. 2037-2051
    • Perrot-Applanat, M.1    Cibert, C.2    Géraud, G.3    Renoir, J.M.4    Baulieu, E.E.5
  • 25
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana, M. D., Radanyi, C., Renoir, J. M., Housley, P. R., and Pratt, W. B. (2001) Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J. Biol. Chem. 276, 14884-14889
    • (2001) J. Biol. Chem , vol.276 , pp. 14884-14889
    • Galigniana, M.D.1    Radanyi, C.2    Renoir, J.M.3    Housley, P.R.4    Pratt, W.B.5
  • 26
    • 2542482495 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins links p53 to dynein during p53 transport to the nucleus
    • Galigniana, M. D., Harell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) Hsp90-binding immunophilins links p53 to dynein during p53 transport to the nucleus. J. Biol. Chem. 279, 22483-22489
    • (2004) J. Biol. Chem , vol.279 , pp. 22483-22489
    • Galigniana, M.D.1    Harell, J.M.2    O'Hagen, H.M.3    Ljungman, M.4    Pratt, W.B.5
  • 28
    • 0033034203 scopus 로고    scopus 로고
    • Immunophilin FK506-binding protein 52 (not FK506-binding protein 12) mediates the neurotrophic action of FK506
    • Gold, B. G., Densmore, V., Shou, W., Matzuk, M. M., and Gordon, H. S. (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
  • 29
    • 0042970735 scopus 로고    scopus 로고
    • FK506 and its analogs - therapeutic potential for neurological disorders
    • Klettner, A., and Herdegen, T. (2003) FK506 and its analogs - therapeutic potential for neurological disorders. Curr. Drug Targets CNS Neurol. Disord. 2, 153-162
    • (2003) Curr. Drug Targets CNS Neurol. Disord , vol.2 , pp. 153-162
    • Klettner, A.1    Herdegen, T.2
  • 30
    • 2442537231 scopus 로고    scopus 로고
    • Role of hsp90 and the hsp90-binding immunophimins in signalling protein movement
    • Pratt, W. B., Galigniana, M. D., Harell, J. M., and DeFranco, D. B. (2004) Role of hsp90 and the hsp90-binding immunophimins in signalling protein movement. Cell Signal. 16, 857-872
    • (2004) Cell Signal , vol.16 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harell, J.M.3    DeFranco, D.B.4
  • 31
    • 0141595912 scopus 로고    scopus 로고
    • Neuroimmunophilin ligands: The development of novel neurogenerative/neuroprotective compounds
    • Gold, B. G., and Villafranca, J. E. (2003) Neuroimmunophilin ligands: the development of novel neurogenerative/neuroprotective compounds. Curr. Top. Med. Chem. 3, 1368-1375
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 1368-1375
    • Gold, B.G.1    Villafranca, J.E.2
  • 32
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing, K. H. (2000) Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 16, 89-111
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 33
  • 34
    • 0033199627 scopus 로고    scopus 로고
    • Establishment and plasticity of neuronal polarity
    • Mattson, M. P. (1999) Establishment and plasticity of neuronal polarity. J. Neurosci. Res. 57, 577-589
    • (1999) J. Neurosci. Res , vol.57 , pp. 577-589
    • Mattson, M.P.1
  • 35
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T., and Kirschner, M. (1984) Dynamic instability of microtubule growth. Nature 312, 237-242
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 37
    • 0345393105 scopus 로고    scopus 로고
    • Purification of brain tubulin through two cycles of polymerization-depolymerization in high-molarity buffer
    • Castoldi, M., and Popov, A. V. (2003) Purification of brain tubulin through two cycles of polymerization-depolymerization in high-molarity buffer. Protein Exp. Purif. 32, 83-88
    • (2003) Protein Exp. Purif , vol.32 , pp. 83-88
    • Castoldi, M.1    Popov, A.V.2
  • 38
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbaschir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 24, 494-498
    • (2001) Nature , vol.24 , pp. 494-498
    • Elbaschir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 39
    • 0031053574 scopus 로고    scopus 로고
    • Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with HSP90 and progesterone receptor
    • Nair, S. C., Rimerman, R., Toran, E. J., Chen, S., Prapapanich, V., Butts, R. N., and Smith, D. F. (1997) Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with HSP90 and progesterone receptor. Mol. Cell Biol. 17, 594-603
    • (1997) Mol. Cell Biol , vol.17 , pp. 594-603
    • Nair, S.C.1    Rimerman, R.2    Toran, E.J.3    Chen, S.4    Prapapanich, V.5    Butts, R.N.6    Smith, D.F.7
  • 40
    • 0345144024 scopus 로고    scopus 로고
    • Structure of the large FK506-binding protein FKBP51, an HSP90-binding protein and a component of steroid receptor complexes
    • Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F., and Clardy, J. (2003) Structure of the large FK506-binding protein FKBP51, an HSP90-binding protein and a component of steroid receptor complexes. Proc. Natl. Acad. Sci. U. S. A. 100, 868-873
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 868-873
    • Sinars, C.R.1    Cheung-Flynn, J.2    Rimerman, R.A.3    Scammell, J.G.4    Smith, D.F.5    Clardy, J.6
  • 41
    • 0345169048 scopus 로고    scopus 로고
    • Post translational modifications regulate microtubule function
    • Westermann, S., and Weber, K. (2003) Post translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4, 938-947
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 43
    • 0033965785 scopus 로고    scopus 로고
    • Microtubule dynamics and tubulin interacting proteins
    • Walczak, C. E. (2000) Microtubule dynamics and tubulin interacting proteins. Curr. Opin. Cell Biol. 12, 52-56
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 52-56
    • Walczak, C.E.1
  • 44
    • 0033534575 scopus 로고    scopus 로고
    • Kin I kinesins are microtubule-destabilizing enzymes
    • Desai, A., Verma, S., Mitchison, T. J., and Walczak, C. E. (1999) Kin I kinesins are microtubule-destabilizing enzymes. Cell 96, 69-78
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1    Verma, S.2    Mitchison, T.J.3    Walczak, C.E.4
  • 46
    • 0018650541 scopus 로고
    • Fine structure of initial outgrowth of processes induced in a pheochromocytoma cell line (PC12) by nerve growth factor
    • Luckenbill-Edds, L., Van Horn, C., and Greene, L. A. (1979) Fine structure of initial outgrowth of processes induced in a pheochromocytoma cell line (PC12) by nerve growth factor. J. Neurocytol. 8, 493-511
    • (1979) J. Neurocytol , vol.8 , pp. 493-511
    • Luckenbill-Edds, L.1    Van Horn, C.2    Greene, L.A.3
  • 47
    • 0021035904 scopus 로고
    • Microtubule proteins in PC12 pheochromocytoma cells. Isolation, composition and in vitro phosphorylation
    • Richter-Landsberg, C., Landreth, G. E., and Shooter, E. M. (1983-1984) Microtubule proteins in PC12 pheochromocytoma cells. Isolation, composition and in vitro phosphorylation. Dev. Neurosci. 6, 32-44
    • (1983) Dev. Neurosci , vol.6 , pp. 32-44
    • Richter-Landsberg, C.1    Landreth, G.E.2    Shooter, E.M.3
  • 48
    • 16844372144 scopus 로고    scopus 로고
    • Structural rearrangements in tubulin following microtubule formation
    • Krebs, A., Goldie, K. N., and Hoenger, A. (2005) Structural rearrangements in tubulin following microtubule formation. EMBO Rep. 6, 227-232
    • (2005) EMBO Rep , vol.6 , pp. 227-232
    • Krebs, A.1    Goldie, K.N.2    Hoenger, A.3
  • 49
    • 0020317964 scopus 로고
    • Two opposing effects of calmodulin on microtubule assembly depend on the presence of microtubule-associated proteins
    • Lee, Y. C., and Wolff, J. (1982) Two opposing effects of calmodulin on microtubule assembly depend on the presence of microtubule-associated proteins. J. Biol. Chem. 257, 6306-6310
    • (1982) J. Biol. Chem , vol.257 , pp. 6306-6310
    • Lee, Y.C.1    Wolff, J.2
  • 53
    • 0035494477 scopus 로고    scopus 로고
    • Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth and microtubule organization
    • Teng, J., Takei, Y., Harada, A., Nakata, T., Chen, J., and Hirokawa, N. (2001) Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth and microtubule organization. J. Cell Biol. 155, 65-76
    • (2001) J. Cell Biol , vol.155 , pp. 65-76
    • Teng, J.1    Takei, Y.2    Harada, A.3    Nakata, T.4    Chen, J.5    Hirokawa, N.6
  • 54
    • 0032230312 scopus 로고    scopus 로고
    • Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 Binding and association with progesterone receptor complexes
    • Barent, R. L., Nair, S. C., Carr, D. C., Ruan, Y., Rimerman, R. A., Fulton, J., Zhang, Y., and Smith, D. F. (1998) Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 Binding and association with progesterone receptor complexes. Mol. Endocrinol. 12, 342-354
    • (1998) Mol. Endocrinol , vol.12 , pp. 342-354
    • Barent, R.L.1    Nair, S.C.2    Carr, D.C.3    Ruan, Y.4    Rimerman, R.A.5    Fulton, J.6    Zhang, Y.7    Smith, D.F.8
  • 55
    • 0038269022 scopus 로고    scopus 로고
    • C-terminal sequences outside the tetratricopetide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90
    • Cheung-Flynn, J., Roberts, P. J., Riggs, D. L., and Smith, D. F. (2003) C-terminal sequences outside the tetratricopetide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90. J. Biol. Chem. 278, 17388-17394
    • (2003) J. Biol. Chem , vol.278 , pp. 17388-17394
    • Cheung-Flynn, J.1    Roberts, P.J.2    Riggs, D.L.3    Smith, D.F.4
  • 56
    • 0031473847 scopus 로고    scopus 로고
    • Swiss model and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) Swiss model and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.