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Volumn 49, Issue 6, 2006, Pages 2063-2076

Synthesis and biological evaluation of purealin and analogues as cytoplasmic dynein heavy chain inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

3 [4 (3 AMINOPROPOXY) 3 BROMOPHENYL] N [2 (4 CHLOROPHENYL)ETHYL] 2 HYDROXYIMINOPROPANAMIDE; ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE INHIBITOR; ENZYME INHIBITOR; NATURAL PRODUCT; PUREALIDIN A; PUREALIN; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33645410730     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm051030l     Document Type: Article
Times cited : (40)

References (58)
  • 1
    • 0023205148 scopus 로고
    • Retrograde transport by the microtubule-associated protein MAP 1C
    • Paschal, B. M.; Vallee, R. B. Retrograde transport by the microtubule-associated protein MAP 1C. Nature 1987, 330, 181-183.
    • (1987) Nature , vol.330 , pp. 181-183
    • Paschal, B.M.1    Vallee, R.B.2
  • 2
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal, B. M.; Sheptner, H. S.; Vallee, R. B. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J. Cell Biol. 1987, 105, 1273-1282.
    • (1987) J. Cell Biol. , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Sheptner, H.S.2    Vallee, R.B.3
  • 3
    • 0028170819 scopus 로고
    • Dyneins; molecular structure and cellular function
    • Holzbaur, E. L.; VallEe, R. B. Dyneins; molecular structure and cellular function. Annu. Rev. Cell Biol. 1994, 10, 339-372.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 4
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale, R. D. The molecular motor toolbox for intracellular transport. Cell 2003, 112, 467-480.
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 5
    • 0027952753 scopus 로고
    • Phylogeny and expression of axonemal and cytoplasmic dynein genes in sea urchins
    • Gibbons, B. H.; Asai, D. J.; Tang, W. J.; Hays, T. S.; Gibbons, I. R. Phylogeny and expression of axonemal and cytoplasmic dynein genes in sea urchins. Mol. Biol. Cell 1994, 5, 57-70.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 57-70
    • Gibbons, B.H.1    Asai, D.J.2    Tang, W.J.3    Hays, T.S.4    Gibbons, I.R.5
  • 6
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R. B.; Williams, J. C.; Varma, D.; Barnhart, L. E. Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 2004, 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 7
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai, A. W.; Chuang, J. Z.; Bode, C.; Wolfrum, U.; Sung, C. H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 1999, 97, 877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 11
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B.; Ebersold, M. W.; Helenius, A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 1997, 136, 1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 12
    • 0032502017 scopus 로고    scopus 로고
    • Fluorescent virions: Dynamic tracking of the pathway of adenoviral gene transfer vectors in living cells
    • Leopold, P. L.; Ferris, B.; Grinberg, I.; Worgall, S.; Hackett, N. R.; Crystal, R. G. Fluorescent virions: dynamic tracking of the pathway of adenoviral gene transfer vectors in living cells. Hum. Gene Ther. 1998, 9, 367-378.
    • (1998) Hum. Gene Ther. , vol.9 , pp. 367-378
    • Leopold, P.L.1    Ferris, B.2    Grinberg, I.3    Worgall, S.4    Hackett, N.R.5    Crystal, R.G.6
  • 15
    • 0023266240 scopus 로고
    • Purealin, a novel activator of skeletal muscle actomyosin ATPase and myosin EDTA-ATPase that enhanced the superprecipitation of actomyosin
    • Nakamura, Y.; Kobayashi, M.; Nakamura, H.; Wu, H.; Kobayashi, J.; Ohizumi, Y. Purealin, a novel activator of skeletal muscle actomyosin ATPase and myosin EDTA-ATPase that enhanced the superprecipitation of actomyosin. Eur. J. Biochem. 1987, 167, 1-6.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 1-6
    • Nakamura, Y.1    Kobayashi, M.2    Nakamura, H.3    Wu, H.4    Kobayashi, J.5    Ohizumi, Y.6
  • 16
    • 0031454572 scopus 로고    scopus 로고
    • Purealin blocks the sliding movement of sea urchin flagellar axonemes by selective inhibition of half the ATPase activity of axonemal dyneins
    • Fang, Y. I.; Yokota, E.; Mabuchi, I.; Nakamura, H.; Ohizumi, Y. Purealin blocks the sliding movement of sea urchin flagellar axonemes by selective inhibition of half the ATPase activity of axonemal dyneins. Biochemistry 1997, 36, 15561-15567.
    • (1997) Biochemistry , vol.36 , pp. 15561-15567
    • Fang, Y.I.1    Yokota, E.2    Mabuchi, I.3    Nakamura, H.4    Ohizumi, Y.5
  • 17
    • 0023001902 scopus 로고
    • Purealin, a novel stabilizer of smooth muscle myosin filaments that modulates ATPase activity of dephosphorylated myosin
    • Takito, J.; Nakamura, H.; Kobayashi, J.; Ohizumi, Y.; Ebisawa, K.; Nonomura, Y. Purealin, a novel stabilizer of smooth muscle myosin filaments that modulates ATPase activity of dephosphorylated myosin. J. Biol. Chem. 1986, 261, 13861-13865.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13861-13865
    • Takito, J.1    Nakamura, H.2    Kobayashi, J.3    Ohizumi, Y.4    Ebisawa, K.5    Nonomura, Y.6
  • 18
    • 0022376954 scopus 로고
    • Physiologically active marine natural products from Porifera. IX. Purealin, a novel enzyme activator from the Okinawan marine sponge Psammaplysilla purea
    • Nakamura, H.; Wu, H.; Kobayashi, J.; Nakamura, Y.; Ohizumi, Y.; Hirata, Y. Physiologically active marine natural products from Porifera. IX. Purealin, a novel enzyme activator from the Okinawan marine sponge Psammaplysilla purea. Tetrahedron Lett. 1985, 26, 4517-4520.
    • (1985) Tetrahedron Lett. , vol.26 , pp. 4517-4520
    • Nakamura, H.1    Wu, H.2    Kobayashi, J.3    Nakamura, Y.4    Ohizumi, Y.5    Hirata, Y.6
  • 19
    • 0025881628 scopus 로고
    • Purealidin A, a new cytotoxic bromotyrosine-derived alkaloid from the Okinawan marine sponge Psammaplysilla purea
    • Ishibashi, M.; Tsuda, M.; Ohizumi, Y.; Sasaki, T.; Kobayashi, J. Purealidin A, a new cytotoxic bromotyrosine-derived alkaloid from the Okinawan marine sponge Psammaplysilla purea. Experientia 1991, 47, 299-300.
    • (1991) Experientia , vol.47 , pp. 299-300
    • Ishibashi, M.1    Tsuda, M.2    Ohizumi, Y.3    Sasaki, T.4    Kobayashi, J.5
  • 20
    • 0001675345 scopus 로고
    • Lipopurealins, novel bromotyrosine derivatives with long chain acyl groups from the marine sponge Psammaplysilla purea
    • Wu, H.; Nakamura, H.; Kobayashi, J.; Ohizumi, Y.; Hirata, Y. Lipopurealins, novel bromotyrosine derivatives with long chain acyl groups from the marine sponge Psammaplysilla purea. Experientia 1986, 42, 855-856.
    • (1986) Experientia , vol.42 , pp. 855-856
    • Wu, H.1    Nakamura, H.2    Kobayashi, J.3    Ohizumi, Y.4    Hirata, Y.5
  • 21
    • 0022298152 scopus 로고
    • Total synthesis of (±)-aerothionin. (±)-homoaerothinonin, and (±)-aerophobin-1
    • (a) Nishiyama, S.; Yamamura. S. Total synthesis of (±)- aerothionin. (±)-homoaerothinonin, and (±)-aerophobin-1. Bull. Chem. Soc. Jpn. 1985, 58, 3453-3456.
    • (1985) Bull. Chem. Soc. Jpn. , vol.58 , pp. 3453-3456
    • Nishiyama, S.1    Yamamura, S.2
  • 22
    • 0015276428 scopus 로고
    • Aeroplysinin-1, an antibacterial bromo-compound from the sponge Verongia aerophoba
    • (b) Fattorusso, E.; Minale, L.; Sodano, G. Aeroplysinin-1, an antibacterial bromo-compound from the sponge Verongia aerophoba. J. Chem. Soc., Perkin Trans. 1 1972, 16-18.
    • (1972) J. Chem. Soc., Perkin Trans. 1 , pp. 16-18
    • Fattorusso, E.1    Minale, L.2    Sodano, G.3
  • 23
    • 37049128554 scopus 로고
    • Aerothionin, a tetrabromo-compound from Aplysina aerophoba and Verongia thiona
    • Fattorusso, E.; Minale, L.; Sodano, G.; Moody, K.; Thomson, R. H. Aerothionin, a tetrabromo-compound from Aplysina aerophoba and Verongia thiona. Chem. Commun. 1970, 752-753.
    • (1970) Chem. Commun. , pp. 752-753
    • Fattorusso, E.1    Minale, L.2    Sodano, G.3    Moody, K.4    Thomson, R.H.5
  • 24
    • 0030592824 scopus 로고    scopus 로고
    • Oxidative cyclisation of o-phenolic oxime-acid derivatives using phenyliodonium diacetate: Synthesis of spiroisoxazoline derivatives
    • Murakata, M.; Yamada, K.; Hoshino, O. Oxidative cyclisation of o-phenolic oxime-acid derivatives using phenyliodonium diacetate: synthesis of spiroisoxazoline derivatives. Tetrahedron 1996, 52, 14713-14722.
    • (1996) Tetrahedron , vol.52 , pp. 14713-14722
    • Murakata, M.1    Yamada, K.2    Hoshino, O.3
  • 25
    • 0022499278 scopus 로고
    • Synthesis of the proposed penultimate biosynthetic triene intermediate of monensin A
    • Patel, D. V.; VanMiddlesworth, F.; Donaubauer, J.; Gannett, P.; Sih, C. J. Synthesis of the proposed penultimate biosynthetic triene intermediate of monensin A. J. Am. Chem. Soc. 1986, 105, 4603-4614.
    • (1986) J. Am. Chem. Soc. , vol.105 , pp. 4603-4614
    • Patel, D.V.1    Vanmiddlesworth, F.2    Donaubauer, J.3    Gannett, P.4    Sih, C.J.5
  • 27
    • 0005258794 scopus 로고
    • Solvolytic elimination and hydrolysis promoted by an aromatic hydroxy group. Part 1. The reaction of 2,6-dibromo-4-dibromomethylphenol and of 2,6-dibromo-4-bromomethylenecyclohexa-2,5-dienone with water in 95% 1.4-dioxane
    • De la Mare, P. B. D.; Newman, P. A. Solvolytic elimination and hydrolysis promoted by an aromatic hydroxy group. Part 1. The reaction of 2,6-dibromo-4-dibromomethylphenol and of 2,6-dibromo-4-bromomethylenecyclohexa- 2,5-dienone with water in 95% 1.4-dioxane. J. Chem. Soc., Perkin Trans. 2 1984, 2, 231-238.
    • (1984) J. Chem. Soc., Perkin Trans. 2 , vol.2 , pp. 231-238
    • De La Mare, P.B.D.1    Newman, P.A.2
  • 28
    • 0000069626 scopus 로고    scopus 로고
    • Studies on synthesis of araplysillins via oxidative cyclisation of o-phenolic oxime-acid derivatives using phenyliodonium diacetate
    • Murakata, M.; Yamada, K.; Hoshino, O. Studies on synthesis of araplysillins via oxidative cyclisation of o-phenolic oxime-acid derivatives using phenyliodonium diacetate. Heterocycles 1998, 47, 921-931.
    • (1998) Heterocycles , vol.47 , pp. 921-931
    • Murakata, M.1    Yamada, K.2    Hoshino, O.3
  • 29
    • 0021307326 scopus 로고
    • Imidazole H-2 agonists. Synthesis and activity of 2-(2-amino-4- imidazolyl)ethylamine(2-aminohistamine) dihydrochloride
    • (a) Vitali, T.; Impicciatore, M.; Plazzi, P. V.; Bordi, F.; Vitto, M. Imidazole H-2 agonists. Synthesis and activity of 2-(2-amino-4-imidazolyl) ethylamine(2-aminohistamine) dihydrochloride. Farm., Sci. Ed. 1984, 39, 70-80.
    • (1984) Farm., Sci. Ed. , vol.39 , pp. 70-80
    • Vitali, T.1    Impicciatore, M.2    Plazzi, P.V.3    Bordi, F.4    Vitto, M.5
  • 30
    • 0015888244 scopus 로고
    • Synthesis of 2-amino-L-histidine and 2-aminohistamine
    • (b) Nagai, W.; Kirk, K. L.; Cohen, L. A. Synthesis of 2-amino-L-histidine and 2-aminohistamine. J. Org. Chem. 1973, 38, 1971-1974.
    • (1973) J. Org. Chem. , vol.38 , pp. 1971-1974
    • Nagai, W.1    Kirk, K.L.2    Cohen, L.A.3
  • 31
    • 0542430100 scopus 로고
    • Quantitative dealkylation of alkyl ethers via treatment with trimethylsilyl iodide. A new method for ether hydrolysis
    • Jung, M. E.; Lyster, M. A. Quantitative dealkylation of alkyl ethers via treatment with trimethylsilyl iodide. A new method for ether hydrolysis. J. Org. Chem. 1977, 42, 3761-3764.
    • (1977) J. Org. Chem. , vol.42 , pp. 3761-3764
    • Jung, M.E.1    Lyster, M.A.2
  • 33
    • 46149140781 scopus 로고
    • On the selectivity of deprotection of benzyl, MPM (4-methoxybenzyl) and DMPM (3,4-dimethoxybenzyl) protecting groups for hydroxy functions
    • (a) Horita, K.; Yoshioka, T.; Tanaka, T.; Oikawa, Y.; Yonemitsu, O. On the selectivity of deprotection of benzyl, MPM (4-methoxybenzyl) and DMPM (3,4-dimethoxybenzyl) protecting groups for hydroxy functions. Tetrahedron 1986, 42, 3021-3028.
    • (1986) Tetrahedron , vol.42 , pp. 3021-3028
    • Horita, K.1    Yoshioka, T.2    Tanaka, T.3    Oikawa, Y.4    Yonemitsu, O.5
  • 34
    • 0000244323 scopus 로고
    • Chiral synthesis of polyketide-derived natural products. Part 9. Total synthesis of tylonolide, the aglycone of the 16-membered ring macrolide tylosin, from D-glucose. Selective application of MPM and DMPM protecting groups for hydroxy functions
    • (b) Tanaka, T.; Oikawa, Y.; Hamada, T.; Yonemitsu, O. Chiral synthesis of polyketide-derived natural products. Part 9. Total synthesis of tylonolide, the aglycone of the 16-membered ring macrolide tylosin, from D-glucose. Selective application of MPM and DMPM protecting groups for hydroxy functions. Tetrahedron Lett. 1986, 27, 3651-3654.
    • (1986) Tetrahedron Lett. , vol.27 , pp. 3651-3654
    • Tanaka, T.1    Oikawa, Y.2    Hamada, T.3    Yonemitsu, O.4
  • 35
    • 0000192963 scopus 로고
    • Specific removal of O-methoxybenzyl protection by DDQ oxidation
    • Oikawa, Y.; Yoshioka, T.; Yonemitsu, O. Specific removal of O-methoxybenzyl protection by DDQ oxidation. Tetrahedron Lett. 1982, 23, 885-888.
    • (1982) Tetrahedron Lett. , vol.23 , pp. 885-888
    • Oikawa, Y.1    Yoshioka, T.2    Yonemitsu, O.3
  • 36
    • 0025881628 scopus 로고
    • Purealidin A, a new cytotoxic bromotyrosine derived alkaloid from the Okinawan marine sponge Psammaplysilla purea
    • Ishibashi, M.; Tsuda, M.; Ohizumi, Y.; Sasaki, T.; Kobayashi, J. Purealidin A, a new cytotoxic bromotyrosine derived alkaloid from the Okinawan marine sponge Psammaplysilla purea. Experientia 1991, 47, 299-300.
    • (1991) Experientia , vol.47 , pp. 299-300
    • Ishibashi, M.1    Tsuda, M.2    Ohizumi, Y.3    Sasaki, T.4    Kobayashi, J.5
  • 37
    • 0001675345 scopus 로고
    • Lipopurealins, novel bromotyrosine derivatives with long chain acyl groups from the marine sponge Psammaplysilla purea
    • Wu, H.; Nakamura, H.; Kobayashi, J.; Ohizumi, Y.; Hirata, Y. Lipopurealins, novel bromotyrosine derivatives with long chain acyl groups from the marine sponge Psammaplysilla purea. Experientia 1986, 42, 855-856.
    • (1986) Experientia , vol.42 , pp. 855-856
    • Wu, H.1    Nakamura, H.2    Kobayashi, J.3    Ohizumi, Y.4    Hirata, Y.5
  • 38
    • 0037093942 scopus 로고    scopus 로고
    • Total synthesis of the ramoplanin A2 and ramoplanose aglycon
    • (a) Jiang, W.; Wanner, J.; Lee, R. J.; Bounaud, P. Y.; Boger, D. L. Total synthesis of the ramoplanin A2 and ramoplanose aglycon. J. Am. Chem. Soc. 2002, 124, 5288-5290.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5288-5290
    • Jiang, W.1    Wanner, J.2    Lee, R.J.3    Bounaud, P.Y.4    Boger, D.L.5
  • 39
    • 0027139933 scopus 로고
    • (-)-Sandramycin: Total synthesis and preliminary DNA binding properties
    • (b) Boger, D. L.; Chen, J.-H. (-)-Sandramycin: total synthesis and preliminary DNA binding properties. J. Am. Chem. Soc. 1993, 115, 11624-11625.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11624-11625
    • Boger, D.L.1    Chen, J.-H.2
  • 40
    • 25444452497 scopus 로고    scopus 로고
    • Long-range allosteric control of cytoplasmic dynein ATPase activity by the stalk and C-terminal domains
    • Hook, P.; Mikami, A.; Shafer, B.; Chait, B. T.; Rosenfeld, S. S.; Vallee, R. B. Long-range allosteric control of cytoplasmic dynein ATPase activity by the stalk and C-terminal domains. J. Biol. Chem. 2005, 280, 33045-33054.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33045-33054
    • Hook, P.1    Mikami, A.2    Shafer, B.3    Chait, B.T.4    Rosenfeld, S.S.5    Vallee, R.B.6
  • 42
    • 1242319567 scopus 로고    scopus 로고
    • Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae
    • Reck-Peterson, S. L.; Vale, R. D. Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 1491-1495.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1491-1495
    • Reck-Peterson, S.L.1    Vale, R.D.2
  • 44
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath, H.; Huang, D. C; O'Reilly, L. A.; King, S. M.; Strasser, A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell 1999, 3, 287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 45
    • 0033759911 scopus 로고    scopus 로고
    • Mitotic phosphorylation of the dynein light intermediate chain is mediated by cdc2 kinase
    • Dell, K. R.; Turck, C. W.; Vale, R. D. Mitotic phosphorylation of the dynein light intermediate chain is mediated by cdc2 kinase. Traffic 2000, 1, 38-44.
    • (2000) Traffic , vol.1 , pp. 38-44
    • Dell, K.R.1    Turck, C.W.2    Vale, R.D.3
  • 46
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi, Y.; Kovacs, J. J.; McLaurin, A.; Vance, J. M.; Ito, A.; Yao, T. P. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003, 115, 727-738.
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 47
    • 2542482495 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus
    • Galigniana, M. D.; Harrell, J. M.; O'Hagen, H. M.; Ljungman, M.; Pratt, W. B. Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus. J. Biol. Chem. 2004, 279, 22483-22489.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22483-22489
    • Galigniana, M.D.1    Harrell, J.M.2    O'Hagen, H.M.3    Ljungman, M.4    Pratt, W.B.5
  • 48
    • 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.; Pratt, W. B. 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. 2001, 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
  • 49
    • 0141768258 scopus 로고    scopus 로고
    • The roles of microtubule-based motor proteins in mitosis: Comprehensive RNAi analysis in the Drosophila S2 cell line
    • Goshima, G.; Vale, R. D. The roles of microtubule-based motor proteins in mitosis: comprehensive RNAi analysis in the Drosophila S2 cell line. J. Cell Biol. 2003, 162, 1003-1016.
    • (2003) J. Cell Biol. , vol.162 , pp. 1003-1016
    • Goshima, G.1    Vale, R.D.2
  • 50
    • 0032497694 scopus 로고    scopus 로고
    • The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos
    • Skop, A. R.; White, J. G. The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos. Curr. Biol. 1998, 8, 1110-1116.
    • (1998) Curr. Biol. , vol.8 , pp. 1110-1116
    • Skop, A.R.1    White, J.G.2
  • 51
    • 2342479988 scopus 로고    scopus 로고
    • Interaction of Cep135 with a p50 dynactin subunit in mammalian centrosomes
    • Uetake, Y.; Terada, Y.; Matuliene, J.; Kuriyama, R. Interaction of Cep135 with a p50 dynactin subunit in mammalian centrosomes. Cell Motil. Cytoskeleton 2004, 58, 53-66.
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 53-66
    • Uetake, Y.1    Terada, Y.2    Matuliene, J.3    Kuriyama, R.4
  • 52
    • 5144228139 scopus 로고    scopus 로고
    • Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning
    • Shu, T.; Ayala, R.; Nguyen, M. D.; Xie, Z.; Gleeson, J. G.; Tsai, L. H. Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning. Neuron 2004, 44, 263-277.
    • (2004) Neuron , vol.44 , pp. 263-277
    • Shu, T.1    Ayala, R.2    Nguyen, M.D.3    Xie, Z.4    Gleeson, J.G.5    Tsai, L.H.6
  • 53
    • 24944431844 scopus 로고    scopus 로고
    • LIS1 RNA interference blocks neural stem cell division, morphogenesis, and motility at multiple stages
    • Tsai, J. W.; Chen, Y.; Kriegstein, A. R.; Vallee, R. B. LIS1 RNA interference blocks neural stem cell division, morphogenesis, and motility at multiple stages. J. Cell Biol. 2005, 170, 935-945.
    • (2005) J. Cell Biol. , vol.170 , pp. 935-945
    • Tsai, J.W.1    Chen, Y.2    Kriegstein, A.R.3    Vallee, R.B.4
  • 54
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • Kon, T.; Nishiura, M.; Ohkura, R.; Toyoshima, Y. Y.; Sutoh, K. Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein. Biochemistry 2004, 43, 11266-11274.
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 56
    • 0025899234 scopus 로고
    • Use of an aqueous soluble tetrazolium/formazan assay for cell growth assays in culture
    • Cory, A. H.; Owen, T. C.; Barltrop, J. A.; Cory, J. G. Use of an aqueous soluble tetrazolium/formazan assay for cell growth assays in culture. Cancer Commun. 1991, 3, 207-212.
    • (1991) Cancer Commun. , vol.3 , pp. 207-212
    • Cory, A.H.1    Owen, T.C.2    Barltrop, J.A.3    Cory, J.G.4
  • 57
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantition of microgram quantities of protein utilizing the principle of dye-binding
    • Bradford, M., A rapid and sensitive method for the quantition of microgram quantities of protein utilizing the principle of dye-binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 58


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