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Volumn 19, Issue 2, 1999, Pages 1486-1497

Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor protein

Author keywords

[No Author keywords available]

Indexed keywords

5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; DACTINOMYCIN; GENE PRODUCT; GLUCOSE TRANSPORTER; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; LEPTOMYCIN B; MESSENGER RNA; VASCULOTROPIN;

EID: 0344026345     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.19.2.1486     Document Type: Article
Times cited : (115)

References (70)
  • 1
    • 0032557655 scopus 로고    scopus 로고
    • The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm
    • Afonina, E., R. Stauber, and G. N. Pavlakis. 1998. The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm. J. Biol. Chem. 273:13015-13021.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13015-13021
    • Afonina, E.1    Stauber, R.2    Pavlakis, G.N.3
  • 2
    • 0029084914 scopus 로고
    • Elongin (SIII). A multisubunit regulator of elongation by RNA polymerase II
    • Aso, T., W. S. Lane, J. W. Conaway, and R. C. Conaway. 1995. Elongin (SIII). A multisubunit regulator of elongation by RNA polymerase II. Science 269: 1439-1443.
    • (1995) Science , vol.269 , pp. 1439-1443
    • Aso, T.1    Lane, W.S.2    Conaway, J.W.3    Conaway, R.C.4
  • 3
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., P. Sen, K. Hofmann, L. Ma, M. Goebl, J. W. Harper, and S. J. Elledge. 1996. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86:263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 4
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres, J. F., G. R. Screaton, and A. R. Krainer. 1998. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 12:55-66.
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 5
    • 0028981766 scopus 로고
    • Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: Correlations with phenotype
    • Chen, F., T. Kishida, M. Yao, T. Hustad, D. Glavac, et al. 1995. Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: correlations with phenotype. Hum. Mutat. 5:66-75.
    • (1995) Hum. Mutat. , vol.5 , pp. 66-75
    • Chen, F.1    Kishida, T.2    Yao, M.3    Hustad, T.4    Glavac, D.5
  • 6
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole, N. B., N. Sciaky, A. Marotta, J. Song, and J. Lippincott-Schwartz. 1996. Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell 7:631-650.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 7
    • 0030948396 scopus 로고    scopus 로고
    • Immunostaining of the von Hippel-Lindau gene product in normal and neoplastic human tissues
    • Corless, C. L., A. Kibel, O. Iliopoulos, and W. G. Kaelin. 1997. Immunostaining of the von Hippel-Lindau gene product in normal and neoplastic human tissues. Hum. Pathol. 28:459-464.
    • (1997) Hum. Pathol. , vol.28 , pp. 459-464
    • Corless, C.L.1    Kibel, A.2    Iliopoulos, O.3    Kaelin, W.G.4
  • 11
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNA
    • Fischer, U., J. Huber, W. C. Boelens, I. W. Mattaj, and R. Luhrmann. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNA. Cell 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 13
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 15
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., S. Asano, T. Nakamura, M. Adachi, M. Yoshida, M. Yanagida, and E. Nishida. 1997. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390:308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 16
    • 0029786994 scopus 로고    scopus 로고
    • 2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal
    • 2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J. Biol. Chem. 271:20024-20028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3    Nishida, E.4
  • 17
    • 0344330996 scopus 로고    scopus 로고
    • Molecular cloning of the von Hippel-Lindau tumor suppressor gene and its role in renal carcinoma
    • Gnarra, J. R., D. R. Duan, Y. Weng, J. S. Humphrey, D. Y. T. Chen, S. Lee, A. Pause, et al. 1996. Molecular cloning of the von Hippel-Lindau tumor suppressor gene and its role in renal carcinoma. Biochim. Biophys. Acta 1242:201-210.
    • (1996) Biochim. Biophys. Acta , vol.1242 , pp. 201-210
    • Gnarra, J.R.1    Duan, D.R.2    Weng, Y.3    Humphrey, J.S.4    Chen, D.Y.T.5    Lee, S.6    Pause, A.7
  • 20
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich, D., and I. W. Mattaj. 1996. Nucleocytoplasmic transport. Science 271:1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 23
    • 0029090338 scopus 로고
    • Tumor suppression by the von Hippel-Lindau gene product
    • Iliopoulos, O., A. Kibel, S. Gray, and W. G. Kaelin, 1995. Tumor suppression by the von Hippel-Lindau gene product. Nat. Med. 1:822-826.
    • (1995) Nat. Med. , vol.1 , pp. 822-826
    • Iliopoulos, O.1    Kibel, A.2    Gray, S.3    Kaelin, W.G.4
  • 25
    • 0029147430 scopus 로고
    • Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C
    • Kibel, A., O. Iliopoulos, J. A. DeCaprio, and W. G. Kaelin. 1995. Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C. Science 269:1444-1446.
    • (1995) Science , vol.269 , pp. 1444-1446
    • Kibel, A.1    Iliopoulos, O.2    DeCaprio, J.A.3    Kaelin, W.G.4
  • 26
    • 0029953780 scopus 로고    scopus 로고
    • Cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family
    • Kipreos, E. T., L. E. Lander, J. P. Wing, W. W. He, and E. M. Hedgecock. 1996. Cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell 85:829-839.
    • (1996) Cell , vol.85 , pp. 829-839
    • Kipreos, E.T.1    Lander, L.E.2    Wing, J.P.3    He, W.W.4    Hedgecock, E.M.5
  • 27
    • 0031964099 scopus 로고    scopus 로고
    • Transforming growth factor alpha is a target for the von Hippel-Lindau tumor suppressor
    • Knebelmann, B., S. Ananth, H. T. Cohen, and V. P. Sukhalme. 1998. Transforming growth factor alpha is a target for the von Hippel-Lindau tumor suppressor. Cancer Res. 58:226-231.
    • (1998) Cancer Res. , vol.58 , pp. 226-231
    • Knebelmann, B.1    Ananth, S.2    Cohen, H.T.3    Sukhalme, V.P.4
  • 28
    • 0027504088 scopus 로고
    • Antioncogenes and human cancer
    • Knudson, A. G. 1993. Antioncogenes and human cancer. Proc. Natl. Acad. Sci. USA 90:10914-10921.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10914-10921
    • Knudson, A.G.1
  • 29
    • 0030701840 scopus 로고    scopus 로고
    • Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins
    • Kudo, N., S. Khochbin, K. Nishi, K. Kitano, M. Yanagida, M. Yoshida, and S. Horinouchi. 1997. Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J. Biol. Chcm. 272:29742-29749.
    • (1997) J. Biol. Chcm. , vol.272 , pp. 29742-29749
    • Kudo, N.1    Khochbin, S.2    Nishi, K.3    Kitano, K.4    Yanagida, M.5    Yoshida, M.6    Horinouchi, S.7
  • 31
    • 0029946004 scopus 로고    scopus 로고
    • Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density
    • Lee, S., D. Y. T. Chen, J. S. Humphrey, J. R. Gnarra, W. M. Linehan, and R. D. Klausner. 1996. Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density. Proc. Natl. Acad. Sci. USA 93:1770-1775.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1770-1775
    • Lee, S.1    Chen, D.Y.T.2    Humphrey, J.S.3    Gnarra, J.R.4    Linehan, W.M.5    Klausner, R.D.6
  • 32
    • 0030044039 scopus 로고    scopus 로고
    • Post-transcriptional regulation of vascular endothelial growth factor by hypoxia
    • Levy, A. P., N. S. Levy, and M. A. Goldberg. 1996. Post-transcriptional regulation of vascular endothelial growth factor by hypoxia. J. Biol. Chem. 271:2746-2753.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2746-2753
    • Levy, A.P.1    Levy, N.S.2    Goldberg, M.A.3
  • 33
    • 0029795584 scopus 로고    scopus 로고
    • Hypoxia-inducible protein binding to vascular endothelial growth factor mRNA and its modulation by the von Hippel-Lindau protein
    • Levy, A. P., N. S. Levy, and M. A. Goldberg. 1996. Hypoxia-inducible protein binding to vascular endothelial growth factor mRNA and its modulation by the von Hippel-Lindau protein. J. Biol. Chem. 271:25492-25497.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25492-25497
    • Levy, A.P.1    Levy, N.S.2    Goldberg, M.A.3
  • 34
    • 0028887421 scopus 로고
    • Identification of the von Hippel-Lindau (VHL) gene. Its role in renal cancer
    • Linehan, W. M., M. I. Lerman, and B. Zbar. 1995. Identification of the von Hippel-Lindau (VHL) gene. Its role in renal cancer. JAMA 273:564-570.
    • (1995) JAMA , vol.273 , pp. 564-570
    • Linehan, W.M.1    Lerman, M.I.2    Zbar, B.3
  • 35
    • 0345420460 scopus 로고    scopus 로고
    • Uses of GFP in mammalian cells
    • M. Chalfic et al. (ed.), in press. John Wiley and Sons, New York, N.Y.
    • Lippincott-Schwartz, J. Uses of GFP in mammalian cells. In M. Chalfic et al. (ed.), Applications of green fluorescent proteins, in press. John Wiley and Sons, New York, N.Y.
    • Applications of Green Fluorescent Proteins
    • Lippincott-Schwartz, J.1
  • 36
    • 0031907152 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2
    • Lonergan, K. M., O. Iliopoulos, M. Ohh, T. Kamura, R. C. Conaway, J. W. Conaway, and W. G. Kaelin, Jr. 1998. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2. Mol. Cell. Biol. 18:732-741.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 732-741
    • Lonergan, K.M.1    Iliopoulos, O.2    Ohh, M.3    Kamura, T.4    Conaway, R.C.5    Conaway, J.W.6    Kaelin W.G., Jr.7
  • 38
    • 0029847090 scopus 로고    scopus 로고
    • Allelic deletions of the VHL gene detected in multiple microscopic clear cell renal lesions in von Hippel-Lindau disease patients
    • Lubensky, I. A., J. R. Gnarra, P. Bertheau, M. M. Walther, and W. M. Linehan. 1996. Allelic deletions of the VHL gene detected in multiple microscopic clear cell renal lesions in von Hippel-Lindau disease patients. Am. J. Pathol. 149:2089-2095.
    • (1996) Am. J. Pathol. , vol.149 , pp. 2089-2095
    • Lubensky, I.A.1    Gnarra, J.R.2    Bertheau, P.3    Walther, M.M.4    Linehan, W.M.5
  • 40
    • 0028239268 scopus 로고
    • The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm
    • Meyer, B. E., and M. H. Malim. 1994. The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm. Genes Dev. 8:1538-1547.
    • (1994) Genes Dev. , vol.8 , pp. 1538-1547
    • Meyer, B.E.1    Malim, M.H.2
  • 41
    • 0028845313 scopus 로고
    • Nuclear export signal in hnRNP Al: A signal-mediated temperature-dependent nuclear protein export pathway
    • Michael, W. M., M. D. Choi, and G. Dreyfuss. 1995. Nuclear export signal in hnRNP Al: a signal-mediated temperature-dependent nuclear protein export pathway. Cell 83:415-422.
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.D.2    Dreyfuss, G.3
  • 42
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein
    • Michael, W. M., P. S. Eder, and G. Dreyfuss. 1997. The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J. 16:3587-3598.
    • (1997) EMBO J. , vol.16 , pp. 3587-3598
    • Michael, W.M.1    Eder, P.S.2    Dreyfuss, G.3
  • 43
    • 0032518468 scopus 로고    scopus 로고
    • Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis
    • Nakielny, S., and G. Dreyfuss. 1998. Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis. Curr. Biol. 8:89-95.
    • (1998) Curr. Biol. , vol.8 , pp. 89-95
    • Nakielny, S.1    Dreyfuss, G.2
  • 45
    • 0031260540 scopus 로고    scopus 로고
    • The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export
    • Neville, M., F. Stutz, L. Lee, L. I. Davis, and M. Rosbash. 1997 The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr. Biol. 7:767-775.
    • (1997) Curr. Biol. , vol.7 , pp. 767-775
    • Neville, M.1    Stutz, F.2    Lee, L.3    Davis, L.I.4    Rosbash, M.5
  • 46
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg, E. A. 1997. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386:779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 47
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1. A fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi, K., M. Yoshida, D. Fujiwara, M. Nishikawa, S. Horinouchi, and T. Beppu. 1994. Leptomycin B targets a regulatory cascade of crm1. a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269:6320-6324.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6320-6324
    • Nishi, K.1    Yoshida, M.2    Fujiwara, D.3    Nishikawa, M.4    Horinouchi, S.5    Beppu, T.6
  • 48
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the local contact protein, zyxin: A potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix, D. A., and M. C. Beckerle. 1997. Nuclear-cytoplasmic shuttling of the local contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 138:1139-1147.
    • (1997) J. Cell Biol. , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 49
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno, M., M. Fornerod, and I. W. Mattaj. 1998. Nucleocytoplasmic transport: the last 200 nanometers. Cell 92:327-336.
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 50
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 1997. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278:141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 51
    • 0030953635 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
    • Pause, A., S. Lee, R. A. Worrell, D. Y. T. Chen, W. H. Burgess, W. M. Linehan, and R. D. Klausner. 1997. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins. Proc. Natl. Acad. Sci. USA 94:2156-2161.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2156-2161
    • Pause, A.1    Lee, S.2    Worrell, R.A.3    Chen, D.Y.T.4    Burgess, W.H.5    Linehan, W.M.6    Klausner, R.D.7
  • 52
    • 0026339487 scopus 로고
    • Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins
    • Pinol-Roma, S., and G. Dreyfuss. 1991. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science 253: 312-314.
    • (1991) Science , vol.253 , pp. 312-314
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 53
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma, S., and G. Dreyfuss. 1992. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355:730-732.
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 55
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus Rev protein
    • Roth, J., M. Dobbelstein, D. A. Freedman, T. Shenk, and A. J. Levine. 1998. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus Rev protein. EMBO J. 17:554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 56
    • 0025130815 scopus 로고
    • Nuclear localization of c-Fos. But not v-Fos proteins, is controlled by extracellular signals
    • Roux, P., J. M. Blanchard, A. Fernandez, N. Lamb, P. Jeanteur, and M. Piechaczyk. 1990. Nuclear localization of c-Fos. but not v-Fos proteins, is controlled by extracellular signals. Cell 63:341-351.
    • (1990) Cell , vol.63 , pp. 341-351
    • Roux, P.1    Blanchard, J.M.2    Fernandez, A.3    Lamb, N.4    Jeanteur, P.5    Piechaczyk, M.6
  • 57
    • 0032521214 scopus 로고    scopus 로고
    • ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motif
    • Sandri-Goldin, R. M. 1998. ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motif. Genes Dev. 12:868-879.
    • (1998) Genes Dev. , vol.12 , pp. 868-879
    • Sandri-Goldin, R.M.1
  • 58
    • 0029920054 scopus 로고    scopus 로고
    • Reversion of deregulated expression of vascular endothelial growth factor in human renal carcinoma cells by von Hippel-Lindau tumor suppressor gene
    • Seimeister, G., K. Weidel, K. Mohrs, B. Barleon, G. Martiny-Baron, and U. Marne. 1996. Reversion of deregulated expression of vascular endothelial growth factor in human renal carcinoma cells by von Hippel-Lindau tumor suppressor gene. Cancer Res. 56:2299-2301.
    • (1996) Cancer Res. , vol.56 , pp. 2299-2301
    • Seimeister, G.1    Weidel, K.2    Mohrs, K.3    Barleon, B.4    Martiny-Baron, G.5    Marne, U.6
  • 61
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C. S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 62
    • 0028786017 scopus 로고
    • Analysis of trafficking of Rev and transdominant Rev proteins in living cells using green fluorescent protein fusions: Transdominant Rev blocks the export of Rev from the nucleus to the cytoplasm
    • Stauber, R., G. A. Gaitanaris, and G. N. Pavlakis. 1995. Analysis of trafficking of Rev and transdominant Rev proteins in living cells using green fluorescent protein fusions: transdominant Rev blocks the export of Rev from the nucleus to the cytoplasm. Virology 213:439-449.
    • (1995) Virology , vol.213 , pp. 439-449
    • Stauber, R.1    Gaitanaris, G.A.2    Pavlakis, G.N.3
  • 64
    • 0029941650 scopus 로고    scopus 로고
    • Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product
    • Tsuchiya, H., T. Iseda, and O. Hino. 1996. Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product. Cancer Res. 56:2881-2885.
    • (1996) Cancer Res. , vol.56 , pp. 2881-2885
    • Tsuchiya, H.1    Iseda, T.2    Hino, O.3
  • 65
    • 0028800884 scopus 로고
    • Prevalence of microscopic lesions in grossly normal renal parenchyma from patients with von Hippel-Lindau disease, sporadic renal cell carcinoma and no renal disease: Clinical implications
    • Walther, M. M., I. A. Lubensky, D. Venzon, B. Zbar, and W. M. Linehan. 1995. Prevalence of microscopic lesions in grossly normal renal parenchyma from patients with von Hippel-Lindau disease, sporadic renal cell carcinoma and no renal disease: clinical implications. J. Urol. 154:2010-2014.
    • (1995) J. Urol. , vol.154 , pp. 2010-2014
    • Walther, M.M.1    Lubensky, I.A.2    Venzon, D.3    Zbar, B.4    Linehan, W.M.5
  • 66
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J. L. Meinkoth, R. Y. Tsien, and S. S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 68
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff, B., J. J. Sanglier, and Y. Wang. 1997. Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol. 4:139-147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 69
    • 0032481283 scopus 로고    scopus 로고
    • Tolerance of diverse amino acid substitutions at conserved positions in the nuclear export signal (NES) of HIV-1 Rev
    • Zhang, M. J., and A. I. Dayton. 1998. Tolerance of diverse amino acid substitutions at conserved positions in the nuclear export signal (NES) of HIV-1 Rev. Biochem. Biophys. Res. Commun. 243:113-116.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 113-116
    • Zhang, M.J.1    Dayton, A.I.2
  • 70
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner, H., J. Sok, D. Immanuel, Y. Yin, and D. Ron. 1997. TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J. Cell Sci. 110:1741-1750.
    • (1997) J. Cell Sci. , vol.110 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5


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