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Volumn 10, Issue 5-6, 2002, Pages 231-242

Identification and characterization of nine novel human small GTPases showing variable expressions in liver cancer tissues

Author keywords

ARF SAR1; Cloning; Expression; Liver cancer; RAB

Indexed keywords

GUANOSINE TRIPHOSPHATASE; RAB PROTEIN; RAS PROTEIN; COMPLEMENTARY DNA;

EID: 0036419738     PISSN: 10522166     EISSN: None     Source Type: Journal    
DOI: 10.3727/000000002783992406     Document Type: Article
Times cited : (121)

References (25)
  • 3
    • 0024276910 scopus 로고
    • Do GTPases direct membrane traffic in secretion?
    • Bourne, H. R. Do GTPases direct membrane traffic in secretion? Cell 53:669-671; 1988.
    • (1988) Cell , vol.53 , pp. 669-671
    • Bourne, H.R.1
  • 4
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R.; Sanders, D. A.; McCormick, F. The GTPase superfamily: A conserved switch for diverse cell functions. Nature 348:125-132; 1990.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 5
    • 0031910613 scopus 로고    scopus 로고
    • Up-regulation of beta-actin, cyclophilin and GAPDH in N1S1 rat hepatoma
    • Chang, T. J.; Juan, C. C.; Yin, P. H.; Chi, C. W.; Tsay, H. J. Up-regulation of beta-actin, cyclophilin and GAPDH in N1S1 rat hepatoma. Oncol. Rep. 5(2):469-471; 1998.
    • (1998) Oncol. Rep. , vol.5 , Issue.2 , pp. 469-471
    • Chang, T.J.1    Juan, C.C.2    Yin, P.H.3    Chi, C.W.4    Tsay, H.J.5
  • 6
    • 0033180113 scopus 로고    scopus 로고
    • The role of ARF and Rab GTPases in membrane transport
    • Chavrier, P.; Goud, B. The role of ARF and Rab GTPases in membrane transport. Curr. Opin. Cell Biol. 11:466-475; 1999.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 466-475
    • Chavrier, P.1    Goud, B.2
  • 8
    • 0034635551 scopus 로고    scopus 로고
    • Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells
    • Erdman, R. A.; Shellenberger, K. E.; Overmeyer, J. H.; Maltese, W. A. Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells. J. Biol. Chem. 275(6):3848-3856; 2000.
    • (2000) J. Biol. Chem. , vol.275 , Issue.6 , pp. 3848-3856
    • Erdman, R.A.1    Shellenberger, K.E.2    Overmeyer, J.H.3    Maltese, W.A.4
  • 9
    • 0028135348 scopus 로고
    • Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A
    • Farnsworth, C. C.; Seabra, M. C.; Ericsson, L. H.; Gelb, M. H.; Glomset, J. A. Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc. Natl. Acad. Sci. USA 91(25):11963-11967; 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.25 , pp. 11963-11967
    • Farnsworth, C.C.1    Seabra, M.C.2    Ericsson, L.H.3    Gelb, M.H.4    Glomset, J.A.5
  • 10
    • 0026743307 scopus 로고
    • Fine structure of adrenal cortex in rats harbouring a medullary thyroid carcinoma transfected with a corticotrophin-releasing hormone cDNA expression vector
    • Feinmesser, M.; Asa, S. L.; Kovacs, K.; Low, M. J. Fine structure of adrenal cortex in rats harbouring a medullary thyroid carcinoma transfected with a corticotrophin-releasing hormone cDNA expression vector. J. Endocrinol. 11:271-277; 1992.
    • (1992) J. Endocrinol. , vol.11 , pp. 271-277
    • Feinmesser, M.1    Asa, S.L.2    Kovacs, K.3    Low, M.J.4
  • 11
    • 0032147185 scopus 로고    scopus 로고
    • Endocytosis proteins and cancer: A potential link?
    • Floyd, S.; Camilli, P. Endocytosis proteins and cancer: A potential link? Trends Cell Biol. 8:299-301; 1998.
    • (1998) Trends Cell Biol. , vol.8 , pp. 299-301
    • Floyd, S.1    Camilli, P.2
  • 12
    • 0032546799 scopus 로고    scopus 로고
    • Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1)
    • Hong, J. X.; Lee, F. J.; Patton, W. A.; Lin, C. Y.; Moss, J.; Vaughan, M. Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1). J. Biol. Chem. 273(25):15872-15876; 1998.
    • (1998) J. Biol. Chem. , vol.273 , Issue.25 , pp. 15872-15876
    • Hong, J.X.1    Lee, F.J.2    Patton, W.A.3    Lin, C.Y.4    Moss, J.5    Vaughan, M.6
  • 13
    • 0021250807 scopus 로고
    • Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin
    • Kahn, R. A.; Gilman, A. G. Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin. J. Biol. Chem. 259:6228-6234; 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6228-6234
    • Kahn, R.A.1    Gilman, A.G.2
  • 14
    • 0030609041 scopus 로고    scopus 로고
    • Vesicular transport, how many Ypt/Rab-GTPases make a eukaryotic cell?
    • Lazar, T.; Gotte, M.; Gallwitz, D. Vesicular transport, how many Ypt/Rab-GTPases make a eukaryotic cell? Trends Biochem. Sci. 22:468-472; 1997.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 468-472
    • Lazar, T.1    Gotte, M.2    Gallwitz, D.3
  • 15
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss, J.; Vaughan, M. Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270(21):12327-12330; 1995.
    • (1995) J. Biol. Chem. , vol.270 , Issue.21 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 16
    • 0025909492 scopus 로고
    • The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway
    • Nashikawa, S.; Nakano, A. The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway. Biochim. Biophys. Acta 1093 (2-3):135-143; 1991.
    • (1991) Biochim. Biophys. Acta , vol.1093 , Issue.2-3 , pp. 135-143
    • Nashikawa, S.1    Nakano, A.2
  • 18
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P.; Zerial, M. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9:496-504; 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 19
    • 0028239912 scopus 로고
    • GTPases, multifunctional molecular switches regulating vesicular traffic
    • Nuoffer, C.; Balch, W. E. GTPases, multifunctional molecular switches regulating vesicular traffic. Annu. Rev. Biochem. 63:949-990; 1994.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 20
    • 0025743409 scopus 로고
    • Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport
    • Oka, T.; Nishikawa, S.; Nakano, A. Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport. J. Cell Biol. 114:671-679; 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 671-679
    • Oka, T.1    Nishikawa, S.2    Nakano, A.3
  • 21
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • Salama, N. R.; Yeung, T.; Schekman, R. W. The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J. 12:4073-4082; 1993.
    • (1993) EMBO J. , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 22
    • 0023930341 scopus 로고
    • Stimulation of choleragen enzymatic activities by GTP and two soluble proteins purified from bovine brain
    • Tsai, S. C.; Noda, M.; Adamik, R.; Chang, P. P.; Chen, H. C.; Moss, J.; Vaughan, M. Stimulation of choleragen enzymatic activities by GTP and two soluble proteins purified from bovine brain. J. Biol. Chem. 263: 1768-1772; 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1768-1772
    • Tsai, S.C.1    Noda, M.2    Adamik, R.3    Chang, P.P.4    Chen, H.C.5    Moss, J.6    Vaughan, M.7
  • 23
    • 0034460154 scopus 로고    scopus 로고
    • Evidence of Rab3A expression, regulation of vesicle trafficking, and cellular secretion in response to heregulin in mammary epithelial cells
    • Vadlamudi, R. K.; Wang, R. A.; Talukder, A. H.; Adam, L.; Johnson, R.; Kumar, R. Evidence of Rab3A expression, regulation of vesicle trafficking, and cellular secretion in response to heregulin in mammary epithelial cells. Mol. Cell. Biol. 12:9092-9101; 2000.
    • (2000) Mol. Cell. Biol. , vol.12 , pp. 9092-9101
    • Vadlamudi, R.K.1    Wang, R.A.2    Talukder, A.H.3    Adam, L.4    Johnson, R.5    Kumar, R.6
  • 24
    • 0025908897 scopus 로고
    • The ras protein family: Evolutionary tree and role of conserved amino acids
    • Valencia, A.; Chardin, P.; Wittinghofer, A.; Sander, C. The ras protein family: Evolutionary tree and role of conserved amino acids. Biochemistry 30:4637-4648; 1991.
    • (1991) Biochemistry , vol.30 , pp. 4637-4648
    • Valencia, A.1    Chardin, P.2    Wittinghofer, A.3    Sander, C.4
  • 25
    • 0025740753 scopus 로고
    • The structure of Ras protein: A model for a universal molecular switch
    • Wittinghofer, A.; Pal, E. F. The structure of Ras protein: A model for a universal molecular switch. Trends Biochem. Sci. 16:382-387; 1991.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pal, E.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.