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Volumn 242, Issue 1, 1996, Pages 104-113

Isolation, expression and characterization of the gene for an ADP-ribosylation factor from the human malaria parasite, Plasmodium falciparum

Author keywords

ADP ribosylation factor; Malaria; Plasmodium falciparum

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR;

EID: 0029854188     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0104r.x     Document Type: Article
Times cited : (39)

References (63)
  • 1
    • 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. (1984) 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) J. Biol. Chem. , vol.259 , pp. 6228-6234
    • Kahn, R.A.1    Gilman, A.G.2
  • 2
    • 0025854682 scopus 로고
    • Quantitation and purification of ADP-ribosylation factor
    • Kahn, R. A. (1991) Quantitation and purification of ADP-ribosylation factor, Methods Enzymol. 195, 233-242.
    • (1991) Methods Enzymol. , vol.195 , pp. 233-242
    • Kahn, R.A.1
  • 3
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP-binding protein
    • Kahn, R. A. & Gilman, A. G. (1986) The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP-binding protein, J. Biol. Chem. 261, 7906-7911.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 4
    • 0025174078 scopus 로고
    • ADP-ribosylation factor is functionally and physically associated with the Golgi complex
    • Stearns, T., Willingham, M. C., Bolstein, D. & Kahn, R. A. (1990) ADP-ribosylation factor is functionally and physically associated with the Golgi complex, Proc. Natl. Acad. Sci. USA 87, 1238-1242.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1238-1242
    • Stearns, T.1    Willingham, M.C.2    Bolstein, D.3    Kahn, R.A.4
  • 5
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. (1994) Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 6
    • 0028128334 scopus 로고
    • ARF: A key regulatory switch in membrane traffic and organelle structure
    • Donaldson, J. G. & Klausner, R. D. (1994) ARF: a key regulatory switch in membrane traffic and organelle structure, Curr. Opin. Cell Biol. 6, 527-532.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 527-532
    • Donaldson, J.G.1    Klausner, R.D.2
  • 7
    • 0024801630 scopus 로고
    • Nucleotide binding and cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor
    • Weiss, O., Holden, J., Rulka, C. & Kahn, R. A. (1989) Nucleotide binding and cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor, J. Biol. Chem. 264, 21066-21072.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21066-21072
    • Weiss, O.1    Holden, J.2    Rulka, C.3    Kahn, R.A.4
  • 9
    • 10544246457 scopus 로고
    • Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin
    • Lee, F.-J. S., Moss, J. & Vaughan, M. (1995) Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin, J. Biol. Chem. 267, 24441-24445.
    • (1995) J. Biol. Chem. , vol.267 , pp. 24441-24445
    • Lee, F.-J.S.1    Moss, J.2    Vaughan, M.3
  • 10
    • 0025221221 scopus 로고
    • ADP ribosylation factor is an essential protein in Saccharomyces cerevisiae and is encoded by two genes
    • Stearns, T., Kahn, R. A., Botstein, D. & Hoyt, M. A. (1990) ADP ribosylation factor is an essential protein in Saccharomyces cerevisiae and is encoded by two genes, Mol. Cell. Biol. 10, 6690-6699.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6690-6699
    • Stearns, T.1    Kahn, R.A.2    Botstein, D.3    Hoyt, M.A.4
  • 11
    • 0025731953 scopus 로고
    • Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells
    • Tsuchiya, M., Price, R. S., Tsai, S.-C., Moss, J. & Vaughan, M. (1988) Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells, J. Biol. Chem. 266, 2772-2777.
    • (1988) J. Biol. Chem. , vol.266 , pp. 2772-2777
    • Tsuchiya, M.1    Price, R.S.2    Tsai, S.-C.3    Moss, J.4    Vaughan, M.5
  • 12
    • 0027482720 scopus 로고
    • Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: Cloning of additional human and Drosophila ARF-like genes
    • Clark, J., Moore, L., Krasinkas, A., Way, J., Battey, J., Tamkun, J. & Kahn, R. A. (1993) Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes, Proc. Natl Acad. Sci. USA 90, 8952-8956.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8952-8956
    • Clark, J.1    Moore, L.2    Krasinkas, A.3    Way, J.4    Battey, J.5    Tamkun, J.6    Kahn, R.A.7
  • 13
    • 0024829766 scopus 로고
    • Tissue and species distribution of mRNA encoding two ADP-ribosylation factors, 20-kDa guanine nucleotide binding proteins
    • Tsuchiya, M., Price, R. S., Nightingale, M. S., Moss, J. & Vaughan, M. (1989) Tissue and species distribution of mRNA encoding two ADP-ribosylation factors, 20-kDa guanine nucleotide binding proteins, Biochemistry 28, 9668-9673.
    • (1989) Biochemistry , vol.28 , pp. 9668-9673
    • Tsuchiya, M.1    Price, R.S.2    Nightingale, M.S.3    Moss, J.4    Vaughan, M.5
  • 14
    • 0026329576 scopus 로고
    • Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin
    • Tsai, S.-C., Haun, R. S., Tsuchiya, M., Moss, J. & Vaughan, M. (1991) Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin, J. Biol. Chem. 266, 23053-23059.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23053-23059
    • Tsai, S.-C.1    Haun, R.S.2    Tsuchiya, M.3    Moss, J.4    Vaughan, M.5
  • 15
    • 0026788492 scopus 로고
    • Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin
    • Lee, C. M., Haun, R. S., Tsai, S.-C., Moss, J. & Vaughan, M. (1992) Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin, J. Biol. Chem. 267, 9028-9034.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9028-9034
    • Lee, C.M.1    Haun, R.S.2    Tsai, S.-C.3    Moss, J.4    Vaughan, M.5
  • 16
    • 0026606363 scopus 로고
    • Characterization of the gene for ADP-ribosylation factor (ARF) 2, a developmentally regulated, selectively expressed member of the ARF family of approximately 20-kDa guanine nucleolide-binding proteins
    • Serventi, I. M., Moss, J. & Vaughan, M. (1992) Characterization of the gene for ADP-ribosylation factor (ARF) 2, a developmentally regulated, selectively expressed member of the ARF family of approximately 20-kDa guanine nucleolide-binding proteins, Curr. Top. Microbiol. Immunol. 175, 43-47.
    • (1992) Curr. Top. Microbiol. Immunol. , vol.175 , pp. 43-47
    • Serventi, I.M.1    Moss, J.2    Vaughan, M.3
  • 17
    • 0025773893 scopus 로고
    • Differential expression during development of ADP-ribosylation factors, 20-kDa guanine nucleotide-binding protein activators of cholera toxin
    • Tsai, S.-C., Adamik, R., Tsuchiya, M., Chang, P. P. M., Moss, J. & Vaughan, M. (1991) Differential expression during development of ADP-ribosylation factors, 20-kDa guanine nucleotide-binding protein activators of cholera toxin, J. Biol. Chem. 266, 8213-8219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8213-8219
    • Tsai, S.-C.1    Adamik, R.2    Tsuchiya, M.3    Chang, P.P.M.4    Moss, J.5    Vaughan, M.6
  • 18
    • 0026666365 scopus 로고
    • Effects of phospholipid and GTP on recombinant ADP-ribosylation factors (ARFs)
    • Price, S. R., Welsh, C. F., Haun, R. S., Stanley, S. J., Moss, J. & Vaughan, M. (1992) Effects of phospholipid and GTP on recombinant ADP-ribosylation factors (ARFs). J. Biol. Chem. 267, 17766-17772.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17766-17772
    • Price, S.R.1    Welsh, C.F.2    Haun, R.S.3    Stanley, S.J.4    Moss, J.5    Vaughan, M.6
  • 19
    • 0023928057 scopus 로고
    • Chemical and immunological characterization of the 21 kDa ADP-ribosylation factor of adenylate cyclase
    • Kahn, R. A., Goddad, C. & Newkirk, M. (1988) Chemical and immunological characterization of the 21 kDa ADP-ribosylation factor of adenylate cyclase, J. Biol. Chem. 263, 8282-8287.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8282-8287
    • Kahn, R.A.1    Goddad, C.2    Newkirk, M.3
  • 20
    • 0026667699 scopus 로고
    • Guanine nucleotide-binding proteins in the intestinal parasite Giardia lamblia. Isolation of a gene encoding an approximately 20-kDa ADP-ribosylation factor
    • Murtagh, J. J., Mowatt, M. R., Lee, C.-M., Lee, F.-J. S., Mishima, K., Nash, T., Moss, J. & Vaughan, M. (1992) Guanine nucleotide-binding proteins in the intestinal parasite Giardia lamblia. Isolation of a gene encoding an approximately 20-kDa ADP-ribosylation factor, J. Biol. Chem. 267, 9654-9662.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9654-9662
    • Murtagh, J.J.1    Mowatt, M.R.2    Lee, C.-M.3    Lee, F.-J.S.4    Mishima, K.5    Nash, T.6    Moss, J.7    Vaughan, M.8
  • 21
    • 0025204355 scopus 로고
    • Ultrastructure of malaria infected erythrocytes
    • Atkinson, C. T. & Aikawa, M. (1990) Ultrastructure of malaria infected erythrocytes, Blood Cells (NY) 16, 351-368.
    • (1990) Blood Cells (NY) , vol.16 , pp. 351-368
    • Atkinson, C.T.1    Aikawa, M.2
  • 23
    • 0027674261 scopus 로고
    • Export of proteins to the erythroeyte in Plasmodium falciparum-infected cells
    • Haldar, K. & Holder, A. A. (1993) Export of proteins to the erythroeyte in Plasmodium falciparum-infected cells, Semin. Cell Biol. 4, 345-353.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 345-353
    • Haldar, K.1    Holder, A.A.2
  • 24
    • 0026685816 scopus 로고
    • Nucleotide sequence of a P. falciparum stress protein with similarity to mammalian 78 kDa glucose regulated protein
    • Kumar, N. & Zheng, H. (1992) Nucleotide sequence of a P. falciparum stress protein with similarity to mammalian 78 kDa glucose regulated protein, Mol. Biochem. Parasitol. 56, 353-356.
    • (1992) Mol. Biochem. Parasitol. , vol.56 , pp. 353-356
    • Kumar, N.1    Zheng, H.2
  • 25
    • 0027501330 scopus 로고
    • Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: Separation from sites of sphingomyelin synthesis and implications for organization of the Golgi
    • Elmendorf, H. G. & Haldar, K. (1993) Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: separation from sites of sphingomyelin synthesis and implications for organization of the Golgi, EMBO J. 12, 4763-4773.
    • (1993) EMBO J. , vol.12 , pp. 4763-4773
    • Elmendorf, H.G.1    Haldar, K.2
  • 26
    • 0026579552 scopus 로고
    • Synthesis and secretion of proteins by released malarial parasites
    • Elmendorf, H. G., Bangs, J. D. & Haldar, K. (1992) Synthesis and secretion of proteins by released malarial parasites, Mol. Biochem. Parasitol. 52, 215-230.
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 215-230
    • Elmendorf, H.G.1    Bangs, J.D.2    Haldar, K.3
  • 27
    • 0028130379 scopus 로고
    • Plasmodium yoelii: Brefeldin A-sensitive processing of proteins targeted to the rhoptries
    • Ogun, S. A. & Holder, A. A. (1994) Plasmodium yoelii: brefeldin A-sensitive processing of proteins targeted to the rhoptries, Exp. Parasitol. 79, 270-278.
    • (1994) Exp. Parasitol. , vol.79 , pp. 270-278
    • Ogun, S.A.1    Holder, A.A.2
  • 28
    • 0027193417 scopus 로고
    • Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes
    • Randazzo, P. A., Yang, Y. C., Rulka, C. & Kahn, R. A. (1993) Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and protease-sensitive activating factor on Golgi membranes, J. Biol. Chem. 268, 9555-9563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9555-9563
    • Randazzo, P.A.1    Yang, Y.C.2    Rulka, C.3    Kahn, R.A.4
  • 30
    • 0026461113 scopus 로고
    • A fast and simple way for sequencing plasmid DNA with Sequenase using heat denaturation
    • Mass, M. J. & Roop, B. C. (1992) A fast and simple way for sequencing plasmid DNA with Sequenase using heat denaturation. Biotechniques 13, 676-678.
    • (1992) Biotechniques , vol.13 , pp. 676-678
    • Mass, M.J.1    Roop, B.C.2
  • 32
    • 0028217783 scopus 로고
    • PFGE: Improved conditions for rapid and high resolution separation of Plasmodium falciparum chromosomes
    • Hinterberg, K. & Scherf, A. (1994) PFGE: improved conditions for rapid and high resolution separation of Plasmodium falciparum chromosomes, Parasitol. Today 6, 225.
    • (1994) Parasitol. Today , vol.6 , pp. 225
    • Hinterberg, K.1    Scherf, A.2
  • 33
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 34
    • 0020383019 scopus 로고
    • Biosynthesis and processing of a Plasmodium falciparum schizont antigen recognised by immune serum and a monoclonal antibody
    • Holder, A. A. & Freeman, R. R. (1982) Biosynthesis and processing of a Plasmodium falciparum schizont antigen recognised by immune serum and a monoclonal antibody, J. Exp. Med. 156, 1528-1538.
    • (1982) J. Exp. Med. , vol.156 , pp. 1528-1538
    • Holder, A.A.1    Freeman, R.R.2
  • 35
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythocytic stages in culture
    • Lambros, C. & Vanderberg, J. P. (1979) Synchronization of Plasmodium falciparum erythocytic stages in culture, J. Parasitol. 65, 418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 36
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione 5-transferase
    • Smith, D. B. & Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione 5-transferase, Gene (Amst.) 67, 31-40.
    • (1988) Gene (Amst.) , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0027212498 scopus 로고
    • Stabilization and purification of enzymatically active glutathione-S-transferase (pGEX) fusion proteins
    • Frangioni, J. V. & Neel, B. J. (1993) Stabilization and purification of enzymatically active glutathione-S-transferase (pGEX) fusion proteins, Anal. Biochem. 210, 179-187.
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.J.2
  • 39
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. & von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications, Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, R. A. & Rothman, J. E. (1991 ) ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein, Cell 67, 239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 42
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount, S. M. (1982) A catalogue of splice junction sequences, Nucleic Acids Res. 10, 459-472.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 459-472
    • Mount, S.M.1
  • 43
    • 0013575866 scopus 로고
    • Transcriptional analysis of the major merozoite surface antigen precursor (gp195) gene of Plasmodium falciparum
    • (Agabian, N. & Cerami, A., eds) Wiley-Liss Inc.
    • Myler, P. J. (1990) Transcriptional analysis of the major merozoite surface antigen precursor (gp195) gene of Plasmodium falciparum, in Parasites: molecular biology, drug and vaccine design (Agabian, N. & Cerami, A., eds) pp. 123-137, Wiley-Liss Inc.
    • (1990) Parasites: Molecular Biology, Drug and Vaccine Design , pp. 123-137
    • Myler, P.J.1
  • 45
    • 0028224015 scopus 로고
    • Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite, Plasmodium falciparum
    • Ross-McDonald, P. B., Graeser, R., Kappes, B., Franklin, R. & Williamson, D. H. (1994) Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite, Plasmodium falciparum, Eur. J. Biochem. 220, 693-701.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 693-701
    • Ross-McDonald, P.B.1    Graeser, R.2    Kappes, B.3    Franklin, R.4    Williamson, D.H.5
  • 46
    • 0023892436 scopus 로고
    • Low temperature induction of Glutathione-S-transferase fusion proteins
    • Schein, C. H. & Noteborn, H. M. (1988) Low temperature induction of Glutathione-S-transferase fusion proteins, Biotechnology 6, 291-294.
    • (1988) Biotechnology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, H.M.2
  • 47
    • 0027024348 scopus 로고
    • Preparation of recombinant ADP-ribosylation factor
    • Randazzo, P. A., Weiss, O. & Kahn, R. A. (1992) Preparation of recombinant ADP-ribosylation factor, Methods Enzvmol. 219, 362-369.
    • (1992) Methods Enzvmol. , vol.219 , pp. 362-369
    • Randazzo, P.A.1    Weiss, O.2    Kahn, R.A.3
  • 49
    • 0023690466 scopus 로고
    • Molecular biology of malaria parasites
    • Weber, J. L. (1988) Molecular biology of malaria parasites, Exp. Parasitol. 66, 143-170.
    • (1988) Exp. Parasitol. , vol.66 , pp. 143-170
    • Weber, J.L.1
  • 50
    • 0023263288 scopus 로고
    • Analysis of sequences from the extremely A+T rich genome pf Plasmodium falciparum
    • Weber, J. L. (1987) Analysis of sequences from the extremely A+T rich genome pf Plasmodium falciparum, Gene (Amst.) 52, 103-109.
    • (1987) Gene (Amst.) , vol.52 , pp. 103-109
    • Weber, J.L.1
  • 51
    • 0028093626 scopus 로고
    • Characterization of class II and class III ADP-ribosylation factor genes and proteins in Drosophila melanogaster
    • Lee, F.-J. S., Stevens, L. A., Hall, L. M., Murtagh, J. J. Jr, Kao, Y. L., Moss, J. & Vaughan, M. (1994) Characterization of class II and class III ADP-ribosylation factor genes and proteins in Drosophila melanogaster, J. Biol. Chem. 269, 21 555-21 560.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21555-21560
    • Lee, F.-J.S.1    Stevens, L.A.2    Hall, L.M.3    Murtagh Jr., J.J.4    Kao, Y.L.5    Moss, J.6    Vaughan, M.7
  • 52
    • 0027471198 scopus 로고
    • Characterization of the gene for ADP-ribosylation factor (ARF) 2, a developmentally regulated, selectively expressed member of the ARF family of approximately 20-kDa guanine nucleotide-binding proteins
    • Serventi, I. M., Cavanaugh, E., Moss, J. & Vaughan, M. (1993)(Characterization of the gene for ADP-ribosylation factor (ARF) 2, a developmentally regulated, selectively expressed member of the ARF family of approximately 20-kDa guanine nucleotide-binding proteins, J. Biol. Chem. 268, 4863-4872.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4863-4872
    • Serventi, I.M.1    Cavanaugh, E.2    Moss, J.3    Vaughan, M.4
  • 53
    • 0029007101 scopus 로고
    • The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for interaction with Gs and ARF GTPase-activating protein
    • Randazzo, P. A., Terui, T., Sturch, S., Fales, H. M., Ferrige, A. G. & Kahn, R. A. (1995) The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for interaction with Gs and ARF GTPase-activating protein, J. Biol. Chem. 270, 14809-14815.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14809-14815
    • Randazzo, P.A.1    Terui, T.2    Sturch, S.3    Fales, H.M.4    Ferrige, A.G.5    Kahn, R.A.6
  • 54
    • 0028242486 scopus 로고
    • Effect of ADP-ribosylation factor amino-terminal deletions on its GTP-dependent stimulation of cholera toxin activity
    • published erratum appears in J. Biol. Chem (1994) 269, 16519
    • Hong, J.-X., Haun, R. S., Tsai, S.-C., Moss, J. & Vaughan, M. (1994) Effect of ADP-ribosylation factor amino-terminal deletions on its GTP-dependent stimulation of cholera toxin activity [published erratum appears in J. Biol. Chem (1994) 269, 16519], J. Biol. Chem. 269, 9743-9745.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9743-9745
    • Hong, J.-X.1    Haun, R.S.2    Tsai, S.-C.3    Moss, J.4    Vaughan, M.5
  • 57
    • 0027401676 scopus 로고
    • Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter
    • Haun, R. S., Moss, J. & Vaughan, M. (1993) Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter, J. Biol. Chem. 268, 8793-8800.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8793-8800
    • Haun, R.S.1    Moss, J.2    Vaughan, M.3
  • 58
    • 10544248557 scopus 로고
    • Oxford University Press, Oxford, UK
    • Lewin, B. (1990) Genen IV, 4th edn, Oxford University Press, Oxford, UK.
    • (1990) Genen IV, 4th Edn
    • Lewin, B.1
  • 59
    • 0028008830 scopus 로고
    • Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes
    • Elmendorf, H. G. & Haldar, K. (1994) Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes, J. Cell Biol. 124, 449-462.
    • (1994) J. Cell Biol. , vol.124 , pp. 449-462
    • Elmendorf, H.G.1    Haldar, K.2
  • 60
    • 0027439173 scopus 로고
    • Unusual routes of protein secretion: The easy way out
    • Kuchler, K. (1993) Unusual routes of protein secretion: the easy way out, Trends Cell Biol. 3, 421-426.
    • (1993) Trends Cell Biol. , vol.3 , pp. 421-426
    • Kuchler, K.1
  • 61
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes, M. A. & Rothman, J. E. (1993) The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein, Cell 73, 999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 62
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • Traub, L. M., Ostrom, J. A. & Kornfield, S. (1993) Biochemical dissection of AP-1 recruitment onto Golgi membranes, J. Cell Biol. 123, 561-573.
    • (1993) J. Cell Biol. , vol.123 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfield, S.3


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