메뉴 건너뛰기




Volumn 44, Issue 2, 1999, Pages 119-132

Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP- dependent fashion

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; AMINO ACID; COMPLEMENTARY DNA; GUANOSINE TRIPHOSPHATE; KINESIN; PHOSPHOLIPASE D; TRANSDUCIN;

EID: 0032853557     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C     Document Type: Article
Times cited : (58)

References (69)
  • 1
    • 0032523956 scopus 로고    scopus 로고
    • Pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis
    • Adams RR, Tavares AA, Salzberg A, Bellen HJ, Glover DM. 1998. pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis. Genes Dev 12:1483-1494.
    • (1998) Genes Dev , vol.12 , pp. 1483-1494
    • Adams, R.R.1    Tavares, A.A.2    Salzberg, A.3    Bellen, H.J.4    Glover, D.M.5
  • 3
    • 0028556994 scopus 로고
    • Structure of the human adp-ribosylation factor 1 complexed with GDP
    • Amor J C, Harrison D H, Kahn R A, Ringe D. 1994. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372:704-708.
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 4
    • 0026766151 scopus 로고
    • ADP-ribosylation factor is required for vesicular trafficking between the endoplasmic reticulum and the cis-Golgi compartment
    • Balch W E, Kahn R A, Schwaninger R. 1992. ADP-ribosylation factor is required for vesicular trafficking between the endoplasmic reticulum and the cis-Golgi compartment. J Biol Chem 267: 13053-13061.
    • (1992) J Biol Chem , vol.267 , pp. 13053-13061
    • Balch, W.E.1    Kahn, R.A.2    Schwaninger, R.3
  • 5
    • 0032559708 scopus 로고    scopus 로고
    • Cruising along microtubule highways: How membranes move through the secretory pathway
    • published erratum appears in J Cell Biol 1998 May 18;141:1095
    • Bloom G S, Goldstein L S. 1998. Cruising along microtubule highways: how membranes move through the secretory pathway [published erratum appears in J Cell Biol 1998 May 18;141:1095]. J Cell Biol 140:1277-1280.
    • (1998) J Cell Biol , vol.140 , pp. 1277-1280
    • Bloom, G.S.1    Goldstein, L.S.2
  • 6
    • 0028904466 scopus 로고
    • Arf proteins: The membrane traffic police?
    • Boman A L, Kahn R A. 1995. Arf proteins: the membrane traffic police? [see comments]. Trends Biochem Sci 20:147-150.
    • (1995) Trends Biochem Sci , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 7
    • 0026682791 scopus 로고
    • A role for ADP-ribosylation factor in nuclear vesicle dynamics
    • Boman A L, Taylor T C, Melancon P, Wilson K L. 1992. A role for ADP-ribosylation factor in nuclear vesicle dynamics. Nature 358:512-514.
    • (1992) Nature , vol.358 , pp. 512-514
    • Boman, A.L.1    Taylor, T.C.2    Melancon, P.3    Wilson, K.L.4
  • 12
    • 0029559920 scopus 로고
    • Site-directed mutagenic alteration of potential active-site residues of the A subunit of Escherichia coli heat-labile enterotoxin. Evidence for a catalytic role for glutamic acid 112
    • Cieplak W Jr, Mead D J, Messer R J, Grant C C. 1995. Site-directed mutagenic alteration of potential active-site residues of the A subunit of Escherichia coli heat-labile enterotoxin. Evidence for a catalytic role for glutamic acid 112. J Biol Chem 270:30545-30550.
    • (1995) J Biol Chem , vol.270 , pp. 30545-30550
    • Cieplak W., Jr.1    Mead, D.J.2    Messer, R.J.3    Grant, C.C.4
  • 13
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization
    • Cukierman E, Huber I, Rotman M, Cassel D. 1995. The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science 270:1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 14
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher C, Balch W E. 1994. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J Biol Chem 269:1437-1448.
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 15
    • 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
  • 16
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey C, Li G, Colombo M I, Stahl P D. 1995. A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267: 1175-1178.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 19
    • 0031870960 scopus 로고    scopus 로고
    • Expression of the mitotic motor protein CHO1/MKLP1 in postmitotic neurons
    • Ferhat L, Kuriyama R, Lyons G E, Micales B, Baas P W. 1998. Expression of the mitotic motor protein CHO1/MKLP1 in postmitotic neurons. Eur J Neurosci 10:1383-1393.
    • (1998) Eur J Neurosci , vol.10 , pp. 1383-1393
    • Ferhat, L.1    Kuriyama, R.2    Lyons, G.E.3    Micales, B.4    Baas, P.W.5
  • 20
    • 0030882002 scopus 로고    scopus 로고
    • ARF is not required for nuclear vesicle fusion or mitotic membrane disassembly in vitro: Evidence for a non-ARF GTPase in fusion
    • Gant T M, Wilson K L. 1997. ARF is not required for nuclear vesicle fusion or mitotic membrane disassembly in vitro: evidence for a non-ARF GTPase in fusion. Eur J Cell Biol 74:10-19.
    • (1997) Eur J Cell Biol , vol.74 , pp. 10-19
    • Gant, T.M.1    Wilson, K.L.2
  • 21
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente L. 1983. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol 101:181-191.
    • (1983) Methods Enzymol , vol.101 , pp. 181-191
    • Guarente, L.1
  • 22
    • 0032498542 scopus 로고    scopus 로고
    • Cell-free transport to distinct Golgi cisternae is compartment specific and ARF independent
    • Happe S, Weidman P. 1998. Cell-free transport to distinct Golgi cisternae is compartment specific and ARF independent. J Cell Biol 140:511-523.
    • (1998) J Cell Biol , vol.140 , pp. 511-523
    • Happe, S.1    Weidman, P.2
  • 23
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. 1998. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279:519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 24
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman C S, Winston F. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 25
    • 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 Jun 10;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 Jun 10;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
  • 26
    • 0032544657 scopus 로고    scopus 로고
    • Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein
    • Huber I, Cukierman E, Rotman M, Aoe T, Hsu V W, Cassel D. 1998. Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein. J Biol Chem 273:24786-24791.
    • (1998) J Biol Chem , vol.273 , pp. 24786-24791
    • Huber, I.1    Cukierman, E.2    Rotman, M.3    Aoe, T.4    Hsu, V.W.5    Cassel, D.6
  • 27
    • 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
  • 28
    • 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
  • 29
    • 0025894953 scopus 로고
    • Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins
    • Kahn R A, Kern F G, Clark J, Gelmann E P, Rulka C. 1991. Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. J Biol Chem 266:2606-2614.
    • (1991) J Biol Chem , vol.266 , pp. 2606-2614
    • Kahn, R.A.1    Kern, F.G.2    Clark, J.3    Gelmann, E.P.4    Rulka, C.5
  • 30
    • 0026708135 scopus 로고
    • The amino terminus of ADP-ribosylation factor ARF is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport
    • Kahn R A, Randazzo P, Serafini T, Weiss O, Rulka C, Clark J, Amherdt M, Roller P, Orci L, Rothman J E. 1992. The amino terminus of ADP-ribosylation factor (ARF is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport. J Biol Chem 267:13039-13046.
    • (1992) J Biol Chem , vol.267 , pp. 13039-13046
    • Kahn, R.A.1    Randazzo, P.2    Serafini, T.3    Weiss, O.4    Rulka, C.5    Clark, J.6    Amherdt, M.7    Roller, P.8    Orci, L.9    Rothman, J.E.10
  • 32
    • 0031041589 scopus 로고    scopus 로고
    • Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes
    • Kanoh H, Williger B T, Exton, J H. 1997. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. J Biol Chem 272:5421-5429.
    • (1997) J Biol Chem , vol.272 , pp. 5421-5429
    • Kanoh, H.1    Williger, B.T.2    Exton, J.H.3
  • 33
    • 0032576544 scopus 로고    scopus 로고
    • Nonuniform microtubular polarity established by CHO1/ MKLP1 motor protein is necessary for process formation of podocytes
    • Kobayashi N, Reiser J, Kriz W, Kuriyama R, Mundel P. 1998. Nonuniform microtubular polarity established by CHO1/ MKLP1 motor protein is necessary for process formation of podocytes. J Cell Biol 143:1961-1970.
    • (1998) J Cell Biol , vol.143 , pp. 1961-1970
    • Kobayashi, N.1    Reiser, J.2    Kriz, W.3    Kuriyama, R.4    Mundel, P.5
  • 34
    • 0025909488 scopus 로고
    • Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins
    • Lee C M, Chang P P, Tsai S C, Adamik R, Price S R, Kunz B C, Moss J, Twiddy E M, Holmes R K. 1991. Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins. J Clin Invest 87:1780-1786.
    • (1991) J Clin Invest , vol.87 , pp. 1780-1786
    • Lee, C.M.1    Chang, P.P.2    Tsai, S.C.3    Adamik, R.4    Price, S.R.5    Kunz, B.C.6    Moss, J.7    Twiddy, E.M.8    Holmes, R.K.9
  • 35
    • 0028884602 scopus 로고
    • Plk is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO1/MKLP-1
    • Lee K S, Yuan Y L, Kuriyama R, Erikson R L. 1995. Plk is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO1/MKLP-1. Mol Cell Biol 15:7143-7151.
    • (1995) Mol Cell Biol , vol.15 , pp. 7143-7151
    • Lee, K.S.1    Yuan, Y.L.2    Kuriyama, R.3    Erikson, R.L.4
  • 36
    • 0026632366 scopus 로고
    • Evidence for ADP-ribosylation factor ARF as a regulator of in vitro endosome-endosome fusion
    • Lenhard J M, Kahn R A, Stahl P D. 1992. Evidence for ADP-ribosylation factor (ARF as a regulator of in vitro endosome-endosome fusion. J Biol Chem 267:13047-13052.
    • (1992) J Biol Chem , vol.267 , pp. 13047-13052
    • Lenhard, J.M.1    Kahn, R.A.2    Stahl, P.D.3
  • 37
    • 0029103105 scopus 로고
    • Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex
    • Lippincott-Schwartz J, Cole N B. 1995. Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex. Biochem Soc Trans 23:544-548.
    • (1995) Biochem Soc Trans , vol.23 , pp. 544-548
    • Lippincott-Schwartz, J.1    Cole, N.B.2
  • 38
    • 0027466663 scopus 로고
    • Interaction of ADP-ribosylation factor with Escherichia coli enterotoxin that contains an inactivating lysine 112 substitution
    • Moss J, Stanley S J, Vaughan M, Tsuji T. 1993. Interaction of ADP-ribosylation factor with Escherichia coli enterotoxin that contains an inactivating lysine 112 substitution. J Biol Chem 268:6383-6387.
    • (1993) J Biol Chem , vol.268 , pp. 6383-6387
    • Moss, J.1    Stanley, S.J.2    Vaughan, M.3    Tsuji, T.4
  • 39
    • 0025930764 scopus 로고
    • Activation of cholera toxin and Escherichia coli heat-labile enterotoxins by ADP-ribosylation factors, a family of 20 kDa guanine nucleotide-binding proteins
    • Moss J, Vaughan M. 1991. Activation of cholera toxin and Escherichia coli heat-labile enterotoxins by ADP-ribosylation factors, a family of 20 kDa guanine nucleotide-binding proteins. Mol Microbiol 5:2621-2627.
    • (1991) Mol Microbiol , vol.5 , pp. 2621-2627
    • Moss, J.1    Vaughan, M.2
  • 40
    • 0032488847 scopus 로고    scopus 로고
    • Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase
    • Mossessova E, Gulbis J M, Goldberg J. 1998. Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase. Cell 92:415-423.
    • (1998) Cell , vol.92 , pp. 415-423
    • Mossessova, E.1    Gulbis, J.M.2    Goldberg, J.3
  • 41
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad D, Hunter R, Parker R. 1992. A rapid method for localized mutagenesis of yeast genes. Yeast 8:79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 42
    • 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 Jr, Mowatt MR, Lee C M, Lee F J, Mishima K, Nash TE, 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., Jr.1    Mowatt, M.R.2    Lee, C.M.3    Lee, F.J.4    Mishima, K.5    Nash, T.E.6    Moss, J.7    Vaughan, M.8
  • 43
    • 0025351621 scopus 로고
    • A monoclonal antibody to a mitotic microtubule-associated protein blocks mitotic progression
    • Nislow C, Sellitto C, Kuriyama R, McIntosh J R. 1990. A monoclonal antibody to a mitotic microtubule-associated protein blocks mitotic progression. J Cell Biol 111:511-522.
    • (1990) J Cell Biol , vol.111 , pp. 511-522
    • Nislow, C.1    Sellitto, C.2    Kuriyama, R.3    McIntosh, J.R.4
  • 44
    • 0026781685 scopus 로고
    • A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles
    • Nislow C, Lombillo V A, Kuriyama R, McIntosh J R. 1992. A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles [see comments]. Nature 359:543-547.
    • (1992) Nature , vol.359 , pp. 543-547
    • Nislow, C.1    Lombillo, V.A.2    Kuriyama, R.3    McIntosh, J.R.4
  • 45
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer D J, Helms J B, Beckers C J, Orci L, Rothman J E. 1993. Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J Biol Chem 268:12083-12089.
    • (1993) J Biol Chem , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 46
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W R, Lipman D J. 1988. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85:2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 47
    • 0028951905 scopus 로고
    • Overexpression of wild-type and mutant ARF1 and ARF6: Distinct perturbations of nonoverlapping membrane compartments
    • Peters P J, Hsu V W, Ooi C E, Finazzi D, Teal S B, Oorschot V, Donaldson J G, Klausner R D. 1995. Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J Cell Biol 128:1003-1017.
    • (1995) J Cell Biol , vol.128 , pp. 1003-1017
    • Peters, P.J.1    Hsu, V.W.2    Ooi, C.E.3    Finazzi, D.4    Teal, S.B.5    Oorschot, V.6    Donaldson, J.G.7    Klausner, R.D.8
  • 48
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea 1 protein
    • Peyroche A, Paris S, Jackson C L. 1996. Nucleotide exchange on ARF mediated by yeast Gea 1 protein. Nature 384:479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 50
    • 0032497690 scopus 로고    scopus 로고
    • A nematode kinesin required for cleavage furrow advancement
    • Powers J, Bossinger O, Rose D, Strome S, Saxton W. 1998. A nematode kinesin required for cleavage furrow advancement. Curr Biol 8:1133-1136.
    • (1998) Curr Biol , vol.8 , pp. 1133-1136
    • Powers, J.1    Bossinger, O.2    Rose, D.3    Strome, S.4    Saxton, W.5
  • 51
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids
    • published erratum appears in J Biol Chem 1994 Jun 10;269:16519.
    • Randazzo P A, Kahn R A. 1994. GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids [published erratum appears in J Biol Chem 1994 Jun 10;269:16519]. J Biol Chem 269:10758-19763.
    • (1994) J Biol Chem , vol.269 , pp. 10758-19763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 52
    • 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 Enzymol 219:362-369.
    • (1992) Methods Enzymol , vol.219 , pp. 362-369
    • Randazzo, P.A.1    Weiss, O.2    Kahn, R.A.3
  • 53
    • 0027942397 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, Kahn R A. 1994. The amino terminus of ADP-ribosylation factor (ARF 1 is essential for interaction with Gs and ARF GTPase-activating protein. J Biol Chem 269:29490-29494.
    • (1994) J Biol Chem , vol.269 , pp. 29490-29494
    • Randazzo, P.A.1    Terui, T.2    Sturch, S.3    Kahn, R.A.4
  • 55
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner W, Weissmann C. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem 56:502-514.
    • (1973) Anal Biochem , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 56
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl R H, Gietz R D. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genet 16:339-346.
    • (1989) Curr Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 57
    • 0023878456 scopus 로고
    • Distribution of a matrix component of the midbody during the cell cycle in Chinese hamster ovary cells
    • Sellitto C, Kuriyama R. 1988. Distribution of a matrix component of the midbody during the cell cycle in Chinese hamster ovary cells. J Cell Biol 106:431-439.
    • (1988) J Cell Biol , vol.106 , pp. 431-439
    • Sellitto, C.1    Kuriyama, R.2
  • 58
    • 0024043912 scopus 로고
    • Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins
    • Sewell J L, Kahn R A. 1988. Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins. Proc Natl Acad Sci USA 85:4620-4624.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4620-4624
    • Sewell, J.L.1    Kahn, R.A.2
  • 59
    • 0030857398 scopus 로고    scopus 로고
    • Identification of a microtubule-associated motor protein essential for dendritic differentiation
    • Sharp D J, Yu W, Ferhat L, Kuriyama R, Rueger D C, Baas P W. 1997b. Identification of a microtubule-associated motor protein essential for dendritic differentiation. J Cell Biol 138:833-843.
    • (1997) J Cell Biol , vol.138 , pp. 833-843
    • Sharp, D.J.1    Yu, W.2    Ferhat, L.3    Kuriyama, R.4    Rueger, D.C.5    Baas, P.W.6
  • 60
    • 0030467271 scopus 로고    scopus 로고
    • Microtubule motor complexes moving membranous organelles
    • Sheetz M P. 1996. Microtubule motor complexes moving membranous organelles. Cell Struct Funct 21:369-373.
    • (1996) Cell Struct Funct , vol.21 , pp. 369-373
    • Sheetz, M.P.1
  • 62
    • 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
  • 63
    • 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
  • 64
    • 0026718327 scopus 로고
    • Two distinct members of the ADP-ribosylation factor family of GTP-binding proteins regulate cell-free intra-Golgi transport
    • Taylor T C, Kahn R A, Melancon P. 1992. Two distinct members of the ADP-ribosylation factor family of GTP-binding proteins regulate cell-free intra-Golgi transport. Cell 70:69-79.
    • (1992) Cell , vol.70 , pp. 69-79
    • Taylor, T.C.1    Kahn, R.A.2    Melancon, P.3
  • 65
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee R B, Sheetz M P. 1996. Targeting of motor proteins. Science 271:1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 66
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac 1-interacting protein involved in membrane ruffling
    • Van Aelst L, Joneson T, Bar-Sagi D. 1996. Identification of a novel Rac 1-interacting protein involved in membrane ruffling. Embo J 15:3778-3786.
    • (1996) Embo J , vol.15 , pp. 3778-3786
    • Van Aelst, L.1    Joneson, T.2    Bar-Sagi, D.3
  • 67
    • 0031050564 scopus 로고    scopus 로고
    • Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells
    • Yu W, Sharp D J, Kuriyama R, Mallik P, Baas P W. 1997. Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells. J Cell Biol 136:659-668.
    • (1997) J Cell Biol , vol.136 , pp. 659-668
    • Yu, W.1    Sharp, D.J.2    Kuriyama, R.3    Mallik, P.4    Baas, P.W.5
  • 69
    • 0032584676 scopus 로고    scopus 로고
    • A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae
    • Zhang C J, Cavenagh M M, Kahn, R A. 1998. A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J Biol Chem 273:19792-19796.
    • (1998) J Biol Chem , vol.273 , pp. 19792-19796
    • Zhang, C.J.1    Cavenagh, M.M.2    Kahn, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.