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Volumn 47, Issue 2, 1999, Pages 124-134

Dictyostelium as model system for studies of the actin cytoskeleton by molecular genetics

Author keywords

Actin binding proteins; Cell motility; Cytoskeleton; Dictyostelium; Genome project; Green fluorescent protein

Indexed keywords

CYTOLOGY; FLUORESCENCE; GENES; MOLECULAR BIOLOGY; PROTEINS;

EID: 0344069462     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0029(19991015)47:2<124::AID-JEMT5>3.0.CO;2-8     Document Type: Article
Times cited : (42)

References (115)
  • 1
    • 0028670206 scopus 로고
    • Isolation of Dictyostelium discoideum cytokinesis mutants by restriction enzyme-mediated integration of the blasticidin S resistance marker
    • Adachi H, Hasebe T, Yoshinaga K, Ohta T, Sutoh K. 1994. Isolation of Dictyostelium discoideum cytokinesis mutants by restriction enzyme-mediated integration of the blasticidin S resistance marker. Biochem Biophys Res Commun 205:1808-1814.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1808-1814
    • Adachi, H.1    Hasebe, T.2    Yoshinaga, K.3    Ohta, T.4    Sutoh, K.5
  • 2
    • 0028921277 scopus 로고
    • Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum
    • Aizawa H, Sutoh K, Tsubuki S, Kawashima S, Ishii A, Yahara I. 1995. Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum. J Biol Chem 270:10923-10932.
    • (1995) J Biol Chem , vol.270 , pp. 10923-10932
    • Aizawa, H.1    Sutoh, K.2    Tsubuki, S.3    Kawashima, S.4    Ishii, A.5    Yahara, I.6
  • 3
    • 0030033237 scopus 로고    scopus 로고
    • Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling and cell movement in Dictyostelium
    • Aizawa H, Sutoh K, Yahara I. 1996. Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling and cell movement in Dictyostelium. J Cell Biol 132:335-344.
    • (1996) J Cell Biol , vol.132 , pp. 335-344
    • Aizawa, H.1    Sutoh, K.2    Yahara, I.3
  • 4
    • 0030859055 scopus 로고    scopus 로고
    • A green fluorescent protein-actin fusion protein dominantly inhibits cytokinesis, cell spreading, and locomotion in Dictyostelium
    • Aizawa H, Sameshima M, Yahara I. 1997a. A green fluorescent protein-actin fusion protein dominantly inhibits cytokinesis, cell spreading, and locomotion in Dictyostelium. Cell Struct Funct 22:335-345.
    • (1997) Cell Struct Funct , vol.22 , pp. 335-345
    • Aizawa, H.1    Sameshima, M.2    Yahara, I.3
  • 5
    • 0001081894 scopus 로고    scopus 로고
    • Live dynamics of Dictyostelium cofilin suggests a role in remodeling actin latticework into bundles
    • Aizawa H, Fukui Y, Yahara I. 1997b. Live dynamics of Dictyostelium cofilin suggests a role in remodeling actin latticework into bundles. J Cell Sci 110:2333-2344.
    • (1997) J Cell Sci , vol.110 , pp. 2333-2344
    • Aizawa, H.1    Fukui, Y.2    Yahara, I.3
  • 6
    • 0032005265 scopus 로고    scopus 로고
    • Myosins: Matching functions with motors
    • Baker JP, Titus MA. 1998. Myosins: matching functions with motors. Curr Biol 10:80-86.
    • (1998) Curr Biol , vol.10 , pp. 80-86
    • Baker, J.P.1    Titus, M.A.2
  • 7
    • 85165103620 scopus 로고    scopus 로고
    • The actin-associated protein coronin in chemotaxis, cytokinesis, and phagocytosis of Dictyostelium discoideum
    • in press
    • Barisić K, Ecke M, Heizer C, Maniak M, Westphal M, Albrecht R, Gerisch G. 1999. The actin-associated protein coronin in chemotaxis, cytokinesis, and phagocytosis of Dictyostelium discoideum. Trends Cell Biol (in press).
    • (1999) Trends Cell Biol
    • Barisić, K.1    Ecke, M.2    Heizer, C.3    Maniak, M.4    Westphal, M.5    Albrecht, R.6    Gerisch, G.7
  • 8
    • 0029366794 scopus 로고
    • Setting the pace of cell movement
    • Barkalow K, Hartwig JH. 1995. Setting the pace of cell movement. Curr Biol 5:1000-1002.
    • (1995) Curr Biol , vol.5 , pp. 1000-1002
    • Barkalow, K.1    Hartwig, J.H.2
  • 9
    • 0024242826 scopus 로고
    • Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae
    • Bennett H, Condeelis J. 1988. Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae. Cell Motil Cytoskeleton 11:303-317.
    • (1988) Cell Motil Cytoskeleton , vol.11 , pp. 303-317
    • Bennett, H.1    Condeelis, J.2
  • 11
    • 0032006817 scopus 로고    scopus 로고
    • Control of actin dynamics
    • Carlier MF. 1998. Control of actin dynamics. Curr Opin Cell Biol 10:45-51.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 45-51
    • Carlier, M.F.1
  • 12
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier MF, Pantaloni D. 1997. Control of actin dynamics in cell motility. J Mol Biol 269:459-467.
    • (1997) J Mol Biol , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 13
  • 14
    • 0027482361 scopus 로고
    • Understanding the cortex of crawling cells: Insights from Dictyostelium
    • Condeelis J. 1993. Understanding the cortex of crawling cells: insights from Dictyostelium. Trends Cell Biol 3:371-376.
    • (1993) Trends Cell Biol , vol.3 , pp. 371-376
    • Condeelis, J.1
  • 16
    • 0028919541 scopus 로고
    • Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods
    • Cox D, Ridsdale JA, Condeelis J, Hartwig J. 1995. Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods. J Cell Biol 128:819-835.
    • (1995) J Cell Biol , vol.128 , pp. 819-835
    • Cox, D.1    Ridsdale, J.A.2    Condeelis, J.3    Hartwig, J.4
  • 17
    • 0026041203 scopus 로고
    • Coronin, an actin-binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein βsubunits
    • de Hostos EL, Bradtke B, Lottspeich F, Guggenheim R, Gerisch G. 1991. Coronin, an actin-binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G protein βsubunits. EMBO J 10:4097-4104.
    • (1991) EMBO J , vol.10 , pp. 4097-4104
    • De Hostos, E.L.1    Bradtke, B.2    Lottspeich, F.3    Guggenheim, R.4    Gerisch, G.5
  • 18
    • 0027389812 scopus 로고
    • Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility
    • de Hostos EL, Rehfuess C, Bradtke B, Waddell DR, Albrecht R, Murphy J, Gerisch G. 1993. Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility. J Cell Biol 120:163-173.
    • (1993) J Cell Biol , vol.120 , pp. 163-173
    • De Hostos, E.L.1    Rehfuess, C.2    Bradtke, B.3    Waddell, D.R.4    Albrecht, R.5    Murphy, J.6    Gerisch, G.7
  • 19
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • De Lozanne A, Spudich JA. 1987. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236:1086-1091.
    • (1987) Science , vol.236 , pp. 1086-1091
    • De Lozanne, A.1    Spudich, J.A.2
  • 20
    • 0024147085 scopus 로고
    • Chemotaxis in eukaryotic cells: A focus on leukocytes and Dictyostelium
    • Devreotes PN, Zigmond SH. 1988. Chemotaxis in eukaryotic cells: a focus on leukocytes and Dictyostelium. Ann Rev Cell Biol 4:649-686.
    • (1988) Ann Rev Cell Biol , vol.4 , pp. 649-686
    • Devreotes, P.N.1    Zigmond, S.H.2
  • 21
    • 0026080022 scopus 로고
    • Dictyostelium annexin VII (synexin) cDNA sequence and isolation of a gene disruption mutant
    • Döring V, Schleicher M, Noegel AA. 1991. Dictyostelium annexin VII (synexin) cDNA sequence and isolation of a gene disruption mutant. J Biol Chem 266:17509-17515.
    • (1991) J Biol Chem , vol.266 , pp. 17509-17515
    • Döring, V.1    Schleicher, M.2    Noegel, A.A.3
  • 22
    • 0030581758 scopus 로고    scopus 로고
    • A major agonist-regulated capping activity in Dictyostelium is due to the capping protein, cap32/34
    • Eddy RJ, Han J, Sauterer RA, Condeelis JS. 1996. A major agonist-regulated capping activity in Dictyostelium is due to the capping protein, cap32/34. Biochim Biophys Acta 1314:247-259.
    • (1996) Biochim Biophys Acta , vol.1314 , pp. 247-259
    • Eddy, R.J.1    Han, J.2    Sauterer, R.A.3    Condeelis, J.S.4
  • 23
    • 0030728491 scopus 로고    scopus 로고
    • Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium
    • Eddy RJ, Han J, Condeelis JS. 1997. Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J Cell Biol 139:1243-1253.
    • (1997) J Cell Biol , vol.139 , pp. 1243-1253
    • Eddy, R.J.1    Han, J.2    Condeelis, J.S.3
  • 26
    • 0026078290 scopus 로고
    • Domain structure in actin-binding proteins: Expression and functional characterisation of truncated severin
    • Eichinger L, Noegel AA, Schleicher M. 1991. Domain structure in actin-binding proteins: expression and functional characterisation of truncated severin. J Cell Biol 112:665-676.
    • (1991) J Cell Biol , vol.112 , pp. 665-676
    • Eichinger, L.1    Noegel, A.A.2    Schleicher, M.3
  • 27
    • 0030069057 scopus 로고    scopus 로고
    • Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants
    • Eichinger L, Koeppel B, Noegel AA, Schleicher M, Schliwa M, Weijer K, Witke W, Janmey PA. 1996. Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants. Biophys J 70:1054-1060.
    • (1996) Biophys J , vol.70 , pp. 1054-1060
    • Eichinger, L.1    Koeppel, B.2    Noegel, A.A.3    Schleicher, M.4    Schliwa, M.5    Weijer, K.6    Witke, W.7    Janmey, P.A.8
  • 28
    • 0032557547 scopus 로고    scopus 로고
    • Characterization and cloning of a Dictyostelium Ste-20-like protein kinase that phosphorylates the actin-binding protein severin
    • Eichinger L, Baehler M, Dietz M, Eckerskorn C, Schleicher M. 1998. Characterization and cloning of a Dictyostelium Ste-20-like protein kinase that phosphorylates the actin-binding protein severin. J Biol Chem 273:12952-12959.
    • (1998) J Biol Chem , vol.273 , pp. 12952-12959
    • Eichinger, L.1    Baehler, M.2    Dietz, M.3    Eckerskorn, C.4    Schleicher, M.5
  • 30
    • 0031282292 scopus 로고    scopus 로고
    • Photosensory and thermosensory responses in Dictyostelium slugs are specifically impaired by absence of the F-actin crosslinking gelation factor (ABP-120)
    • Fisher PF, Noegel AA, Fechheimer M, Rivero F, Prassler J, Gerisch G. 1997. Photosensory and thermosensory responses in Dictyostelium slugs are specifically impaired by absence of the F-actin crosslinking gelation factor (ABP-120). Curr Biol 7:889-892.
    • (1997) Curr Biol , vol.7 , pp. 889-892
    • Fisher, P.F.1    Noegel, A.A.2    Fechheimer, M.3    Rivero, F.4    Prassler, J.5    Gerisch, G.6
  • 31
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoebae
    • Fukui Y, Lynch TJ, Brzeska H, Korn ED. 1989. Myosin I is located at the leading edges of locomoting Dictyostelium amoebae. Nature 341:329-331.
    • (1989) Nature , vol.341 , pp. 329-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 32
    • 0029411196 scopus 로고
    • Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein
    • Gerisch G, Albrecht R, Heizer C, Hodgkinson S, Maniak M. 1995. Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein. Curr Biol 5:1280-1285.
    • (1995) Curr Biol , vol.5 , pp. 1280-1285
    • Gerisch, G.1    Albrecht, R.2    Heizer, C.3    Hodgkinson, S.4    Maniak, M.5
  • 33
    • 0030063258 scopus 로고    scopus 로고
    • Identification of a cyclase-associated protein (CAP) homologue in Dictyostelium discoideum and characterization of its interaction with actin
    • Gottwald U, Brokamp R, Karakesisoglou I Schleicher M, Noegel AA. 1996. Identification of a cyclase-associated protein (CAP) homologue in Dictyostelium discoideum and characterization of its interaction with actin. Mol Biol Cell 7:261-272.
    • (1996) Mol Biol Cell , vol.7 , pp. 261-272
    • Gottwald, U.1    Brokamp, R.2    Karakesisoglou, I.3    Schleicher, M.4    Noegel, A.A.5
  • 34
    • 0031046060 scopus 로고    scopus 로고
    • Fluid-phase uptake by macropinocytosis in Dictyostelium
    • Hacker U, Albrecht R, Maniak M. 1997. Fluid-phase uptake by macropinocytosis in Dictyostelium. J Cell Sci 110:105-112.
    • (1997) J Cell Sci , vol.110 , pp. 105-112
    • Hacker, U.1    Albrecht, R.2    Maniak, M.3
  • 35
    • 0024453412 scopus 로고
    • Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: Their regulation by chemotactic stimulation
    • Hall AL, Warren V, Dharmawardhane S, Condeelis J. 1989. Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: their regulation by chemotactic stimulation. J Cell Biol 109:2207-2213.
    • (1989) J Cell Biol , vol.109 , pp. 2207-2213
    • Hall, A.L.1    Warren, V.2    Dharmawardhane, S.3    Condeelis, J.4
  • 36
    • 0029977873 scopus 로고    scopus 로고
    • Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: Intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein
    • Hanakam F, Albrecht R, Eckerskorn C, Matzner M, Gerisch G. 1996. Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein. EMBO J 15:2935-2943.
    • (1996) EMBO J , vol.15 , pp. 2935-2943
    • Hanakam, F.1    Albrecht, R.2    Eckerskorn, C.3    Matzner, M.4    Gerisch, G.5
  • 38
    • 0030604703 scopus 로고    scopus 로고
    • Tertiary structure of destrin and structural similarity between two actin-regulating protein families
    • Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F. 1996. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell 85:1047-1055.
    • (1996) Cell , vol.85 , pp. 1047-1055
    • Hatanaka, H.1    Ogura, K.2    Moriyama, K.3    Ichikawa, S.4    Yahara, I.5    Inagaki, F.6
  • 39
    • 0025950142 scopus 로고
    • Dictyostelium discoideum contains two profilin isoforms that differ in structure and function
    • Haugwitz M, Noegel AA, Rieger D, Lottspeich F, Schleicher M. 1991. Dictyostelium discoideum contains two profilin isoforms that differ in structure and function. J Cell Sci 100:481-489.
    • (1991) J Cell Sci , vol.100 , pp. 481-489
    • Haugwitz, M.1    Noegel, A.A.2    Rieger, D.3    Lottspeich, F.4    Schleicher, M.5
  • 40
    • 0028004565 scopus 로고
    • Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz M, Noegel AA, Karakesisoglou J, Schleicher M. 1994. Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79:303-314.
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 41
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim R, Tsien RY. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Biol 6:178-182.
    • (1996) Curr Biol , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 42
    • 0027933857 scopus 로고
    • Ponticulin is an atypical membrane protein
    • Hitt AL, Lu TH, Luna EJ. 1994. Ponticulin is an atypical membrane protein. J Cell Biol 126:1421-1431.
    • (1994) J Cell Biol , vol.126 , pp. 1421-1431
    • Hitt, A.L.1    Lu, T.H.2    Luna, E.J.3
  • 43
    • 0023091904 scopus 로고
    • Isolation of a 240-kilodalton actin-binding protein from Dictyostelium discoideum
    • Hock RS, Condeelis JS. 1987. Isolation of a 240-kilodalton actin-binding protein from Dictyostelium discoideum. J Biol Chem 262: 394-400.
    • (1987) J Biol Chem , vol.262 , pp. 394-400
    • Hock, R.S.1    Condeelis, J.S.2
  • 44
    • 0027244276 scopus 로고
    • The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype ("protovillin")
    • Hofmann A, Noegel AA, Bomblies L, Lottspeich F, Schleicher M. 1993. The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype ("protovillin"). FEBS Lett 328:71-76.
    • (1993) FEBS Lett , vol.328 , pp. 71-76
    • Hofmann, A.1    Noegel, A.A.2    Bomblies, L.3    Lottspeich, F.4    Schleicher, M.5
  • 45
    • 0024296379 scopus 로고
    • Establishment of a transient expression system for Dictyostelium discoideum
    • Howard PK, Ahern KG, Firtel RA. 1988. Establishment of a transient expression system for Dictyostelium discoideum. Nucleic Acids Res 16:2613-2623.
    • (1988) Nucleic Acids Res , vol.16 , pp. 2613-2623
    • Howard, P.K.1    Ahern, K.G.2    Firtel, R.A.3
  • 47
    • 0029958869 scopus 로고    scopus 로고
    • Linking microfilaments to intracellular membranes: The actin-binding and vesicle-associated protein comitin exhibits a mannose-specific lectin activity
    • Jung E, Fucini P, Stewart M, Noegel AA, Schleicher M. 1996. Linking microfilaments to intracellular membranes: the actin-binding and vesicle-associated protein comitin exhibits a mannose-specific lectin activity. EMBO J 15:1238-1246.
    • (1996) EMBO J , vol.15 , pp. 1238-1246
    • Jung, E.1    Fucini, P.2    Stewart, M.3    Noegel, A.A.4    Schleicher, M.5
  • 48
    • 0025975846 scopus 로고
    • Positive selection for Dictyostelium discoideum mutants lacking UMP synthase activity based on resistance to 5-fluoroorotic acid
    • Kalpaxis D, Zundorf I, Werner H, Reindl N, Boy-Marcotte E, Jacquet M, Dingermann T. 1991. Positive selection for Dictyostelium discoideum mutants lacking UMP synthase activity based on resistance to 5-fluoroorotic acid. Mol Gen Genet 225:492-500.
    • (1991) Mol Gen Genet , vol.225 , pp. 492-500
    • Kalpaxis, D.1    Zundorf, I.2    Werner, H.3    Reindl, N.4    Boy-Marcotte, E.5    Jacquet, M.6    Dingermann, T.7
  • 49
    • 0033526050 scopus 로고    scopus 로고
    • Identification of a suppressor of the Dictyostelium profilin-minus phenotype as a CD36/LIMPII homologue
    • in press
    • Karakesisoglou I, Janssen K-P, Eichinger L, Noegel AA, Schleicher M. 1999. Identification of a suppressor of the Dictyostelium profilin-minus phenotype as a CD36/LIMPII homologue. J Cell Biol (in press).
    • (1999) J Cell Biol
    • Karakesisoglou, I.1    Janssen, K.-P.2    Eichinger, L.3    Noegel, A.A.4    Schleicher, M.5
  • 50
    • 0023189474 scopus 로고
    • Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum
    • Knecht DA, Loomis WF. 1987. Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science 236:1081-1086.
    • (1987) Science , vol.236 , pp. 1081-1086
    • Knecht, D.A.1    Loomis, W.F.2
  • 51
    • 0028919857 scopus 로고
    • A talin homologue at Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant
    • Kreitmeier M, Gerisch G, Heizer C, Mueller-Taubenberger A. 1995. A talin homologue at Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant. J Cell Biol 129:179-188.
    • (1995) J Cell Biol , vol.129 , pp. 179-188
    • Kreitmeier, M.1    Gerisch, G.2    Heizer, C.3    Mueller-Taubenberger, A.4
  • 52
    • 0026646765 scopus 로고
    • Tagging developmental genes in dictyostelium by restriction enzyme-mediated integration of plasmid DNA
    • Kuspa A, Loomis WF. 1992. Tagging developmental genes in Dictyostelium by restriction enzyme-mediated integration of plasmid DNA. Proc Natl Acad Sc USA 89:8803-8807.
    • (1992) Proc Natl Acad Sc USA , vol.89 , pp. 8803-8807
    • Kuspa, A.1    Loomis, W.F.2
  • 53
    • 0032966363 scopus 로고    scopus 로고
    • Function of gelsolin:Motility, signaling, apoptosis, cancer
    • Kwiatkowski DJ. 1999. Function of gelsolin:motility, signaling, apoptosis, cancer. Curr Opin Cell Biol 11:103-108.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 103-108
    • Kwiatkowski, D.J.1
  • 54
    • 0025872009 scopus 로고
    • The ble gene of streptoalloteichus hindustanus as a new selectable marker for Dictyostelium discoideum confers resistance to phleomycin
    • Leiting B, Noegel AA. 1991. The ble gene of Streptoalloteichus hindustanus as a new selectable marker for Dictyostelium discoideum confers resistance to phleomycin. Biochem Biophys Res Commun 180:1403-1407.
    • (1991) Biochem Biophys Res Commun , vol.180 , pp. 1403-1407
    • Leiting, B.1    Noegel, A.A.2
  • 55
    • 0027080273 scopus 로고
    • Inducible expression of calmodulin antisense RNA in Dictyostelium cells inhibits the completion of cytokinesis
    • Liu T, Williams JG, Clarke M. 1992. Inducible expression of calmodulin antisense RNA in Dictyostelium cells inhibits the completion of cytokinesis. Mol Biol Cell 3:1403-1413.
    • (1992) Mol Biol Cell , vol.3 , pp. 1403-1413
    • Liu, T.1    Williams, J.G.2    Clarke, M.3
  • 56
    • 0029869044 scopus 로고    scopus 로고
    • Genetic networks that regulate development in Dictyostelium cells
    • Loomis WF. 1996. Genetic networks that regulate development in Dictyostelium cells. Microbiol Rev 60:135-150.
    • (1996) Microbiol Rev , vol.60 , pp. 135-150
    • Loomis, W.F.1
  • 57
    • 0002421307 scopus 로고    scopus 로고
    • The genome of Dictyostelium discoideum
    • Maeda Y, Inouye K, Takeuchi I, editors. Tokyo Japan: Universal Academy Press
    • Loomis WF, Kuspa A. 1997. The genome of Dictyostelium discoideum. In: Maeda Y, Inouye K, Takeuchi I, editors. Dictyostelium: a model system for cell and developmental biology. Tokyo Japan: Universal Academy Press. p 15-30.
    • (1997) Dictyostelium: a Model System for Cell and Developmental Biology , pp. 15-30
    • Loomis, W.F.1    Kuspa, A.2
  • 58
    • 0031963216 scopus 로고    scopus 로고
    • GFP illuminates the cytoskeleton
    • Ludin B, Matus A. 1998. GFP illuminates the cytoskeleton. Trends Cell Biol 8:72-77.
    • (1998) Trends Cell Biol , vol.8 , pp. 72-77
    • Ludin, B.1    Matus, A.2
  • 59
    • 0031887131 scopus 로고    scopus 로고
    • How ADF/cofilin depolymerizes actin filaments
    • Maciver SK. 1998. How ADF/cofilin depolymerizes actin filaments. Curr Opin Cell Biol 10:140-144.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 140-144
    • Maciver, S.K.1
  • 60
    • 0029583095 scopus 로고
    • Coronin involved in phagocytosis: Dynamics of particle-induced relocalization visualized by a green fluorescent protein tag
    • Maniak M, Rauchenberger R, Albrecht R, Murphy J, Gerisch G. 1995. Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein tag. Cell 83:915-924.
    • (1995) Cell , vol.83 , pp. 915-924
    • Maniak, M.1    Rauchenberger, R.2    Albrecht, R.3    Murphy, J.4    Gerisch, G.5
  • 61
    • 0024634880 scopus 로고
    • Gene replacement in Dictyostelium: Generation of myosin null mutants
    • Manstein DJ, Titus MA, De Lozanne A, Spudich JA. 1989. Gene replacement in Dictyostelium: Generation of myosin null mutants. EMBO J 8:923-932.
    • (1989) EMBO J , vol.8 , pp. 923-932
    • Manstein, D.J.1    Titus, M.A.2    De Lozanne, A.3    Spudich, J.A.4
  • 62
    • 0027829334 scopus 로고
    • Myosin function in the motile behaviour of cells
    • Manstein DJ. 1993. Myosin function in the motile behaviour of cells. Symp Soc Exp Biol 47:375-381.
    • (1993) Symp Soc Exp Biol , vol.47 , pp. 375-381
    • Manstein, D.J.1
  • 63
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira P. 1991. Modular organization of actin crosslinking proteins. Trends Biol Sci 16:87-92.
    • (1991) Trends Biol Sci , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 64
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin P, Gooch JT, Mannherz H-G, Weeds AG. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 65
    • 0022217740 scopus 로고
    • Effects of cytochalasin B on cell movements and chemoattractant-elicited actin changes of dictyostelium
    • McRobbie SJ, Newell PC. 1985. Effects of cytochalasin B on cell movements and chemoattractant-elicited actin changes of Dictyostelium. Exp Cell Res 160:275-286.
    • (1985) Exp Cell Res , vol.160 , pp. 275-286
    • McRobbie, S.J.1    Newell, P.C.2
  • 68
    • 0030783741 scopus 로고    scopus 로고
    • A novel, negative selectable marker for gene disruption in Dictyostelium
    • Morrison A, Marschalek R, Dingermann T, Harwood AJ. 1997. A novel, negative selectable marker for gene disruption in Dictyostelium. Gene 202:171-176.
    • (1997) Gene , vol.202 , pp. 171-176
    • Morrison, A.1    Marschalek, R.2    Dingermann, T.3    Harwood, A.J.4
  • 69
    • 0027550516 scopus 로고
    • Small actin-binding proteins: The β-thymosin family
    • Nachmias VT. 1993. Small actin-binding proteins: the β-thymosin family. Curr Opin Cell Biol 5:56-62.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 56-62
    • Nachmias, V.T.1
  • 70
    • 0021737746 scopus 로고
    • DNA-mediated transformation in Dictyostelium discoideum: Regulated expression of an actin gene fusion
    • Nellen W, Silan C, Firtel RA. 1984, DNA-mediated transformation in Dictyostelium discoideum: Regulated expression of an actin gene fusion. Mol Cell Biol 4:2890-2898.
    • (1984) Mol Cell Biol , vol.4 , pp. 2890-2898
    • Nellen, W.1    Silan, C.2    Firtel, R.A.3
  • 71
    • 0031049976 scopus 로고    scopus 로고
    • Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: Redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow
    • Neujahr R, Heizer C, Gerisch G. 1997a. Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow. J Cell Sci 110:123-137.
    • (1997) J Cell Sci , vol.110 , pp. 123-137
    • Neujahr, R.1    Heizer, C.2    Gerisch, G.3
  • 72
    • 0031408781 scopus 로고    scopus 로고
    • Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells
    • Neujahr R, Heizer C, Albrecht R, Ecke M, Schwartz JM, Weber I, Gerisch G. 1997b. Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells. J Cell Biol 139:1793-1804.
    • (1997) J Cell Biol , vol.139 , pp. 1793-1804
    • Neujahr, R.1    Heizer, C.2    Albrecht, R.3    Ecke, M.4    Schwartz, J.M.5    Weber, I.6    Gerisch, G.7
  • 73
    • 0031802611 scopus 로고    scopus 로고
    • Microtubule-mediated centrosome motility and the positioning of cleavage furrows in multinucleate myosin II-null cells
    • Neujahr R, Albrecht R, Koehler J, Matzner M, Schwartz JM, Westphal M, Gerisch G. 1998. Microtubule-mediated centrosome motility and the positioning of cleavage furrows in multinucleate myosin II-null cells. J Cell Sci 111:1227-1240.
    • (1998) J Cell Sci , vol.111 , pp. 1227-1240
    • Neujahr, R.1    Albrecht, R.2    Koehler, J.3    Matzner, M.4    Schwartz, J.M.5    Westphal, M.6    Gerisch, G.7
  • 74
    • 0029550552 scopus 로고
    • Signal transduction and motility of Dictyostelium
    • Newell PC. 1995. Signal transduction and motility of Dictyostelium. Biosci Rep 15:445-462.
    • (1995) Biosci Rep , vol.15 , pp. 445-462
    • Newell, P.C.1
  • 75
    • 0039728833 scopus 로고    scopus 로고
    • Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis
    • Nieẅoehner J, Weber I, Maniak M, Muellerl-Taubenberger A, Gerisch G. 1997. Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis. J Cell Biol 138:349-361.
    • (1997) J Cell Biol , vol.138 , pp. 349-361
    • Nieẅoehner, J.1    Weber, I.2    Maniak, M.3    Muellerl-Taubenberger, A.4    Gerisch, G.5
  • 76
    • 0029565191 scopus 로고
    • The Dictyostelium cytoskeleton
    • Noegel AA, Luna JE. 1995. The Dictyostelium cytoskeleton. Experientia 51:1135-1143.
    • (1995) Experientia , vol.51 , pp. 1135-1143
    • Noegel, A.A.1    Luna, J.E.2
  • 78
    • 0024335961 scopus 로고
    • The Dictyostelium gelation factor shares a putative actin-binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
    • Noegel AA, Rapp S, Lottspeich F, Schleicher M, Stewart M. 1989. The Dictyostelium gelation factor shares a putative actin-binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation. J Cell Biol 109:607-618.
    • (1989) J Cell Biol , vol.109 , pp. 607-618
    • Noegel, A.A.1    Rapp, S.2    Lottspeich, F.3    Schleicher, M.4    Stewart, M.5
  • 79
    • 0001462976 scopus 로고    scopus 로고
    • Use of a fusion protein between GFP and an actin-binding domain to visualize transient filamentous actin structures
    • Pang KM, Lee E, Knecht DA. 1998. Use of a fusion protein between GFP and an actin-binding domain to visualize transient filamentous actin structures. Curr Biol 8:405-408.
    • (1998) Curr Biol , vol.8 , pp. 405-408
    • Pang, K.M.1    Lee, E.2    Knecht, D.A.3
  • 80
    • 0029943450 scopus 로고    scopus 로고
    • Molecular genetics of signal transduction in Dictyostelium
    • Parent CA, Devreotes PN. 1996. Molecular genetics of signal transduction in Dictyostelium. Annu Rev Biochem 65:411-440.
    • (1996) Annu Rev Biochem , vol.65 , pp. 411-440
    • Parent, C.A.1    Devreotes, P.N.2
  • 81
    • 0025099508 scopus 로고
    • Length distribution of F-actin in dictyostelium discoideum
    • Podolski JL, Steck TL. 1990. Length distribution of F-actin in Dictyostelium discoideum. J Biol Chem 265:1312-1318.
    • (1990) J Biol Chem , vol.265 , pp. 1312-1318
    • Podolski, J.L.1    Steck, T.L.2
  • 82
    • 0028170812 scopus 로고
    • Structure of actin-binding proteins: Insights about function at atomic resolution
    • Pollard TD, Almo A, Quirk S, Vinson V, Lattman EE. 1994. Structure of actin-binding proteins: insights about function at atomic resolution. Ann Rev Cell Biol 10:207-249.
    • (1994) Ann Rev Cell Biol , vol.10 , pp. 207-249
    • Pollard, T.D.1    Almo, A.2    Quirk, S.3    Vinson, V.4    Lattman, E.E.5
  • 83
    • 0030790823 scopus 로고    scopus 로고
    • Interaction of a Dictyostelium member of the plastin/ fimbrin family with actin filaments and actin-myosin complexes
    • Prassler J, Stocker S, Marriott G, Heidecker M, Kellermann J, Gerisch G. 1997. Interaction of a Dictyostelium member of the plastin/ fimbrin family with actin filaments and actin-myosin complexes. Mol Biol Cell 8:83-95.
    • (1997) Mol Biol Cell , vol.8 , pp. 83-95
    • Prassler, J.1    Stocker, S.2    Marriott, G.3    Heidecker, M.4    Kellermann, J.5    Gerisch, G.6
  • 84
    • 0000038872 scopus 로고
    • Dictyostelium discoideum, a new species of slime mold from decaying forest leaves
    • Raper KB. 1935. Dictyostelium discoideum, a new species of slime mold from decaying forest leaves. J Agric Res 50:133-147.
    • (1935) J Agric Res , vol.50 , pp. 133-147
    • Raper, K.B.1
  • 85
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • Rivero F, Koeppel B, Peracino B, Bozzaro S, Siegert F, Wejjer CJ, Schleicher M, Albrecht R, Noegel AA. 1996. The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J Cell Sci 109:2679-2691.
    • (1996) J Cell Sci , vol.109 , pp. 2679-2691
    • Rivero, F.1    Koeppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Wejjer, C.J.6    Schleicher, M.7    Albrecht, R.8    Noegel, A.A.9
  • 86
    • 0031852649 scopus 로고    scopus 로고
    • Interaptin, and actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments
    • Rivero F, Kuspa A, Brokamp R, Matzner M, Noegel AA. 1998. Interaptin, and actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments. J Cell Biol 142:735-750.
    • (1998) J Cell Biol , vol.142 , pp. 735-750
    • Rivero, F.1    Kuspa, A.2    Brokamp, R.3    Matzner, M.4    Noegel, A.A.5
  • 87
    • 0032565877 scopus 로고    scopus 로고
    • Actin, cofilin and cognition
    • Rosenblatt J, Mitchison TJ. 1998. Actin, cofilin and cognition. Nature 393:739-740.
    • (1998) Nature , vol.393 , pp. 739-740
    • Rosenblatt, J.1    Mitchison, T.J.2
  • 88
    • 0030663097 scopus 로고    scopus 로고
    • Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells
    • Sabry JH, Moores SL, Ryan S, Zang JH, Spudich JS. 1997. Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells. Mol Biol Cell 8:2605-2615.
    • (1997) Mol Biol Cell , vol.8 , pp. 2605-2615
    • Sabry, J.H.1    Moores, S.L.2    Ryan, S.3    Zang, J.H.4    Spudich, J.S.5
  • 90
    • 0026860948 scopus 로고
    • Dynamics of the Dictyostelium cytoskeleton during chemotaxis
    • Schleicher M, Noegel AA. 1992. Dynamics of the Dictyostelium cytoskeleton during chemotaxis. The New Biologist 4:461-472.
    • (1992) The New Biologist , vol.4 , pp. 461-472
    • Schleicher, M.1    Noegel, A.A.2
  • 91
    • 0001604571 scopus 로고
    • New actin-binding proteins from Dictyostelium discoideum
    • Schleicher M, Gerisch G, Isenberg G. 1984. New actin-binding proteins from Dictyostelium discoideum. EMBO J 3:2095-2100.
    • (1984) EMBO J , vol.3 , pp. 2095-2100
    • Schleicher, M.1    Gerisch, G.2    Isenberg, G.3
  • 92
    • 0024015069 scopus 로고
    • A Dictyostelium mutant with severe defects in alpha-actinin: Its characterization using cDNA probes and monoclonal antibodies
    • Schleicher M, Noegel AA, Schwarz T, Wallraff E, Brink M, Faix J, Gerisch G, Isenberg G. 1988. A Dictyostelium mutant with severe defects in alpha-actinin: its characterization using cDNA probes and monoclonal antibodies. J Cell Sci 90:59-71.
    • (1988) J Cell Sci , vol.90 , pp. 59-71
    • Schleicher, M.1    Noegel, A.A.2    Schwarz, T.3    Wallraff, E.4    Brink, M.5    Faix, J.6    Gerisch, G.7    Isenberg, G.8
  • 95
    • 0028464361 scopus 로고
    • Profilin: At the crossroads of signal transduction and the actin cytoskeleton
    • Sohn RH, Goldschmidt-Clermont PJ. 1994. Profilin: at the crossroads of signal transduction and the actin cytoskeleton. Bioessays 16:465-472.
    • (1994) Bioessays , vol.16 , pp. 465-472
    • Sohn, R.H.1    Goldschmidt-Clermont, P.J.2
  • 96
    • 0024755672 scopus 로고
    • In pursuit of myosin function
    • Spudich JA. 1989. In pursuit of myosin function. Cell Regul 1:1-11.
    • (1989) Cell Regul , vol.1 , pp. 1-11
    • Spudich, J.A.1
  • 97
    • 0029885430 scopus 로고    scopus 로고
    • Structure/function studies on the pH-dependent actin-binding protein hisactophilin in Dictyostelium mutants
    • Stoeckelhuber M, Noegel AA, Eckerskorn C, Koehler J, Rieger D, Schleicher M. 1996. Structure/function studies on the pH-dependent actin-binding protein hisactophilin in Dictyostelium mutants. J Cell Sci 109:1825-1835.
    • (1996) J Cell Sci , vol.109 , pp. 1825-1835
    • Stoeckelhuber, M.1    Noegel, A.A.2    Eckerskorn, C.3    Koehler, J.4    Rieger, D.5    Schleicher, M.6
  • 100
    • 0032917452 scopus 로고    scopus 로고
    • Taking the plunge: Terminal differentiation in Dictyostelium
    • Thomason P, Traynor D, Kay R. 1999. Taking the plunge: terminal differentiation in Dictyostelium. Trends Genet 15:15-19.
    • (1999) Trends Genet , vol.15 , pp. 15-19
    • Thomason, P.1    Traynor, D.2    Kay, R.3
  • 102
    • 0003822180 scopus 로고    scopus 로고
    • The myosins of Dictyostelium
    • Maeda Y, Inouye K, Takeuchi I, editors. Tokyo, Japan: Universal Academy Press Inc.
    • Uyeda TQP, Titus MA. 1997. The myosins of Dictyostelium. In: Maeda Y, Inouye K, Takeuchi I, editors. Dictyostelium: A model system for cell and developmental biology. Tokyo, Japan: Universal Academy Press Inc., p 43-64.
    • (1997) Dictyostelium: A Model System for Cell and Developmental Biology , pp. 43-64
    • Uyeda, T.Q.P.1    Titus, M.A.2
  • 103
    • 0028866902 scopus 로고
    • Expression of csA-hm2 fusion in Dictyostelium discoideum under the control of the Dictyostelium ras promoter reveals functional muscarinic receptors
    • Voith G, Dingermann T. 1995. Expression of csA-hm2 fusion in Dictyostelium discoideum under the control of the Dictyostelium ras promoter reveals functional muscarinic receptors. Pharmazie 50:758-762.
    • (1995) Pharmazie , vol.50 , pp. 758-762
    • Voith, G.1    Dingermann, T.2
  • 104
    • 0028227833 scopus 로고
    • Implications for bed mRNA localization from spatial distribution of exu protein in drosophila oogenesis
    • Wang S, Hazelrigg T. 1994. Implications for bed mRNA localization from spatial distribution of exu protein in Drosophila oogenesis. Nature 369:400-403.
    • (1994) Nature , vol.369 , pp. 400-403
    • Wang, S.1    Hazelrigg, T.2
  • 105
    • 0014841120 scopus 로고
    • Growth of myxamoebae of the cellular slime mould Dictyostelium discoideum in axenic culture
    • Watts DJ, Ashworth JM. 1970. Growth of myxamoebae of the cellular slime mould Dictyostelium discoideum in axenic culture. Biochem J 119:171-174.
    • (1970) Biochem J , vol.119 , pp. 171-174
    • Watts, D.J.1    Ashworth, J.M.2
  • 108
  • 110
    • 0023661339 scopus 로고
    • Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of the protein
    • Witke W, Nellen W, Noegel A. 1987. Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of the protein. EMBO J 6:4143-4148.
    • (1987) EMBO J , vol.6 , pp. 4143-4148
    • Witke, W.1    Nellen, W.2    Noegel, A.3
  • 111
    • 0026593102 scopus 로고
    • Redundancy in the microfilament system: Abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins
    • Witke W, Schleicher M, Noegel AA. 1992. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell 68:53-62.
    • (1992) Cell , vol.68 , pp. 53-62
    • Witke, W.1    Schleicher, M.2    Noegel, A.A.3
  • 114
    • 0032506022 scopus 로고    scopus 로고
    • Myosin II localization during cytokinesis occurs by a mechanism that does not require its motor domain
    • Zang JH, Spudich JA. 1998. Myosin II localization during cytokinesis occurs by a mechanism that does not require its motor domain. Proc Natl Acad Sci 95:13652-13657.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 13652-13657
    • Zang, J.H.1    Spudich, J.A.2
  • 115
    • 0030690360 scopus 로고    scopus 로고
    • On the role of myosin-II in cytokinesis: Division of Dictyostelium cells under adhesive and nonadhesive conditions
    • Zang JH, Cavet G, Sabry JH, Wagner P, Moores SL, Spudich JA. 1997. On the role of myosin-II in cytokinesis: division of Dictyostelium cells under adhesive and nonadhesive conditions. Mol Biol Cell 8:2617-2629.
    • (1997) Mol Biol Cell , vol.8 , pp. 2617-2629
    • Zang, J.H.1    Cavet, G.2    Sabry, J.H.3    Wagner, P.4    Moores, S.L.5    Spudich, J.A.6


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