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Volumn 146, Issue 1-2, 2004, Pages 58-71

Design and regulation of the AAA+ microtubule motor dynein

Author keywords

AAA + Proteins; Dynein; Flagella; Microtubule; Motility

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE; IMMUNOGLOBULIN LIGHT CHAIN; NUCLEOTIDE;

EID: 1642321118     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.09.026     Document Type: Conference Paper
Times cited : (92)

References (148)
  • 1
    • 0031890532 scopus 로고    scopus 로고
    • A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation
    • Aitken R.J., Harkiss D., Knox W., Paterson M., Irvine D.S. A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation. J. Cell Sci. 111:1997;645-656.
    • (1997) J. Cell Sci. , vol.111 , pp. 645-656
    • Aitken, R.J.1    Harkiss, D.2    Knox, W.3    Paterson, M.4    Irvine, D.S.5
  • 2
    • 0027991637 scopus 로고
    • Regulation of 22S dynein by a 29-kDa light chain
    • Barkalow K., Hamasaki T., Satir P. Regulation of 22S dynein by a 29-kDa light chain. J. Cell Biol. 126:1994;727-735.
    • (1994) J. Cell Biol. , vol.126 , pp. 727-735
    • Barkalow, K.1    Hamasaki, T.2    Satir, P.3
  • 3
    • 0033152573 scopus 로고    scopus 로고
    • Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the γ heavy chain
    • Benashski S.E., Patel-King R.S., King S.M. Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the γ heavy chain. Biochemistry. 38:1999;7253-7264.
    • (1999) Biochemistry , vol.38 , pp. 7253-7264
    • Benashski, S.E.1    Patel-King, R.S.2    King, S.M.3
  • 4
    • 0019050328 scopus 로고
    • Calcium control of waveform in isolated flagellar axonemes of Chlamydomonas
    • Bessen M., Fay R.B., Witman G.B. Calcium control of waveform in isolated flagellar axonemes of Chlamydomonas. J. Cell Biol. 86:1980;446-455.
    • (1980) J. Cell Biol. , vol.86 , pp. 446-455
    • Bessen, M.1    Fay, R.B.2    Witman, G.B.3
  • 5
    • 0032559690 scopus 로고    scopus 로고
    • Leading the procession: New insights into kinesin motors
    • Block S.M. Leading the procession: new insights into kinesin motors. J. Cell Biol. 140:1998;1281-1284.
    • (1998) J. Cell Biol. , vol.140 , pp. 1281-1284
    • Block, S.M.1
  • 6
    • 0033549485 scopus 로고    scopus 로고
    • Drosophila roadblock and Chlamydomonas LC7: A conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis
    • Bowman A.B., Patel-King R.S., Benashski S.E., McCaffery J.M., Goldstein L.S., King S.M. Drosophila roadblock and Chlamydomonas LC7: a conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis. J. Cell Biol. 146:1999;165-180.
    • (1999) J. Cell Biol. , vol.146 , pp. 165-180
    • Bowman, A.B.1    Patel-King, R.S.2    Benashski, S.E.3    McCaffery, J.M.4    Goldstein, L.S.5    King, S.M.6
  • 7
    • 0023083510 scopus 로고
    • Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function
    • Brokaw C.J., Kamiya R. Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function. Cell Motil. Cytoskeleton. 8:1987;68-75.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 68-75
    • Brokaw, C.J.1    Kamiya, R.2
  • 9
    • 0141632803 scopus 로고    scopus 로고
    • DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC
    • Casey D., Inaba K., Pazour G., Takada S., Wakabayashi K., Wilkerson C., Kamiya R., Witman G. DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC. Mol. Biol. Cell. 14:2003;3650-3663.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3650-3663
    • Casey, D.1    Inaba, K.2    Pazour, G.3    Takada, S.4    Wakabayashi, K.5    Wilkerson, C.6    Kamiya, R.7    Witman, G.8
  • 10
    • 0142211197 scopus 로고    scopus 로고
    • DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redox-sensitive calcium-binding protein
    • in press
    • Casey, D., Yagi, T., Kamiya, R., Witman, G., 2003b. DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redox-sensitive calcium-binding protein. J. Biol. Chem., in press
    • (2003) J. Biol. Chem.
    • Casey, D.1    Yagi, T.2    Kamiya, R.3    Witman, G.4
  • 11
    • 0031750484 scopus 로고    scopus 로고
    • Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons
    • Cole D.G., Diener D.R., Himelblau A.L., Beech P.L., Fuster J.C., Rosenbaum J.L. Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons. J. Cell Biol. 141:1998;993-1008.
    • (1998) J. Cell Biol. , vol.141 , pp. 993-1008
    • Cole, D.G.1    Diener, D.R.2    Himelblau, A.L.3    Beech, P.L.4    Fuster, J.C.5    Rosenbaum, J.L.6
  • 12
    • 0034833751 scopus 로고    scopus 로고
    • Dynein motors of the Chlamydomonas flagellum
    • DiBella L.M., King S.M. Dynein motors of the Chlamydomonas flagellum. Int. Rev. Cytol. 210:2001;227-268.
    • (2001) Int. Rev. Cytol. , vol.210 , pp. 227-268
    • Dibella, L.M.1    King, S.M.2
  • 13
    • 0029127761 scopus 로고
    • Functional dissection of the dynein motor domain
    • Eshel D. Functional dissection of the dynein motor domain. Cell Motil. Cytoskeleton. 32:1995;133-135.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 133-135
    • Eshel, D.1
  • 14
    • 0035853275 scopus 로고    scopus 로고
    • Antibodies to cytoplasmic dynein heavy chain map the surface and inhibit motility
    • Fan J., Amos L.A. Antibodies to cytoplasmic dynein heavy chain map the surface and inhibit motility. J. Mol. Biol. 307:2001;1317-1327.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1317-1327
    • Fan, J.1    Amos, L.A.2
  • 15
    • 0035897417 scopus 로고    scopus 로고
    • Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP)
    • Gaillard A., Diener D., Rosenbaum J., Sale W. Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP). J. Cell Biol. 153:2001;443-448.
    • (2001) J. Cell Biol. , vol.153 , pp. 443-448
    • Gaillard, A.1    Diener, D.2    Rosenbaum, J.3    Sale, W.4
  • 16
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee M.A., Heuser J.E., Vallee R.B. An extended microtubule-binding structure within the dynein motor domain. Nature. 390:1997;636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 17
    • 0023871621 scopus 로고
    • Tracking kinesin-driven movements with nanometre-scale precision
    • Gelles J., Schnapp B.J., Sheetz M.P. Tracking kinesin-driven movements with nanometre-scale precision. Nature. 331:1988;450-453.
    • (1988) Nature , vol.331 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3
  • 18
    • 0018785964 scopus 로고
    • A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella
    • Gibbons I.R., Fronk E. A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella. J. Biol. Chem. 254:1979;187-196.
    • (1979) J. Biol. Chem. , vol.254 , pp. 187-196
    • Gibbons, I.R.1    Fronk, E.2
  • 19
    • 0028334031 scopus 로고
    • Characterization of DLC-A and DLC-B, two families of cytoplasmic dynein light chain subunits
    • Gill S.R., Cleveland D.W., Schroer T.A. Characterization of DLC-A and DLC-B, two families of cytoplasmic dynein light chain subunits. Mol. Biol. Cell. 5:1994;645-654.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 645-654
    • Gill, S.R.1    Cleveland, D.W.2    Schroer, T.A.3
  • 20
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill S.R., Schroer T.A., Szilak I., Steuer E.R., Sheetz M.P., Cleveland D.W. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115:1991;1639-1650.
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 21
    • 0021630304 scopus 로고
    • Structural comparison of purified dynein proteins with in situ dynein arms
    • Goodenough U., Heuser J. Structural comparison of purified dynein proteins with in situ dynein arms. J. Mol. Biol. 180:1984;1083-1118.
    • (1984) J. Mol. Biol. , vol.180 , pp. 1083-1118
    • Goodenough, U.1    Heuser, J.2
  • 22
    • 0037241834 scopus 로고    scopus 로고
    • Cloning, localization, and axonemal function of Tetrahymena centrin
    • Guerra C., Wada Y., Leick V., Bell A., Satir P. Cloning, localization, and axonemal function of Tetrahymena centrin. Mol. Biol. Cell. 14:2003;251-261.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 251-261
    • Guerra, C.1    Wada, Y.2    Leick, V.3    Bell, A.4    Satir, P.5
  • 23
    • 0031022258 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by phosphorylation of a 138-kDa inner arm dynein intermediate chain
    • Habermacher G., Sale W.S. Regulation of flagellar dynein by phosphorylation of a 138-kDa inner arm dynein intermediate chain. J. Cell Biol. 136:1997;167-176.
    • (1997) J. Cell Biol. , vol.136 , pp. 167-176
    • Habermacher, G.1    Sale, W.S.2
  • 24
    • 0037734370 scopus 로고    scopus 로고
    • Mutations in dynein link motor neuron degeneration to defects in retrograde transport
    • Hafezparast M.et al. Mutations in dynein link motor neuron degeneration to defects in retrograde transport. Science. 300:2003;808-812.
    • (2003) Science , vol.300 , pp. 808-812
    • Hafezparast, M.1
  • 25
    • 0025881253 scopus 로고
    • CAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium
    • Hamasaki T., Barkalow K., Richmond J., Satir P. cAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium. Proc. Natl. Acad. Sci. USA. 88:1991;7918-7922.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7918-7922
    • Hamasaki, T.1    Barkalow, K.2    Richmond, J.3    Satir, P.4
  • 26
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada A., Takei Y., Kanai Y., Tanaka Y., Nonaka S., Hirokawa N. Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 141:1998;51-59.
    • (1998) J. Cell Biol. , vol.141 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 27
    • 0032498901 scopus 로고    scopus 로고
    • Identification of the t complex-encoded cytoplasmic dynein light chain tctex1 in inner arm I1 supports the involvement of flagellar dyneins in meiotic drive
    • Harrison A., Olds-Clarke P., King S.M. Identification of the. t complex-encoded cytoplasmic dynein light chain tctex1 in inner arm I1 supports the involvement of flagellar dyneins in meiotic drive J. Cell Biol. 140:1998;1137-1147.
    • (1998) J. Cell Biol. , vol.140 , pp. 1137-1147
    • Harrison, A.1    Olds-Clarke, P.2    King, S.M.3
  • 29
    • 0023460829 scopus 로고
    • Stimulation of in vitro motility of Chlamydomonas axonemes by inhibition of cAMP-dependent phosphorylation
    • Hasegawa E., Hayashi H., Asakura S., Kamiya R. Stimulation of in vitro motility of Chlamydomonas axonemes by inhibition of cAMP-dependent phosphorylation. Cell Motil. 8:1987;302-311.
    • (1987) Cell Motil. , vol.8 , pp. 302-311
    • Hasegawa, E.1    Hayashi, H.2    Asakura, S.3    Kamiya, R.4
  • 32
    • 0038194599 scopus 로고    scopus 로고
    • A dynein light intermediate chain is required for retrograde intraflagellar transport (IFT)
    • Hou Y., Cole D., Dentler W., Pazour G., Witman G. A dynein light intermediate chain is required for retrograde intraflagellar transport (IFT). Mol. Biol. Cell. 13:2002;41.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 41
    • Hou, Y.1    Cole, D.2    Dentler, W.3    Pazour, G.4    Witman, G.5
  • 33
    • 0023778375 scopus 로고
    • 2+-binding protein: Homology in its protein sequence with calmodulin and the yeast CDC31 gene product
    • 2+-binding protein: homology in its protein sequence with calmodulin and the yeast CDC31 gene product. J. Cell Biol. 107:1988;133-140.
    • (1988) J. Cell Biol. , vol.107 , pp. 133-140
    • Huang, B.1    Mengersen, A.2    Lee, V.D.3
  • 34
    • 0020082250 scopus 로고
    • Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function
    • Huang B., Ramanis Z., Luck D.J. Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function. Cell. 28:1982;115-124.
    • (1982) Cell , vol.28 , pp. 115-124
    • Huang, B.1    Ramanis, Z.2    Luck, D.J.3
  • 35
    • 0028893038 scopus 로고
    • Molecular analysis of a cytoplasmic dynein light intermediate chain reveals homology to a family of ATPases
    • Hughes S.M., Vaughan K.T., Herskovits J.S., Vallee R.B. Molecular analysis of a cytoplasmic dynein light intermediate chain reveals homology to a family of ATPases. J. Cell Sci. 108:1995;17-24.
    • (1995) J. Cell Sci. , vol.108 , pp. 17-24
    • Hughes, S.M.1    Vaughan, K.T.2    Herskovits, J.S.3    Vallee, R.B.4
  • 36
    • 0036033423 scopus 로고    scopus 로고
    • Dephosphorylation of Tctex2-related dynein light chain by type 2A protein phosphatase
    • Inaba K. Dephosphorylation of Tctex2-related dynein light chain by type 2A protein phosphatase. Biochem. Biophys. Res. Commun. 297:2002;800-805.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 800-805
    • Inaba, K.1
  • 37
    • 0033525743 scopus 로고    scopus 로고
    • Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility
    • Inaba K., Kagami O., Ogawa K. Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility. Biochem. Biophys. Res. Commun. 256:1999;177-183.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 177-183
    • Inaba, K.1    Kagami, O.2    Ogawa, K.3
  • 38
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • Kagami O., Kamiya R. Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein. J. Cell Sci. 103:1992;653-664.
    • (1992) J. Cell Sci. , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 39
    • 0025336878 scopus 로고
    • Microtubule translocation caused by three subspecies of inner-arm dynein from Chlamydomonas flagella
    • Kagami O., Takada S., Kamiya R. Microtubule translocation caused by three subspecies of inner-arm dynein from Chlamydomonas flagella. FEBS Lett. 264:1990;179-182.
    • (1990) FEBS Lett. , vol.264 , pp. 179-182
    • Kagami, O.1    Takada, S.2    Kamiya, R.3
  • 40
    • 0028365452 scopus 로고
    • Purification of vicinal dithiol-containing proteins by arsenical-based affinity chromatography
    • Kalef E., Gitler C. Purification of vicinal dithiol-containing proteins by arsenical-based affinity chromatography. Methods Enzymol. 233:1994;395-403.
    • (1994) Methods Enzymol. , vol.233 , pp. 395-403
    • Kalef, E.1    Gitler, C.2
  • 41
    • 0035995284 scopus 로고    scopus 로고
    • Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants
    • Kamiya R. Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants. Int. Rev. Cytol. 219:2002;115-155.
    • (2002) Int. Rev. Cytol. , vol.219 , pp. 115-155
    • Kamiya, R.1
  • 42
    • 0021890914 scopus 로고
    • A mutant of Chlamydomonas reinhardtii that lacks the flagellar outer dynein arm but can swim
    • Kamiya R., Okamoto M. A mutant of Chlamydomonas reinhardtii that lacks the flagellar outer dynein arm but can swim. J. Cell Sci. 74:1985;181-191.
    • (1985) J. Cell Sci. , vol.74 , pp. 181-191
    • Kamiya, R.1    Okamoto, M.2
  • 43
    • 0021335092 scopus 로고
    • Submicromolar levels of calcium control the balance of beating between the two flagella in demembranated models of Chlamydomonas
    • Kamiya R., Witman G.B. Submicromolar levels of calcium control the balance of beating between the two flagella in demembranated models of Chlamydomonas. J. Cell Biol. 98:1984;97-107.
    • (1984) J. Cell Biol. , vol.98 , pp. 97-107
    • Kamiya, R.1    Witman, G.B.2
  • 44
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki S., Holzbaur E.L. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol. Chem. 270:1995;28806-28811.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.2
  • 45
    • 0030983282 scopus 로고    scopus 로고
    • Chlamydomonas inner-arm dynein mutant, ida5, has a mutation in an actin-encoding gene
    • Kato-Minoura T., Hirono M., Kamiya R. Chlamydomonas inner-arm dynein mutant, ida5, has a mutation in an actin-encoding gene. J. Cell Biol. 137:1997;649-656.
    • (1997) J. Cell Biol. , vol.137 , pp. 649-656
    • Kato-Minoura, T.1    Hirono, M.2    Kamiya, R.3
  • 46
    • 0032500890 scopus 로고    scopus 로고
    • Highly divergent actin expressed in a Chlamydomonas mutant lacking the conventional actin gene
    • Kato-Minoura T., Uryu S., Hirono M., Kamiya R. Highly divergent actin expressed in a Chlamydomonas mutant lacking the conventional actin gene. Biochem. Biophys. Res. Commun. 251:1998;71-76.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 71-76
    • Kato-Minoura, T.1    Uryu, S.2    Hirono, M.3    Kamiya, R.4
  • 47
    • 0031012517 scopus 로고    scopus 로고
    • Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains
    • King S.J., Dutcher S.K. Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains. J. Cell Biol. 136:1997;177-191.
    • (1997) J. Cell Biol. , vol.136 , pp. 177-191
    • King, S.J.1    Dutcher, S.K.2
  • 48
    • 0033895197 scopus 로고    scopus 로고
    • AAA domains and organization of the dynein motor unit
    • King S.M. AAA domains and organization of the dynein motor unit. J. Cell Sci. 113:2000;2521-2526.
    • (2000) J. Cell Sci. , vol.113 , pp. 2521-2526
    • King, S.M.1
  • 49
    • 0003332338 scopus 로고    scopus 로고
    • Dynein Motors: Structure, mechanochemistry and regulation
    • M. Schliwa. Weinheim: Wiley-VCH Verlag GmbH
    • King S.M. Dynein Motors: structure, mechanochemistry and regulation. Schliwa M. Molecular Motors. 2002;45-78 Wiley-VCH Verlag GmbH, Weinheim.
    • (2002) Molecular Motors , pp. 45-78
    • King, S.M.1
  • 53
    • 0024970673 scopus 로고
    • Structure of the α and β heavy chains of the outer arm dynein from Chlamydomonas flagella. Nucleotide binding sites
    • King S.M., Haley B.E., Witman G.B. Structure of the α and β heavy chains of the outer arm dynein from Chlamydomonas flagella. Nucleotide binding sites. J. Biol. Chem. 264:1989;10210-10218.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10210-10218
    • King, S.M.1    Haley, B.E.2    Witman, G.B.3
  • 54
    • 0029416922 scopus 로고
    • 2+-binding light chain within Chlamydomonas outer arm dynein
    • 2+-binding light chain within Chlamydomonas outer arm dynein. J. Cell Sci. 108:1995;3757-3764.
    • (1995) J. Cell Sci. , vol.108 , pp. 3757-3764
    • King, S.M.1    Patel-King, R.S.2
  • 55
    • 0028990156 scopus 로고
    • (r)=8000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues
    • (r)=8000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues J. Biol. Chem. 270:1995;11445-11452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11445-11452
    • King, S.M.1    Patel-King, R.S.2
  • 56
    • 0025923808 scopus 로고
    • r 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with α-tubulin in situ
    • r 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with α-tubulin in situ J. Biol. Chem. 266:1991;8401-8407.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8401-8407
    • King, S.M.1    Wilkerson, C.G.2    Witman, G.B.3
  • 57
    • 0023665395 scopus 로고
    • Structure of the α and β heavy chains of the outer arm dynein from Chlamydomonas flagella. Masses of chains and sites of ultraviolet-induced vanadate-dependent cleavage
    • King S.M., Witman G.B. Structure of the α and β heavy chains of the outer arm dynein from Chlamydomonas flagella. Masses of chains and sites of ultraviolet-induced vanadate-dependent cleavage. J. Biol. Chem. 262:1987;17596-17604.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17596-17604
    • King, S.M.1    Witman, G.B.2
  • 58
    • 0028095507 scopus 로고
    • Multiple sites of phosphorylation within the α heavy chain of Chlamydomonas outer arm dynein
    • King S.M., Witman G.B. Multiple sites of phosphorylation within the α heavy chain of Chlamydomonas outer arm dynein. J. Biol. Chem. 269:1994;5452-5457.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5452-5457
    • King, S.M.1    Witman, G.B.2
  • 59
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11:2001;725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 61
    • 0028277915 scopus 로고
    • Error-prone replication of repeated DNA sequences by T7 DNA polymerase in the absence of its processivity subunit
    • Kunkel T.A., Patel S.M., Johnson K.A. Error-prone replication of repeated DNA sequences by T7 DNA polymerase in the absence of its processivity subunit. Proc. Natl. Acad. Sci. USA. 91:1994;6830-6834.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6830-6834
    • Kunkel, T.A.1    Patel, S.M.2    Johnson, K.A.3
  • 62
    • 0029047003 scopus 로고
    • Ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms
    • LeDizet M., Piperno G. ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms. Mol. Biol. Cell. 6:1995;713-723.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 713-723
    • Ledizet, M.1    Piperno, G.2
  • 63
    • 0029020706 scopus 로고
    • The light chain p28 associates with a subset of inner dynein arm heavy chains in Chlamydomonas axonemes
    • LeDizet M., Piperno G. The light chain p28 associates with a subset of inner dynein arm heavy chains in Chlamydomonas axonemes. Mol. Biol. Cell. 6:1995;697-711.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 697-711
    • Ledizet, M.1    Piperno, G.2
  • 64
    • 0022981653 scopus 로고
    • Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate
    • Lee-Eiford A., Ow R.A., Gibbons I.R. Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate. J. Biol. Chem. 261:1986;2337-2342.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2337-2342
    • Lee-Eiford, A.1    Ow, R.A.2    Gibbons, I.R.3
  • 65
    • 0033849936 scopus 로고    scopus 로고
    • Chlamydomonas flagella
    • Mitchell D.R. Chlamydomonas flagella. J. Phycol. 36:2000;261-273.
    • (2000) J. Phycol. , vol.36 , pp. 261-273
    • Mitchell, D.R.1
  • 66
    • 0025770089 scopus 로고
    • Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene
    • Mitchell D.R., Kang Y. Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene. J. Cell Biol. 113:1991;835-842.
    • (1991) J. Cell Biol. , vol.113 , pp. 835-842
    • Mitchell, D.R.1    Kang, Y.2
  • 67
    • 0027170722 scopus 로고
    • Reversion analysis of dynein intermediate chain function
    • Mitchell D.R., Kang Y. Reversion analysis of dynein intermediate chain function. J. Cell Sci. 105:1993;1069-1078.
    • (1993) J. Cell Sci. , vol.105 , pp. 1069-1078
    • Mitchell, D.R.1    Kang, Y.2
  • 68
    • 85012344312 scopus 로고
    • A motile Chlamydomonas flagellar mutant that lacks outer dynein arms
    • Mitchell D.R., Rosenbaum J.L. A motile Chlamydomonas flagellar mutant that lacks outer dynein arms. J. Cell Biol. 100:1985;1228-1234.
    • (1985) J. Cell Biol. , vol.100 , pp. 1228-1234
    • Mitchell, D.R.1    Rosenbaum, J.L.2
  • 69
    • 0029896120 scopus 로고    scopus 로고
    • Phase partition analysis of nucleotide binding to axonemal dynein
    • Mocz G., Gibbons I.R. Phase partition analysis of nucleotide binding to axonemal dynein. Biochemistry. 35:1996;9204-9211.
    • (1996) Biochemistry , vol.35 , pp. 9204-9211
    • Mocz, G.1    Gibbons, I.R.2
  • 70
    • 0035089503 scopus 로고    scopus 로고
    • Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases
    • Mocz G., Gibbons I.R. Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure. 9:2001;93-103.
    • (2001) Structure , vol.9 , pp. 93-103
    • Mocz, G.1    Gibbons, I.R.2
  • 72
    • 0142189946 scopus 로고    scopus 로고
    • Rapid analysis of Chlamydomonas reinhardtii flagellar beat activity with a LSCM
    • Moss A.G., Morgan D.D. Rapid analysis of Chlamydomonas reinhardtii flagellar beat activity with a LSCM. Microsc. Anal. 34:1999;7-9.
    • (1999) Microsc. Anal. , vol.34 , pp. 7-9
    • Moss, A.G.1    Morgan, D.D.2
  • 73
    • 0032544411 scopus 로고    scopus 로고
    • Identification of a dynein molecular motor component in Torpedo electroplax; Binding and phosphorylation of Tctex-1 by Fyn
    • Mou T., Kraas J.R., Fung E.T., Swope S.L. Identification of a dynein molecular motor component in Torpedo electroplax; binding and phosphorylation of Tctex-1 by Fyn. FEBS Lett. 435:1998;275-281.
    • (1998) FEBS Lett. , vol.435 , pp. 275-281
    • Mou, T.1    Kraas, J.R.2    Fung, E.T.3    Swope, S.L.4
  • 74
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:1999;27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 75
    • 0029954709 scopus 로고    scopus 로고
    • Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport
    • Niclas J., Allan V.J., Vale R.D. Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J. Cell Biol. 133:1996;585-593.
    • (1996) J. Cell Biol. , vol.133 , pp. 585-593
    • Niclas, J.1    Allan, V.J.2    Vale, R.D.3
  • 76
    • 1642282850 scopus 로고    scopus 로고
    • The Roadblock light chains of cytoplasmic dynein associate with Hepatitis B X-interacting protein
    • Nikulina K., King S. The Roadblock light chains of cytoplasmic dynein associate with Hepatitis B X-interacting protein. Mol. Biol. Cell. 13:2002;182a.
    • (2002) Mol. Biol. Cell , vol.13
    • Nikulina, K.1    King, S.2
  • 77
    • 0032428685 scopus 로고    scopus 로고
    • Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein
    • Nonaka S., Tanaka Y., Okada Y., Takeda S., Harada A., Kanai Y., Kido M., Hirokawa N. Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein. Cell. 95:1998;829-837.
    • (1998) Cell , vol.95 , pp. 829-837
    • Nonaka, S.1    Tanaka, Y.2    Okada, Y.3    Takeda, S.4    Harada, A.5    Kanai, Y.6    Kido, M.7    Hirokawa, N.8
  • 78
    • 0016608292 scopus 로고
    • Effect of external factors on Chlamydomonas reinhardtii I
    • Nultsch W., Throm G. Effect of external factors on Chlamydomonas reinhardtii I. Light. Arch. Microbiol. 103:1975;175-179.
    • (1975) Light. Arch. Microbiol. , vol.103 , pp. 175-179
    • Nultsch, W.1    Throm, G.2
  • 79
    • 0015518047 scopus 로고
    • Studies on the flagellar ATPase from sea urchin spermatozoa. I. Purification and some properties of the enzyme
    • Ogawa K., Mohri H. Studies on the flagellar ATPase from sea urchin spermatozoa. I. Purification and some properties of the enzyme. Biochim. Biophys. Acta. 256:1972;142-155.
    • (1972) Biochim. Biophys. Acta , vol.256 , pp. 142-155
    • Ogawa, K.1    Mohri, H.2
  • 83
  • 84
    • 0026706148 scopus 로고
    • Homology of the 74-kDa cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function
    • Paschal B.M., Mikami A., Pfister K.K., Vallee R.B. Homology of the 74-kDa cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function. J. Cell Biol. 118:1992;1133-1143.
    • (1992) J. Cell Biol. , vol.118 , pp. 1133-1143
    • Paschal, B.M.1    Mikami, A.2    Pfister, K.K.3    Vallee, R.B.4
  • 85
    • 0023205148 scopus 로고
    • Retrograde transport by the microtubule-associated protein MAP 1C
    • Paschal B.M., Vallee R.B. Retrograde transport by the microtubule-associated protein MAP 1C. Nature. 330:1987;181-183.
    • (1987) Nature , vol.330 , pp. 181-183
    • Paschal, B.M.1    Vallee, R.B.2
  • 86
    • 0029664996 scopus 로고    scopus 로고
    • Two functional thioredoxins containing redox-senesitive vicinal dithiols from the Chlamydomonas outer dynein arm
    • Patel-King R.S., Benashki S.E., Harrison A., King S.M. Two functional thioredoxins containing redox-senesitive vicinal dithiols from the Chlamydomonas outer dynein arm. J. Biol. Chem. 271:1996;6283-6291.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6283-6291
    • Patel-King, R.S.1    Benashki, S.E.2    Harrison, A.3    King, S.M.4
  • 87
    • 0030900133 scopus 로고    scopus 로고
    • A Chlamydomonas homologue of the putative murine t complex distorter Tctex-2 is an outer arm dynein light chain
    • Patel-King R.S., Benashski S.E., Harrison A., King S.M. A Chlamydomonas homologue of the putative murine. t complex distorter Tctex-2 is an outer arm dynein light chain J. Cell Biol. 137:1997;1081-1090.
    • (1997) J. Cell Biol. , vol.137 , pp. 1081-1090
    • Patel-King, R.S.1    Benashski, S.E.2    Harrison, A.3    King, S.M.4
  • 89
    • 0034735526 scopus 로고    scopus 로고
    • Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella
    • Pazour G.J., Dickert B.L., Vucica Y., Seeley E.S., Rosenbaum J.L., Witman G.B., Cole D.G. Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella. J. Cell Biol. 151:2000;709-718.
    • (2000) J. Cell Biol. , vol.151 , pp. 709-718
    • Pazour, G.J.1    Dickert, B.L.2    Vucica, Y.3    Seeley, E.S.4    Rosenbaum, J.L.5    Witman, G.B.6    Cole, D.G.7
  • 90
    • 0033535044 scopus 로고    scopus 로고
    • The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar assembly
    • Pazour G.J., Dickert B.L., Witman G.B. The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar assembly. J. Cell Biol. 144:1999;473-481.
    • (1999) J. Cell Biol. , vol.144 , pp. 473-481
    • Pazour, G.J.1    Dickert, B.L.2    Witman, G.B.3
  • 92
    • 0037019017 scopus 로고    scopus 로고
    • Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease
    • Pazour G.J., San Agustin J.T., Follit J.A., Rosenbaum J.L., Witman G.B. Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr. Biol. 11:2002;R1-R3.
    • (2002) Curr. Biol. , vol.11 , pp. 1-R3
    • Pazour, G.J.1    San Agustin, J.T.2    Follit, J.A.3    Rosenbaum, J.L.4    Witman, G.B.5
  • 93
    • 0031777851 scopus 로고    scopus 로고
    • A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT)
    • Pazour G.J., Wilkerson C.G., Witman G.B. A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT). J. Cell Biol. 141:1998;979-992.
    • (1998) J. Cell Biol. , vol.141 , pp. 979-992
    • Pazour, G.J.1    Wilkerson, C.G.2    Witman, G.B.3
  • 94
    • 0038522846 scopus 로고    scopus 로고
    • A novel dynein light intermediate chain colocalizes with the retrograde motor for intraflagellar transport at sites of axoneme assembly in Chlamydomonas and mammalian cells
    • Perrone C., Tritschler D., Taulman P., Bower R., Yoder B., Porter M. A novel dynein light intermediate chain colocalizes with the retrograde motor for intraflagellar transport at sites of axoneme assembly in Chlamydomonas and mammalian cells. Mol. Biol. Cell. 14:2003;2041-2056.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2041-2056
    • Perrone, C.1    Tritschler, D.2    Taulman, P.3    Bower, R.4    Yoder, B.5    Porter, M.6
  • 96
    • 0020309907 scopus 로고
    • Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella
    • Pfister K.K., Fay R.B., Witman G.B. Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella. Cell Motil. 2:1982;525-547.
    • (1982) Cell Motil. , vol.2 , pp. 525-547
    • Pfister, K.K.1    Fay, R.B.2    Witman, G.B.3
  • 97
    • 0021759692 scopus 로고
    • Subfractionation of Chlamydomonas 18 S dynein into two unique subunits containing ATPase activity
    • Pfister K.K., Witman G.B. Subfractionation of Chlamydomonas 18 S dynein into two unique subunits containing ATPase activity. J. Biol. Chem. 259:1984;12072-12080.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12072-12080
    • Pfister, K.K.1    Witman, G.B.2
  • 98
    • 0019780422 scopus 로고
    • Inner arm dyneins from flagella of Chlamydomonas reinhardtii
    • Piperno G., Luck D.J. Inner arm dyneins from flagella of Chlamydomonas reinhardtii. Cell. 27:1981;331-340.
    • (1981) Cell , vol.27 , pp. 331-340
    • Piperno, G.1    Luck, D.J.2
  • 99
    • 0028176103 scopus 로고
    • Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes
    • Piperno G., Mead K., LeDizet M., Moscatelli A. Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes. J. Cell Biol. 125:1994;1109-1117.
    • (1994) J. Cell Biol. , vol.125 , pp. 1109-1117
    • Piperno, G.1    Mead, K.2    Ledizet, M.3    Moscatelli, A.4
  • 100
    • 0026673055 scopus 로고
    • The inner dynein arms I2 interact with a "dynein regulatory complex" in Chlamydomonas flagella
    • Piperno G., Mead K., Shestak W. The inner dynein arms I2 interact with a "dynein regulatory complex" in Chlamydomonas flagella. J. Cell Biol. 118:1992;1455-1463.
    • (1992) J. Cell Biol. , vol.118 , pp. 1455-1463
    • Piperno, G.1    Mead, K.2    Shestak, W.3
  • 101
    • 0034782383 scopus 로고    scopus 로고
    • Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: Dissociation of dynein-binding properties and transcriptional functionality of P
    • Poisson N., Real E., Gaudin Y., Vaney M.C., King S., Jacob Y., Tordo N., Blondel D. Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P. J. Gen. Virol. 82:2001;2691-2696.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2691-2696
    • Poisson, N.1    Real, E.2    Gaudin, Y.3    Vaney, M.C.4    King, S.5    Jacob, Y.6    Tordo, N.7    Blondel, D.8
  • 102
    • 0032949365 scopus 로고    scopus 로고
    • Cytoplasmic dynein heavy chain 1b is required for flagellar assembly in Chlamydomonas
    • Porter M.E., Bower R., Knott J.A., Byrd P., Dentler W. Cytoplasmic dynein heavy chain 1b is required for flagellar assembly in Chlamydomonas. Mol. Biol. Cell. 10:1999;693-712.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 693-712
    • Porter, M.E.1    Bower, R.2    Knott, J.A.3    Byrd, P.4    Dentler, W.5
  • 103
    • 0028040415 scopus 로고
    • Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the β-dynein heavy chain
    • Porter M.E., Knott J.A., Gardner L.C., Mitchell D.R., Dutcher S.K. Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the β-dynein heavy chain. J. Cell Biol. 126:1994;1495-1507.
    • (1994) J. Cell Biol. , vol.126 , pp. 1495-1507
    • Porter, M.E.1    Knott, J.A.2    Gardner, L.C.3    Mitchell, D.R.4    Dutcher, S.K.5
  • 104
    • 0026674076 scopus 로고
    • Extragenic suppressors of paralyzed flagellar mutations in Chlamydomonas reinhardtii identify loci that alter the inner dynein arms
    • Porter M.E., Power J., Dutcher S.K. Extragenic suppressors of paralyzed flagellar mutations in Chlamydomonas reinhardtii identify loci that alter the inner dynein arms. J. Cell Biol. 118:1992;1163-1176.
    • (1992) J. Cell Biol. , vol.118 , pp. 1163-1176
    • Porter, M.E.1    Power, J.2    Dutcher, S.K.3
  • 105
    • 0034722338 scopus 로고    scopus 로고
    • The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility
    • Porter M.E., Sale W.S. The 9. + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility J. Cell Biol. 151:2000;F37-F42.
    • (2000) J. Cell Biol. , vol.151 , pp. 37-F42
    • Porter, M.E.1    Sale, W.S.2
  • 106
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell. 3:1999;287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 107
  • 109
    • 0030463112 scopus 로고    scopus 로고
    • The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arms by modification of the γ-dynein heavy chain
    • Rupp G., O'Toole E., Gardner L.C., Mitchell B.F., Porter M.E. The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arms by modification of the γ-dynein heavy chain. J. Cell Biol. 135:1996;1853-1865.
    • (1996) J. Cell Biol. , vol.135 , pp. 1853-1865
    • Rupp, G.1    O'Toole, E.2    Gardner, L.C.3    Mitchell, B.F.4    Porter, M.E.5
  • 110
    • 0035206849 scopus 로고    scopus 로고
    • Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains is expressed in human testis germ cells
    • Sadek C.M., Damdimopoulos A.E., Pelto-Huikko M., Gustafsson J.A., Spyrou G., Miranda-Vizuete A. Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains is expressed in human testis germ cells. Genes Cells. 6:2001;1077-1090.
    • (2001) Genes Cells , vol.6 , pp. 1077-1090
    • Sadek, C.M.1    Damdimopoulos, A.E.2    Pelto-Huikko, M.3    Gustafsson, J.A.4    Spyrou, G.5    Miranda-Vizuete, A.6
  • 111
    • 0033527027 scopus 로고    scopus 로고
    • Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
    • Sakakibara H., Kojima H., Sakai Y., Katayama E., Oiwa K. Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor. Nature. 400:1999;586-590.
    • (1999) Nature , vol.400 , pp. 586-590
    • Sakakibara, H.1    Kojima, H.2    Sakai, Y.3    Katayama, E.4    Oiwa, K.5
  • 112
    • 0242384843 scopus 로고    scopus 로고
    • Calcium regulates ATP-sensitive microtubule binding by Chlamydomonas outer arm dynein
    • in press
    • Sakato, M., King, S., 2003. Calcium regulates ATP-sensitive microtubule binding by Chlamydomonas outer arm dynein. J. Biol. Chem., in press
    • (2003) J. Biol. Chem.
    • Sakato, M.1    King, S.2
  • 113
    • 0024110708 scopus 로고
    • Isolated β-heavy chain subunit of dynein translocates microtubules in vitro
    • Sale W.S., Fox L.A. Isolated β-heavy chain subunit of dynein translocates microtubules in vitro. J. Cell Biol. 107:1988;1793-1797.
    • (1988) J. Cell Biol. , vol.107 , pp. 1793-1797
    • Sale, W.S.1    Fox, L.A.2
  • 114
    • 0028928790 scopus 로고
    • Centrin, centrosomes, and meiotic spindle bodies
    • Salisbury J. Centrin, centrosomes, and meiotic spindle bodies. Curr. Opin. Cell Biol. 7:1995;39-45.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 39-45
    • Salisbury, J.1
  • 115
    • 0021132972 scopus 로고
    • Striated flagellar roots: Isolation and partial characterization of a calcium-modulated contractile organelle
    • Salisbury J., Baron A., Surek B., Melkonian M. Striated flagellar roots: isolation and partial characterization of a calcium-modulated contractile organelle. J. Cell Biol. 99:1984;962-970.
    • (1984) J. Cell Biol. , vol.99 , pp. 962-970
    • Salisbury, J.1    Baron, A.2    Surek, B.3    Melkonian, M.4
  • 117
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer D.A., Gill S.R., Cooper J.A., Heuser J.E., Schroer T.A. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol. 126:1994;403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 118
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer F., Bohmann K., Nusslein-Volhard C. The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nat. Cell Biol. 2:2000;185-190.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 119
    • 0016144752 scopus 로고
    • Effects of N-ethylmaleimide on dynein adenosinetriphosphatase activity and its recombining ability with outer fibers
    • Shimizu T., Kimura I. Effects of N-ethylmaleimide on dynein adenosinetriphosphatase activity and its recombining ability with outer fibers. J. Biochem. (Tokyo). 76:1974;1001-1008.
    • (1974) J. Biochem. (Tokyo) , vol.76 , pp. 1001-1008
    • Shimizu, T.1    Kimura, I.2
  • 120
    • 0037694982 scopus 로고    scopus 로고
    • The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding
    • Silvanovich A., Li M.-g., Serr M., Mische S., Hays T. The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding. Mol. Biol. Cell. 14:2003;1355-1365.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1355-1365
    • Silvanovich, A.1    Li, M.-G.2    Serr, M.3    Mische, S.4    Hays, T.5
  • 121
    • 0036732941 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase
    • Smith E.F. Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol. Biol. Cell. 13:2002;3303-3313.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3303-3313
    • Smith, E.F.1
  • 122
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming Herpes simplex virus 1 capsids to the nucleus
    • Sodeik B., Ebersold M.W., Helenius A. Microtubule-mediated transport of incoming Herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136:1997;1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 123
    • 0030656618 scopus 로고    scopus 로고
    • Mutation of an axonemal dynein affects left-right asymmetry in inversus viscerum mice
    • Supp D.M., Witte D.P., Potter S.S., Brueckner M. Mutation of an axonemal dynein affects left-right asymmetry in inversus viscerum mice. Nature. 389:1997;963-966.
    • (1997) Nature , vol.389 , pp. 963-966
    • Supp, D.M.1    Witte, D.P.2    Potter, S.S.3    Brueckner, M.4
  • 124
    • 0023665337 scopus 로고
    • Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates
    • Tabor S., Huber H.E., Richardson C.C. Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates. J. Biol. Chem. 262:1987;16212-16232.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16212-16232
    • Tabor, S.1    Huber, H.E.2    Richardson, C.C.3
  • 125
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai A.W., Chuang J.Z., Bode C., Wolfrum U., Sung C.H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell. 97:1999;877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 126
    • 0027071802 scopus 로고
    • Mutational analysis of centrin: An EF-hand protein associated with three distinct contractile fibers in the basal body apparatus of Chlamydomonas
    • Taillon B.E., Adler S.A., Suhan J.P., Jarvik J.W. Mutational analysis of centrin: an EF-hand protein associated with three distinct contractile fibers in the basal body apparatus of Chlamydomonas. J. Cell Biol. 119:1992;1613-1624.
    • (1992) J. Cell Biol. , vol.119 , pp. 1613-1624
    • Taillon, B.E.1    Adler, S.A.2    Suhan, J.P.3    Jarvik, J.W.4
  • 127
    • 0027953834 scopus 로고
    • Functional reconstitution of Chlamydomonas outer dynein arms from α, β and γ subunits: Requirement of a third factor
    • Takada S., Kamiya R. Functional reconstitution of Chlamydomonas outer dynein arms from α, β and γ subunits: requirement of a third factor. J. Cell Biol. 126:1994;737-745.
    • (1994) J. Cell Biol. , vol.126 , pp. 737-745
    • Takada, S.1    Kamiya, R.2
  • 128
    • 0034693225 scopus 로고    scopus 로고
    • Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin
    • Tynan S.H., Purohit A., Doxsey S.J., Vallee R.B. Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin. J. Biol. Chem. 275:2000;32763-32768.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32763-32768
    • Tynan, S.H.1    Purohit, A.2    Doxsey, S.J.3    Vallee, R.B.4
  • 129
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale R.D. AAA proteins. Lords of the ring. J. Cell Biol. 150:2000;F13-F19.
    • (2000) J. Cell Biol. , vol.150 , pp. 13-F19
    • Vale, R.D.1
  • 130
    • 0027070849 scopus 로고
    • Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins
    • Vale R.D., Malik F., Brown D. Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins. J. Cell Biol. 119:1992;1589-1596.
    • (1992) J. Cell Biol. , vol.119 , pp. 1589-1596
    • Vale, R.D.1    Malik, F.2    Brown, D.3
  • 131
    • 0024284804 scopus 로고
    • Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia
    • Vale R.D., Toyoshima Y.Y. Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia. Cell. 52:1988;459-469.
    • (1988) Cell , vol.52 , pp. 459-469
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 132
    • 0024687692 scopus 로고
    • Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia
    • Vale R.D., Toyoshima Y.Y. Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia. J. Cell Biol. 108:1989;2327-2334.
    • (1989) J. Cell Biol. , vol.108 , pp. 2327-2334
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 133
    • 1642271560 scopus 로고    scopus 로고
    • The role of dynein in disease
    • M. Schliwa. Weinheim: Wiley-VCH Verlag GmbH
    • Vallee R., Tai C.-Y. The role of dynein in disease. Schliwa M. Molecular Motors. 2002;497-509 Wiley-VCH Verlag GmbH, Weinheim.
    • (2002) Molecular Motors , pp. 497-509
    • Vallee, R.1    Tai, C.-Y.2
  • 134
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang Z., Khan S., Sheetz M.P. Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin. Biophys. J. 69:1995;2011-2023.
    • (1995) Biophys. J. , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 135
    • 0037422637 scopus 로고    scopus 로고
    • Asymmetry of the central apparatus defines the location of active microtubule sliding in Chlamydomonas flagella
    • Wargo M., Smith E. Asymmetry of the central apparatus defines the location of active microtubule sliding in Chlamydomonas flagella. Proc. Natl. Acad. Sci. USA. 100:2003;137-142.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 137-142
    • Wargo, M.1    Smith, E.2
  • 136
    • 0028303437 scopus 로고
    • High level expression in Escherichia coli and characterization of the EF-hand calcium-binding protein caltractin
    • Weber C., Lee V.D., Chazin W.J., Huang B. High level expression in Escherichia coli and characterization of the EF-hand calcium-binding protein caltractin. J. Biol. Chem. 269:1994;15795-15802.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15795-15802
    • Weber, C.1    Lee, V.D.2    Chazin, W.J.3    Huang, B.4
  • 138
    • 0031881230 scopus 로고    scopus 로고
    • Studies on the eel sperm flagellum. 2. The kinematics of normal motility
    • Woolley D.M. Studies on the eel sperm flagellum. 2. The kinematics of normal motility. Cell Motil. Cytoskeleton. 39:1998;233-245.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 233-245
    • Woolley, D.M.1
  • 139
    • 0347296376 scopus 로고    scopus 로고
    • Relaxation-based structure refinement and backbone molecular dynamics of the dynein motor domain-associated light chain
    • Wu H., Blackledge M., Maciejewski M.W., Mullen G.P., King S.M. Relaxation-based structure refinement and backbone molecular dynamics of the dynein motor domain-associated light chain. Biochemistry. 42:2003;57-71.
    • (2003) Biochemistry , vol.42 , pp. 57-71
    • Wu, H.1    Blackledge, M.2    MacIejewski, M.W.3    Mullen, G.P.4    King, S.M.5
  • 140
    • 0037381916 scopus 로고    scopus 로고
    • Backbone dynamics of dynein light chains
    • Wu H., King S. Backbone dynamics of dynein light chains. Cell Motil. Cytoskeleton. 54:2003;267-273.
    • (2003) Cell Motil. Cytoskeleton , vol.54 , pp. 267-273
    • Wu, H.1    King, S.2
  • 142
    • 0034533181 scopus 로고    scopus 로고
    • ADP-dependent microtubule translocation by flagellar inner-arm dyneins
    • Yagi T. ADP-dependent microtubule translocation by flagellar inner-arm dyneins. Cell Struct. Funct. 25:2000;263-267.
    • (2000) Cell Struct. Funct. , vol.25 , pp. 263-267
    • Yagi, T.1
  • 143
    • 0033841837 scopus 로고    scopus 로고
    • Vigourous beating of Chlamydomonas axonemes lacking central pair/radial spoke structures in the presence of salts and organic compounds
    • Yagi T., Kamiya R. Vigourous beating of Chlamydomonas axonemes lacking central pair/radial spoke structures in the presence of salts and organic compounds. Cell Motil. Cytoskeleton. 46:2000;190-199.
    • (2000) Cell Motil. Cytoskeleton , vol.46 , pp. 190-199
    • Yagi, T.1    Kamiya, R.2
  • 144
    • 0035955340 scopus 로고    scopus 로고
    • Association between actin and light chains in Chlamydomonas flagellar inner-arm dyneins
    • Yanagisawa H.A., Kamiya R. Association between actin and light chains in Chlamydomonas flagellar inner-arm dyneins. Biochem. Biophys. Res. Commun. 288:2001;443-447.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 443-447
    • Yanagisawa, H.A.1    Kamiya, R.2
  • 145
    • 0035844885 scopus 로고    scopus 로고
    • Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes
    • Yang P., Diener D.R., Rosenbaum J.L., Sale W.S. Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes. J. Cell Biol. 153:2001;1315-1326.
    • (2001) J. Cell Biol. , vol.153 , pp. 1315-1326
    • Yang, P.1    Diener, D.R.2    Rosenbaum, J.L.3    Sale, W.S.4
  • 146
    • 0033967129 scopus 로고    scopus 로고
    • Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme
    • Yang P., Fox L., Colbran R.J., Sale W.S. Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme. J. Cell Sci. 113:2000;91-102.
    • (2000) J. Cell Sci. , vol.113 , pp. 91-102
    • Yang, P.1    Fox, L.2    Colbran, R.J.3    Sale, W.S.4
  • 147
    • 0031593475 scopus 로고    scopus 로고
    • r 140,000 intermediate chain of Chlamydomonas flagellar inner arm dynein is a WD-repeat protein implicated in dynein arm anchoring
    • r 140,000 intermediate chain of Chlamydomonas flagellar inner arm dynein is a WD-repeat protein implicated in dynein arm anchoring Mol. Biol. Cell. 9:1998;3335-3349.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3335-3349
    • Yang, P.1    Sale, W.S.2
  • 148
    • 0034705378 scopus 로고    scopus 로고
    • Casein kinase I is anchored on axonemal doublet microtubules and regulates flagellar dynein phosphorylation and activity
    • Yang P., Sale W.S. Casein kinase I is anchored on axonemal doublet microtubules and regulates flagellar dynein phosphorylation and activity. J. Biol. Chem. 275:2000;18905-18912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18905-18912
    • Yang, P.1    Sale, W.S.2


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