메뉴 건너뛰기




Volumn 14, Issue 4, 2003, Pages 1355-1365

The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DYNEIN ADENOSINE TRIPHOSPHATASE; MOLECULAR MOTOR;

EID: 0037694982     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-10-0675     Document Type: Article
Times cited : (94)

References (69)
  • 1
    • 0032005265 scopus 로고    scopus 로고
    • Myosins: Matching functions with motors
    • Baker, J.P., and Titus, M.A. (1998). Myosins: matching functions with motors. Curr. Opin. Cell Biol. 10, 80-86.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 80-86
    • Baker, J.P.1    Titus, M.A.2
  • 2
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-ii regulation
    • Bresnick, A. (1999). Molecular mechanisms of nonmuscle myosin-ii regulation. Curr. Opin. Cell Biol. 11, 26-33.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 26-33
    • Bresnick, A.1
  • 3
    • 0036052865 scopus 로고    scopus 로고
    • Kinesin I-dependent cortical exclusion restricts pole plasm to the oocyte posterior
    • Cha, B.J., Serbus, L.R., Koppetsch, B.S., and Theurkauf, W.E. (2002). Kinesin I-dependent cortical exclusion restricts pole plasm to the oocyte posterior. Nat. Cell Biol. 4, 592-598.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 592-598
    • Cha, B.J.1    Serbus, L.R.2    Koppetsch, B.S.3    Theurkauf, W.E.4
  • 4
    • 0029127761 scopus 로고
    • Functional dissection of the dynein motor domain
    • Eshel, D. (1995). Functional dissection of the dynein motor domain. Cell Motil. Cytoskel. 32, 133-135.
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 133-135
    • Eshel, D.1
  • 5
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee, M.A., Heuser, J.E., and Vallee, R.B. (1997). An extended microtubule-binding structure within the dynein motor domain. Nature 390, 636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 7
    • 0029084610 scopus 로고
    • Dynein family of motor proteins: Present status and future questions
    • Gibbons, I.R. (1995). Dynein family of motor proteins: present status and future questions. Cell Motil. Cytoskel. 32, 136-144.
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 136-144
    • Gibbons, I.R.1
  • 8
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of dynein beta heavy chain
    • Gibbons, I.R., Gibbons, B.H., Mocz, G., and Asai, D.J. (1991). Multiple nucleotide-binding sites in the sequence of dynein beta heavy chain [see comments]. Nature 352, 640-643.
    • (1991) Nature , vol.352 , pp. 640-643
    • Gibbons, I.R.1    Gibbons, B.H.2    Mocz, G.3    Asai, D.J.4
  • 9
    • 0023664034 scopus 로고
    • Photosensitized cleavage of dynein heavy chains. Cleavage at the "V1 site" by irradiation at 365 nm in the presence of ATP and vanadate
    • Gibbons, I.R., Lee-Eiford, A., Mocz, G., Phillipson, C.A., Tang, W.J., and Gibbons, B.H. (1987). Photosensitized cleavage of dynein heavy chains. Cleavage at the "V1 site" by irradiation at 365 nm in the presence of ATP and vanadate. J. Biol. Chem. 262, 2780-2786.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2780-2786
    • Gibbons, I.R.1    Lee-Eiford, A.2    Mocz, G.3    Phillipson, C.A.4    Tang, W.J.5    Gibbons, B.H.6
  • 10
    • 0025780531 scopus 로고
    • Photocatalytic cleavage of proteins with vanadate and other transition metal complexes
    • Gibbons, I.R., and Mocz, G. (1991). Photocatalytic cleavage of proteins with vanadate and other transition metal complexes. Methods Enzymol. 196, 428-442.
    • (1991) Methods Enzymol. , vol.196 , pp. 428-442
    • Gibbons, I.R.1    Mocz, G.2
  • 11
    • 0028363064 scopus 로고
    • Molecular phylogeny of the kinesin family of microtubule motor proteins
    • Goodson, H.V., Kang, S.J., and Endow, S.A. (1994). Molecular phylogeny of the kinesin family of microtubule motor proteins. J. Cell Sci. 107, 1875-1884.
    • (1994) J. Cell Sci. , vol.107 , pp. 1875-1884
    • Goodson, H.V.1    Kang, S.J.2    Endow, S.A.3
  • 12
    • 0033767835 scopus 로고    scopus 로고
    • The fusome organizes the microtubule network during oocyte differentiation in Drosophila
    • Grieder, N.C., de Cuevas, M., and Spradling, A.C. (2000). The fusome organizes the microtubule network during oocyte differentiation in Drosophila. Development 127, 4253-4264.
    • (2000) Development , vol.127 , pp. 4253-4264
    • Grieder, N.C.1    De Cuevas, M.2    Spradling, A.C.3
  • 13
    • 0029873077 scopus 로고    scopus 로고
    • The kinetic cycles of myosin, kinesin, and dynein
    • Hackney, D.D. (1996). The kinetic cycles of myosin, kinesin, and dynein. Annu. Rev. Physiol. 58, 731-750.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 731-750
    • Hackney, D.D.1
  • 14
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 15
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman, J.J., and Vale, R.D. (1999). Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286, 782-785.
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 16
    • 0028243677 scopus 로고
    • A cytoplasmic dynein motor in Drosophila: Identification and localization during embryogenesis
    • Hays, T.S., Porter, M.E., McGrail, M., Grissom, P., Gosch, P., Fuller, M.T., and McIntosh, J.R. (1994). A cytoplasmic dynein motor in Drosophila: identification and localization during embryogenesis. J. Cell Sci. 107, 1557-1569.
    • (1994) J. Cell Sci. , vol.107 , pp. 1557-1569
    • Hays, T.S.1    Porter, M.E.2    McGrail, M.3    Grissom, P.4    Gosch, P.5    Fuller, M.T.6    McIntosh, J.R.7
  • 17
    • 0032005975 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins in organelle transport and cell division
    • Hirokawa, N., Noda, Y., and Okada, Y. (1998). Kinesin and dynein superfamily proteins in organelle transport and cell division. Curr. Opin. Cell Biol. 10, 60-73.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 60-73
    • Hirokawa, N.1    Noda, Y.2    Okada, Y.3
  • 18
    • 0024445251 scopus 로고
    • Microtubules accelerate ADP release by dynein
    • Holzbaur, E.L., and Johnson, K.A. (1989). Microtubules accelerate ADP release by dynein. Biochemistry 28, 7010-7016.
    • (1989) Biochemistry , vol.28 , pp. 7010-7016
    • Holzbaur, E.L.1    Johnson, K.A.2
  • 19
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J. (1997). Molecular motors: structural adaptations to cellular functions [see comments]. Nature 389, 561-567.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 20
    • 0033565826 scopus 로고    scopus 로고
    • Evidence for cooperative interactions between the two motor domains of cytoplasmic dynein
    • in press
    • Iyadurai, S.J., Li, M.-G., Gilbert, S., and Hays, T.S. (1999). Evidence for cooperative interactions between the two motor domains of cytoplasmic dynein. Curr. Biol. (in press).
    • (1999) Curr. Biol.
    • Iyadurai, S.J.1    Li, M.-G.2    Gilbert, S.3    Hays, T.S.4
  • 21
    • 0021975705 scopus 로고
    • Pathway of the microtubule-dynein ATPase and the structure of dynein: A comparison with actomyosin
    • Johnson, K.A. (1985). Pathway of the microtubule-dynein ATPase and the structure of dynein: a comparison with actomyosin. Annu. Rev. Biophys. Biophys. Chem. 14, 161-188.
    • (1985) Annu. Rev. Biophys. Biophys. Chem. , vol.14 , pp. 161-188
    • Johnson, K.A.1
  • 22
    • 0021178140 scopus 로고
    • Mechanism of force production for microtubule-dependent movements
    • Johnson, K.A., Porter, M.E., and Shimizu, T. (1984). Mechanism of force production for microtubule-dependent movements. J. Cell Biol. 99, 132s-136s.
    • (1984) J. Cell Biol. , vol.99
    • Johnson, K.A.1    Porter, M.E.2    Shimizu, T.3
  • 23
    • 0021473294 scopus 로고
    • Analysis of P transposable element functions in Drosophila
    • Karess, R.E., and Rubin, G.M. (1984). Analysis of P transposable element functions in Drosophila. Cell 38, 135-146.
    • (1984) Cell , vol.38 , pp. 135-146
    • Karess, R.E.1    Rubin, G.M.2
  • 24
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S., and Holzbaur, E.L. (1999). Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 11, 45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 25
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S.M. (2000a). The dynein microtubule motor. Biochim. Biophys. Acta 1496, 60-75.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 26
    • 0033895197 scopus 로고    scopus 로고
    • AAA domains and organization of the dynein motor unit
    • King, S.M. (2000b). AAA domains and organization of the dynein motor unit. J. Cell Sci. 113, 2521-2526.
    • (2000) J. Cell Sci. , vol.113 , pp. 2521-2526
    • King, S.M.1
  • 28
    • 0030877444 scopus 로고    scopus 로고
    • Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain
    • Koonce, M.P. (1997). Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain. J. Biol. Chem. 272, 19714-19718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19714-19718
    • Koonce, M.P.1
  • 29
    • 0027050116 scopus 로고
    • Dynein from dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein
    • Koonce, M.P., Grissom, P.M., and McIntosh, J.R. (1992). Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein. J. Cell Biol. 119, 1597-1604.
    • (1992) J. Cell Biol. , vol.119 , pp. 1597-1604
    • Koonce, M.P.1    Grissom, P.M.2    McIntosh, J.R.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0015273435 scopus 로고
    • Genetic duplication in the white-split interval of the X chromosome in Drosophila melanogaster
    • Lefebrve, G., and Green, M.M. (1972). Genetic duplication in the white-split interval of the X chromosome in Drosophila melanogaster. Genetics 36, 391-412.
    • (1972) Genetics , vol.36 , pp. 391-412
    • Lefebrve, G.1    Green, M.M.2
  • 32
    • 0028144963 scopus 로고
    • Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte
    • Li, M., McGrail, M., Serr, M., and Hays, T.S. (1994). Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte. J. Cell Biol. 126, 1475-1494.
    • (1994) J. Cell Biol. , vol.126 , pp. 1475-1494
    • Li, M.1    McGrail, M.2    Serr, M.3    Hays, T.S.4
  • 33
    • 0027293707 scopus 로고
    • Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli
    • Logan, K.M., and Knight, K.L. (1993). Mutagenesis of the P-loop motif in the ATP binding site of the RecA protein from Escherichia coli. J. Mol. Biol. 232, 1048-1059.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1048-1059
    • Logan, K.M.1    Knight, K.L.2
  • 34
    • 0028787443 scopus 로고
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex
    • McGrail, M., Gepner, J., Silvanovich, A., Ludmann, S., Serr, M., and Hays, T.S. (1995). Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex. J. Cell Biol. 131, 411-425.
    • (1995) J. Cell Biol. , vol.131 , pp. 411-425
    • McGrail, M.1    Gepner, J.2    Silvanovich, A.3    Ludmann, S.4    Serr, M.5    Hays, T.S.6
  • 35
    • 0030762577 scopus 로고    scopus 로고
    • The microtubule motor cytoplasmic dynein is required for spindle orientation during germline cell divisions and oocyte differentiation in drosophila
    • McGrail, M., and Hays, T.S. (1997). The microtubule motor cytoplasmic dynein is required for spindle orientation during germline cell divisions and oocyte differentiation in Drosophila. Development 124, 2409-2419.
    • (1997) Development , vol.124 , pp. 2409-2419
    • McGrail, M.1    Hays, T.S.2
  • 36
    • 0025309665 scopus 로고
    • KAR3, a kinesin-related gene required for yeast nuclear fusion
    • published erratum appears in Cell 1990 May 4;61(3):548
    • Meluh, P.B., and Rose, M.D. (1990). KAR3, a kinesin-related gene required for yeast nuclear fusion [published erratum appears in Cell 1990 May 4;61(3):548]. Cell 60, 1029-1041.
    • (1990) Cell , vol.60 , pp. 1029-1041
    • Meluh, P.B.1    Rose, M.D.2
  • 37
    • 0028177644 scopus 로고
    • Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification
    • Michael, S.F. (1994). Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification. Biotechniques 16, 410-412.
    • (1994) Biotechniques , vol.16 , pp. 410-412
    • Michael, S.F.1
  • 38
    • 0027264943 scopus 로고
    • Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C)
    • Mikami, A., Paschal, B.M., Mazumdar, M., and Vallee, R.B. (1993). Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C). Neuron 10, 787-796.
    • (1993) Neuron , vol.10 , pp. 787-796
    • Mikami, A.1    Paschal, B.M.2    Mazumdar, M.3    Vallee, R.B.4
  • 39
    • 0025327217 scopus 로고
    • Iron(IlI)-mediated photolysis of outer arm dynein ATPase from sea urchin sperm flagella
    • Mocz, G., and Gibbons, I.R. (1990). Iron(IlI)-mediated photolysis of outer arm dynein ATPase from sea urchin sperm flagella. J. Biol. Chem. 265, 2917-2922.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2917-2922
    • Mocz, G.1    Gibbons, I.R.2
  • 40
    • 0029896120 scopus 로고    scopus 로고
    • Phase partition analysis of nucleotide binding to axonemal dynein
    • Mocz, G., and Gibbons, I.R. (1996). Phase partition analysis of nucleotide binding to axonemal dynein. Biochemistry 35, 9204-9211.
    • (1996) Biochemistry , vol.35 , pp. 9204-9211
    • Mocz, G.1    Gibbons, I.R.2
  • 41
    • 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., and Gibbons, IR. (2001). Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure (Camb) 9, 93-103.
    • (2001) Structure (Camb) , vol.9 , pp. 93-103
    • Mocz, G.1    Gibbons, I.R.2
  • 42
    • 0032493320 scopus 로고    scopus 로고
    • Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-methylanthraniloyl)-adenosine 5′-triphosphate
    • Mocz, G., Helms, M.K., Jameson, D.M., and Gibbons, I.R. (1998). Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-methylanthraniloyl)-adenosine 5′-triphosphate. Biochemistry 37, 9862-9869.
    • (1998) Biochemistry , vol.37 , pp. 9862-9869
    • Mocz, G.1    Helms, M.K.2    Jameson, D.M.3    Gibbons, I.R.4
  • 43
    • 0028871742 scopus 로고
    • Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport
    • Nakata, T., and Hirokawa, N. (1995). Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport. J. Cell Biol. 131, 1039-1053.
    • (1995) J. Cell Biol. , vol.131 , pp. 1039-1053
    • Nakata, T.1    Hirokawa, N.2
  • 44
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon, A., and Goldberg, A.L. (2001). Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8, 1339-49.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 45
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V. (1999). AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 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
  • 46
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the beta heavy chain of dynein
    • Ogawa, K. (1991). Four ATP-binding sites in the midregion of the beta heavy chain of dynein [see comments]. Nature 352, 643-645.
    • (1991) Nature , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 47
    • 0021111979 scopus 로고
    • Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules
    • Porter, M.E., and Johnson, K.A. (1983a). Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules. J. Biol. Chem. 258, 6575-6581.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6575-6581
    • Porter, M.E.1    Johnson, K.A.2
  • 48
    • 0021112029 scopus 로고
    • Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex
    • Porter, M.E., and Johnson, K.A. (1983b). Transient state kinetic analysis of the ATP-induced dissociation of the dynein-microtubule complex. J. Biol. Chem. 258, 6582-6587.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6582-6587
    • Porter, M.E.1    Johnson, K.A.2
  • 49
    • 0026050710 scopus 로고
    • The lethal(1)TW-6cs mutation of Drosophila melanogaster is a dominant antimorphic allele of nod and is associated with a single base change in the putative ATP-binding domain
    • Rasooly, R.S., New, C.M., Zhang, P., Hawley, R.S., and Baker, B.S. (1991). The lethal(1)TW-6cs mutation of Drosophila melanogaster is a dominant antimorphic allele of nod and is associated with a single base change in the putative ATP-binding domain. Genetics 129, 409-422.
    • (1991) Genetics , vol.129 , pp. 409-422
    • Rasooly, R.S.1    New, C.M.2    Zhang, P.3    Hawley, R.S.4    Baker, B.S.5
  • 53
    • 0029731663 scopus 로고    scopus 로고
    • Structure-function analysis of the motor domain of myosin
    • Ruppel, K.M., and Spudich, J.A. (1996a). Structure-function analysis of the motor domain of myosin. Annu. Rev. Cell Dev. Biol. 12, 543-573.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 543-573
    • Ruppel, K.M.1    Spudich, J.A.2
  • 54
    • 0030035665 scopus 로고    scopus 로고
    • Structure-function studies of the myosin motor domain: Importance of the 50-kDa cleft
    • Ruppel, K.M., and Spudich, J.A. (1996b). Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft. Mol. Biol. Cell 7, 1123-1136.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1123-1136
    • Ruppel, K.M.1    Spudich, J.A.2
  • 55
    • 0034081637 scopus 로고    scopus 로고
    • Molecular chaperones: Containers and surfaces for folding, stabilizing or unfolding proteins
    • Saibil, H. (2000). Molecular chaperones: containers and surfaces for folding, stabilizing or unfolding proteins. Curr. Opin. Struct. Biol 10, 251-258.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 251-258
    • Saibil, H.1
  • 56
    • 0032513004 scopus 로고    scopus 로고
    • Structural characterization of a dynein motor domain
    • Samso, M., Radermacher, M., Frank, J., and Koonce, M.P. (1998). Structural characterization of a dynein motor domain. J. Mol. Biol. 276, 927-937.
    • (1998) J. Mol. Biol. , vol.276 , pp. 927-937
    • Samso, M.1    Radermacher, M.2    Frank, J.3    Koonce, M.P.4
  • 57
    • 0031672952 scopus 로고    scopus 로고
    • Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II
    • Sasaki, N., and Sutoh, K. (1998). Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II. Adv. Biophys. 35, 1-24.
    • (1998) Adv. Biophys. , vol.35 , pp. 1-24
    • Sasaki, N.1    Sutoh, K.2
  • 58
    • 0028338693 scopus 로고
    • Primary structural constraints of P-loop of mitochondrial F1-ATPase from yeast
    • Shen, H., Yao, B.Y., and Mueller, D.M. (1994). Primary structural constraints of P-loop of mitochondrial F1-ATPase from yeast. J. Biol. Chem. 269, 9424-9428.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9424-9428
    • Shen, H.1    Yao, B.Y.2    Mueller, D.M.3
  • 59
    • 0021020392 scopus 로고
    • Kinetic evidence for multiple dynein ATPase sites
    • Shimizu, T., and Johnson, K.A. (1983). Kinetic evidence for multiple dynein ATPase sites. J. Biol. Chem. 258, 13841-13846.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13841-13846
    • Shimizu, T.1    Johnson, K.A.2
  • 60
    • 0032563329 scopus 로고    scopus 로고
    • Inferences about the catalytic domain of P-type ATPases from the tertiary structures of enzymes that catalyze the same elementary reaction
    • Smirnova, I.N., Kasho, V.N., and Faller, L.D. (1998). Inferences about the catalytic domain of P-type ATPases from the tertiary structures of enzymes that catalyze the same elementary reaction. FEBS Lett. 431, 309-314.
    • (1998) FEBS Lett. , vol.431 , pp. 309-314
    • Smirnova, I.N.1    Kasho, V.N.2    Faller, L.D.3
  • 61
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R.M., and Steitz, T.A. (1992). Structure of the recA protein-ADP complex [see comments]. Nature 355, 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 62
    • 0029919076 scopus 로고    scopus 로고
    • Mutational analysis of motor proteins
    • Sweeney, H.L., and Holzbaur, E.L. (1996). Mutational analysis of motor proteins. Annu. Rev. Physiol. 58, 751-792.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 751-792
    • Sweeney, H.L.1    Holzbaur, E.L.2
  • 63
    • 0028130363 scopus 로고
    • Microtubules and cytoplasm organization during Drosophila oogenesis
    • Theurkauf, W.E. (1994). Microtubules and cytoplasm organization during Drosophila oogenesis. Dev. Biol. 165, 352-360.
    • (1994) Dev. Biol. , vol.165 , pp. 352-360
    • Theurkauf, W.E.1
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 65
    • 0026509543 scopus 로고
    • The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation
    • Tyers, M., Tokiwa, G., Nash, R., and Futcher, B. (1992). The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation. EMBO J. 11, 1773-1784.
    • (1992) EMBO J. , vol.11 , pp. 1773-1784
    • Tyers, M.1    Tokiwa, G.2    Nash, R.3    Futcher, B.4
  • 66
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale, R.D. (2000). AAA proteins. Lords of the ring. J. Cell Biol. 150, F13-F19.
    • (2000) J. Cell Biol. , vol.150
    • Vale, R.D.1
  • 69
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB-Holliday junction complex
    • Yu, X., West, S.C., and Egelman, E.H. (1997). Structure and subunit composition of the RuvAB-Holliday junction complex. J. Mol. Biol. 266, 217-222.
    • (1997) J. Mol. Biol. , vol.266 , pp. 217-222
    • Yu, X.1    West, S.C.2    Egelman, E.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.