메뉴 건너뛰기




Volumn 85, Issue 1, 2003, Pages 525-536

Order, disorder, and perturbations in actin-aldolase rafts

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FRUCTOSE BISPHOSPHATE ALDOLASE;

EID: 0037635961     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74497-X     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0014349824 scopus 로고
    • Binding of glycolytic enzymes to structure proteins of the muscle
    • Arnold, H., and D. Pette. 1968. Binding of glycolytic enzymes to structure proteins of the muscle. Eur. J. Biochem. 6:163-171.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 163-171
    • Arnold, H.1    Pette, D.2
  • 2
    • 0031024620 scopus 로고    scopus 로고
    • Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase
    • Blom, N., and J. Sygusch. 1997. Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Nat. Struct. Biol. 4:36-39.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 36-39
    • Blom, N.1    Sygusch, J.2
  • 3
    • 0033613116 scopus 로고    scopus 로고
    • Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 Å
    • Choi, K. H., A. S. Mazurkie, A. J. Morris, D. Utheza, D. R. Tolan, and K. N. Allen. 1999. Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 Å. Biochemistry. 38:12655-12664.
    • (1999) Biochemistry , vol.38 , pp. 12655-12664
    • Choi, K.H.1    Mazurkie, A.S.2    Morris, A.J.3    Utheza, D.4    Tolan, D.R.5    Allen, K.N.6
  • 4
    • 0017189627 scopus 로고
    • Aldolase binding to actin-containing filaments. Formation of paracrystals
    • Clarke, F. M., and D. J. Morton. 1976. Aldolase binding to actin-containing filaments. Formation of paracrystals. Biochem. J. 159:797-798.
    • (1976) Biochem. J. , vol.159 , pp. 797-798
    • Clarke, F.M.1    Morton, D.J.2
  • 6
    • 0019880376 scopus 로고
    • Structure of F-actin needles from extracts of sea urchin oocytes
    • DeRosier, D. J., and R. Censullo. 1981. Structure of F-actin needles from extracts of sea urchin oocytes. J. Mol. Biol. 146:77-99.
    • (1981) J. Mol. Biol. , vol.146 , pp. 77-99
    • DeRosier, D.J.1    Censullo, R.2
  • 7
    • 0017378495 scopus 로고
    • Structure of actin-containing filaments from two types of non-muscle cells
    • DeRosier, D., E. Mandelkow, A. Silliman, L. Tilney, and R. Kane. 1977. Structure of actin-containing filaments from two types of non-muscle cells. J. Mol. Biol. 113:679-695.
    • (1977) J. Mol. Biol. , vol.113 , pp. 679-695
    • DeRosier, D.1    Mandelkow, E.2    Silliman, A.3    Tilney, L.4    Kane, R.5
  • 8
    • 0021605430 scopus 로고
    • How to build a bend into an actin bundle
    • DeRosier, D. J., and L. G. Tilney. 1984. How to build a bend into an actin bundle. J. Mol. Biol. 175:57-73.
    • (1984) J. Mol. Biol. , vol.175 , pp. 57-73
    • DeRosier, D.J.1    Tilney, L.G.2
  • 9
    • 0019324859 scopus 로고
    • A change in the twist of the actin-containing filaments occurs during the extension of the acrosomal process in Limulus sperm
    • DeRosier, D., L. Tilney, and P. Flicker. 1980a. A change in the twist of the actin-containing filaments occurs during the extension of the acrosomal process in Limulus sperm. J. Mol. Biol. 137:375-389.
    • (1980) J. Mol. Biol. , vol.137 , pp. 375-389
    • DeRosier, D.1    Tilney, L.2    Flicker, P.3
  • 10
    • 0019302885 scopus 로고
    • Actin in the inner ear: The remarkable structure of the stereocilium
    • DeRosier, D. J., L. G. Tilney, and E. Egelman. 1980b. Actin in the inner ear: the remarkable structure of the stereocilium. Nature. 287:291-296.
    • (1980) Nature , vol.287 , pp. 291-296
    • DeRosier, D.J.1    Tilney, L.G.2    Egelman, E.3
  • 11
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman, E. H., N. Francis, and D. J. DeRosier. 1982. F-actin is a helix with a random variable twist. Nature. 298:131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 13
    • 0013823053 scopus 로고
    • A new method of preparation of a self-perforated micro plastic grid and its application
    • Fukami, A., and K. Adachi. 1965. A new method of preparation of a self-perforated micro plastic grid and its application. J Electron Microsc. (Tokyo). 14:112-118.
    • (1965) J Electron Microsc. (Tokyo) , vol.14 , pp. 112-118
    • Fukami, A.1    Adachi, K.2
  • 14
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • Galkin, V. E., A. Orlova, N. Lukoyanova, W. Wriggers, and E. H. Egelman. 2001. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 153:75-86.
    • (2001) J. Cell Biol. , vol.153 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggers, W.4    Egelman, E.H.5
  • 16
    • 0031215010 scopus 로고    scopus 로고
    • Mode of interactions of human aldolase isozymes with cytoskeletons
    • Kusakabe, T., K. Motoki, and K. Hori. 1997. Mode of interactions of human aldolase isozymes with cytoskeletons. Arch. Biochem. Biophys. 344:184-193.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 184-193
    • Kusakabe, T.1    Motoki, K.2    Hori, K.3
  • 17
    • 0020678649 scopus 로고
    • Structural and functional relationship between the membrane and the cytoskeleton in brush border microvilli
    • Matsudaira, P. T. 1983. Structural and functional relationship between the membrane and the cytoskeleton in brush border microvilli. Ciba Found. Symp. 95:233-252.
    • (1983) Ciba Found. Symp. , vol.95 , pp. 233-252
    • Matsudaira, P.T.1
  • 18
    • 0017669788 scopus 로고
    • An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments
    • Morton, D. J., F. M. Clarke, and C. J. Masters. 1977. An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments. J. Cell Biol. 74:1016-1023.
    • (1977) J. Cell Biol. , vol.74 , pp. 1016-1023
    • Morton, D.J.1    Clarke, F.M.2    Masters, C.J.3
  • 19
    • 0034068931 scopus 로고    scopus 로고
    • F-actin retains a memory of angular order
    • Orlova, A., and E. H. Egelman. 2000. F-actin retains a memory of angular order. Biophys. J. 78:2180-2185.
    • (2000) Biophys. J. , vol.78 , pp. 2180-2185
    • Orlova, A.1    Egelman, E.H.2
  • 20
  • 21
    • 0029916489 scopus 로고    scopus 로고
    • Image analysis of helical objects: The Brandeis helical package
    • Owen, C. H., D. G. Morgan, and D. J. DeRosier. 1996. Image analysis of helical objects: The Brandeis helical package. J. Struct. Biol. 116:167-175.
    • (1996) J. Struct. Biol. , vol.116 , pp. 167-175
    • Owen, C.H.1    Morgan, D.G.2    DeRosier, D.J.3
  • 23
    • 0014502990 scopus 로고
    • Intracellular localization of glycogenolytic and glycolytic enzymes in white and red rabbit skeletal muscle: A gel film method for coupled enzyme reactions in histochemistry
    • Sigel, P., and D. Pette. 1969. Intracellular localization of glycogenolytic and glycolytic enzymes in white and red rabbit skeletal muscle: a gel film method for coupled enzyme reactions in histochemistry. J. Histochem. Cytochem. 17:225-237.
    • (1969) J. Histochem. Cytochem. , vol.17 , pp. 225-237
    • Sigel, P.1    Pette, D.2
  • 24
    • 0018781932 scopus 로고
    • Structure of actin filament bundles from microvilli of sea urchin eggs
    • Spudich, J. A., and L. A. Amos. 1979. Structure of actin filament bundles from microvilli of sea urchin eggs. J. Mol. Biol. 129:319-331.
    • (1979) J. Mol. Biol. , vol.129 , pp. 319-331
    • Spudich, J.A.1    Amos, L.A.2
  • 25
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 26
    • 0018899656 scopus 로고
    • Interaction of aldolase with actin-containing filaments. Structural studies
    • Stewart, M., D. J. Morton, and F. M. Clarke. 1980. Interaction of aldolase with actin-containing filaments. Structural studies. Biochem. J. 186:99-104.
    • (1980) Biochem. J. , vol.186 , pp. 99-104
    • Stewart, M.1    Morton, D.J.2    Clarke, F.M.3
  • 27
    • 0032509093 scopus 로고    scopus 로고
    • How to analyze electron micrographs of rafts of actin filaments crosslinked by actin-binding proteins
    • Sukow, C., and D. DeRosier. 1998. How to analyze electron micrographs of rafts of actin filaments crosslinked by actin-binding proteins. J. Mol. Biol. 284:1039-1050.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1039-1050
    • Sukow, C.1    DeRosier, D.2
  • 28
    • 0026506363 scopus 로고
    • Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants
    • Taylor, K. A., and D. W. Taylor. 1992. Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants. J. Struct. Biol. 108:140-147.
    • (1992) J. Struct. Biol. , vol.108 , pp. 140-147
    • Taylor, K.A.1    Taylor, D.W.2
  • 29
    • 0027992919 scopus 로고
    • Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: Demonstration of unipolar alpha-actinin-F-actin crosslinking
    • Taylor, K. A., and D. W. Taylor. 1994. Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar alpha-actinin-F-actin crosslinking. Biophys. J. 67:1976-1983.
    • (1994) Biophys. J. , vol.67 , pp. 1976-1983
    • Taylor, K.A.1    Taylor, D.W.2
  • 30
    • 0033391273 scopus 로고    scopus 로고
    • Structural studies of cytoskeletal arrays formed on lipid monolayers
    • Taylor, K. A., and D. W. Taylor. 1999. Structural studies of cytoskeletal arrays formed on lipid monolayers. J. Struct. Biol. 128:75-81.
    • (1999) J. Struct. Biol. , vol.128 , pp. 75-81
    • Taylor, K.A.1    Taylor, D.W.2
  • 31
    • 0019307051 scopus 로고
    • The organization of actin filaments in the stereocilia of cochlear hair cells
    • Tilney, L. G., D. J. Derosier, and M. J. Mulroy. 1980. The organization of actin filaments in the stereocilia of cochlear hair cells. J. Cell Biol. 86:244-259.
    • (1980) J. Cell Biol. , vol.86 , pp. 244-259
    • Tilney, L.G.1    Derosier, D.J.2    Mulroy, M.J.3
  • 32
    • 0023261436 scopus 로고
    • Movement of the actin filament bundle in Mytilus sperm: A new mechanism is proposed
    • Tilney, L. G., Y. Fukui, and D. J. DeRosier. 1987. Movement of the actin filament bundle in Mytilus sperm: a new mechanism is proposed. J. Cell Biol. 104:981-993.
    • (1987) J. Cell Biol. , vol.104 , pp. 981-993
    • Tilney, L.G.1    Fukui, Y.2    DeRosier, D.J.3
  • 33
    • 0022740263 scopus 로고
    • Interpretation of electron micrographs of adenovirus hexon arrays using a crystallographic molecular model
    • van Oostrum, J., P. R. Smith, M. Mohraz, and R. M. Bumett. 1986. Interpretation of electron micrographs of adenovirus hexon arrays using a crystallographic molecular model. J. Ultrastruct. Mol. Struct. Res. 96:77-90.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.96 , pp. 77-90
    • Van Oostrum, J.1    Smith, P.R.2    Mohraz, M.3    Bumett, R.M.4
  • 34
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • Volkmann, N., D. DeRosier, P. Matsudaira, and D. Hanein. 2001. An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 153:947-956.
    • (2001) J. Cell Biol. , vol.153 , pp. 947-956
    • Volkmann, N.1    DeRosier, D.2    Matsudaira, P.3    Hanein, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.