메뉴 건너뛰기




Volumn 3, Issue C, 1996, Pages 359-404

The cytoskeleton of the intestinal epithelium. Components, assembly, and dynamic rearrangements

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77957150954     PISSN: 18746020     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6020(96)80015-2     Document Type: Review
Times cited : (31)

References (201)
  • 1
    • 0024370276 scopus 로고
    • Role of microtubules in polarized delivery of apical proteins to the brush border of the intestinal epithelium
    • Achler C., Filmer D., Merte C., and Drenckhahn D. Role of microtubules in polarized delivery of apical proteins to the brush border of the intestinal epithelium. J. Cell Biol. 109 (1989) 179-189
    • (1989) J. Cell Biol. , vol.109 , pp. 179-189
    • Achler, C.1    Filmer, D.2    Merte, C.3    Drenckhahn, D.4
  • 2
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain M., Turunen O., Vaheri A., Louvard D., and Arpin M. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120 (1993) 129-139
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 4
    • 0023850804 scopus 로고
    • Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains
    • Andre E., Lottspeich F., Schleicher M., and Noegel A. Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains. J. Biol. Chem. 263 (1993) 722-727
    • (1993) J. Biol. Chem. , vol.263 , pp. 722-727
    • Andre, E.1    Lottspeich, F.2    Schleicher, M.3    Noegel, A.4
  • 5
    • 0023812318 scopus 로고
    • Sequence of human villin: A large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity
    • Arpin M., Pringault E., Finidori J., Garcia A., Jeltsch J.-M., Vandekerckhove J., and Louvard D. Sequence of human villin: A large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity. J. Cell Biol. 107 (1988) 1759-1766
    • (1988) J. Cell Biol. , vol.107 , pp. 1759-1766
    • Arpin, M.1    Pringault, E.2    Finidori, J.3    Garcia, A.4    Jeltsch, J.-M.5    Vandekerckhove, J.6    Louvard, D.7
  • 6
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby Canine Kidney cells during the formation of a polarized epithelium
    • Bacallao A., Dotti C., C.Karsenti E., Steltzer E.H.K., and Simons K. The subcellular organization of Madin-Darby Canine Kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109 (1989) 2817-2832
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, A.1    Dotti, C.2    C.Karsenti, E.3    Steltzer, E.H.K.4    Simons, K.5
  • 7
    • 0025757105 scopus 로고
    • Elevation of intracellular free calcium levels in HEp-2 cells infected with enteropathogenic Escherichia coli
    • Baldwin T.J., Ward W., Aitken A., Knutton S., and Williams P.H. Elevation of intracellular free calcium levels in HEp-2 cells infected with enteropathogenic Escherichia coli. Infect. Immun. 59 (1991) 1599-1604
    • (1991) Infect. Immun. , vol.59 , pp. 1599-1604
    • Baldwin, T.J.1    Ward, W.2    Aitken, A.3    Knutton, S.4    Williams, P.H.5
  • 9
    • 0026010423 scopus 로고
    • Analysis of inducible contractile rings suggests a role for protein kinase C in embryonic cytokinesis and wound healing
    • Bement W.M., and Capco D.G. Analysis of inducible contractile rings suggests a role for protein kinase C in embryonic cytokinesis and wound healing. Cell Motil. Cytoskel. 20 (1992) 145-157
    • (1992) Cell Motil. Cytoskel. , vol.20 , pp. 145-157
    • Bement, W.M.1    Capco, D.G.2
  • 10
    • 0027176798 scopus 로고
    • A novel cytoskeletal structure involved in purse string wound closure and cell polarity maintenance
    • Bement W.M., Forscher P., and Mooseker M.S. A novel cytoskeletal structure involved in purse string wound closure and cell polarity maintenance. J. Cell Biol. 121 (1993) 565-578
    • (1993) J. Cell Biol. , vol.121 , pp. 565-578
    • Bement, W.M.1    Forscher, P.2    Mooseker, M.S.3
  • 12
    • 0028231886 scopus 로고
    • Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types
    • Bement W.M., Hasson T.B., Wirth J.A., Cheney R.E., and Mooseker M.S. Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Proc. Natl. Acad. Sci. USA 91 (1994) 6549-6553
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6549-6553
    • Bement, W.M.1    Hasson, T.B.2    Wirth, J.A.3    Cheney, R.E.4    Mooseker, M.S.5
  • 13
    • 85063072510 scopus 로고
    • Cross-talk between apoptotic epithelial cells and their neighbors
    • Bement W.M., and Mooseker M.S. Cross-talk between apoptotic epithelial cells and their neighbors. Mol. Biol. Cell 4 (1993) 334a
    • (1993) Mol. Biol. Cell , vol.4
    • Bement, W.M.1    Mooseker, M.S.2
  • 14
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman M., Franck Z., and Bretscher A. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J. Cell Sci. 105 (1993) 1025-1043
    • (1993) J. Cell Sci. , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 15
    • 0027459202 scopus 로고
    • Zipper protein, a newly described tropomyosin-like protein of the intestinal brush border
    • Bickle D.D., Munson S., Morrison N., and Eisman J. Zipper protein, a newly described tropomyosin-like protein of the intestinal brush border. J. Biol. Chem. 268 (1993) 620-626
    • (1993) J. Biol. Chem. , vol.268 , pp. 620-626
    • Bickle, D.D.1    Munson, S.2    Morrison, N.3    Eisman, J.4
  • 16
    • 77957112103 scopus 로고
    • Localization of phosphotyrosine-containing proteins in the intestinal epithelium
    • Black J.D., Saxon M.L., and Ren J. Localization of phosphotyrosine-containing proteins in the intestinal epithelium. J. Cell Biol. 115 (1991) 274a
    • (1991) J. Cell Biol. , vol.115
    • Black, J.D.1    Saxon, M.L.2    Ren, J.3
  • 17
    • 0020598145 scopus 로고
    • Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin). A new actin assembly assay using the Limulus acrosomal process
    • Bonder E.M., and Mooseker M.S. Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin). A new actin assembly assay using the Limulus acrosomal process. J. Cell Biol. 96 (1983) 1097-1107
    • (1983) J. Cell Biol. , vol.96 , pp. 1097-1107
    • Bonder, E.M.1    Mooseker, M.S.2
  • 18
    • 0020804117 scopus 로고
    • Purification of an 80,000 dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    • Bretscher A. Purification of an 80,000 dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. J. Cell Biol. 97 (1983) 425-432
    • (1983) J. Cell Biol. , vol.97 , pp. 425-432
    • Bretscher, A.1
  • 19
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    • Bretscher A. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J. Cell Biol. 108 (1989) 921-930
    • (1989) J. Cell Biol. , vol.108 , pp. 921-930
    • Bretscher, A.1
  • 20
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher A. Microfilament structure and function in the cortical cytoskeleton. Ann. Rev. Cell Biol. 7 (1991) 337-374
    • (1991) Ann. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 21
    • 0018233556 scopus 로고
    • Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy
    • Bretscher A., and Weber K. Localization of actin and microfilament-associated proteins in the microvilli and terminal web of the intestinal brush border by immunofluorescence microscopy. J. Cell Biol. 79 (1978) 839-845
    • (1978) J. Cell Biol. , vol.79 , pp. 839-845
    • Bretscher, A.1    Weber, K.2
  • 22
    • 0019313223 scopus 로고
    • Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures
    • Bretscher A., and Weber K. Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. J. Cell Biol. 86 (1980) 335-340
    • (1980) J. Cell Biol. , vol.86 , pp. 335-340
    • Bretscher, A.1    Weber, K.2
  • 23
    • 0021914106 scopus 로고
    • Identification and localization of caldesmon in smooth and nonmuscle cells: A comparison with the distributions of tropomyosin and alpha-actinin
    • Bretscher A., and Lynch W. Identification and localization of caldesmon in smooth and nonmuscle cells: A comparison with the distributions of tropomyosin and alpha-actinin. J. Cell Biol. 100 (1985) 1656-1663
    • (1985) J. Cell Biol. , vol.100 , pp. 1656-1663
    • Bretscher, A.1    Lynch, W.2
  • 24
    • 0022172244 scopus 로고
    • Microtubule Organizing Centers
    • Brinkley B.R. Microtubule Organizing Centers. Ann. Rev. Cell Biol. 1 (1985) 145-172
    • (1985) Ann. Rev. Cell Biol. , vol.1 , pp. 145-172
    • Brinkley, B.R.1
  • 25
    • 0021021559 scopus 로고
    • Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton
    • Broschat K.O., Stidwell R.P., and Burgess D.R. Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton. Cell 35 (1983) 561-571
    • (1983) Cell , vol.35 , pp. 561-571
    • Broschat, K.O.1    Stidwell, R.P.2    Burgess, D.R.3
  • 26
    • 0020410981 scopus 로고
    • Reactivation of intestinal epithelial brush border motility. ATP-dependent contraction of via a terminal web contractile ring
    • Burgess D.R. Reactivation of intestinal epithelial brush border motility. ATP-dependent contraction of via a terminal web contractile ring. J. Cell Biol. 95 (1982) 853-866
    • (1982) J. Cell Biol. , vol.95 , pp. 853-866
    • Burgess, D.R.1
  • 27
    • 0016200516 scopus 로고
    • Alterations in morphology of developing microvilli elicited by cytochalasin B
    • Burgess D.R., and Grey R.D. Alterations in morphology of developing microvilli elicited by cytochalasin B. J. Cell Biol. 62 (1974) 566-574
    • (1974) J. Cell Biol. , vol.62 , pp. 566-574
    • Burgess, D.R.1    Grey, R.D.2
  • 28
    • 0023139873 scopus 로고
    • Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins
    • Burgess D.R., Broschat K.O., and Hayden J.M. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J. Cell Biol. 104 (1987) 29-40
    • (1987) J. Cell Biol. , vol.104 , pp. 29-40
    • Burgess, D.R.1    Broschat, K.O.2    Hayden, J.M.3
  • 29
    • 0024424369 scopus 로고
    • Intestinal crypt stem cells possess high levels of cytoskeletal-associated phosphotyrosine-containing proteins and tyrosine kinase activity relative to differentiated enterocytes
    • Burgess D.R., Jiang W., Mamajiwalla S., and Kinsey W. Intestinal crypt stem cells possess high levels of cytoskeletal-associated phosphotyrosine-containing proteins and tyrosine kinase activity relative to differentiated enterocytes. J. Cell Biol. 109 (1989) 2139-2144
    • (1989) J. Cell Biol. , vol.109 , pp. 2139-2144
    • Burgess, D.R.1    Jiang, W.2    Mamajiwalla, S.3    Kinsey, W.4
  • 30
    • 0021923779 scopus 로고
    • Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets
    • Burn P., Rotman A., Meyer R.K., and Burger M.M. Diacylglycerol in large alpha-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature 314 (1985) 469-472
    • (1985) Nature , vol.314 , pp. 469-472
    • Burn, P.1    Rotman, A.2    Meyer, R.K.3    Burger, M.M.4
  • 31
    • 0023549663 scopus 로고
    • Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells
    • Carboni J.M., Howe C.L., West A.B., Barwick K.W., Mooseker M.S., and Morrow J.S. Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. Am. J. Path. 129 (1987) 589-600
    • (1987) Am. J. Path. , vol.129 , pp. 589-600
    • Carboni, J.M.1    Howe, C.L.2    West, A.B.3    Barwick, K.W.4    Mooseker, M.S.5    Morrow, J.S.6
  • 32
    • 0024110376 scopus 로고
    • Structural and immunological characterization of the intestinal microvillar 110K-calmodulin complex: Evidence for discrete myosin head and calmodulin-binding domains
    • Carboni J.M., Conzelman K.A., Adams R.A., Kaiser D.A., Pollard T.D., and Mooseker M.S. Structural and immunological characterization of the intestinal microvillar 110K-calmodulin complex: Evidence for discrete myosin head and calmodulin-binding domains. J. Cell Biol. 107 (1988) 1749-1757
    • (1988) J. Cell Biol. , vol.107 , pp. 1749-1757
    • Carboni, J.M.1    Conzelman, K.A.2    Adams, R.A.3    Kaiser, D.A.4    Pollard, T.D.5    Mooseker, M.S.6
  • 33
    • 0022409832 scopus 로고
    • Biochemical abnormality in brush border membrane protein of a patient with congenital microvillus atrophy
    • Carruthers L., Phillips A.D., Dourmashkin R., and Walker-Smith J.A. Biochemical abnormality in brush border membrane protein of a patient with congenital microvillus atrophy. J. Ped. Gastro. Nutr. 4 (1985) 902-907
    • (1985) J. Ped. Gastro. Nutr. , vol.4 , pp. 902-907
    • Carruthers, L.1    Phillips, A.D.2    Dourmashkin, R.3    Walker-Smith, J.A.4
  • 35
    • 0023034626 scopus 로고
    • Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments
    • Casella J.F., Maack D.J., and Lin S. Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments. J. Biol. Chem. (1986) 10915-10921
    • (1986) J. Biol. Chem. , pp. 10915-10921
    • Casella, J.F.1    Maack, D.J.2    Lin, S.3
  • 36
    • 0023372284 scopus 로고
    • Cap-Z (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • Casella J.F., Craig S.W., Maack D.J., and Brown A.E. Cap-Z (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J. Cell Biol. 105 (1987) 371-379
    • (1987) J. Cell Biol. , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 37
    • 0018580385 scopus 로고
    • Development of the structural components of the brush border in absorptive cells of the chick intestine
    • Chambers C., and Grey R.D. Development of the structural components of the brush border in absorptive cells of the chick intestine. Cell Tiss. Res. 204 (1979) 387-405
    • (1979) Cell Tiss. Res. , vol.204 , pp. 387-405
    • Chambers, C.1    Grey, R.D.2
  • 38
    • 0026044919 scopus 로고
    • Identification and characterization of rat intestinal keratins
    • Chandler J.S., Calnek D., and Quaroni A. Identification and characterization of rat intestinal keratins. J. Biol. Chem. 266 (1991) 11932-11938
    • (1991) J. Biol. Chem. , vol.266 , pp. 11932-11938
    • Chandler, J.S.1    Calnek, D.2    Quaroni, A.3
  • 44
    • 0021714282 scopus 로고
    • The 110,000-Dalton actin- and calmodulin-binding protein from intestinal brush border is a myosin-like ATPase
    • Collins J.H., and Borysenko C.W. The 110,000-Dalton actin- and calmodulin-binding protein from intestinal brush border is a myosin-like ATPase. J. Biol. Chem. 259 (1984) 14128-14135
    • (1984) J. Biol. Chem. , vol.259 , pp. 14128-14135
    • Collins, J.H.1    Borysenko, C.W.2
  • 45
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin-I (110K-calmodulin) activity in vitro
    • Collins K., Sellers J.R., and Matsudaira P.T. Calmodulin dissociation regulates brush border myosin-I (110K-calmodulin) activity in vitro. J. Cell Biol. 110 (1990) 1137-1147
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1    Sellers, J.R.2    Matsudaira, P.T.3
  • 46
    • 0026329258 scopus 로고
    • Identification of the microvillar 110K-calmodulin complex (myosin-I) in kidney
    • Coluccio L.M. Identification of the microvillar 110K-calmodulin complex (myosin-I) in kidney. Eur. J. Cell Biol. 56 (1991) 286-294
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 286-294
    • Coluccio, L.M.1
  • 47
    • 0023375128 scopus 로고
    • Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to f-actin: Formation of decorated filaments
    • Coluccio L.M., and Bretscher A. Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to f-actin: Formation of decorated filaments. J. Cell Biol. (1987) 325-333
    • (1987) J. Cell Biol. , pp. 325-333
    • Coluccio, L.M.1    Bretscher, A.2
  • 48
    • 0023871582 scopus 로고
    • Mapping of the microvillar 110K-calmodulin complex: Calmodulin-associated or -free fragments of the 110-kD polypeptide bind f-actin and retain ATPase activity
    • Coluccio L.M., and Bretscher A. Mapping of the microvillar 110K-calmodulin complex: Calmodulin-associated or -free fragments of the 110-kD polypeptide bind f-actin and retain ATPase activity. J. Cell Biol. 106 (1988) 367-373
    • (1988) J. Cell Biol. , vol.106 , pp. 367-373
    • Coluccio, L.M.1    Bretscher, A.2
  • 49
    • 0024498207 scopus 로고
    • Reassociation of microvillar core proteins: Making a microvillar core in vitro
    • Coluccio L.M., and Bretscher A. Reassociation of microvillar core proteins: Making a microvillar core in vitro. J. Cell Biol. 108 (1989) 495-502
    • (1989) J. Cell Biol. , vol.108 , pp. 495-502
    • Coluccio, L.M.1    Bretscher, A.2
  • 50
    • 0023368572 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase
    • Conzelman K.A., and Mooseker M.S. The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase. J. Cell Biol. 105 (1987) 313-324
    • (1987) J. Cell Biol. , vol.105 , pp. 313-324
    • Conzelman, K.A.1    Mooseker, M.S.2
  • 51
    • 0342662339 scopus 로고
    • Characterization of an integral membrane glycoprotein associated with the microfilaments of pig intestinal microvilli
    • Coudrier E., Reggio H., and Louvard D. Characterization of an integral membrane glycoprotein associated with the microfilaments of pig intestinal microvilli. EMBO J. 2 (1983) 469-475
    • (1983) EMBO J. , vol.2 , pp. 469-475
    • Coudrier, E.1    Reggio, H.2    Louvard, D.3
  • 52
    • 0018345918 scopus 로고
    • Alpha actinin localization in the junctional complex of intestinal epithelial cells
    • Craig S.W., and Pardo J.V. Alpha actinin localization in the junctional complex of intestinal epithelial cells. J. Cell Biol. 80 (1979) 203-210
    • (1979) J. Cell Biol. , vol.80 , pp. 203-210
    • Craig, S.W.1    Pardo, J.V.2
  • 53
    • 0024509966 scopus 로고
    • Microvillus inclusion disease: An inherited defect of brush border assembly and differentiation
    • Cutz E., Rhoads J.M., Drumm B., Sherman P.M., Durie P.R., and Forstner G.G. Microvillus inclusion disease: An inherited defect of brush border assembly and differentiation. New Eng. J. Med. 320 (1989) 646-651
    • (1989) New Eng. J. Med. , vol.320 , pp. 646-651
    • Cutz, E.1    Rhoads, J.M.2    Drumm, B.3    Sherman, P.M.4    Durie, P.R.5    Forstner, G.G.6
  • 54
    • 0018178824 scopus 로고
    • Familial enteropathy: A syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy
    • Davidson G.P., Cutz E., Hamilton J.R., and Gall D.G. Familial enteropathy: A syndrome of protracted diarrhea from birth, failure to thrive, and hypoplastic villus atrophy. Gastroenterology 75 (1978) 783-790
    • (1978) Gastroenterology , vol.75 , pp. 783-790
    • Davidson, G.P.1    Cutz, E.2    Hamilton, J.R.3    Gall, D.G.4
  • 56
    • 0024510008 scopus 로고
    • Actin cytoskeletal lesions in differentiated human colon carcinoma cells after exposure to soybean agglutinin
    • Draaijer M., Koninkx J., Hendriks H., Kik M., Van Dijk J., and Mouwen J. Actin cytoskeletal lesions in differentiated human colon carcinoma cells after exposure to soybean agglutinin. Biol. Cell 65 (1989) 29-35
    • (1989) Biol. Cell , vol.65 , pp. 29-35
    • Draaijer, M.1    Koninkx, J.2    Hendriks, H.3    Kik, M.4    Van Dijk, J.5    Mouwen, J.6
  • 57
    • 0019309694 scopus 로고
    • Localization of myosin, actin, and tropomyosin in rat intestinal epithelium: Immunohistochemical studies at the light and electron microscope levels
    • Drenckhahn D., and Groschel-Stewart U. Localization of myosin, actin, and tropomyosin in rat intestinal epithelium: Immunohistochemical studies at the light and electron microscope levels. J. Cell Biol. 86 (1980) 475-482
    • (1980) J. Cell Biol. , vol.86 , pp. 475-482
    • Drenckhahn, D.1    Groschel-Stewart, U.2
  • 58
    • 0024078086 scopus 로고
    • Organization of the actin filament cytoskeleton in the intestinal brush border: A quantitative and qualitative immunoelectron microscope study
    • Drenckhahn D., and Dermietzel R. Organization of the actin filament cytoskeleton in the intestinal brush border: A quantitative and qualitative immunoelectron microscope study. J. Cell Biol. 107 (1988) 1037-1048
    • (1988) J. Cell Biol. , vol.107 , pp. 1037-1048
    • Drenckhahn, D.1    Dermietzel, R.2
  • 59
    • 0023179251 scopus 로고
    • Changes in villin synthesis and subcellular distribution during intestinal differentiation of HT29-18 clones
    • Dudouet B., Robine S., Huet C., Sahuquillo-Merino C., Blair L., Coudrier E., and Louvard D. Changes in villin synthesis and subcellular distribution during intestinal differentiation of HT29-18 clones. J. Cell Biol. 105 (1987) 359-369
    • (1987) J. Cell Biol. , vol.105 , pp. 359-369
    • Dudouet, B.1    Robine, S.2    Huet, C.3    Sahuquillo-Merino, C.4    Blair, L.5    Coudrier, E.6    Louvard, D.7
  • 60
    • 0026730042 scopus 로고
    • Identification and characterization of two huge protein components of the brush border cytoskeleton: Evidence for a cellular form of titin
    • Eilertsen K.J., and Keller T.C.S. Identification and characterization of two huge protein components of the brush border cytoskeleton: Evidence for a cellular form of titin. J. Cell Biol. 119 (1992) 549-557
    • (1992) J. Cell Biol. , vol.119 , pp. 549-557
    • Eilertsen, K.J.1    Keller, T.C.S.2
  • 61
    • 0022921941 scopus 로고
    • Colchicine-induced tubular, vesicular and cisternal organelle aggregates in absorbtive cells of the small intestine of the rat. II. Endocytosis studies
    • Ellinger A., and Pavelka M. Colchicine-induced tubular, vesicular and cisternal organelle aggregates in absorbtive cells of the small intestine of the rat. II. Endocytosis studies. Biol. Cell 58 (1986) 31-42
    • (1986) Biol. Cell , vol.58 , pp. 31-42
    • Ellinger, A.1    Pavelka, M.2
  • 63
    • 0024410166 scopus 로고
    • Differential localization of villin and fimbrin during development of the mouse visceral endoderm and intestinal epithelium
    • Ezzell R.M., Chafel M.M., and Matsudaira P.T. Differential localization of villin and fimbrin during development of the mouse visceral endoderm and intestinal epithelium. Development 106 (1989) 407-419
    • (1989) Development , vol.106 , pp. 407-419
    • Ezzell, R.M.1    Chafel, M.M.2    Matsudaira, P.T.3
  • 64
    • 0027933182 scopus 로고
    • Differential regulation of skeletal muscle myosin-II and brush border myosin-I: Enzymology and mechanochemistry by bacterially produced tropomyosins
    • Fanning A.S., Wolenski J.S., Mooseker M.S., and Izant J.G. Differential regulation of skeletal muscle myosin-II and brush border myosin-I: Enzymology and mechanochemistry by bacterially produced tropomyosins. Cell Motil. Cytoskel. 29 (1994) 29-45
    • (1994) Cell Motil. Cytoskel. , vol.29 , pp. 29-45
    • Fanning, A.S.1    Wolenski, J.S.2    Mooseker, M.S.3    Izant, J.G.4
  • 65
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M.G., and Palade G.E. Junctional complexes in various epithelia. J. Cell Biol. 17 (1963) 375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 66
    • 0025289278 scopus 로고
    • Cytoskeletal protein and mRNA accumulation during brush border formation in adult chicken enterocytes
    • Fath K.R., Obenhauf S.D., and Burgess D.R. Cytoskeletal protein and mRNA accumulation during brush border formation in adult chicken enterocytes. Development 109 (1990) 449-459
    • (1990) Development , vol.109 , pp. 449-459
    • Fath, K.R.1    Obenhauf, S.D.2    Burgess, D.R.3
  • 67
    • 85063072504 scopus 로고
    • Association with myosin-I and dynein with Golgi vesicles
    • Fath K., and Burgess D. Association with myosin-I and dynein with Golgi vesicles. Mol. Biol. Cell 3 (1992) 52a
    • (1992) Mol. Biol. Cell , vol.3
    • Fath, K.1    Burgess, D.2
  • 68
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath K.R., and Burgess D.R. Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. J. Cell Biol. 120 (1993) 117-127
    • (1993) J. Cell Biol. , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 71
    • 0025992780 scopus 로고
    • Characterization of interactions of enteropathogenic Escherichia coli 0127:H6 with mammalian cells in vitro
    • Francis C.L., Jerse A.E., Kaper J.B., and Falkow S. Characterization of interactions of enteropathogenic Escherichia coli 0127:H6 with mammalian cells in vitro. J. Infect. Dis. 164 (1991) 693-703
    • (1991) J. Infect. Dis. , vol.164 , pp. 693-703
    • Francis, C.L.1    Jerse, A.E.2    Kaper, J.B.3    Falkow, S.4
  • 72
    • 0025612125 scopus 로고
    • Microinjection of villin into cultured cells induces longlasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling
    • Franck Z., Footer M., and Bretscher A. Microinjection of villin into cultured cells induces longlasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling. J. Cell Biol. 111 (1990) 2475-2485
    • (1990) J. Cell Biol. , vol.111 , pp. 2475-2485
    • Franck, Z.1    Footer, M.2    Bretscher, A.3
  • 74
    • 0024317269 scopus 로고
    • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    • Friederich E., Huet C., Arpin M., and Louvard D. Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Cell 59 (1989) 461-475
    • (1989) Cell , vol.59 , pp. 461-475
    • Friederich, E.1    Huet, C.2    Arpin, M.3    Louvard, D.4
  • 75
    • 0027222064 scopus 로고
    • Villin-induced growth of microvilli is reversibly inhibited by cytochalasin D
    • Friederich E., Kreis T.E., and Louvard D. Villin-induced growth of microvilli is reversibly inhibited by cytochalasin D. J. Cell Sci. 105 (1993) 765-775
    • (1993) J. Cell Sci. , vol.105 , pp. 765-775
    • Friederich, E.1    Kreis, T.E.2    Louvard, D.3
  • 76
    • 0024848148 scopus 로고
    • Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus show that this mechanoenzyme is a member of the myosin-1 family
    • Garcia A., Coudrier E., Carboni J., Anderson J., Vandekerckhove J., Mooseker M., Louvard D., and Arpin M. Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus show that this mechanoenzyme is a member of the myosin-1 family. J. Cell Biol. 109 (1989) 2895-2903
    • (1989) J. Cell Biol. , vol.109 , pp. 2895-2903
    • Garcia, A.1    Coudrier, E.2    Carboni, J.3    Anderson, J.4    Vandekerckhove, J.5    Mooseker, M.6    Louvard, D.7    Arpin, M.8
  • 77
    • 0027548587 scopus 로고
    • Desmosomes and hemidesmosomes
    • Garrod D.R. Desmosomes and hemidesmosomes. Curr. Op. Cell Biol. 5 (1993) 30-40
    • (1993) Curr. Op. Cell Biol. , vol.5 , pp. 30-40
    • Garrod, D.R.1
  • 78
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y., Sherman Y., and Ben-Sasson S.A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119 (1992) 493-501
    • (1992) J. Cell Biol. , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 79
    • 0018757599 scopus 로고
    • Immunocytochemical localization of alpha-actinin in intestinal epithelial cells
    • Geiger B., Tokuyasu K.T., and Singer S.J. Immunocytochemical localization of alpha-actinin in intestinal epithelial cells. Proc. Natl. Acad. Sci. USA 76 (1979) 2833-2837
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2833-2837
    • Geiger, B.1    Tokuyasu, K.T.2    Singer, S.J.3
  • 80
    • 0024791813 scopus 로고
    • 2+/phospholipid-binding proteins
    • 2+/phospholipid-binding proteins. Cell Motil. Cytoskel. 14 (1989) 449-454
    • (1989) Cell Motil. Cytoskel. , vol.14 , pp. 449-454
    • Gerke, V.1
  • 81
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders: Calcium-dependent binding to nonerythroid spectrin and Factin
    • Gerke V., and Weber K. Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders: Calcium-dependent binding to nonerythroid spectrin and Factin. EMBO J. 3 (1984) 227-233
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 82
    • 0025905152 scopus 로고
    • Microtubule organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells
    • Gilbert T., Le Bivic A., Quaroni A., and Rodriguez-Boulan E. Microtubule organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells. J. Cell Biol. 113 (1991) 275-288
    • (1991) J. Cell Biol. , vol.113 , pp. 275-288
    • Gilbert, T.1    Le Bivic, A.2    Quaroni, A.3    Rodriguez-Boulan, E.4
  • 83
    • 0019780969 scopus 로고
    • F-actin binding and bundling and bundling properties of fimbrin, a major cytoskeletal protein of the microvillus core filaments
    • Glenney J.R., Kaulfus P., Matsudaira P., and Weber K. F-actin binding and bundling and bundling properties of fimbrin, a major cytoskeletal protein of the microvillus core filaments. J. Biol. Chem. 256 (1981) 9283-9288
    • (1981) J. Biol. Chem. , vol.256 , pp. 9283-9288
    • Glenney, J.R.1    Kaulfus, P.2    Matsudaira, P.3    Weber, K.4
  • 84
    • 0020562993 scopus 로고
    • Fodrin is the general spectrin-like protein found in most cells whereas spectrin and the TW protein have a restricted distribution
    • Glenney J.R., and Glenney P. Fodrin is the general spectrin-like protein found in most cells whereas spectrin and the TW protein have a restricted distribution. Cell 34 (1983) 503-512
    • (1983) Cell , vol.34 , pp. 503-512
    • Glenney, J.R.1    Glenney, P.2
  • 85
    • 0020507554 scopus 로고
    • The spectrin-related molecule, TW 260/240, cross-links actin bundles of the microvillus rootlets in the brush borders of intestinal epithelial cells
    • Glenney J.R., Glenney P., and Weber K. The spectrin-related molecule, TW 260/240, cross-links actin bundles of the microvillus rootlets in the brush borders of intestinal epithelial cells. J. Cell Biol. 96 (1983) 1491-1496
    • (1983) J. Cell Biol. , vol.96 , pp. 1491-1496
    • Glenney, J.R.1    Glenney, P.2    Weber, K.3
  • 86
    • 0026564844 scopus 로고
    • Functional coupling to brush border creatine kinase imparts a selective energetic advantage to contractile ring myosin in intestinal epithelial cells
    • Gordon P.V., and Keller T.C.S. Functional coupling to brush border creatine kinase imparts a selective energetic advantage to contractile ring myosin in intestinal epithelial cells. Cell Motil. Cytoskel. 21 (1992) 38-44
    • (1992) Cell Motil. Cytoskel. , vol.21 , pp. 38-44
    • Gordon, P.V.1    Keller, T.C.S.2
  • 87
    • 0021362113 scopus 로고
    • The 46,000 dalton tyrosine kinase substrate is widespread, whereas the 36,000 dalton substrate is expressed at high levels in certain rodent tissues
    • Gould K.L., Cooper J.A., and Hunter T. The 46,000 dalton tyrosine kinase substrate is widespread, whereas the 36,000 dalton substrate is expressed at high levels in certain rodent tissues. J. Cell Biol. 98 (1984) 487-497
    • (1984) J. Cell Biol. , vol.98 , pp. 487-497
    • Gould, K.L.1    Cooper, J.A.2    Hunter, T.3
  • 88
    • 0022589111 scopus 로고
    • The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein
    • Gould K.L., Cooper J.A., Bretscher A., and Hunter T. The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein. J. Cell Biol. 102 (1986) 660-669
    • (1986) J. Cell Biol. , vol.102 , pp. 660-669
    • Gould, K.L.1    Cooper, J.A.2    Bretscher, A.3    Hunter, T.4
  • 89
    • 0021332781 scopus 로고
    • Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues
    • Greenberg M.E., Brackenbury R., and Edelman G.M. Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues. J. Cell Biol. 98 (1984) 473-486
    • (1984) J. Cell Biol. , vol.98 , pp. 473-486
    • Greenberg, M.E.1    Brackenbury, R.2    Edelman, G.M.3
  • 90
    • 0023357333 scopus 로고
    • Demonstration of microtubules in the terminal web of mature absorptive cells from the small intestine of the rat
    • Hagen S.J., Allan C.H., and Trier J.S. Demonstration of microtubules in the terminal web of mature absorptive cells from the small intestine of the rat. Cell Tiss. Res. 248 (1987) 709-712
    • (1987) Cell Tiss. Res. , vol.248 , pp. 709-712
    • Hagen, S.J.1    Allan, C.H.2    Trier, J.S.3
  • 91
    • 0025769919 scopus 로고
    • The secretion-stimulated 80K phosphoprotein of parietal cell is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli
    • Hanzel D., Reggio H., Bretscher A., Forte J.G., and Mangeat P. The secretion-stimulated 80K phosphoprotein of parietal cell is ezrin, and has properties of a membrane cytoskeletal linker in the induced apical microvilli. EMBO J. 10 (1991) 2363-2373
    • (1991) EMBO J. , vol.10 , pp. 2363-2373
    • Hanzel, D.1    Reggio, H.2    Bretscher, A.3    Forte, J.G.4    Mangeat, P.5
  • 92
    • 0024333549 scopus 로고
    • Expression of actin isoforms in developing rat intestinal epithelium
    • Hartman A.L., Sawtell N.M., and Lessard J.L. Expression of actin isoforms in developing rat intestinal epithelium. J. Histochem. Cytochem. 37 (1989) 1225-1233
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1225-1233
    • Hartman, A.L.1    Sawtell, N.M.2    Lessard, J.L.3
  • 93
    • 0027993176 scopus 로고
    • Porcine myosin-VI: Characterization of a new mammalian unconventional myosin
    • Hasson T.B., and Mooseker M.S. Porcine myosin-VI: Characterization of a new mammalian unconventional myosin. J. Cell Biol. 127 (1994) 425-440
    • (1994) J. Cell Biol. , vol.127 , pp. 425-440
    • Hasson, T.B.1    Mooseker, M.S.2
  • 94
    • 0025365190 scopus 로고
    • Binding of brush border myosin-1 to phospholipid vesicles
    • Hayden S.M., Wolenski J.S., and Mooseker M.S. Binding of brush border myosin-1 to phospholipid vesicles. J. Cell Biol. 111 (1990) 443-451
    • (1990) J. Cell Biol. , vol.111 , pp. 443-451
    • Hayden, S.M.1    Wolenski, J.S.2    Mooseker, M.S.3
  • 95
    • 0024204607 scopus 로고
    • Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers
    • Hecht G., Pothoulakis C., LaMont J.T., and Madara J.L. Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers. J. Clin. Invest. 82 (1988) 1516-1524
    • (1988) J. Clin. Invest. , vol.82 , pp. 1516-1524
    • Hecht, G.1    Pothoulakis, C.2    LaMont, J.T.3    Madara, J.L.4
  • 96
    • 0025055579 scopus 로고
    • Assembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine
    • Heintzelman M.B., and Mooseker M.S. Assembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine. Cell Motil. Cytoskel. 15 (1990) 12-22
    • (1990) Cell Motil. Cytoskel. , vol.15 , pp. 12-22
    • Heintzelman, M.B.1    Mooseker, M.S.2
  • 97
    • 0025293087 scopus 로고
    • Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo
    • Heintzelman M.B., and Mooseker M.S. Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo. Differentiation 43 (1990) 175-182
    • (1990) Differentiation , vol.43 , pp. 175-182
    • Heintzelman, M.B.1    Mooseker, M.S.2
  • 98
    • 0026472782 scopus 로고
    • Assembly of the intestinal brush border cytoskeleton
    • Heintzelman M.B., and Mooseker M.S. Assembly of the intestinal brush border cytoskeleton. Curr. Topics Dev. Biol. 26 (1992) 93-122
    • (1992) Curr. Topics Dev. Biol. , vol.26 , pp. 93-122
    • Heintzelman, M.B.1    Mooseker, M.S.2
  • 99
    • 0028569487 scopus 로고
    • Multiple unconventional myosin domains of the intestinal brush border cytoskeleton
    • Heintzelman M.B., Hasson T., and Mooseker M.S. Multiple unconventional myosin domains of the intestinal brush border cytoskeleton. J. Cell Sci. 107 (1994) 3535-3543
    • (1994) J. Cell Sci. , vol.107 , pp. 3535-3543
    • Heintzelman, M.B.1    Hasson, T.2    Mooseker, M.S.3
  • 102
    • 0019975040 scopus 로고
    • The organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells
    • Hirokawa N., Tilney L.G., Fujiwara K., and Heuser J.E. The organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells. J. Cell Biol. 94 (1982) 425-443
    • (1982) J. Cell Biol. , vol.94 , pp. 425-443
    • Hirokawa, N.1    Tilney, L.G.2    Fujiwara, K.3    Heuser, J.E.4
  • 103
    • 0020966680 scopus 로고
    • Mechanism of brush border contractility studied by the quick-freeze-deep-etch method
    • Hirokawa N., Keller T.C.S., Chasen R., and Mooseker M.S. Mechanism of brush border contractility studied by the quick-freeze-deep-etch method. J. Cell Biol. 96 (1983) 1325-1336
    • (1983) J. Cell Biol. , vol.96 , pp. 1325-1336
    • Hirokawa, N.1    Keller, T.C.S.2    Chasen, R.3    Mooseker, M.S.4
  • 104
    • 0020728714 scopus 로고
    • Location of a protein of the fodrin-spectrin-TW 260/240 family in the mouse intestinal brush border
    • Hirokawa N., Cheney R.E., and Willard M. Location of a protein of the fodrin-spectrin-TW 260/240 family in the mouse intestinal brush border. Cell 32 (1983) 953-965
    • (1983) Cell , vol.32 , pp. 953-965
    • Hirokawa, N.1    Cheney, R.E.2    Willard, M.3
  • 105
    • 0027244276 scopus 로고
    • The 100 kDa F-actin capping protein of Dictyostelium is a villin prototype ("protovillin")
    • Hofman A., Noegel A.A., Bomblies L., Lottspeich F., and Schleicher M. The 100 kDa F-actin capping protein of Dictyostelium is a villin prototype ("protovillin"). FEBS Lett. 328 (1993) 71-76
    • (1993) FEBS Lett. , vol.328 , pp. 71-76
    • Hofman, A.1    Noegel, A.A.2    Bomblies, L.3    Lottspeich, F.4    Schleicher, M.5
  • 106
    • 0023665165 scopus 로고
    • Identification of a new type of mammalian myosin heavy chain by molecular cloning
    • Hoshimaru M., and Nakanishi S. Identification of a new type of mammalian myosin heavy chain by molecular cloning. J. Biol. Chem. 262 (1987) 14625-14632
    • (1987) J. Biol. Chem. , vol.262 , pp. 14625-14632
    • Hoshimaru, M.1    Nakanishi, S.2
  • 107
    • 0020636102 scopus 로고
    • Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells
    • Howe C.L., and Mooseker M.S. Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells. J. Cell Biol. 97 (1983) 974-985
    • (1983) J. Cell Biol. , vol.97 , pp. 974-985
    • Howe, C.L.1    Mooseker, M.S.2
  • 108
    • 0023202014 scopus 로고
    • Absorbtive and mucus-secreting subclones isolated from a multipotent intestinal cell line (HT-29) provide new models for cell polarity and terminal differentiation
    • Huet C., Sahuquillo-Merino C., Coudrier E., and Louvard D. Absorbtive and mucus-secreting subclones isolated from a multipotent intestinal cell line (HT-29) provide new models for cell polarity and terminal differentiation. J. Cell Biol. 105 (1987) 345-357
    • (1987) J. Cell Biol. , vol.105 , pp. 345-357
    • Huet, C.1    Sahuquillo-Merino, C.2    Coudrier, E.3    Louvard, D.4
  • 109
    • 0018411023 scopus 로고
    • The terminal web. A re-evaluation of its structure and function
    • Hull B.E., and Staehelin L.A. The terminal web. A re-evaluation of its structure and function. J. Cell Biol. 81 (1979) 67-82
    • (1979) J. Cell Biol. , vol.81 , pp. 67-82
    • Hull, B.E.1    Staehelin, L.A.2
  • 110
    • 0020368721 scopus 로고
    • ++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction
    • ++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction. J. Cell Biol. 95 (1982) 943-959
    • (1982) J. Cell Biol. , vol.95 , pp. 943-959
    • Keller, T.C.S.1    Mooseker, M.S.2
  • 111
    • 0021907521 scopus 로고
    • The role of myosin in terminal web contraction in isolated intestinal epithelial brush borders
    • Keller T.C.S., Conzelman K.A., Chasan R., and Mooseker M.S. The role of myosin in terminal web contraction in isolated intestinal epithelial brush borders. J. Cell Biol. 100 (1985) 1647-1655
    • (1985) J. Cell Biol. , vol.100 , pp. 1647-1655
    • Keller, T.C.S.1    Conzelman, K.A.2    Chasan, R.3    Mooseker, M.S.4
  • 112
    • 0025821188 scopus 로고
    • Discrete subcellular localization of a cytoplasmic and a mitochondrial isozyme of creatine kinase in intestinal epithelial cells
    • Keller T.C.S., and Gordon P.V. Discrete subcellular localization of a cytoplasmic and a mitochondrial isozyme of creatine kinase in intestinal epithelial cells. Cell Motil. Cytoskel. 19 (1991) 169-179
    • (1991) Cell Motil. Cytoskel. , vol.19 , pp. 169-179
    • Keller, T.C.S.1    Gordon, P.V.2
  • 113
    • 0026475396 scopus 로고
    • An unconventional myosin heavy chain gene from Drosophila melanogaster
    • Kellerman K.A., and Miller K.G. An unconventional myosin heavy chain gene from Drosophila melanogaster. J. Cell Biol. 119 (1992) 823-834
    • (1992) J. Cell Biol. , vol.119 , pp. 823-834
    • Kellerman, K.A.1    Miller, K.G.2
  • 114
    • 0024565478 scopus 로고
    • Actin accumulation at sites of bacterial adhesion to tissue culture cells: Basis of a new diagnostic test for enteropathogenic and enterohemorrhagic Escherichia coli
    • Knutton S., Baldwin T., Williams P.H., and McNeish A.S. Actin accumulation at sites of bacterial adhesion to tissue culture cells: Basis of a new diagnostic test for enteropathogenic and enterohemorrhagic Escherichia coli. Infect. Immun. 57 (1989) 1290-1298
    • (1989) Infect. Immun. , vol.57 , pp. 1290-1298
    • Knutton, S.1    Baldwin, T.2    Williams, P.H.3    McNeish, A.S.4
  • 115
    • 0015337184 scopus 로고
    • Transient shortening of microvilli induced by cycloheximide in the duodenal epithelium of the chicken
    • Lecount T.S., and Grey R.D. Transient shortening of microvilli induced by cycloheximide in the duodenal epithelium of the chicken. J. Cell Biol. 53 (1972) 601-605
    • (1972) J. Cell Biol. , vol.53 , pp. 601-605
    • Lecount, T.S.1    Grey, R.D.2
  • 116
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller J.P., and Helfman D.M. The molecular basis for tropomyosin isoform diversity. BioEssays 13 (1991) 429-437
    • (1991) BioEssays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 117
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard J.L. Two monoclonal antibodies to actin: One muscle selective and one generally reactive. Cell Motil. Cytoskel. 10 (1988) 349-362
    • (1988) Cell Motil. Cytoskel. , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 118
    • 0024362690 scopus 로고
    • The function of the major cytoskeletal components of the brush border
    • Louvard D. The function of the major cytoskeletal components of the brush border. Curr. Opin. Cell Biol. 1 (1989) 51-57
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 51-57
    • Louvard, D.1
  • 119
    • 0026685853 scopus 로고
    • The differentiating intestinal epithelial cell: Establishment and maintenance of functions through interactions between cellular structures
    • Louvard D., Kedinger M., and Hauri H.P. The differentiating intestinal epithelial cell: Establishment and maintenance of functions through interactions between cellular structures. Ann. Rev. Cell Biol. 8 (1992) 157-195
    • (1992) Ann. Rev. Cell Biol. , vol.8 , pp. 157-195
    • Louvard, D.1    Kedinger, M.2    Hauri, H.P.3
  • 120
    • 0020582481 scopus 로고
    • Increases in guinea pig small intestinal transepithelial resistance induced by osmotic loads are accompanied by rapid alterations in absorptive-cell tight junction structure
    • Madara J.L. Increases in guinea pig small intestinal transepithelial resistance induced by osmotic loads are accompanied by rapid alterations in absorptive-cell tight junction structure. J. Cell Biol. 97 (1983) 125-136
    • (1983) J. Cell Biol. , vol.97 , pp. 125-136
    • Madara, J.L.1
  • 121
    • 0023176321 scopus 로고
    • Intestinal absorbtive cell tight junctions are linked to cytoskeleton
    • Madara J.L. Intestinal absorbtive cell tight junctions are linked to cytoskeleton. Am. J. Phys. 253 (1987) C171-C175
    • (1987) Am. J. Phys. , vol.253
    • Madara, J.L.1
  • 122
    • 0025286406 scopus 로고
    • Maintenance of the macromolecular barrier at cell extrusions sites in intestinal epithelium: Physiological rearrangement of tight junctions
    • Madara J.L. Maintenance of the macromolecular barrier at cell extrusions sites in intestinal epithelium: Physiological rearrangement of tight junctions. J. Memb. Biol. 116 (1990) 177-184
    • (1990) J. Memb. Biol. , vol.116 , pp. 177-184
    • Madara, J.L.1
  • 123
    • 0022451875 scopus 로고
    • Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity
    • Madara J.L., Barenberg D., and Carlson S. Effects of cytochalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity. J. Cell Biol. 102 (1986) 2125-2136
    • (1986) J. Cell Biol. , vol.102 , pp. 2125-2136
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 124
    • 0023631266 scopus 로고
    • Alteration of intestinal tight junction structure and permeability by cytoskeletal contraction
    • Madara J.L., Moore R., and Carlson S. Alteration of intestinal tight junction structure and permeability by cytoskeletal contraction. Am. J. Phys. 253 (1987) C854-C861
    • (1987) Am. J. Phys. , vol.253
    • Madara, J.L.1    Moore, R.2    Carlson, S.3
  • 125
    • 0023887063 scopus 로고
    • Tyrosine phosphorylated proteins in different tissues during chick embryo development
    • Maher P.A., and Pasquale E.B. Tyrosine phosphorylated proteins in different tissues during chick embryo development. J. Cell Biol. 106 (1988) 1747-1755
    • (1988) J. Cell Biol. , vol.106 , pp. 1747-1755
    • Maher, P.A.1    Pasquale, E.B.2
  • 127
    • 0026598934 scopus 로고
    • Intestinal epithelial cell protein phosphorylation in enteropathogenic Escherichia coli diarrhoea
    • Manjarrez-Hernandez H.A., Baldwin T.J., Aitken A., Knutton S., and Williams P.H. Intestinal epithelial cell protein phosphorylation in enteropathogenic Escherichia coli diarrhoea. Lancet 339 (1992) 521-523
    • (1992) Lancet , vol.339 , pp. 521-523
    • Manjarrez-Hernandez, H.A.1    Baldwin, T.J.2    Aitken, A.3    Knutton, S.4    Williams, P.H.5
  • 128
    • 0026452888 scopus 로고
    • Actin cables and epidermal movement in embryonic wound healing
    • Martin P., and Lewis J. Actin cables and epidermal movement in embryonic wound healing. Nature 360 (1992) 179-183
    • (1992) Nature , vol.360 , pp. 179-183
    • Martin, P.1    Lewis, J.2
  • 129
    • 0018578513 scopus 로고
    • Identification and organization of the components of the isolated microvillus cytoskeleton
    • Matsudaira P., and Burgess D.R. Identification and organization of the components of the isolated microvillus cytoskeleton. J. Cell Biol. 83 (1979) 667-673
    • (1979) J. Cell Biol. , vol.83 , pp. 667-673
    • Matsudaira, P.1    Burgess, D.R.2
  • 130
    • 0020655456 scopus 로고
    • Role of fimbrin and villin in determining the interfilament distances of actin bundles
    • Matsudaira P., Mandelkow E., Renner W., Hesterberg L.K., and Weber K. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Nature 301 (1983) 209-214
    • (1983) Nature , vol.301 , pp. 209-214
    • Matsudaira, P.1    Mandelkow, E.2    Renner, W.3    Hesterberg, L.K.4    Weber, K.5
  • 132
    • 0024119220 scopus 로고
    • Villin expression in the visceral endoderm and in the gut anlage during early embryogenesis
    • Maunoury R., Robine S., Pringault E., Huet C., Guenet J.L., Gaillard J.A., and Louvard D. Villin expression in the visceral endoderm and in the gut anlage during early embryogenesis. EMBO J. 7 (1988) 3321-3329
    • (1988) EMBO J. , vol.7 , pp. 3321-3329
    • Maunoury, R.1    Robine, S.2    Pringault, E.3    Huet, C.4    Guenet, J.L.5    Gaillard, J.A.6    Louvard, D.7
  • 133
    • 85063072553 scopus 로고
    • Migration of IEC-6 cells: A model for mucosal healing
    • McCormack S.A., Viar M.J., and Johnson L.R. Migration of IEC-6 cells: A model for mucosal healing. Am. J. Physiol. 257 (1992) G274-G283
    • (1992) Am. J. Physiol. , vol.257
    • McCormack, S.A.1    Viar, M.J.2    Johnson, L.R.3
  • 134
    • 0027317966 scopus 로고
    • Cellular and molecular adaptations to injurious mechanical stress
    • McNeii P.L. Cellular and molecular adaptations to injurious mechanical stress. Trends Cell Biol. 3 (1993) 302-307
    • (1993) Trends Cell Biol. , vol.3 , pp. 302-307
    • McNeii, P.L.1
  • 135
    • 0024602753 scopus 로고
    • Gastrointestinal cell plasma membrane wounding and resealing in vivo
    • McNeil P.L., and Ito S. Gastrointestinal cell plasma membrane wounding and resealing in vivo. Gastroenterology 96 (1989) 1238-1248
    • (1989) Gastroenterology , vol.96 , pp. 1238-1248
    • McNeil, P.L.1    Ito, S.2
  • 136
    • 0019194079 scopus 로고
    • Intestinal microvilli: Responses to feeding and fasting
    • Misch D.W., Giebel P.E., and Faust R.G. Intestinal microvilli: Responses to feeding and fasting. Eur. J. Cell Biol. 21 (1980) 269-279
    • (1980) Eur. J. Cell Biol. , vol.21 , pp. 269-279
    • Misch, D.W.1    Giebel, P.E.2    Faust, R.G.3
  • 137
    • 0024554192 scopus 로고
    • Rapid restitution in an in vitro model of intestinal epithelial injury
    • Moore R., Carlson S., and Madara J.L. Rapid restitution in an in vitro model of intestinal epithelial injury. Lab. Invest. 60 (1989) 237-244
    • (1989) Lab. Invest. , vol.60 , pp. 237-244
    • Moore, R.1    Carlson, S.2    Madara, J.L.3
  • 138
    • 0024426122 scopus 로고
    • Villus contraction aids repair of intestinal epithelium after injury
    • (Gastrointest. Liver Physiol. 20)
    • (Gastrointest. Liver Physiol. 20). Moore R., Carlson S., and Madara J.L. Villus contraction aids repair of intestinal epithelium after injury. Am. J. Physiol. 257 (1989) G274-G283
    • (1989) Am. J. Physiol. , vol.257
    • Moore, R.1    Carlson, S.2    Madara, J.L.3
  • 139
    • 0017135416 scopus 로고
    • Brush border motility, Microvillar contraction in triton-treated brush borders isolated from intestinal epithelium
    • Mooseker M.S. Brush border motility, Microvillar contraction in triton-treated brush borders isolated from intestinal epithelium. J. Cell Biol. 71 (1976) 417-432
    • (1976) J. Cell Biol. , vol.71 , pp. 417-432
    • Mooseker, M.S.1
  • 140
    • 0022172245 scopus 로고
    • Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker M.S. Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Ann. Rev. Cell Biol. 1 (1985) 209-241
    • (1985) Ann. Rev. Cell Biol. , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 141
    • 0344914021 scopus 로고
    • A multitude of myosins
    • Mooseker M.S. A multitude of myosins. Curr. Biol. 3 (1993) 245-248
    • (1993) Curr. Biol. , vol.3 , pp. 245-248
    • Mooseker, M.S.1
  • 142
    • 0016776375 scopus 로고
    • Organization of an actin filament-membrane complex. Filament polarity and membrane attachment of the microvilli of intestinal epithelial cells
    • Mooseker M.S., and Tilney L.G. Organization of an actin filament-membrane complex. Filament polarity and membrane attachment of the microvilli of intestinal epithelial cells. J. Cell Biol. 67 (1975) 725-743
    • (1975) J. Cell Biol. , vol.67 , pp. 725-743
    • Mooseker, M.S.1    Tilney, L.G.2
  • 143
    • 0018094857 scopus 로고
    • Characterization and localization of myosin in the brush border of intestinal epithelial cells
    • Mooseker M.S., Pollard T.D., and Fujiwara K. Characterization and localization of myosin in the brush border of intestinal epithelial cells. J. Cell Biol. 79 (1978) 444-453
    • (1978) J. Cell Biol. , vol.79 , pp. 444-453
    • Mooseker, M.S.1    Pollard, T.D.2    Fujiwara, K.3
  • 145
    • 0020440480 scopus 로고
    • Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border
    • Mooseker M.S., Pollard T.D., and Wharton K.A. Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border. J. Cell Biol. 95 (1982) 222-233
    • (1982) J. Cell Biol. , vol.95 , pp. 222-233
    • Mooseker, M.S.1    Pollard, T.D.2    Wharton, K.A.3
  • 147
    • 0024312342 scopus 로고
    • The 110-kD protein calmodulin complex of the intestinal microvillus (brush border myosin-I) is a mechanoenzyme
    • Mooseker M.S., and Coleman T.R. The 110-kD protein calmodulin complex of the intestinal microvillus (brush border myosin-I) is a mechanoenzyme. J. Cell Biol. 108 (1989) 2395-2400
    • (1989) J. Cell Biol. , vol.108 , pp. 2395-2400
    • Mooseker, M.S.1    Coleman, T.R.2
  • 148
    • 0024417596 scopus 로고
    • Characterization of intestinal microvillar membrane discs: Detergent-resistant membrane sheets enriched in associated brush border myosin-1 (110K-calmodulin)
    • Mooseker M.S., Conzelman K.A., Coleman T.R., Heuser J.E., and Sheetz M.P. Characterization of intestinal microvillar membrane discs: Detergent-resistant membrane sheets enriched in associated brush border myosin-1 (110K-calmodulin). J. Cell Biol. 109 (1989) 1153-1161
    • (1989) J. Cell Biol. , vol.109 , pp. 1153-1161
    • Mooseker, M.S.1    Conzelman, K.A.2    Coleman, T.R.3    Heuser, J.E.4    Sheetz, M.P.5
  • 149
    • 0023942168 scopus 로고
    • Distribution of actin, vinculin, and fibronectin in the duodenum of developing chick embryos: Immunohistochemical studies at the light microscopic level
    • Noda S., and Mitsui T. Distribution of actin, vinculin, and fibronectin in the duodenum of developing chick embryos: Immunohistochemical studies at the light microscopic level. Dev. Growth Differ. 30 (1988) 271-282
    • (1988) Dev. Growth Differ. , vol.30 , pp. 271-282
    • Noda, S.1    Mitsui, T.2
  • 150
    • 0026691975 scopus 로고
    • Intestinal epithelial restitution. Characterization of a cell culture model and mapping of cytoskeletal elements in migrating cells
    • Nusrat A., Delp C., and Madara J.L. Intestinal epithelial restitution. Characterization of a cell culture model and mapping of cytoskeletal elements in migrating cells. J. Clin. Invest. 89 (1992) 1501-1511
    • (1992) J. Clin. Invest. , vol.89 , pp. 1501-1511
    • Nusrat, A.1    Delp, C.2    Madara, J.L.3
  • 152
    • 0020355745 scopus 로고
    • Localization of Z-protein in isolated Z-disk sheets of chicken leg muscle
    • Ohashi K., Mikawa T., and Maruyama K. Localization of Z-protein in isolated Z-disk sheets of chicken leg muscle. J. Cell Biol. 95 (1982) 85-90
    • (1982) J. Cell Biol. , vol.95 , pp. 85-90
    • Ohashi, K.1    Mikawa, T.2    Maruyama, K.3
  • 153
    • 0024390191 scopus 로고
    • Z-protein, a component of the skeletal muscle Z-line, is located at the apical tips of microvilli of chicken intestinal epithelial cells
    • Maruyama K. Z-protein, a component of the skeletal muscle Z-line, is located at the apical tips of microvilli of chicken intestinal epithelial cells. J. Biochem. (Tokyo) 106 (1989) 115-118
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 115-118
    • Maruyama, K.1
  • 154
    • 78651158366 scopus 로고
    • Fine structure of cell surface specializations in the maturing duodenal mucosa of the chick
    • Overton J., and Shoup J. Fine structure of cell surface specializations in the maturing duodenal mucosa of the chick. J. Cell Bio. 21 (1964) 75-85
    • (1964) J. Cell Bio. , vol.21 , pp. 75-85
    • Overton, J.1    Shoup, J.2
  • 155
    • 0020964151 scopus 로고
    • Effect of colchicine on rat small intestinal absorptive cells. I. Formation of basolateral microvillus borders
    • Pavelka M., Ellinger A., and Gangl A. Effect of colchicine on rat small intestinal absorptive cells. I. Formation of basolateral microvillus borders. J. Ultrastr. Res. 85 (1983) 249-259
    • (1983) J. Ultrastr. Res. , vol.85 , pp. 249-259
    • Pavelka, M.1    Ellinger, A.2    Gangl, A.3
  • 156
    • 0021351776 scopus 로고
    • Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin
    • Pearl M., Fishkind D., Mooseker M.S., Keene D., and Keller T.C.S. Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin. J. Cell Biol. 98 (1984) 66-78
    • (1984) J. Cell Biol. , vol.98 , pp. 66-78
    • Pearl, M.1    Fishkind, D.2    Mooseker, M.S.3    Keene, D.4    Keller, T.C.S.5
  • 157
    • 0026755585 scopus 로고
    • BBe clones of the human intestinal cell line, Caco-2
    • BBe clones of the human intestinal cell line, Caco-2. J. Cell Sci. 102 (1992) 581-600
    • (1992) J. Cell Sci. , vol.102 , pp. 581-600
    • Peterson, M.D.1    Mooseker, M.S.2
  • 160
    • 0020379671 scopus 로고
    • Enterocytic differentiation of cultured human colon cancer cells by replacement of glucose by galactose in the medium
    • Pinto M., Appay M.D., Simon-Assmann P., Chevalier G., Dracopoli N., Fogh J., and Zweibaum A. Enterocytic differentiation of cultured human colon cancer cells by replacement of glucose by galactose in the medium. Biol. Cell 44 (1982) 193-196
    • (1982) Biol. Cell , vol.44 , pp. 193-196
    • Pinto, M.1    Appay, M.D.2    Simon-Assmann, P.3    Chevalier, G.4    Dracopoli, N.5    Fogh, J.6    Zweibaum, A.7
  • 163
    • 0025951847 scopus 로고
    • Keratin expression in rat intestinal crypt and villus cells
    • Quaroni A., Calnek D., Quaroni E., and Chandler J.S. Keratin expression in rat intestinal crypt and villus cells. J. Biol. Chem. 266 (1991) 11923-11931
    • (1991) J. Biol. Chem. , vol.266 , pp. 11923-11931
    • Quaroni, A.1    Calnek, D.2    Quaroni, E.3    Chandler, J.S.4
  • 164
    • 0026332515 scopus 로고
    • A sialoglycoprotein complex linked to the microvillus cytoskeleton acts as a receptor for pilus (AF/RI) mediated adhesion of enteropathogenic Escherichia coli (RDEC-1) in rabbit small intestine
    • Rafiee P., Leffler H., Byrd J.C., Cassels F.J., Boedeker E.C., and Kim Y.S. A sialoglycoprotein complex linked to the microvillus cytoskeleton acts as a receptor for pilus (AF/RI) mediated adhesion of enteropathogenic Escherichia coli (RDEC-1) in rabbit small intestine. J. Cell Biol. 115 (1991) 1021-1029
    • (1991) J. Cell Biol. , vol.115 , pp. 1021-1029
    • Rafiee, P.1    Leffler, H.2    Byrd, J.C.3    Cassels, F.J.4    Boedeker, E.C.5    Kim, Y.S.6
  • 166
    • 0027229524 scopus 로고
    • Apical orientation of the microtubule organizing center and associated gamma-tubulin during the polarization of the retinal pigment epithelium in vivo
    • Rizzolo L.J., and Joshi H.C. Apical orientation of the microtubule organizing center and associated gamma-tubulin during the polarization of the retinal pigment epithelium in vivo. Dev. Biol. 157 (1993) 147-156
    • (1993) Dev. Biol. , vol.157 , pp. 147-156
    • Rizzolo, L.J.1    Joshi, H.C.2
  • 168
    • 0017087507 scopus 로고
    • Contraction of isolated brush borders from the intestinal epithelium
    • Rodewald R., Newman S.B., and Karnovsky M.J. Contraction of isolated brush borders from the intestinal epithelium. J. Cell Biol. 70 (1976) 541-554
    • (1976) J. Cell Biol. , vol.70 , pp. 541-554
    • Rodewald, R.1    Newman, S.B.2    Karnovsky, M.J.3
  • 170
    • 0026733626 scopus 로고
    • Signal transduction between enteropathogenic Escherichia coli and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake
    • Rosenshine I., Donnenberg M.S., Kaper J.B., and Finlay B.B. Signal transduction between enteropathogenic Escherichia coli and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake. EMBO J. 11 (1992) 3551-3560
    • (1992) EMBO J. , vol.11 , pp. 3551-3560
    • Rosenshine, I.1    Donnenberg, M.S.2    Kaper, J.B.3    Finlay, B.B.4
  • 171
    • 0027352270 scopus 로고
    • Exploitation of host signal transduction pathways and cytoskeletal functions by invasive bacteria
    • Rosenshine I., and Finlay B.B. Exploitation of host signal transduction pathways and cytoskeletal functions by invasive bacteria. Bioessays 15 (1993) 17-24
    • (1993) Bioessays , vol.15 , pp. 17-24
    • Rosenshine, I.1    Finlay, B.B.2
  • 172
    • 0019991952 scopus 로고
    • A clinicopathologic study of enterocyte-adherent Escherichia coli: A cause of protracted diarrhea in infants
    • Rothbaum R., McAdams A.J., Giannella R., and Partin J.C. A clinicopathologic study of enterocyte-adherent Escherichia coli: A cause of protracted diarrhea in infants. Gastroenterology 83 (1982) 441-454
    • (1982) Gastroenterology , vol.83 , pp. 441-454
    • Rothbaum, R.1    McAdams, A.J.2    Giannella, R.3    Partin, J.C.4
  • 173
    • 0022609508 scopus 로고
    • Distribution of microtubules within the intestinal terminal web as revealed by quick-freezing and cryosubstitution
    • Sandoz D., and Laine M.-C. Distribution of microtubules within the intestinal terminal web as revealed by quick-freezing and cryosubstitution. Eur. J. Cell Biol. 39 (1985) 481-484
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 481-484
    • Sandoz, D.1    Laine, M.-C.2
  • 174
    • 0024209184 scopus 로고
    • Unique isoactins in the brush border of rat intestinal epithelial cells
    • Sawtell N.M., Hartman A.L., and Lessard J.L. Unique isoactins in the brush border of rat intestinal epithelial cells. Cell Motil. Cytoskel. 11 (1988) 318-325
    • (1988) Cell Motil. Cytoskel. , vol.11 , pp. 318-325
    • Sawtell, N.M.1    Hartman, A.L.2    Lessard, J.L.3
  • 175
    • 0026772439 scopus 로고
    • Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation
    • Schafer D.A., Mooseker M.S., and Cooper J.A. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. J. Cell Biol. 118 (1992) 335-346
    • (1992) J. Cell Biol. , vol.118 , pp. 335-346
    • Schafer, D.A.1    Mooseker, M.S.2    Cooper, J.A.3
  • 176
    • 0023376195 scopus 로고
    • Assembly of the intestinal brush border: Appearance and redistribution of microvillar core proteins in developing chick enterocytes
    • Shibayama T., Carboni J.M., and Mooseker M.S. Assembly of the intestinal brush border: Appearance and redistribution of microvillar core proteins in developing chick enterocytes. J. Cell Biol. 105 (1987) 335-344
    • (1987) J. Cell Biol. , vol.105 , pp. 335-344
    • Shibayama, T.1    Carboni, J.M.2    Mooseker, M.S.3
  • 178
    • 0021360017 scopus 로고
    • The brush border cytoskeleton is not static: In vivo turnover of proteins
    • Stidwell R.P., Wysolmerski T., and Burgess D.R. The brush border cytoskeleton is not static: In vivo turnover of proteins. J. Cell Biol. 98 (1984) 641-645
    • (1984) J. Cell Biol. , vol.98 , pp. 641-645
    • Stidwell, R.P.1    Wysolmerski, T.2    Burgess, D.R.3
  • 179
    • 0022614143 scopus 로고
    • Regulation of intestinal brush border microvillus length during development by the G- to F-actin ratio
    • Stidwell R.P., and Burgess D.R. Regulation of intestinal brush border microvillus length during development by the G- to F-actin ratio. Dev. Biol. 114 (1986) 381-388
    • (1986) Dev. Biol. , vol.114 , pp. 381-388
    • Stidwell, R.P.1    Burgess, D.R.2
  • 182
    • 0025924752 scopus 로고
    • 2+-ATPase activity of brush border myosin-I with three or four calmodulin light chains but inhibits with less than two bound
    • 2+-ATPase activity of brush border myosin-I with three or four calmodulin light chains but inhibits with less than two bound. J. Biol. Chem. 266 (1991) 1312-1319
    • (1991) J. Biol. Chem. , vol.266 , pp. 1312-1319
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 183
    • 0023892929 scopus 로고
    • Phosphotyrosine-modified proteins are concentrated at the membranes of epithelial and endothelial cells during tissue development in chick embryos
    • Takata K., and Singer S.J. Phosphotyrosine-modified proteins are concentrated at the membranes of epithelial and endothelial cells during tissue development in chick embryos. J. Cell Biol. 106 (1988) 1757-1764
    • (1988) J. Cell Biol. , vol.106 , pp. 1757-1764
    • Takata, K.1    Singer, S.J.2
  • 184
    • 0023820064 scopus 로고
    • Developmental organization of the intestinal brush border cytoskeleton
    • Takemura R., Masaki T., and Hirokawa N. Developmental organization of the intestinal brush border cytoskeleton. Cell Motil. Cytoskel. 9 (1988) 299-311
    • (1988) Cell Motil. Cytoskel. , vol.9 , pp. 299-311
    • Takemura, R.1    Masaki, T.2    Hirokawa, N.3
  • 185
    • 0026509182 scopus 로고
    • The upright position of brush border type microvilli depends on myosin filaments
    • Temm-Grove C., Helbing D., Wiegand C., Honer B., and Jockusch B.M. The upright position of brush border type microvilli depends on myosin filaments. J. Cell Sci. 101 (1992) 599-610
    • (1992) J. Cell Sci. , vol.101 , pp. 599-610
    • Temm-Grove, C.1    Helbing, D.2    Wiegand, C.3    Honer, B.4    Jockusch, B.M.5
  • 186
    • 0015131317 scopus 로고
    • Actin in the brush-border of epithelial cells of the chicken intestine
    • Tilney L.G., and Mooseker M.S. Actin in the brush-border of epithelial cells of the chicken intestine. Proc. Natl. Acad. Sci. USA 68 (1971) 2611-2615
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2611-2615
    • Tilney, L.G.1    Mooseker, M.S.2
  • 187
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick J. Elastic filaments and giant proteins in muscle. Curr. Op. Cell Biol. 3 (1991) 112-119
    • (1991) Curr. Op. Cell Biol. , vol.3 , pp. 112-119
    • Trinick, J.1
  • 188
    • 0024094695 scopus 로고
    • The unusual microtubule polarity in teleost retinal pigment epithelial cells
    • Troutt L.L., and Burnside B. The unusual microtubule polarity in teleost retinal pigment epithelial cells. J. Cell Biol. 107 (1988) 1461-1464
    • (1988) J. Cell Biol. , vol.107 , pp. 1461-1464
    • Troutt, L.L.1    Burnside, B.2
  • 189
    • 0024561065 scopus 로고
    • Isolation of cell-to-cell adherers junctions from rat liver
    • Tsukita S., and Tsukita S. Isolation of cell-to-cell adherers junctions from rat liver. J. Cell Biol. 108 (1989) 31-41
    • (1989) J. Cell Biol. , vol.108 , pp. 31-41
    • Tsukita, S.1    Tsukita, S.2
  • 190
    • 0024785788 scopus 로고
    • A new 400 kD protein from isolated adherers junctions: Its localization at the undercoat of adherers junctions and at microfilament bundles such as stress fibers and circumferential bundles
    • Tsukita S., Itoh M., and Tsukita S. A new 400 kD protein from isolated adherers junctions: Its localization at the undercoat of adherers junctions and at microfilament bundles such as stress fibers and circumferential bundles. J. Cell Biol. 109 (1989) 2905-2915
    • (1989) J. Cell Biol. , vol.109 , pp. 2905-2915
    • Tsukita, S.1    Itoh, M.2    Tsukita, S.3
  • 191
    • 0025913788 scopus 로고
    • Specific proto-ongenic tyrosin kineses of the src family are enriched in cell-to-cell adherers junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita S., Oishi K., Akiyama T., Yamanishi Y., Yammamoto T., and Tsukita S. Specific proto-ongenic tyrosin kineses of the src family are enriched in cell-to-cell adherers junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113 (1991) 867-879
    • (1991) J. Cell Biol. , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanishi, Y.4    Yammamoto, T.5    Tsukita, S.6
  • 192
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-cell adherers junctions
    • Tsukita S., Tsukita S., Nagatuchi A., and Yonemura S. Molecular linkage between cadherins and actin filaments in cell-cell adherers junctions. Curr. Op. Cell Biol. 4 (1992) 834-839
    • (1992) Curr. Op. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, S.1    Tsukita, S.2    Nagatuchi, A.3    Yonemura, S.4
  • 193
    • 0019400605 scopus 로고
    • Actin typing of total cellular extracts
    • Vandekerchove J., and Weber K. Actin typing of total cellular extracts. Eur. J. Biochem. 113 (1981) 595-603
    • (1981) Eur. J. Biochem. , vol.113 , pp. 595-603
    • Vandekerchove, J.1    Weber, K.2
  • 194
    • 0026114963 scopus 로고
    • Modulation of intracellular adherers type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells
    • Volberg T., Geiger G., Dror R., and Zick Y. Modulation of intracellular adherers type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells. Cell Reg. 2 (1991) 105-120
    • (1991) Cell Reg. , vol.2 , pp. 105-120
    • Volberg, T.1    Geiger, G.2    Dror, R.3    Zick, Y.4
  • 195
    • 0026779476 scopus 로고
    • Tissue distribution and subcellular localization of mammalian myosin I
    • Wagner M.C., Barylko B., and Albanesi J.P. Tissue distribution and subcellular localization of mammalian myosin I. J. Cell Biol. 119 (1992) 163-170
    • (1992) J. Cell Biol. , vol.119 , pp. 163-170
    • Wagner, M.C.1    Barylko, B.2    Albanesi, J.P.3
  • 196
    • 0025895403 scopus 로고
    • Sea urchin villin: Identification of villin in a non-epithelial cell from an invertebrate species
    • Wang F.-S., and Bonder E.M. Sea urchin villin: Identification of villin in a non-epithelial cell from an invertebrate species. J. Cell Sci. 100 (1991) 61-71
    • (1991) J. Cell Sci. , vol.100 , pp. 61-71
    • Wang, F.-S.1    Bonder, E.M.2
  • 197
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z-line
    • Wang K., and Wright J. Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z-line. J. Cell Biol. 107 (1988) 2199-2212
    • (1988) J. Cell Biol. , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 199
    • 0024434279 scopus 로고
    • Repair of microvilli in the rat small, intestine after damage with lectins contained in the red kidney bean
    • Weinman M.D., Allan C.H., Trier J.S., and Hagen S.J. Repair of microvilli in the rat small, intestine after damage with lectins contained in the red kidney bean. Gastroenterology 97 (1989) 1193-1204
    • (1989) Gastroenterology , vol.97 , pp. 1193-1204
    • Weinman, M.D.1    Allan, C.H.2    Trier, J.S.3    Hagen, S.J.4
  • 200
    • 0027219972 scopus 로고
    • Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
    • Wolenski J.S., Hayden S.M., Forscher P., and Mooseker M.S. Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. J. Cell Biol. 122 (1993) 613-621
    • (1993) J. Cell Biol. , vol.122 , pp. 613-621
    • Wolenski, J.S.1    Hayden, S.M.2    Forscher, P.3    Mooseker, M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.