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Volumn 22, Issue 5, 1996, Pages 849-857

Identification and cellular localization of the actin-binding protein ABP-120 from Entamoeba histolytica

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN;

EID: 0029848069     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.01535.x     Document Type: Article
Times cited : (42)

References (33)
  • 1
    • 0028803237 scopus 로고
    • Myosin II is involved in capping and uroid formation in the human pathogen Entamoeba histolytica
    • Arhets, P., Gounon, P., Sansonetti, P., and Guillén, N. (1995) Myosin II is involved in capping and uroid formation in the human pathogen Entamoeba histolytica. Infect Immun 63: 4358-4367.
    • (1995) Infect Immun , vol.63 , pp. 4358-4367
    • Arhets, P.1    Gounon, P.2    Sansonetti, P.3    Guillén, N.4
  • 2
    • 0022256476 scopus 로고
    • Rapid polymerization of Entamoeba histolytica actin induced by interaction with target cells
    • Bailey, G.B., Day, D.B., and Gasque, J.W. (1985) Rapid polymerization of Entamoeba histolytica actin induced by interaction with target cells. J Exp Med 162: 546-558.
    • (1985) J Exp Med , vol.162 , pp. 546-558
    • Bailey, G.B.1    Day, D.B.2    Gasque, J.W.3
  • 4
    • 0025734201 scopus 로고
    • Evidence that 27-residue sequence is the actin-binding site of ABP-12
    • Bresnick, A.R., Janmey, P.A., and Condeelis, J. (1991) Evidence that 27-residue sequence is the actin-binding site of ABP-12. Biol Chem 266: 12989-12993.
    • (1991) Biol Chem , vol.266 , pp. 12989-12993
    • Bresnick, A.R.1    Janmey, P.A.2    Condeelis, J.3
  • 5
    • 0027735142 scopus 로고
    • Unusual gene organization in the protozoan parasite Entamoeba histolytica
    • Bruchhaus, I., Leippe, M., Lioutas, C., and Tannich, E. (1993) Unusual gene organization in the protozoan parasite Entamoeba histolytica. DNA Cell Biol 12: 925-933.
    • (1993) DNA Cell Biol , vol.12 , pp. 925-933
    • Bruchhaus, I.1    Leippe, M.2    Lioutas, C.3    Tannich, E.4
  • 6
    • 0024742979 scopus 로고
    • Sequence similarity of the amino-terminal domain of drosophila β-spectrin to α-actinin and distrophin
    • Byers, T.J., Husain, A.C., Dubreuil, R.R., Branton, D., and Goldstein, L.S. (1989) Sequence similarity of the amino-terminal domain of drosophila β-spectrin to α-actinin and distrophin. J Cell Biol 109: 1633-1641.
    • (1989) J Cell Biol , vol.109 , pp. 1633-1641
    • Byers, T.J.1    Husain, A.C.2    Dubreuil, R.R.3    Branton, D.4    Goldstein, L.S.5
  • 7
    • 0026026620 scopus 로고
    • Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
    • Chia, C.P., Hitt, A.L., and Luna, E.J. (1991) Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein. Cell Motil Cytoskeleton 18: 164-179.
    • (1991) Cell Motil Cytoskeleton , vol.18 , pp. 164-179
    • Chia, C.P.1    Hitt, A.L.2    Luna, E.J.3
  • 9
    • 0021886330 scopus 로고
    • Purification from Dictyostelium discoideum of a low-molecular-weight myosin that resembles myosin I from Acanthamoeba castellanii
    • Côte, G.P., Albaresi, J.P., Ueno, T., Hammer, J.A., and Korn, E.D. (1985) Purification from Dictyostelium discoideum of a low-molecular-weight myosin that resembles myosin I from Acanthamoeba castellanii. J Biol Chem 260: 4543-4546.
    • (1985) J Biol Chem , vol.260 , pp. 4543-4546
    • Côte, G.P.1    Albaresi, J.P.2    Ueno, T.3    Hammer, J.A.4    Korn, E.D.5
  • 10
    • 0028919541 scopus 로고
    • Genetic deletion of ABP-120 alteres the three-dimensional organization of actin filaments in Distyostelium pseudopods
    • Cox, D., Ridsdale, A., Condeelis, J., and Hartwig, J. (1995) Genetic deletion of ABP-120 alteres the three-dimensional organization of actin filaments in Distyostelium pseudopods. J Cell Biol 128: 819-835.
    • (1995) J Cell Biol , vol.128 , pp. 819-835
    • Cox, D.1    Ridsdale, A.2    Condeelis, J.3    Hartwig, J.4
  • 11
    • 0026543374 scopus 로고
    • Requirement for actin binding protein for cortical stability and efficient locomotion
    • Cunningham, C.C., Gorlin, J.B., Kwiatkowski, D., Hartwig, J., Janmey, P., and Stossel, T. (1992) Requirement for actin binding protein for cortical stability and efficient locomotion. Science 255: 325-327.
    • (1992) Science , vol.255 , pp. 325-327
    • Cunningham, C.C.1    Gorlin, J.B.2    Kwiatkowski, D.3    Hartwig, J.4    Janmey, P.5    Stossel, T.6
  • 12
    • 0024756462 scopus 로고
    • Characterization of a cytochalasin D-resistant mutant of Entamoeba histolytica
    • De la Garza, M., Gallegos, B., and Meza, I. (1989) Characterization of a cytochalasin D-resistant mutant of Entamoeba histolytica. J Protozool 36: 556-560.
    • (1989) J Protozool , vol.36 , pp. 556-560
    • De La Garza, M.1    Gallegos, B.2    Meza, I.3
  • 13
    • 0024595208 scopus 로고
    • Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum
    • Dharmawardhane, S., Warrer, V., Hall, A.L., and Condeelis, J. (1989) Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum. Cell Motil Cytoskeleton 13: 57-63.
    • (1989) Cell Motil Cytoskeleton , vol.13 , pp. 57-63
    • Dharmawardhane, S.1    Warrer, V.2    Hall, A.L.3    Condeelis, J.4
  • 14
    • 0017846267 scopus 로고
    • A new medium for the exenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond, L.S., Harlow, D.R., and Cunnick, C.C. (1978) A new medium for the exenic cultivation of Entamoeba histolytica and other Entamoeba. Trans R Soc Trop Med Hyg 72: 431-432.
    • (1978) Trans R Soc Trop Med Hyg , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 15
    • 0022398178 scopus 로고
    • Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membrane
    • Fox, J. (1985) Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membrane. J Biol Chem 260: 11970-11977.
    • (1985) J Biol Chem , vol.260 , pp. 11970-11977
    • Fox, J.1
  • 16
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione-S-transferase (pGEX) fusion protein
    • Frangioni, J.V., and Neel, B.G. (1993) Solubilization and purification of enzymatically active glutathione-S-transferase (pGEX) fusion protein. Anal Biochem 210: 179-187.
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 17
    • 0027203434 scopus 로고
    • Cell signalling and motility in Entamoeba histolytica
    • Guillén, N. (1993) Cell signalling and motility in Entamoeba histolytica. Parasitol Today 9: 364-369.
    • (1993) Parasitol Today , vol.9 , pp. 364-369
    • Guillén, N.1
  • 18
    • 0030003312 scopus 로고    scopus 로고
    • Role of signalling and cytoskeletal rearrangements in the pathogenesis of Entamoeba histolytica
    • Guillén, N. (1996) Role of signalling and cytoskeletal rearrangements in the pathogenesis of Entamoeba histolytica. Trends Microbiol 4: 191-196.
    • (1996) Trends Microbiol , vol.4 , pp. 191-196
    • Guillén, N.1
  • 19
    • 0029186874 scopus 로고
    • Actin-binding proteins 1: Spectrin superfamily
    • Sheterline, P. (ed.). London: Academic Press
    • Hartwig, J. (1995) Actin-binding proteins 1: spectrin superfamily. In Protein Profile. Sheterline, P. (ed.). London: Academic Press, 2: pp. 739-746.
    • (1995) Protein Profile , vol.2 , pp. 739-746
    • Hartwig, J.1
  • 20
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp, T.D., and Woods, K.R. (1981) Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 78: 3824-3828.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3824-3828
    • Hopp, T.D.1    Woods, K.R.2
  • 21
    • 0030060536 scopus 로고    scopus 로고
    • Entamoeba histolytica encodes a highly divergent β-tubulin
    • Katiyar, S.K., and Edlind, T.D. (1996) Entamoeba histolytica encodes a highly divergent β-tubulin. J Euk Microbiol 43: 31-34.
    • (1996) J Euk Microbiol , vol.43 , pp. 31-34
    • Katiyar, S.K.1    Edlind, T.D.2
  • 22
    • 0024801639 scopus 로고
    • The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau
    • Noble, M., Lewis, S.A., and Cowan, N.J. (1989) The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau. J Cell Biol 109: 3367-3376.
    • (1989) J Cell Biol , vol.109 , pp. 3367-3376
    • Noble, M.1    Lewis, S.A.2    Cowan, N.J.3
  • 23
    • 0023653358 scopus 로고
    • Calcium-sensitive non-muscle α-actinin contains EF-hand structures and highly conserved regions
    • Noegel, A., Witke, W., and Schleicher, M. (1987) Calcium-sensitive non-muscle α-actinin contains EF-hand structures and highly conserved regions. FEBS Lett 221: 391-396.
    • (1987) FEBS Lett , vol.221 , pp. 391-396
    • Noegel, A.1    Witke, W.2    Schleicher, M.3
  • 24
    • 0024335961 scopus 로고
    • The Dictyostelium gelation factor shares a putative actin binding site with α-actinin and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
    • Noegel, A.A., Rapp, S., Lotspeich, F., Schleicher, M., and Stewart, M. (1989) The Dictyostelium gelation factor shares a putative actin binding site with α-actinin and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation. J Cell Biol 109: 607-618.
    • (1989) J Cell Biol , vol.109 , pp. 607-618
    • Noegel, A.A.1    Rapp, S.2    Lotspeich, F.3    Schleicher, M.4    Stewart, M.5
  • 25
    • 0025943943 scopus 로고
    • Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (FcgRI)
    • Ohta, Y., Stossel, T.P., and Hatwing, J.H. (1991) Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (FcgRI). Cell 67: 275-289.
    • (1991) Cell , vol.67 , pp. 275-289
    • Ohta, Y.1    Stossel, T.P.2    Hatwing, J.H.3
  • 26
    • 0021912911 scopus 로고
    • Other association of glycoprotein Ib and actin-binding protein in human platelets
    • Okita, J.R., Pidard, D., Newman, P.J., Montgomery, R.R., and Kunicki, T.J. (1985) Other association of glycoprotein Ib and actin-binding protein in human platelets. J Cell Biol 100: 317-321.
    • (1985) J Cell Biol , vol.100 , pp. 317-321
    • Okita, J.R.1    Pidard, D.2    Newman, P.J.3    Montgomery, R.R.4    Kunicki, T.J.5
  • 27
    • 0027403318 scopus 로고
    • Localization of myosin heavy chain a in the human pathogen Entamoeba histolytica
    • Rahim, Z., Raymond-Denise, A., Sansonetti, P., and Guillén, N. (1993) Localization of myosin heavy chain A in the human pathogen Entamoeba histolytica. Infect Immun 61: 1048-1054.
    • (1993) Infect Immun , vol.61 , pp. 1048-1054
    • Rahim, Z.1    Raymond-Denise, A.2    Sansonetti, P.3    Guillén, N.4
  • 28
    • 0029018229 scopus 로고
    • Ameobiasis
    • Ravdin, J.I. (1995) Ameobiasis. Clin Infect Dis 20: 1453-1466.
    • (1995) Clin Infect Dis , vol.20 , pp. 1453-1466
    • Ravdin, J.I.1
  • 30
    • 0028023825 scopus 로고
    • Cloning, genomic organization and transcription of the Entamoeba histolytica α-tubulin-encoding gene
    • Sanchez, M.A., Peattie, D.A., Wirth, D., and Orozco, E. (1994) Cloning, genomic organization and transcription of the Entamoeba histolytica α-tubulin-encoding gene. Gene 146: 239-244.
    • (1994) Gene , vol.146 , pp. 239-244
    • Sanchez, M.A.1    Peattie, D.A.2    Wirth, D.3    Orozco, E.4
  • 31
    • 0029442595 scopus 로고
    • Actin
    • Sheterline, P. (ed.). London: Academic Press
    • Sheterline, P., Clayton, J., and Sparrow, J. (1995) Actin, In Protein Profile. Sheterline, P. (ed.). London: Academic Press, 2: pp. 1-2.
    • (1995) Protein Profile , vol.2 , pp. 1-2
    • Sheterline, P.1    Clayton, J.2    Sparrow, J.3
  • 32
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith, D.B., and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67: 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 33
    • 0026642001 scopus 로고
    • Codon usage in pathogenic Entamoeba histolytica
    • Tannich, E., and Hortsmann, R.D. (1992) Codon usage in pathogenic Entamoeba histolytica. J Mol Evol 34: 272-273.
    • (1992) J Mol Evol , vol.34 , pp. 272-273
    • Tannich, E.1    Hortsmann, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.