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Volumn 196, Issue 1-2, 1997, Pages 43-48

Identification of N-WASP homologs in human and rat brain

Author keywords

Actin; DFNB4; Pendred syndrome

Indexed keywords

PROTEIN ANTIBODY; RECOMBINANT PROTEIN;

EID: 0030767455     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00184-4     Document Type: Article
Times cited : (46)

References (20)
  • 1
    • 0343825469 scopus 로고    scopus 로고
    • Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom, P., Lindberg, U., Hall, A., 1996. Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr. Biol. 15, 5725-5731.
    • (1996) Curr. Biol. , vol.15 , pp. 5725-5731
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 3
    • 0023027034 scopus 로고
    • Disordered pathfinding by pioneer neurone growth cones deprived of filopodia by cytocharasin treatment
    • Bentley, D., Toroian-Raymond, A., 1986. Disordered pathfinding by pioneer neurone growth cones deprived of filopodia by cytocharasin treatment. Nature 323, 712-715.
    • (1986) Nature , vol.323 , pp. 712-715
    • Bentley, D.1    Toroian-Raymond, A.2
  • 4
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P.D., Drechsel, D., Hall, A., 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 7
    • 0027488669 scopus 로고
    • Aproline-rich protein, verprolin, involved in cytoskeletal organization andcellular growth in the yeast Saccharomyces cerevisiae
    • Donnelly, S.F., Pocklington, M.J., Pallotta, D., Orr, E., 1993. Aproline-rich protein, verprolin, involved in cytoskeletal organization andcellular growth in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 10, 585-596.
    • (1993) Mol. Microbiol. , vol.10 , pp. 585-596
    • Donnelly, S.F.1    Pocklington, M.J.2    Pallotta, D.3    Orr, E.4
  • 10
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw, J.E., Schmid, S.L., 1995. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374, 190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 12
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signaling proteins
    • Mayer, B.J., Ren, R., Clark, K., Baltimore, D., 1993. A putative modular domain present in diverse signaling proteins. Cell 73, 629-630.
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.3    Baltimore, D.4
  • 13
    • 0028073746 scopus 로고
    • P145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., Takei, K., Schmid, S.L., De Camilli, P., 1994. p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J. Biol. Chem. 269, 30132-30139.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 15
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement ina PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., Miura, K., Takenawa, T., 1996. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement ina PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326-5335.
    • (1996) EMBO J. , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 16
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida, E., Maekawa, S., Sakai, H., 1984. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23, 5307-5317.
    • (1984) Biochemistry , vol.23 , pp. 5307-5317
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 17
    • 0029963073 scopus 로고    scopus 로고
    • Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification
    • Sheffield, V.C., Kraiem, Z., Beck, J.C., Nishimura, D., Stone, E.M., Salameh, M., Sadeh, O., Glaser, B., 1996. Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification. Nature Genet. 12, 424-426.
    • (1996) Nature Genet. , vol.12 , pp. 424-426
    • Sheffield, V.C.1    Kraiem, Z.2    Beck, J.C.3    Nishimura, D.4    Stone, E.M.5    Salameh, M.6    Sadeh, O.7    Glaser, B.8
  • 18
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich Syndrome Protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., Derry, J.M.J., Karlak, B., Jiang, S., Lemahieu, V., McCormick, F., Franke, U., Abo, A., 1996. Wiskott-Aldrich Syndrome Protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84, 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.J.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Franke, U.7    Abo, A.8
  • 19
    • 0028923349 scopus 로고
    • Tubular membrane invagination coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei, K., McPherson, P.S., Schmid, S.L., De Camilli, P., 1995. Tubular membrane invagination coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 374, 186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 20
    • 0002358665 scopus 로고
    • The separationof synaptic vesicles from nerve-ending particles ('synaptosomes')
    • Whittaker, V.P., Michaelson, I.A., Kirkland, R.J., 1964. The separationof synaptic vesicles from nerve-ending particles ('synaptosomes'). Biochem. J. 90, 293-303.
    • (1964) Biochem. J. , vol.90 , pp. 293-303
    • Whittaker, V.P.1    Michaelson, I.A.2    Kirkland, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.