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Volumn 114, Issue 11, 2001, Pages 1973-1980

The Trio family of guanine-nucleotide-exchange factors: Regulators of axon guidance

Author keywords

Actin; Dock; GTPase; Kalirin; Pak; Rac; Rho family

Indexed keywords

ACTIN; CELL PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

EID: 0034960521     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (68)

References (10)
  • 1
    • 10344242949 scopus 로고    scopus 로고
    • Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme
    • Alam, M. R., Caldwell, B. D., Johnson, R. C., Darlington, D. N., Mains, R. E. and Eipper, B. A. (1996). Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme. J. Biol. Chem. 271, 28636-28640.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28636-28640
    • Alam, M.R.1    Caldwell, B.D.2    Johnson, R.C.3    Darlington, D.N.4    Mains, R.E.5    Eipper, B.A.6
  • 2
    • 0030973545 scopus 로고    scopus 로고
    • Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme
    • Alam, M. R., Johnson, R. C., Darlington, D. N., Hand, T. A., Mains, R. E. and Eipper, B. A. (1997). Kalirin, a cytosolic protein with spectrin-like and GDP/GTP exchange factor-like domains that interacts with peptidylglycine alpha-amidating monooxygenase, an integral membrane peptide-processing enzyme. J. Biol. Chem. 272, 12667-12675.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12667-12675
    • Alam, M.R.1    Johnson, R.C.2    Darlington, D.N.3    Hand, T.A.4    Mains, R.E.5    Eipper, B.A.6
  • 3
    • 0034715885 scopus 로고    scopus 로고
    • Regulation and functions of rho-associated kinase
    • Amano, M., Fukata, Y. and Kaibuchi, K. (2000). Regulation and functions of rho-associated kinase. Exp. Cell Res. 261, 44-51.
    • (2000) Exp. Cell Res. , vol.261 , pp. 44-51
    • Amano, M.1    Fukata, Y.2    Kaibuchi, K.3
  • 4
    • 0033695698 scopus 로고    scopus 로고
    • The Drosophila Trio plays an essential role in patterning of axons by regulating their directional extension
    • Awasaki, T., Saito, M., Sone, M., Suzuki, E., Sakai, R., Ito, K. and Hama, C. (2000). The Drosophila Trio plays an essential role in patterning of axons by regulating their directional extension. Neuron 26, 119-131.
    • (2000) Neuron , vol.26 , pp. 119-131
    • Awasaki, T.1    Saito, M.2    Sone, M.3    Suzuki, E.4    Sakai, R.5    Ito, K.6    Hama, C.7
  • 5
    • 0033679001 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Trio mediates axonal development in the Drosophila embryo
    • Bateman, J., Shu, H. and Van Vactor, D. (2000). The guanine nucleotide exchange factor Trio mediates axonal development in the Drosophila embryo. Neuron 26, 93-106.
    • (2000) Neuron , vol.26 , pp. 93-106
    • Bateman, J.1    Shu, H.2    Van Vactor, D.3
  • 6
    • 0032518914 scopus 로고    scopus 로고
    • The two guanine nucleotide exchange factor domains of Trio link the Rac1 and the RhoA pathways in vivo
    • Bellanger, J.-M., Lazaro, J.-B., Diriong, S., Fernandez, A., Lamb, N. and Debant, A. (1998a). The two guanine nucleotide exchange factor domains of Trio link the Rac1 and the RhoA pathways in vivo. Oncogene 16, 147-152.
    • (1998) Oncogene , vol.16 , pp. 147-152
    • Bellanger, J.-M.1    Lazaro, J.-B.2    Diriong, S.3    Fernandez, A.4    Lamb, N.5    Debant, A.6
  • 8
    • 0033662155 scopus 로고    scopus 로고
    • The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin
    • Bellanger, J.-M., Astier, C., Sardet, C., Ohta, Y., Stossel, T. P. and Debant, A. (2000). The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin. Nat. Cell Biol. 2, 888-892.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 888-892
    • Bellanger, J.-M.1    Astier, C.2    Sardet, C.3    Ohta, Y.4    Stossel, T.P.5    Debant, A.6
  • 9
    • 0034053503 scopus 로고    scopus 로고
    • TrioGEF1 controls Rac- and Cdc42-dependent cell structures through the direct activation of RhoG
    • Blangy, A., Vignal, E-, Schmidt, S., Debant, A., Gauthier-Rouviere, C. and Fort, P. (2000). TrioGEF1 controls Rac- and Cdc42-dependent cell structures through the direct activation of RhoG. J. Cell Sci 113, 729-739.
    • (2000) J. Cell Sci , vol.113 , pp. 729-739
    • Blangy, A.1    Vignal, E.2    Schmidt, S.3    Debant, A.4    Gauthier-Rouviere, C.5    Fort, P.6
  • 10
    • 0029911521 scopus 로고    scopus 로고
    • Interaction of the Nc adapter protein with p21-activated kinase (PAK1)
    • Bokoch, G. M., Wang, Y., Bohl, B. P., Sells, M. A., Quilliam, L. A. and Knaus, U. G. (1996). Interaction of the Nc adapter protein with p21-activated kinase (PAK1). J. Biol. Chem. 271, 25746-25749.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25746-25749
    • Bokoch, G.M.1    Wang, Y.2    Bohl, B.P.3    Sells, M.A.4    Quilliam, L.A.5    Knaus, U.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.