메뉴 건너뛰기




Volumn 1, Issue 2, 1999, Pages 106-112

Structure of the Janus-faced C2B domain of rabphilin

Author keywords

[No Author keywords available]

Indexed keywords

JANUS;

EID: 0033143316     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/10076     Document Type: Article
Times cited : (65)

References (50)
  • 1
    • 0030467967 scopus 로고    scopus 로고
    • 2 domain calcium-binding motif: Structural and functional diversity
    • 2 domain calcium-binding motif: structural and functional diversity. Prot. Sci. 5, 2375-2390 (1996).
    • (1996) Prot. Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 3
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka, Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334, 661-665 (1988).
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 4
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin, M. S., Fried, V. A., Mignery, G. A., Jahn, R. & Südhof, T. C. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345, 260-263 (1990).
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Südhof, T.C.5
  • 7
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen, L.-O., Perisic, O., Cheung, R., Katan, M. & Williams, R. L. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602 (1996).
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 9
    • 0031892519 scopus 로고    scopus 로고
    • Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2
    • Perisic, O., Fong, S., Lynch, D. E., Bycroft, M. & Williams, R. L. Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273, 1596-1604 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 1596-1604
    • Perisic, O.1    Fong, S.2    Lynch, D.E.3    Bycroft, M.4    Williams, R.L.5
  • 17
    • 0031019191 scopus 로고    scopus 로고
    • 2+-dependent electrostatic switch
    • 2+-dependent electrostatic switch. Neuron 18, 133-142 (1997).
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1
  • 21
    • 0030222771 scopus 로고    scopus 로고
    • 2 domain proteins that regulate membrane traffic
    • 2 domain proteins that regulate membrane traffic. Neuron, 17, 379-388 (1996).
    • (1996) Neuron , vol.17 , pp. 379-388
    • Südhof, T.C.1    Rizo, J.2
  • 22
    • 0027461829 scopus 로고
    • Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin
    • Shirataki, H. et al. Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol. Cell. Biol. 13, 2061-2068 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2061-2068
    • Shirataki, H.1
  • 25
    • 0030028622 scopus 로고    scopus 로고
    • 2 domains selectively expressed in the rat brain and kidney
    • 2 domains selectively expressed in the rat brain and kidney. FEBS Lett. 378, 135-139 (1996).
    • (1996) FEBS Lett. , vol.378 , pp. 135-139
    • Kwon, O.-J.1    Gainer, H.2    Wray, W.3    Chin, H.4
  • 26
    • 0028061861 scopus 로고
    • 2+ sensor for transmitter release at a central synapse
    • 2+ sensor for transmitter release at a central synapse. Cell 79, 717-727 (1994).
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1
  • 29
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP2: Implications for membrane recycling
    • Zhang, J. Z., Davletov, B. A., Südhof, T. C. & Anderson, R. G. W. Synaptotagmin I is a high affinity receptor for clathrin AP2: implications for membrane recycling. Cell 78, 751-760 (1994).
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Südhof, T.C.3    Anderson, R.G.W.4
  • 31
    • 0029589647 scopus 로고
    • A possible docking and fusion particle for synaptic transmission
    • Schiavo, G., Gmachl, N. J., Stenbeck, G. Sollner, T. H. & Rothman, J. E. A possible docking and fusion particle for synaptic transmission. Nature 378, 733-376 (1995).
    • (1995) Nature , vol.378 , pp. 733-1376
    • Schiavo, G.1    Gmachl, N.J.2    Stenbeck, G.3    Sollner, T.H.4    Rothman, J.E.5
  • 33
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion
    • Chung, S.-H., Takai, Y. & Holz, R. W. Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. J. Biol. Chem. 270, 16714-16718 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 16714-16718
    • Chung, S.-H.1    Takai, Y.2    Holz, R.W.3
  • 34
    • 0032562636 scopus 로고    scopus 로고
    • 2+-dependent manner
    • 2+-dependent manner. J. Biol. Chem. 273, 10240-10248 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10240-10248
    • Chung, S.-H.1
  • 35
    • 0027269605 scopus 로고    scopus 로고
    • 2-domain peptides implicates synaptotagmin in exocytosis
    • 2-domain peptides implicates synaptotagmin in exocytosis. Nature 363, 163-165.
    • Nature , vol.363 , pp. 163-165
    • Bommert, K.1
  • 37
    • 0028206475 scopus 로고
    • The COOH terminus of synaptotagmin mediates interaction with the neurexins
    • Perin, M. S. The COOH terminus of synaptotagmin mediates interaction with the neurexins. J. Biol. Chem. 269, 8576-8581 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8576-8581
    • Perin, M.S.1
  • 38
    • 0028921368 scopus 로고
    • 2+/calmodulin-and cAMP-dependent kinase in vitro
    • 2+/calmodulin-and cAMP-dependent kinase in vitro. J. Neurosci. 15, 2385-2395 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 2385-2395
    • Fykse, E.M.1    Li, C.2    Südhof, T.C.3
  • 39
    • 0028541866 scopus 로고
    • 15N resonance assignments of N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques J. Biomol. NMR 4, 845-858 (1994).
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.4
  • 40
    • 34447505016 scopus 로고
    • Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation
    • Kay, L. E., Xu, G. Y. & Yamazaki, T. Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation J. Magn. Reson. A 109, 129-133 (1994).
    • (1994) J. Magn. Reson. A , vol.109 , pp. 129-133
    • Kay, L.E.1    Xu, G.Y.2    Yamazaki, T.3
  • 41
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R. & Kay, L. E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity J. Magn. Reson. B 103, 203-216 (1994).
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 45
    • 0028545648 scopus 로고
    • a J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • a J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods J. Biomol. NMR 4, 871-878 (1994).
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 46
  • 47
    • 0030621858 scopus 로고    scopus 로고
    • Torsion angle molecular dynamics: A new efficient tool for NMR structure calculation
    • Stein, E.G., Rice, L.M. & Brunger, A.T. Torsion angle molecular dynamics: a new efficient tool for NMR structure calculation J. Mag. Res. Ser. B 124, 154-164 (1997).
    • (1997) J. Mag. Res. Ser. B , vol.124 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brunger, A.T.3
  • 48
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR System: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography and NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 49
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 50
    • 0000243829 scopus 로고
    • PROCHECK: A program to check stereochemical quality of protein structure coordinates
    • Laskowsky, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check stereochemical quality of protein structure coordinates J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowsky, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.