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Volumn 202, Issue 5, 2013, Pages 793-806

Drebrin contains a cryptic F-actin-bundling activity regulated by Cdk5 phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 5; DREBRIN; F ACTIN; SERINE;

EID: 84884189701     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201303005     Document Type: Article
Times cited : (88)

References (46)
  • 1
    • 70349823160 scopus 로고    scopus 로고
    • Drebrin a knockout eliminates the rapid form of homeostatic synaptic plasticity at excitatory synapses of intact adult cerebral cortex
    • Aoki, C., N. Kojima, N. Sabaliauskas, L. Shah, T.H. Ahmed, J. Oakford, T. Ahmed, H. Yamazaki, K. Hanamura, and T. Shirao. 2009. Drebrin a knockout eliminates the rapid form of homeostatic synaptic plasticity at excitatory synapses of intact adult cerebral cortex. J. Comp. Neurol. 517:105-121. http://dx.doi.org/10.1002/cne.22137
    • (2009) J. Comp. Neurol. , vol.517 , pp. 105-121
    • Aoki, C.1    Kojima, N.2    Sabaliauskas, N.3    Shah, L.4    Ahmed, T.H.5    Oakford, J.6    Ahmed, T.7    Yamazaki, H.8    Hanamura, K.9    Shirao, T.10
  • 4
    • 45149090425 scopus 로고    scopus 로고
    • Interactions between drebrin and Ras regulate dendritic spine plasticity
    • Biou, V., H. Brinkhaus, R.C. Malenka, and A. Matus. 2008. Interactions between drebrin and Ras regulate dendritic spine plasticity. Eur. J. Neurosci. 27:2847-2859. http://dx.doi.org/10.1111/j.1460-9568.2008.06269.x
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 2847-2859
    • Biou, V.1    Brinkhaus, H.2    Malenka, R.C.3    Matus, A.4
  • 5
    • 22544480000 scopus 로고    scopus 로고
    • Drebrin E2 is differentially expressed and phosphorylated in parietal cells in the gastric mucosa
    • Chew, C.S., C.T. Okamoto, X. Chen, and R. Thomas. 2005. Drebrin E2 is differentially expressed and phosphorylated in parietal cells in the gastric mucosa. Am. J. Physiol. Gastrointest. Liver Physiol. 289:G320-G331. http://dx.doi.org/10.1152/ajpgi.00002.2005
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.289
    • Chew, C.S.1    Okamoto, C.T.2    Chen, X.3    Thomas, R.4
  • 6
    • 0035140487 scopus 로고    scopus 로고
    • Role of the actin bundling protein fascin in growth cone morphogenesis: localization in filopodia and lamellipodia
    • <109::AID-CM1002>3.0.CO;2-G
    • Cohan, C.S., E.A. Welnhofer, L. Zhao, F. Matsumura, and S. Yamashiro. 2001. Role of the actin bundling protein fascin in growth cone morphogenesis: localization in filopodia and lamellipodia. Cell Motil. Cytoskeleton. 48:109-120. http://dx.doi.org/10.1002/1097-0169(200102)48:2<109::AID-CM1002>3.0.CO;2-G
    • (2001) Cell Motil. Cytoskeleton. , vol.48 , pp. 109-120
    • Cohan, C.S.1    Welnhofer, E.A.2    Zhao, L.3    Matsumura, F.4    Yamashiro, S.5
  • 8
    • 0034193551 scopus 로고    scopus 로고
    • The cyclindependent kinase Cdk5 controls multiple aspects of axon patterning in vivo
    • Connell-Crowley, L., M. Le Gall, D.J. Vo, and E. Giniger. 2000. The cyclindependent kinase Cdk5 controls multiple aspects of axon patterning in vivo. Curr. Biol. 10:599-602. http://dx.doi.org/10.1016/S0960-9822(00)00487-5
    • (2000) Curr. Biol. , vol.10 , pp. 599-602
    • Connell-Crowley, L.1    Le Gall, M.2    Vo, D.J.3    Giniger, E.4
  • 10
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti, C.G., C.A. Sullivan, and G.A. Banker. 1988. The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8:1454-1468.
    • (1988) J. Neurosci. , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 11
    • 77950271947 scopus 로고    scopus 로고
    • Control of cell shape and plasticity during development and disease by the actin-binding protein Drebrin
    • Dun, X.P., and J.K. Chilton. 2010. Control of cell shape and plasticity during development and disease by the actin-binding protein Drebrin. Histol. Histopathol. 25:533-540.
    • (2010) Histol. Histopathol. , vol.25 , pp. 533-540
    • Dun, X.P.1    Chilton, J.K.2
  • 12
    • 84857002700 scopus 로고    scopus 로고
    • Drebrin controls neuronal migration through the formation and alignment of the leading process
    • Dun, X.P., T. Bandeira de Lima, J. Allen, S. Geraldo, P. Gordon-Weeks, and J.K. Chilton. 2012. Drebrin controls neuronal migration through the formation and alignment of the leading process. Mol. Cell. Neurosci. 49:341-350. http://dx.doi.org/10.1016/j.mcn.2012.01.006
    • (2012) Mol. Cell. Neurosci. , vol.49 , pp. 341-350
    • Dun, X.P.1    Bandeira de Lima, T.2    Allen, J.3    Geraldo, S.4    Gordon-Weeks, P.5    Chilton, J.K.6
  • 13
    • 53349165549 scopus 로고    scopus 로고
    • Targeting of the F-actin-binding protein drebrin by the microtubule plus-tip protein EB3 is required for neuritogenesis
    • Geraldo, S., U.K. Khanzada, M. Parsons, J.K. Chilton, and P.R. Gordon-Weeks. 2008. Targeting of the F-actin-binding protein drebrin by the microtubule plus-tip protein EB3 is required for neuritogenesis. Nat. Cell Biol. 10:1181-1189. http://dx.doi.org/10.1038/ncb1778
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1181-1189
    • Geraldo, S.1    Khanzada, U.K.2    Parsons, M.3    Chilton, J.K.4    Gordon-Weeks, P.R.5
  • 14
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode, B.L., A.A. Rodal, G. Barnes, and D.G. Drubin. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:627-634. http://dx.doi.org/10.1083/jcb.153.3.627
    • (2001) J. Cell Biol. , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 16
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya, Y., M. Shoji, T. Shirao, and S. Hirai. 1996. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J. Neurosci. Res. 43:87-92. http://dx.doi.org/10.1002/jnr.490430111
    • (1996) J. Neurosci. Res. , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 17
    • 0033033642 scopus 로고    scopus 로고
    • Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease
    • Hatanpää, K., K.R. Isaacs, T. Shirao, D.R. Brady, and S.I. Rapoport. 1999. Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease. J. Neuropathol. Exp. Neurol. 58:637-643. http://dx.doi.org/10.1097/00005072-199906000-00008
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 637-643
    • Hatanpää, K.1    Isaacs, K.R.2    Shirao, T.3    Brady, D.R.4    Rapoport, S.I.5
  • 18
    • 0033562792 scopus 로고    scopus 로고
    • Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons
    • Hayashi, K., and T. Shirao. 1999. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J. Neurosci. 19:3918-3925.
    • (1999) J. Neurosci. , vol.19 , pp. 3918-3925
    • Hayashi, K.1    Shirao, T.2
  • 19
    • 0033573145 scopus 로고    scopus 로고
    • Domain analysis of the actin-binding and actin-remodeling activities of drebrin
    • Hayashi, K., R. Ishikawa, R. Kawai-Hirai, T. Takagi, A. Taketomi, and T. Shirao. 1999. Domain analysis of the actin-binding and actin-remodeling activities of drebrin. Exp. Cell Res. 253:673-680. http://dx.doi.org/10.1006/excr.1999.4663
    • (1999) Exp. Cell Res. , vol.253 , pp. 673-680
    • Hayashi, K.1    Ishikawa, R.2    Kawai-Hirai, R.3    Takagi, T.4    Taketomi, A.5    Shirao, T.6
  • 20
    • 79958773486 scopus 로고    scopus 로고
    • The neuronal p35 activator of Cdk5 is a novel F-actin binding and bundling protein
    • He, L., Z. Zhang, Y. Yu, S. Ahmed, N.S. Cheung, and R.Z. Qi. 2011. The neuronal p35 activator of Cdk5 is a novel F-actin binding and bundling protein. Cell. Mol. Life Sci. 68:1633-1643. http://dx.doi.org/10.1007/s00018-010-0562-9
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1633-1643
    • He, L.1    Zhang, Z.2    Yu, Y.3    Ahmed, S.4    Cheung, N.S.5    Qi, R.Z.6
  • 21
    • 0142148230 scopus 로고    scopus 로고
    • Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro
    • Ishikawa, R., T. Sakamoto, T. Ando, S. Higashi-Fujime, and K. Kohama. 2003. Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro. J. Neurochem. 87:676-685. http://dx.doi.org/10.1046/j.1471-4159.2003.02058.x
    • (2003) J. Neurochem. , vol.87 , pp. 676-685
    • Ishikawa, R.1    Sakamoto, T.2    Ando, T.3    Higashi-Fujime, S.4    Kohama, K.5
  • 22
    • 77953704732 scopus 로고    scopus 로고
    • Role of drebrin A in dendritic spine plasticity and synaptic function: Implications in neurological disorders
    • Ivanov, A., M. Esclapez, and L. Ferhat. 2009. Role of drebrin A in dendritic spine plasticity and synaptic function: Implications in neurological disorders. Commun. Integr. Biol. 2:268-270. http://dx.doi.org/10.4161/cib.2.3.8166
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 268-270
    • Ivanov, A.1    Esclapez, M.2    Ferhat, L.3
  • 25
    • 0033961903 scopus 로고    scopus 로고
    • Isoform specific expression of the neuronal F-actin binding protein, drebrin, in specialized cells of stomach and kidney epithelia
    • Keon, B.H., P.T. Jedrzejewski, D.L. Paul, and D.A. Goodenough. 2000. Isoform specific expression of the neuronal F-actin binding protein, drebrin, in specialized cells of stomach and kidney epithelia. J. Cell Sci. 113:325-336.
    • (2000) J. Cell Sci. , vol.113 , pp. 325-336
    • Keon, B.H.1    Jedrzejewski, P.T.2    Paul, D.L.3    Goodenough, D.A.4
  • 26
    • 0033980106 scopus 로고    scopus 로고
    • Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation
    • Kessels, M.M., A.E. Engqvist-Goldstein, and D.G. Drubin. 2000. Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol. Biol. Cell. 11:393-412. http://dx.doi.org/10.1091/mbc.11.1.393
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 393-412
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.2    Drubin, D.G.3
  • 27
    • 2342622581 scopus 로고    scopus 로고
    • Antisense knockdown of drebrin A, a dendritic spine protein, causes stronger preference, impaired pre-pulse inhibition, and an increased sensitivity to psychostimulant
    • Kobayashi, R., Y. Sekino, T. Shirao, S. Tanaka, T. Ogura, K. Inada, and M. Saji. 2004. Antisense knockdown of drebrin A, a dendritic spine protein, causes stronger preference, impaired pre-pulse inhibition, and an increased sensitivity to psychostimulant. Neurosci. Res. 49:205-217. http://dx.doi.org/10.1016/j.neures.2004.02.014
    • (2004) Neurosci. Res. , vol.49 , pp. 205-217
    • Kobayashi, R.1    Sekino, Y.2    Shirao, T.3    Tanaka, S.4    Ogura, T.5    Inada, K.6    Saji, M.7
  • 28
    • 70449632127 scopus 로고    scopus 로고
    • Genetic disruption of the alternative splicing of drebrin gene impairs context-dependent fear learning in adulthood
    • Kojima, N., K. Hanamura, H. Yamazaki, T. Ikeda, S. Itohara, and T. Shirao. 2010. Genetic disruption of the alternative splicing of drebrin gene impairs context-dependent fear learning in adulthood. Neuroscience. 165:138-150. http://dx.doi.org/10.1016/j.neuroscience.2009.10.016
    • (2010) Neuroscience. , vol.165 , pp. 138-150
    • Kojima, N.1    Hanamura, K.2    Yamazaki, H.3    Ikeda, T.4    Itohara, S.5    Shirao, T.6
  • 29
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: a highly exploited actin-binding module
    • Lappalainen, P., M.M. Kessels, M.J. Cope, and D.G. Drubin. 1998. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell. 9:1951-1959. http://dx.doi.org/10.1091/mbc.9.8.1951
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.M.2    Cope, M.J.3    Drubin, D.G.4
  • 30
    • 0032952693 scopus 로고    scopus 로고
    • SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors
    • Larbolette, O., B. Wollscheid, J. Schweikert, P.J. Nielsen, and J. Wienands. 1999. SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors. Mol. Cell. Biol. 19: 1539-1546.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1539-1546
    • Larbolette, O.1    Wollscheid, B.2    Schweikert, J.3    Nielsen, P.J.4    Wienands, J.5
  • 31
    • 84864605119 scopus 로고    scopus 로고
    • Presenilin conditional double knockout mice exhibit decreases in drebrin a at hippocampal CA1 synapses
    • Lee, D., and C. Aoki. 2012. Presenilin conditional double knockout mice exhibit decreases in drebrin a at hippocampal CA1 synapses. Synapse. 66:870-879. http://dx.doi.org/10.1002/syn.21578
    • (2012) Synapse. , vol.66 , pp. 870-879
    • Lee, D.1    Aoki, C.2
  • 32
    • 62649134712 scopus 로고    scopus 로고
    • Drebrin E is involved in the regulation of axonal growth through actin-myosin interactions
    • Mizui, T., N. Kojima, H. Yamazaki, M. Katayama, K. Hanamura, and T. Shirao. 2009. Drebrin E is involved in the regulation of axonal growth through actin-myosin interactions. J. Neurochem. 109:611-622. http://dx.doi.org/10.1111/j.1471-4159.2009.05993.x
    • (2009) J. Neurochem. , vol.109 , pp. 611-622
    • Mizui, T.1    Kojima, N.2    Yamazaki, H.3    Katayama, M.4    Hanamura, K.5    Shirao, T.6
  • 33
    • 0029966469 scopus 로고    scopus 로고
    • The cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation
    • Nikolic, M., H. Dudek, Y.T. Kwon, Y.F. Ramos, and L.H. Tsai. 1996. The cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation. Genes Dev. 10:816-825. http://dx.doi.org/10.1101/gad.10.7.816
    • (1996) Genes Dev. , vol.10 , pp. 816-825
    • Nikolic, M.1    Dudek, H.2    Kwon, Y.T.3    Ramos, Y.F.4    Tsai, L.H.5
  • 34
    • 0029768093 scopus 로고    scopus 로고
    • Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death
    • Ohshima, T., J.M. Ward, C.G. Huh, G. Longenecker, H.C. Veeranna, H.C. Pant, R.O. Brady, L.J. Martin, and A.B. Kulkarni. 1996. Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death. Proc. Natl. Acad. Sci. USA. 93:11173-11178. http://dx.doi.org/10.1073/pnas.93.20.11173
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 11173-11178
    • Ohshima, T.1    Ward, J.M.2    Huh, C.G.3    Longenecker, G.4    Veeranna, H.C.5    Pant, H.C.6    Brady, R.O.7    Martin, L.J.8    Kulkarni, A.B.9
  • 35
    • 0001956792 scopus 로고    scopus 로고
    • Isolation of synaptosomes, growth cones and their subcelllular components
    • A.J. Turner and H.S. Bachelard, editors .London, IRL Press
    • Phelan, P., and P.R. Gordon-Weeks. 1997. Isolation of synaptosomes, growth cones and their subcelllular components. Neurochemistry, A Practical Approach. A.J. Turner and H.S. Bachelard, editors. London, IRL Press: 1-38.
    • (1997) Neurochemistry, A Practical Approach. , pp. 1-38
    • Phelan, P.1    Gordon-Weeks, P.R.2
  • 36
    • 21844474822 scopus 로고    scopus 로고
    • Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions
    • Quintero-Monzon, O., A.A. Rodal, B. Strokopytov, S.C. Almo, and B.L. Goode. 2005. Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions. Mol. Biol. Cell. 16:3128-3139. http://dx.doi.org/10.1091/mbc.E05-01-0059
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 3128-3139
    • Quintero-Monzon, O.1    Rodal, A.A.2    Strokopytov, B.3    Almo, S.C.4    Goode, B.L.5
  • 38
    • 69349101851 scopus 로고    scopus 로고
    • Nonprimed and DYRK1A-primed GSK3 beta-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons
    • Scales, T.M., S. Lin, M. Kraus, R.G. Goold, and P.R. Gordon-Weeks. 2009. Nonprimed and DYRK1A-primed GSK3 beta-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons. J. Cell Sci. 122:2424-2435. http://dx.doi.org/10.1242/jcs.040162
    • (2009) J. Cell Sci. , vol.122 , pp. 2424-2435
    • Scales, T.M.1    Lin, S.2    Kraus, M.3    Goold, R.G.4    Gordon-Weeks, P.R.5
  • 39
    • 0019720977 scopus 로고
    • Structural interaction of cytoskeletal components
    • Schliwa, M., and J. van Blerkom. 1981. Structural interaction of cytoskeletal components. J. Cell Biol. 90:222-235. http://dx.doi.org/10.1083/jcb.90.1.222
    • (1981) J. Cell Biol. , vol.90 , pp. 222-235
    • Schliwa, M.1    van Blerkom, J.2
  • 40
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • Shim, K.S., and G. Lubec. 2002. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci. Lett. 324:209-212. http://dx.doi.org/10.1016/S0304-3940(02)00210-0
    • (2002) Neurosci. Lett. , vol.324 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 41
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • Shirao, T., N. Kojima, and K. Obata. 1992. Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. Neuroreport. 3:109-112. http://dx.doi.org/10.1097/00001756-199201000-00029
    • (1992) Neuroreport. , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 42
    • 0027961093 scopus 로고
    • Formation of thick, curving bundles of actin by drebrin A expressed in fibroblasts
    • Shirao, T., K. Hayashi, R. Ishikawa, K. Isa, H. Asada, K. Ikeda, and K. Uyemura. 1994. Formation of thick, curving bundles of actin by drebrin A expressed in fibroblasts. Exp. Cell Res. 215:145-153. http://dx.doi.org/10.1006/excr.1994.1326
    • (1994) Exp. Cell Res. , vol.215 , pp. 145-153
    • Shirao, T.1    Hayashi, K.2    Ishikawa, R.3    Isa, K.4    Asada, H.5    Ikeda, K.6    Uyemura, K.7
  • 43
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Songyang, Z., K.P. Lu, Y.T. Kwon, L.H. Tsai, O. Filhol, C. Cochet, D.A. Brickey, T.R. Soderling, C. Bartleson, D.J. Graves, et al. 1996. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol. Cell. Biol. 16:6486-6493.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 44
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 45
    • 80054045373 scopus 로고    scopus 로고
    • Cyclin-dependent kinases in brain development and disease
    • Su, S.C., and L.H. Tsai. 2011. Cyclin-dependent kinases in brain development and disease. Annu. Rev. Cell Dev. Biol. 27:465-491. http://dx.doi.org/10.1146/annurev-cellbio-092910-154023
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 465-491
    • Su, S.C.1    Tsai, L.H.2
  • 46
    • 33744949077 scopus 로고    scopus 로고
    • The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin
    • Xu, W., and M. Stamnes. 2006. The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin. J. Biol. Chem. 281:11826-11833. http://dx.doi.org/10.1074/jbc.M510141200
    • (2006) J. Biol. Chem. , vol.281 , pp. 11826-11833
    • Xu, W.1    Stamnes, M.2


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