메뉴 건너뛰기




Volumn 48, Issue 2, 2009, Pages 254-263

The SH3 domain of αII spectrin is a target for the fanconi anemia protein, FANCG

Author keywords

[No Author keywords available]

Indexed keywords

CONSENSUS SEQUENCES; DNA REPAIR PROCESS; FANCONI ANEMIAS; IN CELLS; INTERSTRAND CROSS-LINKS; OVERLAPPING REGIONS; REPAIR PROTEINS; SITE-DIRECTED MUTAGENESIS; SPECTRIN; STRUCTURAL PROTEINS; YEAST TWO HYBRIDS;

EID: 59849090474     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801483u     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0002725969 scopus 로고    scopus 로고
    • Fanconi anemia
    • Vogelstein, B, and Kinzler, K. W, Eds, 2nd ed, pp, McGraw-Hill, New York
    • Auerbach, A. D., Buchwald, M., and Joenje, H. (2002) Fanconi anemia, in The Genetic Basis of Human Cancer (Vogelstein, B., and Kinzler, K. W., Eds.) 2nd ed., pp 317-332, McGraw-Hill, New York.
    • (2002) The Genetic Basis of Human Cancer , pp. 317-332
    • Auerbach, A.D.1    Buchwald, M.2    Joenje, H.3
  • 2
    • 0035379611 scopus 로고    scopus 로고
    • The emerging genetic and molecular basis of Fanconi anaemia
    • Joenje, H., and Patel, K. J. (2001) The emerging genetic and molecular basis of Fanconi anaemia. Nat. ReV. Genet. 2, 446-457.
    • (2001) Nat. ReV. Genet , vol.2 , pp. 446-457
    • Joenje, H.1    Patel, K.J.2
  • 3
    • 29144506137 scopus 로고    scopus 로고
    • The Fanconi anemia/BRCA pathway: New faces in the crowd
    • Kennedy, R. D., and D'Andrea, A. D. (2005) The Fanconi anemia/BRCA pathway: new faces in the crowd. Genes DeV. 19, 2925-2940.
    • (2005) Genes DeV , vol.19 , pp. 2925-2940
    • Kennedy, R.D.1    D'Andrea, A.D.2
  • 4
    • 33744481750 scopus 로고    scopus 로고
    • Molecular pathogenesis of Fanconi anemia: Recent progress
    • Taniguchi, T., and D'Andrea, A. D. (2006) Molecular pathogenesis of Fanconi anemia: recent progress. Blood 107, 4223-4233.
    • (2006) Blood , vol.107 , pp. 4223-4233
    • Taniguchi, T.1    D'Andrea, A.D.2
  • 5
    • 0023632030 scopus 로고
    • The fate of 8-methoxypsoralen-photoinduced DNA interstrand crosslinks in Fanconi's anemia cells of defined genetic complementation groups
    • Papadopoulo, D., Averbeck, D., and Moustacchi, E. (1987) The fate of 8-methoxypsoralen-photoinduced DNA interstrand crosslinks in Fanconi's anemia cells of defined genetic complementation groups. Mutat. Res. 184, 271-280.
    • (1987) Mutat. Res , vol.184 , pp. 271-280
    • Papadopoulo, D.1    Averbeck, D.2    Moustacchi, E.3
  • 6
    • 0026809517 scopus 로고
    • Defective DNA endonuclease activities in Fanconi's anemia cells, complementation groups A and B
    • Lambert, M. W., Tsongalis, G. J., Lambert, W. C., Hang, B., and Parrish, D. D. (1992) Defective DNA endonuclease activities in Fanconi's anemia cells, complementation groups A and B. Mutat. Res. 273, 57-71.
    • (1992) Mutat. Res , vol.273 , pp. 57-71
    • Lambert, M.W.1    Tsongalis, G.J.2    Lambert, W.C.3    Hang, B.4    Parrish, D.D.5
  • 7
    • 0031584082 scopus 로고    scopus 로고
    • Correction of the DNA repair defect in Fanconi anemia complementation groups A and D cells
    • Lambert, M. W., Tsongalis, G J., Lambert, W. C., and Parrish, D. D. (1997) Correction of the DNA repair defect in Fanconi anemia complementation groups A and D cells. Biochem. Biophys. Res. Commun. 230, 587-591.
    • (1997) Biochem. Biophys. Res. Commun , vol.230 , pp. 587-591
    • Lambert, M.W.1    Tsongalis, G.J.2    Lambert, W.C.3    Parrish, D.D.4
  • 8
    • 0032846684 scopus 로고    scopus 로고
    • A deficiency in a 230 kDa DNA repair protein in Fanconi anemia complementation group A cells is corrected by the FANCA cDNA
    • Brois, D. W., McMahon, L. W., Ramos, N. I., Anglin, L. M., Walsh, C. E., and Lambert, M. W. (1999) A deficiency in a 230 kDa DNA repair protein in Fanconi anemia complementation group A cells is corrected by the FANCA cDNA. Carcinogenesis 20, 1845-1853.
    • (1999) Carcinogenesis , vol.20 , pp. 1845-1853
    • Brois, D.W.1    McMahon, L.W.2    Ramos, N.I.3    Anglin, L.M.4    Walsh, C.E.5    Lambert, M.W.6
  • 9
    • 0034008802 scopus 로고    scopus 로고
    • Fanconi anemia, complementation group A, cells are defective in ability to produce incisions at sites of psoralen interstrand cross-links
    • Kumaresan, K. R., and Lambert, M. W. (2000) Fanconi anemia, complementation group A, cells are defective in ability to produce incisions at sites of psoralen interstrand cross-links. Carcinogenesis 21, 741-751.
    • (2000) Carcinogenesis , vol.21 , pp. 741-751
    • Kumaresan, K.R.1    Lambert, M.W.2
  • 10
    • 29244489543 scopus 로고    scopus 로고
    • Fanconi anemia (cross)linked to DNA repair
    • Niedernhofer, L. J., Lalai, A. S., and Hoeijmakers, J. H. (2005) Fanconi anemia (cross)linked to DNA repair. Cell 123, 1191-1198.
    • (2005) Cell , vol.123 , pp. 1191-1198
    • Niedernhofer, L.J.1    Lalai, A.S.2    Hoeijmakers, J.H.3
  • 11
    • 37349014537 scopus 로고    scopus 로고
    • Deficiency in incisions produced by XPF at the site of a DNA interstrand cross-link in Fanconi anemia cells
    • Kumaresan, K. R., Sridharan, D. M., McMahon, L. W., and Lambert, M. W. (2007) Deficiency in incisions produced by XPF at the site of a DNA interstrand cross-link in Fanconi anemia cells. Biochemistry 46, 14359-14368.
    • (2007) Biochemistry , vol.46 , pp. 14359-14368
    • Kumaresan, K.R.1    Sridharan, D.M.2    McMahon, L.W.3    Lambert, M.W.4
  • 12
    • 0032704895 scopus 로고    scopus 로고
    • Human R spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex
    • McMahon, L. W., Walsh, C. E., and Lambert, M. W. (1999) Human R spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex. J. Biol. Chem. 274, 32904-32908.
    • (1999) J. Biol. Chem , vol.274 , pp. 32904-32908
    • McMahon, L.W.1    Walsh, C.E.2    Lambert, M.W.3
  • 13
    • 0035912843 scopus 로고    scopus 로고
    • Human R spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links
    • McMahon, L. W., Sangerman, J., Goodman, S. R., Kumaresan, K., and Lambert, M. W. (2001) Human R spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links. Biochemistry 40, 7025-7034.
    • (2001) Biochemistry , vol.40 , pp. 7025-7034
    • McMahon, L.W.1    Sangerman, J.2    Goodman, S.R.3    Kumaresan, K.4    Lambert, M.W.5
  • 14
    • 0037350437 scopus 로고    scopus 로고
    • Nonerythroid αII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links
    • Sridharan, D., Brown, M., Lambert, W. C., McMahon, L. W., and Lambert, M. W. (2003) Nonerythroid αII spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links. J. Cell Sci. 116, 823-835.
    • (2003) J. Cell Sci , vol.116 , pp. 823-835
    • Sridharan, D.1    Brown, M.2    Lambert, W.C.3    McMahon, L.W.4    Lambert, M.W.5
  • 15
    • 33750326176 scopus 로고    scopus 로고
    • αII-Spectrin interacts with five groups of functionally important proteins in the nucleus
    • Sridharan, D. M., McMahon, L. W., and Lambert, M. W. (2006) αII-Spectrin interacts with five groups of functionally important proteins in the nucleus. Cell Biol. Int. 30, 866-878.
    • (2006) Cell Biol. Int , vol.30 , pp. 866-878
    • Sridharan, D.M.1    McMahon, L.W.2    Lambert, M.W.3
  • 16
    • 0042171508 scopus 로고    scopus 로고
    • Fanconi anemia cell lines deficient in αII spectrin express normal levels of αII spectrin mRNA
    • Lefferts, J. A., and Lambert, M. W. (2003) Fanconi anemia cell lines deficient in αII spectrin express normal levels of αII spectrin mRNA. Biochem. Biophys. Res. Commun. 307, 510-515.
    • (2003) Biochem. Biophys. Res. Commun , vol.307 , pp. 510-515
    • Lefferts, J.A.1    Lambert, M.W.2
  • 18
    • 64349123561 scopus 로고    scopus 로고
    • Morrow, J. S., Rimm, D. L., Kennedy, S. P., Cianci, C. D., Sinard, J. H., and Weed, S. A. (1997) Of membrane stability and mosaics: the spectrin cytoskeleton, in Handbook of Physiology (Hoffman, J., and Jamieson, J., Eds.) pp 485-540, Oxford, London.
    • Morrow, J. S., Rimm, D. L., Kennedy, S. P., Cianci, C. D., Sinard, J. H., and Weed, S. A. (1997) Of membrane stability and mosaics: the spectrin cytoskeleton, in Handbook of Physiology (Hoffman, J., and Jamieson, J., Eds.) pp 485-540, Oxford, London.
  • 19
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M. A., and Morrow, J. S. (2000) Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113, 2331-2343.
    • (2000) J. Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 20
    • 0033953154 scopus 로고    scopus 로고
    • New insights into functions of erythroid proteins in nonerythroid cells
    • Gascard, P., and Mohandas, N. (2000) New insights into functions of erythroid proteins in nonerythroid cells. Curr. Opin. Hematol. 7, 123-129.
    • (2000) Curr. Opin. Hematol , vol.7 , pp. 123-129
    • Gascard, P.1    Mohandas, N.2
  • 21
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett, V., and Baines, A. J. (2001) Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81, 1353-1392.
    • (2001) Physiol. Rev , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 22
    • 14344265557 scopus 로고    scopus 로고
    • Spectrin repeat proteins in the nucleus
    • Young, K. G., and Kothary, R. (2005) Spectrin repeat proteins in the nucleus. BioEssays 27, 144-152.
    • (2005) BioEssays , vol.27 , pp. 144-152
    • Young, K.G.1    Kothary, R.2
  • 24
    • 0037138380 scopus 로고    scopus 로고
    • Can we infer peptide recognition specificity mediated by SH3 domains?
    • Cesareni, G., Panni, S., Nardelli, G., and Castagnoli, L. (2002) Can we infer peptide recognition specificity mediated by SH3 domains? FEBS Lett. 513, 38-44.
    • (2002) FEBS Lett , vol.513 , pp. 38-44
    • Cesareni, G.1    Panni, S.2    Nardelli, G.3    Castagnoli, L.4
  • 25
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu, H., Chen, J. K., Feng, S., Dalgarno, D. C., Brauer, A. W., and Schreiber, S. L. (1994) Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76, 933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgarno, D.C.4    Brauer, A.W.5    Schreiber, S.L.6
  • 26
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng, S., Chen, J. K., Yu, H., Simon, J. A., and Schreiber, S. L. (1994) Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1247.
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 27
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim, W. A., Richards, F. M., and Fox, R. O. (1994) Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 28
    • 0029281993 scopus 로고
    • SH3 domains. Minding your p's and q's
    • Mayer, B. J., and Eck, M. J. (1995) SH3 domains. Minding your p's and q's. Curr. Biol. 5, 364-367.
    • (1995) Curr. Biol , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 30
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P., and Sudol, M. (2000) The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 31
    • 34247257776 scopus 로고    scopus 로고
    • Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain
    • Casares, S., Lopez-Mayorga, O., Vega, M. C., Camara-Artigas, A., and Conejero-Lara, F. (2007) Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain. Proteins 67, 531-547.
    • (2007) Proteins , vol.67 , pp. 531-547
    • Casares, S.1    Lopez-Mayorga, O.2    Vega, M.C.3    Camara-Artigas, A.4    Conejero-Lara, F.5
  • 32
  • 36
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann, J. C., and Forget, B. G. (1993) Erythroid and nonerythroid spectrins. Blood 81, 3173-3185.
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.C.1    Forget, B.G.2
  • 37
    • 0032577702 scopus 로고    scopus 로고
    • Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton
    • Ziemnicka-Kotula, D., Xu, J., Gu, H., Potempska, A., Kim, K. S., Jenkins, E. C., Trenkner, E., and Kotula, L. (1998) Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton. J. Biol. Chem. 273, 13681-13692.
    • (1998) J. Biol. Chem , vol.273 , pp. 13681-13692
    • Ziemnicka-Kotula, D.1    Xu, J.2    Gu, H.3    Potempska, A.4    Kim, K.S.5    Jenkins, E.C.6    Trenkner, E.7    Kotula, L.8
  • 38
    • 0026749753 scopus 로고
    • SH3 - an abundant protein domain in search of a function
    • Musacchio, A., Gibson, T, Lehto, V. P., and Saraste, M. (1992) SH3 - an abundant protein domain in search of a function. FEBS Lett. 307, 55-61.
    • (1992) FEBS Lett , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 39
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G B., Ren, R., and Baltimore, D. (1995) Modular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 40
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J., and Cowburn, D. (1997) Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26, 259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 41
    • 0031637561 scopus 로고    scopus 로고
    • SH2 and SH3 domains. Unraveling signaling networks with peptide antagonists
    • Stein, R. (1998) SH2 and SH3 domains. Unraveling signaling networks with peptide antagonists. Methods Mol. Biol. 88, 187-195.
    • (1998) Methods Mol. Biol , vol.88 , pp. 187-195
    • Stein, R.1
  • 42
    • 0033042659 scopus 로고    scopus 로고
    • Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis
    • McPherson, P. S. (1999) Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis. Cell Signall. 11, 229-238.
    • (1999) Cell Signall , vol.11 , pp. 229-238
    • McPherson, P.S.1
  • 43
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren, R., Mayer, B. J., Cicchetti, P., and Baltimore, D. (1993) Identification of a ten-amino acid proline-rich SH3 binding site. Science 259, 1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 44
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B. J. (2001) SH3 domains: complexity in moderation. J. Cell Sci. 114, 1253-1263.
    • (2001) J. Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 46
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio, A., Saraste, M., and Wilmanns, M. (1994) High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol. 1, 546-551.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 47
    • 0031160370 scopus 로고    scopus 로고
    • 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
    • 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure. J. Biomol. NMR 9, 347-357.
    • (1997) J. Biomol. NMR , vol.9 , pp. 347-357
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 49
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng, S., Kasahara, C., Rickles, R. J., and Schreiber, S. L. (1995) Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. U.S.A. 92, 12408-12415.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 12408-12415
    • Feng, S.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 50
    • 0035864856 scopus 로고    scopus 로고
    • Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway
    • Medhurst, A. L., Huber, P. A. J., Waisfisz, Q., de Winter, J. P., and Mathew, C. G (2001) Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway. Hum. Mol. Genet. 10, 423-429.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 423-429
    • Medhurst, A.L.1    Huber, P.A.J.2    Waisfisz, Q.3    de Winter, J.P.4    Mathew, C.G.5
  • 51
    • 0023792182 scopus 로고
    • The calmodulin-binding site in α-fodrin is near the calcium-dependent protease-I cleavage site
    • Harris, A. S., Croall, D. E., and Morrow, J. S. (1988) The calmodulin-binding site in α-fodrin is near the calcium-dependent protease-I cleavage site. J. Biol. Chem. 263, 15754-15761.
    • (1988) J. Biol. Chem , vol.263 , pp. 15754-15761
    • Harris, A.S.1    Croall, D.E.2    Morrow, J.S.3
  • 52
    • 0035807751 scopus 로고    scopus 로고
    • Calpain proteolysis of αII-spectrin in the normal adult human brain
    • Huh, G. Y., Glantz, S. B., Je, S., Morrow, J. S., and Kim, J. H. (2001) Calpain proteolysis of αII-spectrin in the normal adult human brain. Neurosci. Lett. 316, 41-44.
    • (2001) Neurosci. Lett , vol.316 , pp. 41-44
    • Huh, G.Y.1    Glantz, S.B.2    Je, S.3    Morrow, J.S.4    Kim, J.H.5
  • 53
    • 33845953686 scopus 로고    scopus 로고
    • Structure of the calmodulin αII-spectrin complex provides insight into the regulation of cell plasticity
    • Simonovic, M., Zhang, Z., Cianci, C. D., Steitz, T. A., and Morrow, J. S. (2006) Structure of the calmodulin αII-spectrin complex provides insight into the regulation of cell plasticity. J. Biol. Chem. 281, 34333-34340.
    • (2006) J. Biol. Chem , vol.281 , pp. 34333-34340
    • Simonovic, M.1    Zhang, Z.2    Cianci, C.D.3    Steitz, T.A.4    Morrow, J.S.5
  • 54
    • 33846210035 scopus 로고    scopus 로고
    • Sequential degradation of αII and βII spectrin by calpain in glutamate or maitotoxin-stimulated cells
    • Glantz, S. B., Cianci, C. D., Iyer, R., Pradhan, D., Wang, K. K., and Morrow, J. S. (2007) Sequential degradation of αII and βII spectrin by calpain in glutamate or maitotoxin-stimulated cells. Biochemistry 46, 502-513.
    • (2007) Biochemistry , vol.46 , pp. 502-513
    • Glantz, S.B.1    Cianci, C.D.2    Iyer, R.3    Pradhan, D.4    Wang, K.K.5    Morrow, J.S.6
  • 55
    • 0042167442 scopus 로고    scopus 로고
    • Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis
    • Williams, S. T., Smith, A. N., Cianci, C. D., Morrow, J. S., and Brown, T. L. (2003) Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis. Apoptosis 8, 353-361.
    • (2003) Apoptosis , vol.8 , pp. 353-361
    • Williams, S.T.1    Smith, A.N.2    Cianci, C.D.3    Morrow, J.S.4    Brown, T.L.5
  • 56
    • 0023765652 scopus 로고
    • Proteolytic processing of human brain alpha spectrin (fodrin): Identification of a hypersensitive site
    • Harris, A. S., and Morrow, J. S. (1988) Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site. J. Neurosci. 8, 2640-2651.
    • (1988) J. Neurosci , vol.8 , pp. 2640-2651
    • Harris, A.S.1    Morrow, J.S.2
  • 57
    • 0024326027 scopus 로고
    • Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease I
    • Harris, A. S., Croall, D. E., and Morrow, J. S. (1989) Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease I. J. Biol. Chem. 264, 17401-17408.
    • (1989) J. Biol. Chem , vol.264 , pp. 17401-17408
    • Harris, A.S.1    Croall, D.E.2    Morrow, J.S.3
  • 59
    • 0037470058 scopus 로고    scopus 로고
    • c-Src binds αII spectrin's Src homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176
    • Nedrelow, J. H., Cianci, C. D., and Morrow, J. S. (2003) c-Src binds αII spectrin's Src homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176. J. Biol. Chem. 278, 7735-7741.
    • (2003) J. Biol. Chem , vol.278 , pp. 7735-7741
    • Nedrelow, J.H.1    Cianci, C.D.2    Morrow, J.S.3
  • 60
    • 0027936659 scopus 로고
    • Characterization of the interaction of natural proline-rich peptides with five different SH3 domains
    • Viguera, A. R., Arrondo, J. L., Musacchio, A., Saraste, M., and Serrano, L. (1994) Characterization of the interaction of natural proline-rich peptides with five different SH3 domains. Biochemistry 33, 10925-10933.
    • (1994) Biochemistry , vol.33 , pp. 10925-10933
    • Viguera, A.R.1    Arrondo, J.L.2    Musacchio, A.3    Saraste, M.4    Serrano, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.