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Volumn 8, Issue 3, 2004, Pages 281-290

Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: The case of PIN, a protein with multiple natural partners

Author keywords

peptide array; PIN; spot technique

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; GEPHYRIN; MYOSIN V; NITRIC OXIDE SYNTHASE; TRANSCRIPTION FACTOR;

EID: 4043144340     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MODI.0000036242.01129.27     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 0033580887 scopus 로고    scopus 로고
    • Protein interaction methods - Toward an endgame
    • Mendelsohn, A. R. and Brent, R., Protein interaction methods - Toward an endgame, Science, 284 (1999) 1948-1950.
    • (1999) Science , vol.284 , pp. 1948-1950
    • Mendelsohn, A.R.1    Brent, R.2
  • 2
    • 0036898579 scopus 로고    scopus 로고
    • Protein microarrays and proteomics
    • MacBeath, G., Protein microarrays and proteomics, Nat. Genet., 32 Suppl. (2002) 526-532.
    • (2002) Nat. Genet. , vol.32 , Issue.SUPPL. , pp. 526-532
    • MacBeath, G.1
  • 3
    • 0026656122 scopus 로고
    • Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank, R., Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support, Tetrahedron, 48 (1992) 9217-9232.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 5
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices
    • O'Neil, K. T. and DeGrado, W. F., How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices, Trends Biochem. Sci., 15 (1990) 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 6
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S. R. and Snyder, S. H., PIN: An associated protein inhibitor of neuronal nitric oxide synthase, Science, 274 (1996) 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 7
    • 0029784022 scopus 로고    scopus 로고
    • Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain
    • King, S. M., Barbarese, E., Dillman, J. F., Patel-King, R. S., Carson, J. H. and Poster, K. K., Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain, J. Biol. Chem., 271 (1996) 19358-19366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19358-19366
    • King, S.M.1    Barbarese, E.2    Dillman, J.F.3    Patel-King, R.S.4    Carson, J.H.5    Poster, K.K.6
  • 8
    • 0028990156 scopus 로고
    • The M(r) = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues
    • King, S. M. and Patel-King, R. S., The M(r) = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues, J. Biol. Chem., 270 (1995) 11445-11452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11445-11452
    • King, S.M.1    Patel-King, R.S.2
  • 9
    • 0030861056 scopus 로고    scopus 로고
    • Dimerization of the highly conserved light chain shared by dynein and myosin V
    • Benashski, S. E., Harrison, A., Patel-King, R. S. and King, S. M., Dimerization of the highly conserved light chain shared by dynein and myosin V, J. Biol. Chem., 272 (1997) 20929-20935.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20929-20935
    • Benashski, S.E.1    Harrison, A.2    Patel-King, R.S.3    King, S.M.4
  • 10
    • 0033661719 scopus 로고    scopus 로고
    • The light chain composition of chicken brain myosin-Va: Calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN
    • Espindola, F. S., Suter, D. M., Partata, L. B., Cao, T., Wolenski, J. S., Cheney, R. E., King, S. M. and Mooseker, M. S., The light chain composition of chicken brain myosin-Va: Calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN, Cell Motil. Cytoskeleton, 47 (2000) 269-281.
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 269-281
    • Espindola, F.S.1    Suter, D.M.2    Partata, L.B.3    Cao, T.4    Wolenski, J.S.5    Cheney, R.E.6    King, S.M.7    Mooseker, M.S.8
  • 11
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath, H., Huang, D. C., O'Reilly, L. A., King, S. M. and Strasser, A., The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex, Mol. Cell, 3 (1999) 287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 12
    • 0030613781 scopus 로고    scopus 로고
    • I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain
    • Crepieux, P., Kwon, H., Leclerc, N., Spencer, W., Richard, S., Lin, R. and Hiscott, J., I kappaB alpha physically interacts with a cytoskeleton- associated protein through its signal response domain, Mol. Cell. Biol. 17 (1997) 7375-7385.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7375-7385
    • Crepieux, P.1    Kwon, H.2    Leclerc, N.3    Spencer, W.4    Richard, S.5    Lin, R.6    Hiscott, J.7
  • 13
    • 0034515174 scopus 로고    scopus 로고
    • The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase
    • Haraguchi, K., Satoh, K., Yanai, H., Hamada, F., Kawabuchi, M. and Akiyama, T., The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase, Genes Cells, 5 (2000) 905-911.
    • (2000) Genes Cells , vol.5 , pp. 905-911
    • Haraguchi, K.1    Satoh, K.2    Yanai, H.3    Hamada, F.4    Kawabuchi, M.5    Akiyama, T.6
  • 14
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt, S., Valtschanoff, J., Allison, D. W., Sala, C., Kim, E., Craig, A. M., Weinberg, R. J. and Sheng, M., Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein, J. Neurosci., 20 (2000) 4524-4534.
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 15
    • 0034529440 scopus 로고    scopus 로고
    • Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila
    • Herzig, R. P., Andersson, U. and Scarpulla, R. C., Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila, J. Cell Sci., 113 Pt 23 (2000) 4263-4273.
    • (2000) J. Cell Sci. , vol.113 , Issue.23 PART , pp. 4263-4273
    • Herzig, R.P.1    Andersson, U.2    Scarpulla, R.C.3
  • 17
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer, F., Bohmann, K. and Nusslein-Volhard, C., The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes, Nat. Cell Biol., 2 (2000) 185-190.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 18
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob, Y., Badrane, H., Ceccaldi, P. E. and Tordo, N., Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein, J. Virol., 74 (2000) 10217-10222.
    • (2000) J. Virol. , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 19
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux, H., Flamand, A. and Blondel, D., Interaction of the rabies virus P protein with the LC8 dynein light chain, J. Virol., 74 (2000) 10212-10216.
    • (2000) J. Virol. , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 20
    • 0029977560 scopus 로고    scopus 로고
    • Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster
    • Dick, T., Ray, K., Salz, H. K. and Chia, W., Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster, Mol. Cell. Biol., 16 (1996) 1966-1977.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1966-1977
    • Dick, T.1    Ray, K.2    Salz, H.K.3    Chia, W.4
  • 21
    • 0033756160 scopus 로고    scopus 로고
    • Cyclooxygenase 2 promotes cell survival by stimulation of dynein light chain expression and inhibition of neuronal nitric oxide synthase activity
    • Chang, Y. W., Jakobi, R., McGinty, A., Foschi, M., Dunn, M. J. and Sorokin, A., Cyclooxygenase 2 promotes cell survival by stimulation of dynein light chain expression and inhibition of neuronal nitric oxide synthase activity, Mol. Cell. Biol., 20 (2000) 8571-8579.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8571-8579
    • Chang, Y.W.1    Jakobi, R.2    McGinty, A.3    Foschi, M.4    Dunn, M.J.5    Sorokin, A.6
  • 23
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • Fan, J., Zhang, Q., Tochio, H., Li, M. and Zhang, M., Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain, J. Mol. Biol., 306 (2001) 97-108.
    • (2001) J. Mol. Biol. , vol.306 , pp. 97-108
    • Fan, J.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.5
  • 24
    • 0035859852 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar, E., Hare, M., Makokha, M., Barany, G. and Woodward, C., Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein, Biochemistry, 40 (2001) 9734-9742.
    • (2001) Biochemistry , vol.40 , pp. 9734-9742
    • Barbar, E.1    Hare, M.2    Makokha, M.3    Barany, G.4    Woodward, C.5
  • 25
    • 0031791314 scopus 로고    scopus 로고
    • Solution structure of a protein inhibitor of neuronal nitric oxide synthase
    • Tochio, H., Ohki, S., Zhang, Q., Li, M. and Zhang, M., Solution structure of a protein inhibitor of neuronal nitric oxide synthase, Nat. Struct. Biol., 5 (1998) 965-969.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 965-969
    • Tochio, H.1    Ohki, S.2    Zhang, Q.3    Li, M.4    Zhang, M.5
  • 26
    • 0036721676 scopus 로고    scopus 로고
    • Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding
    • Laune, D., Molina, F., Ferrieres, G., Villard, S., Bes, C., Rieunier, F., Chardes, T. and Granier, C., Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding, J. Immunol. Methods, 267 (2002) 53-70.
    • (2002) J. Immunol. Methods , vol.267 , pp. 53-70
    • Laune, D.1    Molina, F.2    Ferrieres, G.3    Villard, S.4    Bes, C.5    Rieunier, F.6    Chardes, T.7    Granier, C.8
  • 27
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo, K. W., Naisbitt, S., Fan, J. S., Sheng, M. and Zhang, M., The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif, J. Biol. Chem., 276 (2001) 14059-14066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.5
  • 28
    • 0035903004 scopus 로고    scopus 로고
    • Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique
    • Rodriguez-Crespo, I., Yelamos, B., Roncal, F., Albar, J. P., Ortiz de Montellano, P. R. and Gavilanes, F., Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique, FEBS Lett., 503 (2001) 135-141.
    • (2001) FEBS Lett. , vol.503 , pp. 135-141
    • Rodriguez-Crespo, I.1    Yelamos, B.2    Roncal, F.3    Albar, J.P.4    Ortiz De Montellano, P.R.5    Gavilanes, F.6
  • 29
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T. D. and Stephens, R. M., Sequence logos: A new way to display consensus sequences, Nucleic Acids Res., 18 (1990) 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 30
    • 0033669189 scopus 로고    scopus 로고
    • A network of protein-protein interactions in yeast
    • Schwikowski, B., Uetz, P. and Fields, S., A network of protein-protein interactions in yeast, Nat. Biotechnol., 18 (2000) 1257-1261.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1257-1261
    • Schwikowski, B.1    Uetz, P.2    Fields, S.3
  • 31
    • 0029996090 scopus 로고    scopus 로고
    • Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria
    • McCarty, J. S., Rudiger, S., Schonfeld, H. J., Schneider-Mergener, J., Nakahigashi, K., Yura, T. and Bukau, B., Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria, J. Mol. Biol., 256 (1996) 829-837.
    • (1996) J. Mol. Biol. , vol.256 , pp. 829-837
    • McCarty, J.S.1    Rudiger, S.2    Schonfeld, H.J.3    Schneider-Mergener, J.4    Nakahigashi, K.5    Yura, T.6    Bukau, B.7
  • 32
    • 0343526912 scopus 로고    scopus 로고
    • Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- And C-terminal low affinity contributing regions
    • Ferrieres, G., Pugniere, M., Mani, J. C., Villard, S., Laprade, M., Doutre, P., Pau, B. and Granier, C., Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- and C-terminal low affinity contributing regions, FEBS Lett., 479 (2000) 99-105.
    • (2000) FEBS Lett. , vol.479 , pp. 99-105
    • Ferrieres, G.1    Pugniere, M.2    Mani, J.C.3    Villard, S.4    Laprade, M.5    Doutre, P.6    Pau, B.7    Granier, C.8
  • 33
    • 0031438526 scopus 로고    scopus 로고
    • Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody
    • Kramer, A., Keitel, T., Winkler, K., Stocklein, W., Hohne, W. and Schneider-Mergener, J., Molecular basis for the binding promiscuity of an anti-p24 (HIV-1) monoclonal antibody, Cell, 91 (1997) 799-809.
    • (1997) Cell , vol.91 , pp. 799-809
    • Kramer, A.1    Keitel, T.2    Winkler, K.3    Stocklein, W.4    Hohne, W.5    Schneider-Mergener, J.6
  • 35
    • 0035996716 scopus 로고    scopus 로고
    • Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity
    • Fan, J. S., Zhang, Q., Tochio, H. and Zhang, M., Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity, J. Biomol. NMR, 23 (2002) 103-114.
    • (2002) J. Biomol. NMR , vol.23 , pp. 103-114
    • Fan, J.S.1    Zhang, Q.2    Tochio, H.3    Zhang, M.4


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