메뉴 건너뛰기




Volumn 45, Issue 41, 2006, Pages 12582-12595

Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BIOASSAY; COMPLEXATION; FILTRATION; GELS;

EID: 33750054653     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060991e     Document Type: Article
Times cited : (49)

References (74)
  • 4
    • 0025967015 scopus 로고
    • Novel myosin heavy chain encoded by murine dilute coat colour locus
    • Mercer, J. A., Seperack, P. K., Strobel, M. C., Copeland, N. G., and Jenkins, N. A. (1991) Novel myosin heavy chain encoded by murine dilute coat colour locus, Nature 349, 709-713.
    • (1991) Nature , vol.349 , pp. 709-713
    • Mercer, J.A.1    Seperack, P.K.2    Strobel, M.C.3    Copeland, N.G.4    Jenkins, N.A.5
  • 6
    • 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. (2000) 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, 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
  • 9
    • 33644548665 scopus 로고    scopus 로고
    • Structural basis for myosin V discrimination between distinct cargoes
    • Pashkova, N., Jin, Y., Ramaswamy, S., and Weisman, L. S. (2006) Structural basis for myosin V discrimination between distinct cargoes, EMBO J. 25, 693-700.
    • (2006) EMBO J. , vol.25 , pp. 693-700
    • Pashkova, N.1    Jin, Y.2    Ramaswamy, S.3    Weisman, L.S.4
  • 10
    • 0029056416 scopus 로고
    • Retroviral sequences located within an intron of the dilute gene alter dilute expression in a tissue-specific manner
    • Seperack, P. K., Mercer, J. A., Strobel, M. C., Copeland, N. G., and Jenkins, N. A. (1995) Retroviral sequences located within an intron of the dilute gene alter dilute expression in a tissue-specific manner, EMBO J. 14, 2326-2332.
    • (1995) EMBO J. , vol.14 , pp. 2326-2332
    • Seperack, P.K.1    Mercer, J.A.2    Strobel, M.C.3    Copeland, N.G.4    Jenkins, N.A.5
  • 13
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/ melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • Fukuda, M., Kuroda, T. S., and Mikoshiba, K. (2002) Slac2-a/ melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport, J Biol. Chem. 277, 12432-12436.
    • (2002) J Biol. Chem. , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 14
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport
    • Strom, M., Hume, A. N., Tarafder, A. K., Barkagianni, E., and Seabra, M. C. (2002) A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport, J. Biol. Chem. 277, 25423-25430.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 17
    • 1642286846 scopus 로고    scopus 로고
    • Myosin V: Regulation by calcium, calmodulin, and the tail domain
    • Krementsov, D. N., Krementsova, E. B., and Trybus, K. M. (2004) Myosin V: Regulation by calcium, calmodulin, and the tail domain, J. Cell Biol. 164, 877-886.
    • (2004) J. Cell Biol. , vol.164 , pp. 877-886
    • Krementsov, D.N.1    Krementsova, E.B.2    Trybus, K.M.3
  • 18
    • 1242317813 scopus 로고    scopus 로고
    • 2+-Induced activation of ATPase activity of myosin Va is accompanied with a large conformational change
    • 2+-Induced activation of ATPase activity of myosin Va is accompanied with a large conformational change, Biochem. Biophys. Res. Commun. 315, 538.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 538
    • Li, X.-D.1    Mabuchi, K.2    Ikebe, R.3    Ikebe, M.4
  • 20
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • Liu, J., Taylor, D. W., Krementsova, E. B., Trybus, K. M., and Taylor, K. A. (2006) Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography, Nature 442, 208-211.
    • (2006) Nature , vol.442 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 21
    • 33746152398 scopus 로고    scopus 로고
    • The cargo-binding domain regulates structure and activity of myosin 5
    • Thirumurugan, K., Sakamoto, T., Hammer, J. A., III, Sellers, J. R., and Knight, P. J. (2006) The cargo-binding domain regulates structure and activity of myosin 5, Nature 442, 212-215.
    • (2006) Nature , vol.442 , pp. 212-215
    • Thirumurugan, K.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Knight, P.J.5
  • 22
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S. M. (2000) The dynein microtubule motor, Biochim. Biophys. Acta 1496, 60-75.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 23
    • 0028990156 scopus 로고
    • r = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues
    • r = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues, J. Biol. Chem. 270, 11445-11452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11445-11452
    • King, S.M.1    Patel-King, R.S.2
  • 24
    • 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. (2001) The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif, J. Biol. Chem. 276, 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
  • 25
    • 0034862996 scopus 로고    scopus 로고
    • Light chains of mammalian cytoplasmic dynein: Identification and characterization of a family of LC8 light chains
    • Wilson, M. J., Salata, M. W., Susalka, S. J., and Pfister, K. K. (2001) Light chains of mammalian cytoplasmic dynein: Identification and characterization of a family of LC8 light chains, Cell Motil. Cytoskeleton 49, 229-240.
    • (2001) Cell Motil. Cytoskeleton , vol.49 , pp. 229-240
    • Wilson, M.J.1    Salata, M.W.2    Susalka, S.J.3    Pfister, K.K.4
  • 26
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S. R., and Snyder, S. H. (1996) PIN: An associated protein inhibitor of neuronal nitric oxide synthase, Science 274, 774-777.
    • (1996) Science , vol.274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 27
    • 0032533611 scopus 로고    scopus 로고
    • Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition
    • Rodriguez-Crespo, I., Straub, W., Gavilanes, F., and Ortiz de Montellano, P. R. (1998) Binding of dynein light chain (PIN) to neuronal nitric oxide synthase in the absence of inhibition, Arch. Biochem. Biophys. 359, 297-304.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 297-304
    • Rodriguez-Crespo, I.1    Straub, W.2    Gavilanes, F.3    Ortiz De Montellano, P.R.4
  • 28
    • 0030613781 scopus 로고    scopus 로고
    • IκBα 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. (1997) IκBα physically interacts with a cytoskeleton-associated protein through its signal response domain, Mol. Cell Biol. 17, 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
  • 29
    • 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. (2000) The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes, Nat. Cell Biol. 2, 185-190.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 30
    • 10644221806 scopus 로고    scopus 로고
    • Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein
    • Wang, L., Hare, M., Hays, T. S., and Barbar, E. (2004) Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein, Biochemistry 43, 4611-4620.
    • (2004) Biochemistry , vol.43 , pp. 4611-4620
    • Wang, L.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 33
    • 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. (2000) The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase, Genes Cells 5, 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
  • 34
    • 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. (2000) Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein, J. Neurosci. 20, 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
  • 36
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath, H., Villunger, A., O'Reilly, L. A., Beaumont, J. G., Coultas, L., Cheney, R. E., Huang, D. C., and Strasser, A. (2001) Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis, Science 293, 1829-1832.
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 37
    • 14844333111 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation
    • Lo, K. W., Kan, H. M., Chan, L. N., Xu, W. G., Wang, K. P., Wu, Z., Sheng, M., and Zhang, M. (2005) The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation, J. Biol. Chem. 280, 8172-8179.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8172-8179
    • Lo, K.W.1    Kan, H.M.2    Chan, L.N.3    Xu, W.G.4    Wang, K.P.5    Wu, Z.6    Sheng, M.7    Zhang, M.8
  • 38
    • 0038356539 scopus 로고    scopus 로고
    • Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique
    • Martinez-Moreno, M., Navarro-Lerida, I., Roncal, F., Albar, J. P., Alonso, C., Gavilanes, F., and Rodriguez-Crespo, I. (2003) Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique, FEBS Lett. 544, 262-267.
    • (2003) FEBS Lett. , vol.544 , pp. 262-267
    • Martinez-Moreno, M.1    Navarro-Lerida, I.2    Roncal, F.3    Albar, J.P.4    Alonso, C.5    Gavilanes, F.6    Rodriguez-Crespo, I.7
  • 39
    • 0034782383 scopus 로고    scopus 로고
    • Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: Dissociation of dynein-binding properties and transcriptional functionality of P
    • Poisson, N., Real, E., Gaudin, Y., Vaney, M. C., King, S., Jacob, Y., Tordo, N., and Blondel, D. (2001) Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: Dissociation of dynein-binding properties and transcriptional functionality of P, J. Gen. Virol. 82, 2691-2696.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2691-2696
    • Poisson, N.1    Real, E.2    Gaudin, Y.3    Vaney, M.C.4    King, S.5    Jacob, Y.6    Tordo, N.7    Blondel, D.8
  • 41
    • 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. (2001) Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique, FEBS Lett. 503, 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
  • 42
    • 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. (1996) Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster, Mol. Cell Biol. 16, 1966-1977.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1966-1977
    • Dick, T.1    Ray, K.2    Salz, H.K.3    Chia, W.4
  • 45
    • 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. (2001) Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain, J. Mol. Biol. 306, 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
  • 46
    • 33750081796 scopus 로고    scopus 로고
    • Alternatively spliced exon B of myosin Va is essential for binding of the tail light chain shared by dynein
    • Hodi, Z. N., A., Hetényi, Cs., Bodor, A., Perczel, A., and Nyitray, L. (2005) Alternatively spliced exon B of myosin Va is essential for binding of the tail light chain shared by dynein, J. Muscle Res. Cell Motil 26, 73.
    • (2005) J. Muscle Res. Cell Motil , vol.26 , pp. 73
    • Hodi, Z.N.1    Hetényi, Cs.2    Bodor, A.3    Perczel, A.4    Nyitray, L.5
  • 47
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 48
    • 0025211779 scopus 로고
    • Quantitation of protein
    • Stoscheck, C. M. (1990) Quantitation of protein, Methods Enzymol. 182, 50-68.
    • (1990) Methods Enzymol. , vol.182 , pp. 50-68
    • Stoscheck, C.M.1
  • 49
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 50
    • 1842295721 scopus 로고    scopus 로고
    • Retinoic acid induced neural differentiation in a neuroectodermal cell line immortalized by p53 deficiency
    • Schlett, K., and Madarasz, E. (1997) Retinoic acid induced neural differentiation in a neuroectodermal cell line immortalized by p53 deficiency, J. Neurosci. Res. 47, 405-415.
    • (1997) J. Neurosci. Res. , vol.47 , pp. 405-415
    • Schlett, K.1    Madarasz, E.2
  • 52
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding, R., Russell, R. B., Neduva, V., and Gibson, T. J. (2003) GlobPlot: Exploring protein sequences for globularity and disorder, Nucleic Acids Res. 31, 3701-3708.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 53
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy, J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 54
    • 0032568543 scopus 로고    scopus 로고
    • The structure of the N-terminus of striated muscle α-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies
    • Greenfield, N. J., Montelione, G. T., Farid, R. S., and Hitchcock-DeGregori, S. E. (1998) The structure of the N-terminus of striated muscle α-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies, Biochemistry 37, 7834-7843.
    • (1998) Biochemistry , vol.37 , pp. 7834-7843
    • Greenfield, N.J.1    Montelione, G.T.2    Farid, R.S.3    Hitchcock-DeGregori, S.E.4
  • 55
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A., and Johnson, W. C., Jr. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication, Anal. Biochem. 155, 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 56
    • 0030874298 scopus 로고    scopus 로고
    • Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides
    • Rohl, C. A., and Baldwin, R. L. (1997) Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides, Biochemistry 36, 8435-8442.
    • (1997) Biochemistry , vol.36 , pp. 8435-8442
    • Rohl, C.A.1    Baldwin, R.L.2
  • 57
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 58
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and van der Spoel, D. (2001) GROMACS 3.0: A package for molecular simulation and trajectory analysis, J. Mol. Model. 8, 306-317.
    • (2001) J. Mol. Model. , vol.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 59
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 60
    • 0141925238 scopus 로고    scopus 로고
    • A comprehensive docking study on the selectivity of binding of aromatic compounds to proteins
    • Hetenyi, C., Maran, U., Karelson, M. (2003) A comprehensive docking study on the selectivity of binding of aromatic compounds to proteins, J. Chem. Inf. Comput. Sci. 43, 1576-1583.
    • (2003) J. Chem. Inf. Comput. Sci. , vol.43 , pp. 1576-1583
    • Hetenyi, C.1    Maran, U.2    Karelson, M.3
  • 61
    • 20444414152 scopus 로고    scopus 로고
    • Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition
    • Fodor, K., Harmat, V., Hetenyi, C., Kardos, J., Antal, J., Perczel, A., Patthy, A., Katona, G., and Graf, L. (2005) Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition, J. Mol. Biol. 350, 156-169.
    • (2005) J. Mol. Biol. , vol.350 , pp. 156-169
    • Fodor, K.1    Harmat, V.2    Hetenyi, C.3    Kardos, J.4    Antal, J.5    Perczel, A.6    Patthy, A.7    Katona, G.8    Graf, L.9
  • 62
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico, E. M., Cheney, R. E., Matteoli, M., Nascimento, A. A., De Camilli, P. V., Larson, R. E., and Mooseker, M. S. (1992) Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains, J. Cell Biol. 119, 1541-1557.
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.4    De Camilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 63
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar, E., Kleinman, B., Imhoff, D., Li, M., Hays, T. S., and Hare, M. (2001) Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein, Biochemistry 40, 1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 64
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils
    • Lau, S. Y., Taneja, A. K., and Hodges, R. S. (1984) Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils, J. Biol. Chem. 259, 13253-13261.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.1    Taneja, A.K.2    Hodges, R.S.3
  • 65
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sonnichsen, F., Van Eyk, J., Hodges, R., and Sykes, B. (1992) Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide, Biochemistry 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, F.1    Van Eyk, J.2    Hodges, R.3    Sykes, B.4
  • 66
    • 0036382925 scopus 로고    scopus 로고
    • Unfolding of a leucine zipper is not a simple two-state transition
    • Dragan, A. I., and Privalov, P. L. (2002) Unfolding of a leucine zipper is not a simple two-state transition, J. Mol. Biol. 321, 891-908.
    • (2002) J. Mol. Biol. , vol.321 , pp. 891-908
    • Dragan, A.I.1    Privalov, P.L.2
  • 67
    • 4043144340 scopus 로고    scopus 로고
    • Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: The case of PIN, a protein with multiple natural partners
    • Lajoix, A. D., Gross, R., Aknin, C., Dietz, S., Granier, C., and Laune, D. (2004) Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: The case of PIN, a protein with multiple natural partners, Mol. Diversity 8, 281-290.
    • (2004) Mol. Diversity , vol.8 , pp. 281-290
    • Lajoix, A.D.1    Gross, R.2    Aknin, C.3    Dietz, S.4    Granier, C.5    Laune, D.6
  • 68
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins, Trends Biochem. Sci. 27, 527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 71
    • 10644253619 scopus 로고    scopus 로고
    • The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8
    • Nyarko, A., Hare, M., Hays, T. S., and Barbar, E. (2004) The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8, Biochemistry 43, 15595-15603.
    • (2004) Biochemistry , vol.43 , pp. 15595-15603
    • Nyarko, A.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 72
    • 20444488809 scopus 로고    scopus 로고
    • Crystal structure of dynein light chain TcTex-1
    • Williams, J. C., Xie, H., and Hendrickson, W. A. (2005) Crystal structure of dynein light chain TcTex-1, J. Biol. Chem. 280, 21981-21986.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21981-21986
    • Williams, J.C.1    Xie, H.2    Hendrickson, W.A.3
  • 73
    • 13844275995 scopus 로고    scopus 로고
    • Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions
    • Wu, H., Maciejewski, M. W., Takebe, S., and King, S. M. (2005) Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions, Structure 13, 213-223.
    • (2005) Structure , vol.13 , pp. 213-223
    • Wu, H.1    Maciejewski, M.W.2    Takebe, S.3    King, S.M.4
  • 74
    • 0035957959 scopus 로고    scopus 로고
    • Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain
    • Mok, Y. K., Lo, K. W., and Zhang, M. (2001) Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain, J. Biol. Chem. 276, 14067-14074.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14067-14074
    • Mok, Y.K.1    Lo, K.W.2    Zhang, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.