메뉴 건너뛰기




Volumn 46, Issue 23, 2007, Pages 6931-6943

Acid-induced equilibrium folding intermediate of human platelet profilin

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; DICHROISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH EFFECTS; PHASE EQUILIBRIA; PLATELETS;

EID: 34250199732     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0602359     Document Type: Article
Times cited : (23)

References (65)
  • 1
    • 0023878565 scopus 로고
    • Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis
    • Kwiatkowski, D. J., and Bruns, G. A. (1988) Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis, J. Biol. Chem. 263, 5910-5915.
    • (1988) J. Biol. Chem , vol.263 , pp. 5910-5915
    • Kwiatkowski, D.J.1    Bruns, G.A.2
  • 2
    • 0024254063 scopus 로고
    • The intron-containing gene for yeast profilin (PFY) encodes a vital function
    • Magdolen, V., Oechsner, U., Muller, G., and Bandlow, W. (1988) The intron-containing gene for yeast profilin (PFY) encodes a vital function, Mol. Cell. Biol. 8, 5108-5115.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 5108-5115
    • Magdolen, V.1    Oechsner, U.2    Muller, G.3    Bandlow, W.4
  • 3
    • 0028212157 scopus 로고
    • Profilin mutations disrupt multiple actin-dependent processes during Drosophila development
    • Verheyen, E. M., and Cooley, L. (1994) Profilin mutations disrupt multiple actin-dependent processes during Drosophila development, Development 120, 717-728.
    • (1994) Development , vol.120 , pp. 717-728
    • Verheyen, E.M.1    Cooley, L.2
  • 4
    • 0027301550 scopus 로고
    • Cloning and expression of a novel human profilin variant, profilin II
    • Honore, B., Madscn, P., Andersen, A. H., and Leffers, H. (1993) Cloning and expression of a novel human profilin variant, profilin II, FEBS Lett. 330, 151-155.
    • (1993) FEBS Lett , vol.330 , pp. 151-155
    • Honore, B.1    Madscn, P.2    Andersen, A.H.3    Leffers, H.4
  • 5
    • 0031024690 scopus 로고    scopus 로고
    • The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences
    • Lambrechts, A., Verschelde, J. L., Jonckheere, V., Goethals, M., Vandekerckhove, J., and Ampe, C. (1997) The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences, EMBO J. 16, 484-494.
    • (1997) EMBO J , vol.16 , pp. 484-494
    • Lambrechts, A.1    Verschelde, J.L.2    Jonckheere, V.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 6
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in nonmuscle cells
    • Carlsson, L., Nystrom, L. E., Sundkvist, I., Markey, F., and Lindberg, U. (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in nonmuscle cells, J. Mol. Biol. 115, 465-483.
    • (1977) J. Mol. Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 7
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard, T. D., and Cooper, J. A. (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation, Biochemistry 23, 6631-66341.
    • (1984) Biochemistry , vol.23 , pp. 6631-66341
    • Pollard, T.D.1    Cooper, J.A.2
  • 8
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont, P. J., Furman, M. I., Wachsstock, D., Safer, D., Nachmias, V. T., and Pollard, T. D. (1992) The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells, Mol. Biol. Cell 3, 1015-1024.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 9
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni, D., and Carlier, M. F. (1993) How profilin promotes actin filament assembly in the presence of thymosin beta 4, Cell 75, 1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 10
    • 0027739978 scopus 로고
    • The three faces of profilin
    • Theriot, J. A., and Mitchison, T. J. (1993) The three faces of profilin, Cell 75, 835-838.
    • (1993) Cell , vol.75 , pp. 835-838
    • Theriot, J.A.1    Mitchison, T.J.2
  • 11
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hvdrolvsis bv phospholipase C
    • Goldschmidt-Clermont, P. J., Machesky, L. M., Baldassare, J. J., and Pollard, T. D. (1990) The actin-binding protein profilin binds to PIP2 and inhibits its hvdrolvsis bv phospholipase C, Science 247, 1575-1578.
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    Machesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 12
    • 0025760751 scopus 로고
    • Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation
    • Goldschmidt-Clermont, P. J., Kim, J. W., Machesky, L. M., Rhee, S. G., and Pollard, T. D. (1991) Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation, Science 251, 1231-1233.
    • (1991) Science , vol.251 , pp. 1231-1233
    • Goldschmidt-Clermont, P.J.1    Kim, J.W.2    Machesky, L.M.3    Rhee, S.G.4    Pollard, T.D.5
  • 13
    • 0033056947 scopus 로고    scopus 로고
    • Profilin binds proline-rich ligands in two distinct amide backbone orientations
    • Mahoney, N. M., Rozwarski, D. A., Fedorov, E., Fedorov, A. A., and Almo, S. C. (1999) Profilin binds proline-rich ligands in two distinct amide backbone orientations, Nat. Struct. Biol. 6, 666-671.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 666-671
    • Mahoney, N.M.1    Rozwarski, D.A.2    Fedorov, E.3    Fedorov, A.A.4    Almo, S.C.5
  • 14
    • 0030710460 scopus 로고    scopus 로고
    • Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation
    • Mahoney, N. M., Janmey, P. A., and Almo, S. C. (1997) Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation, Nat. Struct. Biol. 4, 953-960.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 953-960
    • Mahoney, N.M.1    Janmey, P.A.2    Almo, S.C.3
  • 15
    • 0031446340 scopus 로고    scopus 로고
    • WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
    • Ramesh, N., Anton, I. M., Hartwig, J. H., and Geha, R. S. (1997) WIP, a protein associated with wiskott-aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells, Proc. Natl. Acad. Sci. U.S.A. 94, 14671-14676.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 14671-14676
    • Ramesh, N.1    Anton, I.M.2    Hartwig, J.H.3    Geha, R.S.4
  • 16
    • 0035341466 scopus 로고    scopus 로고
    • A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization
    • Zhao, W. M., Jiang, C., Kroll, T. T., and Huber, P. W. (2001) A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization, EMBO J. 20, 2315-2325.
    • (2001) EMBO J , vol.20 , pp. 2315-2325
    • Zhao, W.M.1    Jiang, C.2    Kroll, T.T.3    Huber, P.W.4
  • 17
    • 0035137208 scopus 로고    scopus 로고
    • Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae
    • Ozaki-Kuroda, K., Yamamoto, Y., Nohara, H., Kinoshita, M., Fujiwara, T., Irie, K., and Takai, Y. (2001) Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae, Mol. Cell. Biol. 21, 827-839.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 827-839
    • Ozaki-Kuroda, K.1    Yamamoto, Y.2    Nohara, H.3    Kinoshita, M.4    Fujiwara, T.5    Irie, K.6    Takai, Y.7
  • 19
    • 0028826707 scopus 로고
    • Regulation of profilin localization in Saccharomyces cerevisiae by phosphoinositide metabolism
    • Ostrander, D. B., Gorman, J. A., and Carman, G. M. (1995) Regulation of profilin localization in Saccharomyces cerevisiae by phosphoinositide metabolism, J. Biol. Chem. 270, 27045-27050.
    • (1995) J. Biol. Chem , vol.270 , pp. 27045-27050
    • Ostrander, D.B.1    Gorman, J.A.2    Carman, G.M.3
  • 20
    • 0024466698 scopus 로고
    • Association of profilin with filament-free regions of human leukocyte and platelet membranes and reversible membrane binding during platelet activation
    • Hartwig, J. H., Chambers, K. A., Hopcia, K. L., and Kwiatkowski, D. J. (1989) Association of profilin with filament-free regions of human leukocyte and platelet membranes and reversible membrane binding during platelet activation, J. Cell Biol. 109, 1571-1579.
    • (1989) J. Cell Biol , vol.109 , pp. 1571-1579
    • Hartwig, J.H.1    Chambers, K.A.2    Hopcia, K.L.3    Kwiatkowski, D.J.4
  • 21
    • 0031937368 scopus 로고    scopus 로고
    • Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acanthamoeba castellanii
    • Bubb, M. R., Baines, I. C., and Korn, E. D. (1998) Localization of actobindin, profilin I, profilin II, and phosphatidylinositol-4,5-bisphosphate (PIP2) in Acanthamoeba castellanii, Cell Motil. Cytoskeleton 39, 134-146.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 134-146
    • Bubb, M.R.1    Baines, I.C.2    Korn, E.D.3
  • 22
    • 0025932041 scopus 로고
    • A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
    • van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H., and Pattus, F. (1991) A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A, Nature 354, 408-410.
    • (1991) Nature , vol.354 , pp. 408-410
    • van der Goot, F.G.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 23
    • 0022537005 scopus 로고
    • Lateral proton conduction at lipid-water interfaces and its implications for the chemiosmotic-coupling hypothesis
    • Prats, M., Teissie, J., and Tocanne, J. F. (1986) Lateral proton conduction at lipid-water interfaces and its implications for the chemiosmotic-coupling hypothesis, Nature 322, 756-758.
    • (1986) Nature , vol.322 , pp. 756-758
    • Prats, M.1    Teissie, J.2    Tocanne, J.F.3
  • 24
    • 0029917563 scopus 로고    scopus 로고
    • Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface
    • Bychkova, V. E., Dujsekina, A. E., Klenin, S. I., Tiktopulo, E. I., Uversky, V. N., and Ptitsyn, O. B. (1996) Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface, Biochemistry 35, 6058-6063.
    • (1996) Biochemistry , vol.35 , pp. 6058-6063
    • Bychkova, V.E.1    Dujsekina, A.E.2    Klenin, S.I.3    Tiktopulo, E.I.4    Uversky, V.N.5    Ptitsyn, O.B.6
  • 25
    • 0034659468 scopus 로고    scopus 로고
    • Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures
    • Tall, E. G., Spector, I., Pentyala, S. N., Bitter, I., and Rebecchi, M. J. (2000) Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures, Curr. Biol. 10, 743-746.
    • (2000) Curr. Biol , vol.10 , pp. 743-746
    • Tall, E.G.1    Spector, I.2    Pentyala, S.N.3    Bitter, I.4    Rebecchi, M.J.5
  • 27
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. (1995) Molten globule and protein folding, Adv. Protein. Chem. 47, 83-229.
    • (1995) Adv. Protein. Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 28
    • 0023029074 scopus 로고
    • Requirement of a transmembrane pH gradient for the entry of diphtheria toxin into cells at low pH
    • Sandvig, K., et al. (1986) Requirement of a transmembrane pH gradient for the entry of diphtheria toxin into cells at low pH, J. Biol. Chem. 261, 11639-11644.
    • (1986) J. Biol. Chem , vol.261 , pp. 11639-11644
    • Sandvig, K.1
  • 29
    • 0036221085 scopus 로고    scopus 로고
    • Protein unfolding by the mitochondrial membrane potential
    • Huang, S., Ratliff, K. S., and Matouschek, A. (2002) Protein unfolding by the mitochondrial membrane potential, Nat. Struct. Biol. 9, 301-307.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 301-307
    • Huang, S.1    Ratliff, K.S.2    Matouschek, A.3
  • 30
    • 0024289542 scopus 로고
    • The use of poly(L-proline)-sepharose in the isolation of profilin and profilactin complexes
    • Lindberg, U., Schutt, C. E., Hellsten, E., Tjader, A. C., and Hult, T. (1988) The use of poly(L-proline)-sepharose in the isolation of profilin and profilactin complexes, Biochim. Biophys. Acta 967, 391-400.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 391-400
    • Lindberg, U.1    Schutt, C.E.2    Hellsten, E.3    Tjader, A.C.4    Hult, T.5
  • 31
    • 0028541866 scopus 로고
    • Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • Zhang, O., Kay, L. E., Olivier, J. P., and Forman-Kay, J. D. (1994) Backbone 1H and 15N resonance assignments of the 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) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 32
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A. S., Hinton, D. P., and Byrd, R. A. (1995) Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements, J. Am. Chem. Soc. 117, 7566-7567.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 34
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 35
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 37
    • 0027731196 scopus 로고
    • Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern
    • Metzler, W. J., Constantine, K. L., Friedrichs, M. S., Bell, A. J., Ernst, E. G., Lavoie, T. B., and Mueller, L. (1993) Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern, Biochemists 32, 13818-29.
    • (1993) Biochemists , vol.32 , pp. 13818-13829
    • Metzler, W.J.1    Constantine, K.L.2    Friedrichs, M.S.3    Bell, A.J.4    Ernst, E.G.5    Lavoie, T.B.6    Mueller, L.7
  • 38
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • Palmer III, A. G., Williams, J., and McDermott, A. (1996) Nuclear magnetic resonance studies of biopolymer dynamics, J. Phys. Chem. 100, 13293-13310.
    • (1996) J. Phys. Chem , vol.100 , pp. 13293-13310
    • Palmer III, A.G.1    Williams, J.2    McDermott, A.3
  • 39
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 40
    • 0031451750 scopus 로고    scopus 로고
    • Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins
    • Yao, J., Dyson, H. J., and Wright, P. E. (1997) Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins, FEBS Lett. 419, 285-289.
    • (1997) FEBS Lett , vol.419 , pp. 285-289
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3
  • 44
    • 0017368283 scopus 로고
    • 1H NMR titration shifts of amide proton resonances in polypeptide chains
    • Bundi, A., and Wuthrich, K. (1977) 1H NMR titration shifts of amide proton resonances in polypeptide chains, FEBS Lett. 77, 11-14.
    • (1977) FEBS Lett , vol.77 , pp. 11-14
    • Bundi, A.1    Wuthrich, K.2
  • 45
    • 0021103512 scopus 로고
    • 1H NMR study on the tautomerism of the imidazole ring of histidine residues. I. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides
    • Tanokura, M. (1983) 1H NMR study on the tautomerism of the imidazole ring of histidine residues. I. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides, Biochim. Biophys. Acta 742, 576-585.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 576-585
    • Tanokura, M.1
  • 46
    • 0014217191 scopus 로고
    • Intrinsic dissociation constants of aspartyl and glutamyl carboxyl groups
    • Nozaki, Y., and Tanford, C. (1967) Intrinsic dissociation constants of aspartyl and glutamyl carboxyl groups, J. Biol. Chem. 242, 4731-4735.
    • (1967) J. Biol. Chem , vol.242 , pp. 4731-4735
    • Nozaki, Y.1    Tanford, C.2
  • 47
    • 0001022707 scopus 로고    scopus 로고
    • Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin
    • Geierstanger, B., Jamin, M., Volkman, B. F., and Baldwin, R. L. (1998) Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin, Biochemists 37, 4254-4265.
    • (1998) Biochemists , vol.37 , pp. 4254-4265
    • Geierstanger, B.1    Jamin, M.2    Volkman, B.F.3    Baldwin, R.L.4
  • 48
    • 0037732539 scopus 로고    scopus 로고
    • Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c
    • Sinibaldi, F., Piro, M. C., Howes, B. D., Smulevich, G., Ascoli, F., and Santucci, R. (2003) Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c, Biochemistry 42, 7604-7610.
    • (2003) Biochemistry , vol.42 , pp. 7604-7610
    • Sinibaldi, F.1    Piro, M.C.2    Howes, B.D.3    Smulevich, G.4    Ascoli, F.5    Santucci, R.6
  • 50
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing, I., and Lindberg, U. (1985) Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin, Nature 314, 472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 51
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of profilin in the assembly of actin for microspike formation
    • Suetsugu, S., Miki, H., and Takenawa, T. (1998) The essential role of profilin in the assembly of actin for microspike formation, EMBO J. 17, 6516-6526.
    • (1998) EMBO J , vol.17 , pp. 6516-6526
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 52
    • 0342327310 scopus 로고    scopus 로고
    • Isolation and characterization of two mutants of human profilin I that do not bind poly(L-proline)
    • Bjorkegren-Sjogren, C., Korenbaum, E., Nordberg, P., Lindberg, U., and Karlsson, R. (1997) Isolation and characterization of two mutants of human profilin I that do not bind poly(L-proline), FEBS Lett. 418, 258-264.
    • (1997) FEBS Lett , vol.418 , pp. 258-264
    • Bjorkegren-Sjogren, C.1    Korenbaum, E.2    Nordberg, P.3    Lindberg, U.4    Karlsson, R.5
  • 55
    • 0029966344 scopus 로고    scopus 로고
    • Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis
    • Kaiser, D. A., and Pollard, T. D. (1996) Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis, J. Mol. Biol. 256, 89-107.
    • (1996) J. Mol. Biol , vol.256 , pp. 89-107
    • Kaiser, D.A.1    Pollard, T.D.2
  • 56
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux, T., Fukami, K., Thelen, M., Golub, T., Frey, D., and Caroni, P. (2000) GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism, J. Cell Biol. 149, 1455-1472.
    • (2000) J. Cell Biol , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 58
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • Pike, L. J., and Casey, L. (1996) Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains, J. Biol. Chem. 271, 26453-26456.
    • (1996) J. Biol. Chem , vol.271 , pp. 26453-26456
    • Pike, L.J.1    Casey, L.2
  • 60
    • 0036783381 scopus 로고    scopus 로고
    • a of histidine side-chains correlates with burial within proteins
    • a of histidine side-chains correlates with burial within proteins, Proteins 49, 1-6.
    • (2002) Proteins , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 61
    • 0036351488 scopus 로고    scopus 로고
    • The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange
    • Halskau, O., Froystein, N. A., Muga, A., and Martinez, A. (2002) The membrane-bound conformation of alpha-lactalbumin studied by NMR-monitored 1H exchange, J. Mol. Biol. 321, 99-110.
    • (2002) J. Mol. Biol , vol.321 , pp. 99-110
    • Halskau, O.1    Froystein, N.A.2    Muga, A.3    Martinez, A.4
  • 62
    • 0037821763 scopus 로고    scopus 로고
    • The interaction of peripheral proteins and membranes studied with alpha-lactalbumin and phospholipid bilayers of various compositions
    • Agasoster, A. V., Halskau, O., Fuglebakk, E., Froystein, N. A., Muga, A., Holmsen, H., and Martinez, A. (2003) The interaction of peripheral proteins and membranes studied with alpha-lactalbumin and phospholipid bilayers of various compositions, J. Biol. Chem. 278, 21790-21797.
    • (2003) J. Biol. Chem , vol.278 , pp. 21790-21797
    • Agasoster, A.V.1    Halskau, O.2    Fuglebakk, E.3    Froystein, N.A.4    Muga, A.5    Holmsen, H.6    Martinez, A.7
  • 64
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke, W., Podtelejnikov, A. V., Di Nardo, A., Sutherland, J. D., Gurniak, C. B., Dotti, C., and Mann, M. (1998) In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly, EMBO J. 17, 967-976.
    • (1998) EMBO J , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    Di Nardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5    Dotti, C.6    Mann, M.7
  • 65
    • 0343488499 scopus 로고    scopus 로고
    • Hartl, F., U. and, and Martin, J. (1997) Curr. Opin. Struct. Biol. 7, 41-52.
    • Hartl, F., U. and, and Martin, J. (1997) Curr. Opin. Struct. Biol. 7, 41-52.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.