메뉴 건너뛰기




Volumn 45, Issue 6, 2006, Pages 1861-1869

Protective and inhibitory effects of various types of amphipols on the Ca 2+-ATPase from sarcoplasmic reticulum: A comparative study

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC POLYMERS; AMPHIPOLS; INHIBITORY EFFECTS; POLYACRYLATE-BASED AMPHIPOL;

EID: 32344440367     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051954a     Document Type: Article
Times cited : (62)

References (53)
  • 1
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire, M., Champeil, P., and Møller, J. V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents, Biochim. Biophys. Acta 1508, 86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 2
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • Garavito, R. M., and Ferguson-Miller, S. (2001) Detergents as tools in membrane biochemistry, J. Biol. Chem. 276, 32403-32406.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32403-32406
    • Garavito, R.M.1    Ferguson-Miller, S.2
  • 3
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U. (2001) Stabilizing membrane proteins, Curr. Opin. Struct. Biol. 11, 397-402.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 6
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C., Audebert, R., and Popot, J.-L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous solutions, Proc. Natl. Acad. Sci. U.S.A. 93, 15047-15050.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 10
    • 0034425014 scopus 로고    scopus 로고
    • Nonionic amphiphilic polymers derived from tris(hydroxymethyl)- acrylamidomethane keep membrane proteins soluble and native in the absence of detergent
    • Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L., and Tribet, C. (2001) Nonionic amphiphilic polymers derived from tris(hydroxymethyl)- acrylamidomethane keep membrane proteins soluble and native in the absence of detergent, Biopolymers 56, 77-84.
    • (2001) Biopolymers , vol.56 , pp. 77-84
    • Prata, C.1    Giusti, F.2    Gohon, Y.3    Pucci, B.4    Popot, J.-L.5    Tribet, C.6
  • 11
    • 0037174145 scopus 로고    scopus 로고
    • Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs physical constraints
    • Martinez, K. L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., and Popot, J.-L. (2002) Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs physical constraints, FEBS Lett. 528, 251-256.
    • (2002) FEBS Lett. , vol.528 , pp. 251-256
    • Martinez, K.L.1    Gohon, Y.2    Corringer, P.-J.3    Tribet, C.4    Mérola, F.5    Changeux, J.-P.6    Popot, J.-L.7
  • 16
  • 17
    • 32344431772 scopus 로고    scopus 로고
    • Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35
    • Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., and Popot, J.-L. (2006) Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35, Langmuir 22, 1281-1290.
    • (2006) Langmuir , vol.22 , pp. 1281-1290
    • Gohon, Y.1    Giusti, F.2    Prata, C.3    Charvolin, D.4    Timmins, P.5    Ebel, C.6    Tribet, C.7    Popot, J.-L.8
  • 18
    • 0021915284 scopus 로고
    • Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosinetriphosphatase as reflected by organic solvent-induced perturbation
    • Champeil, P., Guillain, F., Vénien, C., and Gingold, M. P. (1985) Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosinetriphosphatase as reflected by organic solvent-induced perturbation, Biochemistry 24, 69-81.
    • (1985) Biochemistry , vol.24 , pp. 69-81
    • Champeil, P.1    Guillain, F.2    Vénien, C.3    Gingold, M.P.4
  • 19
    • 0023238002 scopus 로고
    • The use of gel chromatography for the determination of sizes and relative molecular masses of proteins. Interpretation of calibration curves in terms of gel-pore-size distribution
    • le Maire, M., Ghazi, A., Møller, J. V., and Aggerbeck, L. P. (1987) The use of gel chromatography for the determination of sizes and relative molecular masses of proteins. Interpretation of calibration curves in terms of gel-pore-size distribution, Biochem. J. 243, 399-404.
    • (1987) Biochem. J. , vol.243 , pp. 399-404
    • Le Maire, M.1    Ghazi, A.2    Møller, J.V.3    Aggerbeck, L.P.4
  • 20
    • 0037728118 scopus 로고
    • 2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions
    • 2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions, J. Biol. Chem. 255, 1912-1920.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1912-1920
    • Møller, J.V.1    Lind, K.E.2    Andersen, J.P.3
  • 25
    • 0022914647 scopus 로고
    • Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. Rate-limiting step(s) under different conditions
    • Champeil, P., le Maire, M., Andersen, J. P., Guillain, F., Gingold, M., Lund, S., and Møller, J. V. (1986) Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. Rate-limiting step(s) under different conditions, J. Biol. Chem. 261, 16372-16384.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16372-16384
    • Champeil, P.1    Le Maire, M.2    Andersen, J.P.3    Guillain, F.4    Gingold, M.5    Lund, S.6    Møller, J.V.7
  • 26
    • 0021326939 scopus 로고
    • The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies
    • Bayley, P., Ahlström, P., Martin, S. R., and Forsen, S. (1984) The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies, Biochem. Biophys. Res. Commun. 120, 185-181.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 185-1181
    • Bayley, P.1    Ahlström, P.2    Martin, S.R.3    Forsen, S.4
  • 27
    • 0024444011 scopus 로고
    • Fast kinetics of calcium release induced by myo-inositol trisphosphate in permeabilized rat hepatocytes
    • Champeil, P., Combettes, L., Berthon, B., Doucet, E., Orlowski, S., and Claret, M. (1989) Fast kinetics of calcium release induced by myo-inositol trisphosphate in permeabilized rat hepatocytes, J. Biol. Chem. 264, 17665-17673.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17665-17673
    • Champeil, P.1    Combettes, L.2    Berthon, B.3    Doucet, E.4    Orlowski, S.5    Claret, M.6
  • 30
    • 0000183168 scopus 로고
    • Aggregation of hydrophobically modified polyelectrolytes in dilute solution: Ionic strength effects
    • (Dubin, Bock, Davis, Schultz, and Thies, Eds.), Springer-Verlag, Berlin and Heidelberg
    • Magny, B., Iliopoulos, I., and Audebert, R. (1994) Aggregation of hydrophobically modified polyelectrolytes in dilute solution: ionic strength effects, in Macromolecular Complexes in Chemistry and Biology (Dubin, Bock, Davis, Schultz, and Thies, Eds.) pp 51 -62, Springer-Verlag, Berlin and Heidelberg.
    • (1994) Macromolecular Complexes in Chemistry and Biology , pp. 51-62
    • Magny, B.1    Iliopoulos, I.2    Audebert, R.3
  • 31
    • 0001126675 scopus 로고
    • Aqueous solution behavior of hydrophobically modified poly(acrylic acid)
    • (Shalaby, S. W., McCormick, C. L., and Butler, G. B., Eds.), ACS Symposium Series, Washington, DC
    • Wang, T. K., Iliopoulos, I., and Audebert, R. (1991) Aqueous solution behavior of hydrophobically modified poly(acrylic acid), in Water-Soluble Polymers: synthesis, solution properties, and applications (Shalaby, S. W., McCormick, C. L., and Butler, G. B., Eds.) pp 218-231, ACS Symposium Series, Washington, DC.
    • (1991) Water-Soluble Polymers: Synthesis, Solution Properties, and Applications , pp. 218-231
    • Wang, T.K.1    Iliopoulos, I.2    Audebert, R.3
  • 32
    • 0028515708 scopus 로고
    • Mixed micelles formed by cationic surfactants and anionic hydrophobically modified polyelectrolytes
    • Magny, B., Iliopoulos, I., Zana, R., and Audebert, R. (1994) Mixed micelles formed by cationic surfactants and anionic hydrophobically modified polyelectrolytes, Langmuir 10, 3180-3187.
    • (1994) Langmuir , vol.10 , pp. 3180-3187
    • Magny, B.1    Iliopoulos, I.2    Zana, R.3    Audebert, R.4
  • 33
    • 0000552973 scopus 로고
    • Interactions of hydrophobically modified poly(sodium acrylate) with globular proteins
    • Petit, F., Audebert, R., and Iliopoulos, I. (1995) Interactions of hydrophobically modified poly(sodium acrylate) with globular proteins, Colloid Polym. Sci. 273, 777-781.
    • (1995) Colloid Polym. Sci. , vol.273 , pp. 777-781
    • Petit, F.1    Audebert, R.2    Iliopoulos, I.3
  • 34
    • 0031249290 scopus 로고    scopus 로고
    • Stabilization of hydrophobic colloidal dispersions in water with amphiphilic polymers: Application to integral membrane proteins
    • Tribet, C., Audebert, R., and Popot, J.-L. (1997) Stabilization of hydrophobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins, Langmuir 13, 5570-5576.
    • (1997) Langmuir , vol.13 , pp. 5570-5576
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 35
    • 32344431887 scopus 로고    scopus 로고
    • Amphipols: Strategies for an improved PS2 environment in aqueous solution
    • Miyake, J., Ed. Elsevier, Dordrecht, The Netherlands
    • Nowaczyk, M., Oworah-Nkruma, R., Zoonens, M., Rögner, M., and Popot, J.-L. (2004) Amphipols: strategies for an improved PS2 environment in aqueous solution, in Biohydrogen III (Miyake, J., Ed.) pp 151-159, Elsevier, Dordrecht, The Netherlands.
    • (2004) Biohydrogen III , pp. 151-159
    • Nowaczyk, M.1    Oworah-Nkruma, R.2    Zoonens, M.3    Rögner, M.4    Popot, J.-L.5
  • 36
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405, 633-634.
    • (2000) Nature , vol.405 , pp. 633-634
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 37
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium, Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 42
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • Cantor, R. S. (1997) The lateral pressure profile in membranes: a physical mechanism of general anesthesia, Biochemistry 36, 2339-2344.
    • (1997) Biochemistry , vol.36 , pp. 2339-2344
    • Cantor, R.S.1
  • 43
    • 0001768593 scopus 로고    scopus 로고
    • High-pressure stopped-flow spectrometer for kinetic studies of fast bioorganic reactions by absorbance and fluorecence detection
    • (Heremans, K., Ed.), Leuven University Press, Belgium
    • Bugnon, P., Doludda, M., Grell, E., and Merlbach, A. E. (1997) High-pressure stopped-flow spectrometer for kinetic studies of fast bioorganic reactions by absorbance and fluorecence detection, in High-Pressure Research in the Biosciences and Biotechnology (Heremans, K., Ed.) pp 143-146, Leuven University Press, Belgium.
    • (1997) High-Pressure Research in the Biosciences and Biotechnology , pp. 143-146
    • Bugnon, P.1    Doludda, M.2    Grell, E.3    Merlbach, A.E.4
  • 44
    • 0024118603 scopus 로고
    • Pressure effects on the interactions of the sarcoplasmic reticulum calcium transport enzyme with calcium and dinitrophenyl phosphate
    • Hasselbach, W. (1988) Pressure effects on the interactions of the sarcoplasmic reticulum calcium transport enzyme with calcium and dinitrophenyl phosphate, Z. Naturforsch. C 43, 929-937.
    • (1988) Z. Naturforsch. C , vol.43 , pp. 929-937
    • Hasselbach, W.1
  • 45
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C., and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue, Nature 430, 529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 46
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H., and Tsuda, T. (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues, Nature 442, 361-368.
    • (2004) Nature , vol.442 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 47
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sørensen, T. L.-M., Møller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sørensen, T.L.-M.1    Møller, J.V.2    Nissen, P.3
  • 48
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen, C., Sørensen, T. L.-M., Nielsen, R. C., Møller, J. V., and Nissen, P. (2005) Dephosphorylation of the calcium pump coupled to counterion occlusion, Science 306, 2251-2255.
    • (2005) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sørensen, T.L.-M.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 49
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. (1995) Acetylcholine receptor channel imaged in the open state, Nature 373, 37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 50
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • Unwin, N. (2003) Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy, FEBS Lett. 555, 91-95.
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 51
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Fujiyoshi, Y., and Unwin, N. (2003) Structure and gating mechanism of the acetylcholine receptor pore, Nature 423, 949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.