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1
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0344589334
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Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labeling
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Marsh D., and Horvath L.I. Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labeling. Biochimica et Biophysica Acta, Rev Biomembr 1376 (1998) 267-296
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Marsh, D.1
Horvath, L.I.2
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2
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0025146398
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Cardiolipin-depleted bovine heart cytochrome c oxidase: binding stoichiometry and affinity for cardiolipin derivatives
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Robinson N.C., Zborowski J., and Talbert L.H. Cardiolipin-depleted bovine heart cytochrome c oxidase: binding stoichiometry and affinity for cardiolipin derivatives. Biochemistry 29 (1990) 8962-8969
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Robinson, N.C.1
Zborowski, J.2
Talbert, L.H.3
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0023567929
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Spin-label studies on the specificity of interaction of cardiolipin with beef heart cytochrome oxidase
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Powell G.L., Knowles P.F., and Marsh D. Spin-label studies on the specificity of interaction of cardiolipin with beef heart cytochrome oxidase. Biochemistry 26 (1987) 8138-8145
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Powell, G.L.1
Knowles, P.F.2
Marsh, D.3
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33746349218
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Energy transduction: proton transfer through the respiratory complexes
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Hosler J.P., Ferguson-Miller S., and Mills D.A. Energy transduction: proton transfer through the respiratory complexes. Annu Rev Biochem 75 (2006) 165-187
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Annu Rev Biochem
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Hosler, J.P.1
Ferguson-Miller, S.2
Mills, D.A.3
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5
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0038303147
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A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis
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Zhang H., Kurisu G., Smith J.L., and Cramer W.A. A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis. Proc Natl Acad Sci USA 100 (2003) 5160-5163
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Proc Natl Acad Sci USA
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Zhang, H.1
Kurisu, G.2
Smith, J.L.3
Cramer, W.A.4
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6
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32444433628
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Manipulating phospholipids for crystallization of a membrane transport protein
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By manipulating phospholipid contents in various lactose permease preparations, the authors are able to obtain different crystal forms with different X-ray diffraction quality.
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Guan L., Smirnova I.N., Verner G., Nagamori S., and Kaback H.R. Manipulating phospholipids for crystallization of a membrane transport protein. Proc Natl Acad Sci USA 103 (2006) 1723-1726. By manipulating phospholipid contents in various lactose permease preparations, the authors are able to obtain different crystal forms with different X-ray diffraction quality.
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Proc Natl Acad Sci USA
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, pp. 1723-1726
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Guan, L.1
Smirnova, I.N.2
Verner, G.3
Nagamori, S.4
Kaback, H.R.5
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7
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34548844554
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The purification of G-protein coupled receptors for crystallization
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Warne T., and Schertler G.F.X. The purification of G-protein coupled receptors for crystallization. Struct Biol Membr Protein (2006) 51-71
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Struct Biol Membr Protein
, pp. 51-71
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Warne, T.1
Schertler, G.F.X.2
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9
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33947602374
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Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase
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This paper describes the use of mass spectrometry to understand the detailed structures of the 13 lipids resolved in the bovine CcO structure, including the exact chain lengths and positions of the unsaturated bonds.
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Shinzawa-Itoh K., Aoyama H., Muramoto K., Terada H., Kurauchi T., Tadehara Y., Yamasaki A., Sugimura T., Kurono S., Tsujimoto K., et al. Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase. EMBO J 26 (2007) 1713-1725. This paper describes the use of mass spectrometry to understand the detailed structures of the 13 lipids resolved in the bovine CcO structure, including the exact chain lengths and positions of the unsaturated bonds.
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(2007)
EMBO J
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, pp. 1713-1725
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Shinzawa-Itoh, K.1
Aoyama, H.2
Muramoto, K.3
Terada, H.4
Kurauchi, T.5
Tadehara, Y.6
Yamasaki, A.7
Sugimura, T.8
Kurono, S.9
Tsujimoto, K.10
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10
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33750807024
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Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
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This paper presents a 2.0 Å structure of the catalytic core of RsCcO, as well as the finding that certain detergents with the right headgroup and tail characteristics can mimic lipids and occupy lipid-binding sites on membrane proteins.
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Qin L., Hiser C., Mulichak A., Garavito R.M., and Ferguson-Miller S. Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 103 (2006) 16117-16122. This paper presents a 2.0 Å structure of the catalytic core of RsCcO, as well as the finding that certain detergents with the right headgroup and tail characteristics can mimic lipids and occupy lipid-binding sites on membrane proteins.
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(2006)
Proc Natl Acad Sci USA
, vol.103
, pp. 16117-16122
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Qin, L.1
Hiser, C.2
Mulichak, A.3
Garavito, R.M.4
Ferguson-Miller, S.5
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11
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0036382724
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The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
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Svensson-Ek M., Abramson J., Larsson G., Tornroth S., Brzezinski P., and Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J Mol Biol 321 (2002) 329-339
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J Mol Biol
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Svensson-Ek, M.1
Abramson, J.2
Larsson, G.3
Tornroth, S.4
Brzezinski, P.5
Iwata, S.6
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12
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0033585083
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The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
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Harrenga A., and Michel H. The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J Biol Chem 274 (1999) 33296-33299
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J Biol Chem
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Harrenga, A.1
Michel, H.2
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13
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0030886203
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Structure at 2.7.ANG. resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
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Ostermeier C., Harrenga A., Ermler U., and Michel H. Structure at 2.7.ANG. resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc Natl Acad Sci USA 94 (1997) 10547-10553
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Proc Natl Acad Sci USA
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Ostermeier, C.1
Harrenga, A.2
Ermler, U.3
Michel, H.4
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14
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27844436560
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Specific protein-lipid interactions in membrane proteins
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Hunte C. Specific protein-lipid interactions in membrane proteins. Biochem Soc Trans 33 (2005) 938-942
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Biochem Soc Trans
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Hunte, C.1
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15
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0033609904
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Structure of bacteriorhodopsin at 1.55.ANG. resolution
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Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., and Lanyi J.K. Structure of bacteriorhodopsin at 1.55.ANG. resolution. J Mol Biol 291 (1999) 899-911
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J Mol Biol
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Luecke, H.1
Schobert, B.2
Richter, H.-T.3
Cartailler, J.-P.4
Lanyi, J.K.5
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16
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17844369968
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Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
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Murata T., Yamato I., Kakinuma Y., Leslie A.G.W., and Walker J.E. Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science (Washington, DC, USA) 308 (2005) 654-659
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Murata, T.1
Yamato, I.2
Kakinuma, Y.3
Leslie, A.G.W.4
Walker, J.E.5
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17
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0035115358
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Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?
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Wakeham M.C., Sessions R.B., Jones M.R., and Fyfe P.K. Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?. Biophys J 80 (2001) 1395-1405
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Wakeham, M.C.1
Sessions, R.B.2
Jones, M.R.3
Fyfe, P.K.4
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18
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33947381395
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Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides
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Externally added brominated phospholipids are used to distinguish between tails of lipids and tails of detergents in the case of the reaction center from R. sphaeroides
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Roszak A.W., Gardiner A.T., Isaacs N.W., and Cogdell R.J. Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides. Biochemistry 46 (2007) 2909-2916. Externally added brominated phospholipids are used to distinguish between tails of lipids and tails of detergents in the case of the reaction center from R. sphaeroides
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Biochemistry
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Roszak, A.W.1
Gardiner, A.T.2
Isaacs, N.W.3
Cogdell, R.J.4
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19
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Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
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Castresana J., Luebben M., Saraste M., and Higgins D.G. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J 13 (1994) 2516-2525
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Castresana, J.1
Luebben, M.2
Saraste, M.3
Higgins, D.G.4
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20
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24044442616
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A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus
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Hunsicker-Wang L.M., Pacoma R.L., Chen Y., Fee J.A., and Stout C.D. A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus. Acta Crystallogr, Section D: Biol Crystallogr D61 (2005) 340-343
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Acta Crystallogr, Section D: Biol Crystallogr
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Hunsicker-Wang, L.M.1
Pacoma, R.L.2
Chen, Y.3
Fee, J.A.4
Stout, C.D.5
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21
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33845573535
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Altering conserved lipid binding sites in cytochrome c oxidase of Rhodobacter sphaeroides perturbs the interaction between subunits I and III and promotes suicide inactivation of the enzyme
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The first mutational studies of the conserved lipid-binding sites in CcO show that the disruption of lipid interactions lead to an altered binding of subunit III and enzyme complex that displays suicide inactivation.
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Varanasi L., Mills D., Murphree A., Gray J., Purser C., Baker R., and Hosler J. Altering conserved lipid binding sites in cytochrome c oxidase of Rhodobacter sphaeroides perturbs the interaction between subunits I and III and promotes suicide inactivation of the enzyme. Biochemistry 45 (2006) 14896-14907. The first mutational studies of the conserved lipid-binding sites in CcO show that the disruption of lipid interactions lead to an altered binding of subunit III and enzyme complex that displays suicide inactivation.
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Biochemistry
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Varanasi, L.1
Mills, D.2
Murphree, A.3
Gray, J.4
Purser, C.5
Baker, R.6
Hosler, J.7
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22
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0033534165
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Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site
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Bratton M.R., Pressler M.A., and Hosler J.P. Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry 38 (1999) 16236-16245
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Biochemistry
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Bratton, M.R.1
Pressler, M.A.2
Hosler, J.P.3
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23
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0347362791
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Cardiolipin stabilizes respiratory chain supercomplexes
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Pfeiffer K., Gohil V., Stuart R.A., Hunte C., Brandt U., Greenberg M.L., and Schaegger H. Cardiolipin stabilizes respiratory chain supercomplexes. J Biol Chem 278 (2003) 52873-52880
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Pfeiffer, K.1
Gohil, V.2
Stuart, R.A.3
Hunte, C.4
Brandt, U.5
Greenberg, M.L.6
Schaegger, H.7
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24
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23844540312
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Cardiolipin Is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
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Zhang M., Mileykovskaya E., and Dowhan W. Cardiolipin Is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria. J Biol Chem 280 (2005) 29403-29408
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J Biol Chem
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Zhang, M.1
Mileykovskaya, E.2
Dowhan, W.3
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Lipid-assisted protein folding
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Bogdanov M., and Dowhan W. Lipid-assisted protein folding. J Biol Chem 274 (1999) 36827-36830
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Dowhan, W.2
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0036566310
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A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
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Bogdanov M., Heacock P.N., and Dowhan W. A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition. EMBO J 21 (2002) 2107-2116
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Bogdanov, M.1
Heacock, P.N.2
Dowhan, W.3
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27
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33745860369
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Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease
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The paper shows that LacY function and correct topology can be restored in a PE-deficient strain of E. coli, by a foreign lipid, monoglucosyldiacylglycerol, which is similar to PE in terms of its non-bilayer prone property, lack of net charge, and the ability of its headgroup to form hydrogen bonds.
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Xie J., Bogdanov M., Heacock P., and Dowhan W. Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease. J Biol Chem 281 (2006) 19172-19178. The paper shows that LacY function and correct topology can be restored in a PE-deficient strain of E. coli, by a foreign lipid, monoglucosyldiacylglycerol, which is similar to PE in terms of its non-bilayer prone property, lack of net charge, and the ability of its headgroup to form hydrogen bonds.
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J Biol Chem
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Xie, J.1
Bogdanov, M.2
Heacock, P.3
Dowhan, W.4
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