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Volumn 365, Issue 1, 2008, Pages 8-15

Lipid dependant disorder-to-order conformational transitions in apolipoprotein CI derived peptides

Author keywords

Apolipoprotein CI; Disorder to order transitions; Molecular switch

Indexed keywords

APOLIPOPROTEIN C1; LIPID; PHOSPHOLIPID; WATER;

EID: 36048938680     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.112     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 0028243107 scopus 로고
    • Denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii I., Kataoka M., Tokunaga F., and Goto Y. Denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 33 (1994) 4903-4909
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 3
    • 0018223550 scopus 로고
    • Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits
    • Bloomer A.C., Champness J.N., Bricogne G., Staden R., and Klug A. Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits. Nature 276 (1978) 362-368
    • (1978) Nature , vol.276 , pp. 362-368
    • Bloomer, A.C.1    Champness, J.N.2    Bricogne, G.3    Staden, R.4    Klug, A.5
  • 4
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution
    • Bode W., Schwager P., and Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution. J. Mol. Biol. 118 (1978) 99-112
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 5
    • 0032539846 scopus 로고    scopus 로고
    • Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex
    • Nolte R.T., Conlin R.M., Harrison S.C., and Brown R.S. Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex. Proc. Natl. Acad. Sci. USA 95 (1998) 2938-2943
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2938-2943
    • Nolte, R.T.1    Conlin, R.M.2    Harrison, S.C.3    Brown, R.S.4
  • 6
    • 0000197231 scopus 로고    scopus 로고
    • The sequence attribute method for determining relationships between sequence and protein disorder
    • Xie Q., Arnold G.E., Romero P., Obradovic Z., Garner E., and Dunker A.K. The sequence attribute method for determining relationships between sequence and protein disorder. Genome Info. 9 (1998) 193-200
    • (1998) Genome Info. , vol.9 , pp. 193-200
    • Xie, Q.1    Arnold, G.E.2    Romero, P.3    Obradovic, Z.4    Garner, E.5    Dunker, A.K.6
  • 10
    • 2942741104 scopus 로고    scopus 로고
    • Phase transitions of phospholipid monolayers penetrated by apolipoproteins
    • Xicohtencatl-Cortes J., Castillo R., and Mas-Oliva J. Phase transitions of phospholipid monolayers penetrated by apolipoproteins. J. Phys. Chem. B 108 (2004) 7307-7315
    • (2004) J. Phys. Chem. B , vol.108 , pp. 7307-7315
    • Xicohtencatl-Cortes, J.1    Castillo, R.2    Mas-Oliva, J.3
  • 12
    • 11344289669 scopus 로고    scopus 로고
    • Interaction and conformations of α-helical human apolipoprotein Cl on hydrophobic and hydrophilic substrates
    • Campos-Terán J., Mas-Oliva J., and Castillo R. Interaction and conformations of α-helical human apolipoprotein Cl on hydrophobic and hydrophilic substrates. J. Phys. Chem. B 108 (2004) 20442-20450
    • (2004) J. Phys. Chem. B , vol.108 , pp. 20442-20450
    • Campos-Terán, J.1    Mas-Oliva, J.2    Castillo, R.3
  • 13
    • 1842855016 scopus 로고    scopus 로고
    • Overexpression of apoC-I in apoE-null mice: severe hypertriglyceridemia due to inhibition of hepatic lipase
    • Conde-Knape K., Bensadoun A., Sobel J.H., Cohn J.S., and Shachter N.S. Overexpression of apoC-I in apoE-null mice: severe hypertriglyceridemia due to inhibition of hepatic lipase. J. Lipid Res. 43 (2002) 2136-2145
    • (2002) J. Lipid Res. , vol.43 , pp. 2136-2145
    • Conde-Knape, K.1    Bensadoun, A.2    Sobel, J.H.3    Cohn, J.S.4    Shachter, N.S.5
  • 14
    • 0017072997 scopus 로고
    • Effect of serum and C apoproteins from very low density lipoproteins on human postheparin plasma hepatic lipase
    • Kinnunen P.K., and Ehnolm C. Effect of serum and C apoproteins from very low density lipoproteins on human postheparin plasma hepatic lipase. FEBS Lett. 65 (1976) 354-357
    • (1976) FEBS Lett. , vol.65 , pp. 354-357
    • Kinnunen, P.K.1    Ehnolm, C.2
  • 15
    • 0016814761 scopus 로고
    • Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin: cholesterol acyl-transferase
    • Soutar A.K., Garner C.W., Baker H.N., Sparrow J.T., Jackson R.L., Gotto Jr. A.M., and Smith L.C. Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin: cholesterol acyl-transferase. Biochemistry 14 (1975) 3057-3064
    • (1975) Biochemistry , vol.14 , pp. 3057-3064
    • Soutar, A.K.1    Garner, C.W.2    Baker, H.N.3    Sparrow, J.T.4    Jackson, R.L.5    Gotto Jr., A.M.6    Smith, L.C.7
  • 16
    • 0034534981 scopus 로고    scopus 로고
    • Human apolipoprotein C-I accounts for the ability of plasma high density lipoproteins to inhibit the cholesteryl ester transfer protein activity
    • Gautier T., Masson D., de Barros J.P., Athias A., Gambert P., Aunis D., Metz-Boutique M.-H., and Lagrost L. Human apolipoprotein C-I accounts for the ability of plasma high density lipoproteins to inhibit the cholesteryl ester transfer protein activity. J. Biol. Chem. 275 (2000) 37504-37509
    • (2000) J. Biol. Chem. , vol.275 , pp. 37504-37509
    • Gautier, T.1    Masson, D.2    de Barros, J.P.3    Athias, A.4    Gambert, P.5    Aunis, D.6    Metz-Boutique, M.-H.7    Lagrost, L.8
  • 17
    • 0040177065 scopus 로고
    • Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins
    • Kowal R.C., Herz J., Goldstein J.L., Esser V., and Brown M.S. Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins. Proc. Natl. Acad. Sci. USA 86 (1989) 5810-5814
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5810-5814
    • Kowal, R.C.1    Herz, J.2    Goldstein, J.L.3    Esser, V.4    Brown, M.S.5
  • 18
    • 0025302165 scopus 로고
    • Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein
    • Kowal R.C., Herz J., Weisgraber K.H., Mahley R.W., Brown M.S., and Goldstein J.L. Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein. J. Biol. Chem. 265 (1990) 10771-10779
    • (1990) J. Biol. Chem. , vol.265 , pp. 10771-10779
    • Kowal, R.C.1    Herz, J.2    Weisgraber, K.H.3    Mahley, R.W.4    Brown, M.S.5    Goldstein, J.L.6
  • 19
    • 0025611153 scopus 로고
    • Apolipoprotein C-I modulates the interaction of apolipoprotein E with beta-migrating very low density lipoproteins (beta-VLDL) and inhibits binding of beta-VLDL to low density lipoprotein receptor-related protein
    • Weisgraber K.H., Mahley R.W., Kowal R.C., Herz J., Goldstein J.L., and Brown M.S. Apolipoprotein C-I modulates the interaction of apolipoprotein E with beta-migrating very low density lipoproteins (beta-VLDL) and inhibits binding of beta-VLDL to low density lipoprotein receptor-related protein. J. Biol. Chem. 265 (1990) 22453-22459
    • (1990) J. Biol. Chem. , vol.265 , pp. 22453-22459
    • Weisgraber, K.H.1    Mahley, R.W.2    Kowal, R.C.3    Herz, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 22
  • 23
    • 0032247180 scopus 로고    scopus 로고
    • Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulphate
    • Rozek A., Sparrow J.T., Weisgraber K.H., and Cushley R.J. Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulphate. Biochem. Cell Biol. 76 (1998) 267-275
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 267-275
    • Rozek, A.1    Sparrow, J.T.2    Weisgraber, K.H.3    Cushley, R.J.4
  • 24
    • 26444511231 scopus 로고    scopus 로고
    • Atheroprotective effects of high-density lipoprotein-associated lysosphingolipids
    • Jerzy-Roch N., and Assmann G. Atheroprotective effects of high-density lipoprotein-associated lysosphingolipids. Trends Cardiovasc. Med. 15 (2005) 265-271
    • (2005) Trends Cardiovasc. Med. , vol.15 , pp. 265-271
    • Jerzy-Roch, N.1    Assmann, G.2
  • 25
    • 0030852392 scopus 로고    scopus 로고
    • Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and (1)H NMR spectroscopy
    • Rozek A., Buchko G.W., Kanda P., and Cushley R.J. Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and (1)H NMR spectroscopy. Protein Sci. 6 (1997) 1858-1868
    • (1997) Protein Sci. , vol.6 , pp. 1858-1868
    • Rozek, A.1    Buchko, G.W.2    Kanda, P.3    Cushley, R.J.4
  • 26
    • 0026794065 scopus 로고
    • Target enzymes recognition by calmodulin: 2.4 Å structure of a camodulin-peptide complex
    • Meador W.E., Means A.R., and Quiocho F.A. Target enzymes recognition by calmodulin: 2.4 Å structure of a camodulin-peptide complex. Science 257 (1992) 1251-1255
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 28
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei A., Rubin H., Cooperman B.S., and Christianson D.W. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nat. Struct. Biol. 1 (1994) 251-258
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 29
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of betalactoglobulin, a predominantly beta-sheet protein
    • Hamada D., Segawa S., and Goto Y. Non-native alpha-helical intermediate in the refolding of betalactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 3 (1996) 868-873
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.