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185 related items for PubMed ID: 6323380
1. A spin-label and hydrogen-deuterium exchange reaction kinetics study of protein-lipid interactions in lipid-replaced Ca2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. Higashi K, Kirino Y. J Biochem; 1983 Dec; 94(6):1769-79. PubMed ID: 6323380 [Abstract] [Full Text] [Related]
2. Phase behavior of membranes reconstituted from dipentadecanoylphosphatidylcholine and the Mg2+-dependent, Ca2+-stimulated adenosinetriphosphatase of sarcoplasmic reticulum: evidence for a disrupted lipid domain surrounding protein. Lentz BR, Clubb KW, Alford DR, Höchli M, Meissner G. Biochemistry; 1985 Jan 15; 24(2):433-42. PubMed ID: 3156634 [Abstract] [Full Text] [Related]
3. A saturation transfer electron spin resonance study on the break in the Arrhenius plot for the rotational motion of Ca2+-dependent adenosine triphosphatase molecules in purified and lipid-replaced preparations of rabbit skeletal muscle sarcoplasmic reticulum. Kaizu T, Kirino Y, Shimizu H. J Biochem; 1980 Dec 15; 88(6):1837-43. PubMed ID: 6257672 [Abstract] [Full Text] [Related]
9. Effect of phospholipid substitution on the mobility of spin labels bound to the ATPase of sarcoplasmic reticulum. Nakamura H, Martonosi AN. J Biochem; 1981 Jan 15; 89(1):21-8. PubMed ID: 6260760 [Abstract] [Full Text] [Related]
10. [Interaction of spin-labelled phosphatidyl choline with Ca-dependent ATPase from sarcoplasmic reticulum]. Ritov VB, Artemova LG, Azizova OA, Komarov PG, Maksina AG. Biokhimiia; 1982 Dec 15; 47(12):2042-7. PubMed ID: 6297625 [Abstract] [Full Text] [Related]
11. Gel to liquid crystalline phase transition promotes a conformational reorganization of Ca2+, Mg2+-ATPase from sarcoplasmic reticulum in dimyristoylphosphatidylcholine reconstituted systems. Gutiérrez Merino C. Arch Biochem Biophys; 1987 Jan 15; 252(1):303-14. PubMed ID: 2949696 [Abstract] [Full Text] [Related]
12. Effects of gel phase phospholipid on the Ca(2+)-ATPase. Starling AP, East JM, Lee AG. Biochemistry; 1995 Mar 07; 34(9):3084-91. PubMed ID: 7893721 [Abstract] [Full Text] [Related]
13. Effect of temperature on Ca-ATPase from sarcoplasmic reticulum membranes: ESR studies. Rubtsov AM, Sentjurc M, Schara M. Gen Physiol Biophys; 1986 Oct 07; 5(5):551-61. PubMed ID: 3026890 [Abstract] [Full Text] [Related]
14. State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using saturation-transfer electron spin resonance. Napier RM, East JM, Lee AG. Biochim Biophys Acta; 1987 Oct 02; 903(2):365-73. PubMed ID: 2820492 [Abstract] [Full Text] [Related]
15. [Incorporation of synthetic phospholipids into the membranes of the sarcoplasmic reticulum from the rabbit muscle]. Moshkovskiĭ IuSh, Tat'ianenko LV, Nekrasova NA. Mol Biol (Mosk); 1983 Oct 02; 17(2):410-7. PubMed ID: 6304494 [Abstract] [Full Text] [Related]
16. Phosphorylation of phospholamban by cAMP-dependent protein kinase enhances interactions between Ca-ATPase polypeptide chains in cardiac sarcoplasmic reticulum membranes. Negash S, Chen LT, Bigelow DJ, Squier TC. Biochemistry; 1996 Sep 03; 35(35):11247-59. PubMed ID: 8784178 [Abstract] [Full Text] [Related]
17. Effect of the lipid environment on protein motion and enzymatic activity of sarcoplasmic reticulum calcium ATPase. Hidalgo C, Thomas DD, Ikemoto N. J Biol Chem; 1978 Oct 10; 253(19):6879-87. PubMed ID: 211134 [Abstract] [Full Text] [Related]
18. Membrane fluidity is not an important physiological regulator of the (Ca2+-Mg2+)-dependent ATPase of sarcoplasmic reticulum. East JM, Jones OT, Simmonds AC, Lee AG. J Biol Chem; 1984 Jul 10; 259(13):8070-1. PubMed ID: 6145709 [Abstract] [Full Text] [Related]
19. [Conformational mobility and enzymatic activity of Ca2+-ATPase from sarcoplasmic reticulum]. Ritov VB, Murzakhmetova MK, Livshits VA, Kuznetsov VA, Azizova OA. Biokhimiia; 1983 Nov 10; 48(11):1890-6. PubMed ID: 6318838 [Abstract] [Full Text] [Related]
20. Rotational motion of the sarcoplasmic reticulum Ca2+-ATPase. Thomas DD, Hidalgo C. Proc Natl Acad Sci U S A; 1978 Nov 10; 75(11):5488-92. PubMed ID: 214789 [Abstract] [Full Text] [Related] Page: [Next] [New Search]