N Mullner
Duke University
5 Papers
73 Citations
N Mullner is an academic researcher from Duke University. The author has contributed to research in topics: Endoplasmic reticulum & Calcium ATPase. The author has an hindex of 5, co-authored 5 publications.
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Papers
Pressure effects on sarcoplasmic reticulum.
TL;DR: Protection against pressure inactivation was also observed in the presence of sucrose, glycerol, ethylene glycol and 1 M KCl, suggesting that water density modifying groups significantly affect the stability of Ca2+-ATPase under pressure.
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•Journal Article
Structure of Ca2+-ATPase in sarcoplasmic reticulum.
Anthony Martonosi,László Dux,Kenneth A. Taylor,H.P. Ting-Beall,S Varga,P. Csermely,N Mullner,Sandor Papp,Istvan Jona +8 more
TL;DR: In this paper, the morphology of sarcoplasmic reticulum, classification of Ca(2+)-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology is reviewed.
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Electron microscope observations on Ca2+-ATPase microcrystals in detergent-solubilized sarcoplasmic reticulum.
TL;DR: Cross-linking of Ca2+-ATPase crystals with glutaraldehyde protects the structure against conditions such as low Ca2+, high pH, elevated temperature, SH group reagents, high concentration of detergents, and removal of phospholipids by extraction with organic solvents that disrupt unfixed preparations.
Infrared spectroscopic characterization of the structural changes connected with the E1----E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum.
TL;DR: The Fourier transform infrared spectra of sarcoplasmic reticulum vesicles in the presence of 20 mM Ca2+ suggest the stabilization of a protein conformation similar to the E2 state except for differences in the behavior of COO- and phospholipid ester C = O groups that may reflect charge effects of the bound Ca2+.
Crystallization of Ca2+-ATPase in detergent-solubilized sarcoplasmic reticulum.
TL;DR: Microcrystalline arrays of Ca2+-transporting ATPase develop in detergent-solubilized sarcoplasmic reticulum upon exposure to 10-20 mM CaCl2 at pH 6.0 for several weeks at 2 degrees C, in a crystallization medium that preserves the ATPase activity for several months.