Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
7185 |
Chemical Shifts: 1 set |
An ARC/MEDIATOR subunit required for SREBP gene activation and regulation of cholesterol and fatty acid homeostasis |
An ARC/Mediator subunit required for SREBP control of cholesterol and lipid homeostasis
|
A C Hart, A K Walker, A M Naar, B W Vought, C Macol, F Yang, G Wagner, J L Watts, J S Satterlee, L Iyer, R DeBeaumont, R M Saito, R Tjian, S G Hyberts, S van den Heuvel, S Yang, Z Y Jim_Sun |
1775 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1777 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1779 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1781 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1783 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1785 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1787 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1789 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1791 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1793 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
331 |
Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
|
James D Satterlee, Susan J Moench |
499 |
Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
|
James D Satterlee, Susan J Moench |
500 |
Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
|
James D Satterlee, Susan J Moench |
1795 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1797 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
2488 |
Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
|
Daina Z Avizonis, James D Satterlee, Susan J Moench |
2489 |
Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
|
Daina Z Avizonis, James D Satterlee, Susan J Moench |
330 |
Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
|
James D Satterlee, Susan J Moench |
1889 |
Chemical Shifts: 1 set |
Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example |
Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example
|
David J Russell, James D Satterlee, James E Erman |
1192 |
Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |
1194 |
Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |