Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|---|
51008 | 2022-02-25 | Chemical Shifts: 2 sets |
A novel in vitro Ab40 polymorph, which was used to study the PET agent flutemetamol binding to Ab40. | Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's beta-Amyloid Fibrils Studied Using 19 F Solid-State NMR | Aurelio J Dregni, Gayani Wijegunawardena, Haifan Wu, Harrison K Wang, Kelly J Chen, Mei Hong, Pu Duan |
51009 | 2022-02-25 | Chemical Shifts: 2 sets |
A novel in vitro Ab40 polymorph, which was used to study the PET agent flutemetamol binding to Ab40. | Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's beta-Amyloid Fibrils Studied Using 19 F Solid-State NMR | Aurelio J Dregni, Gayani Wijegunawardena, Haifan Wu, Harrison K Wang, Kelly J Chen, Mei Hong, Pu Duan |
50785 | 2021-05-18 | Chemical Shifts: 1 set |
In Vitro Fibrillized 0N3R Tau | Inclusion of the C-Terminal Domain in the beta-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy | Aurelio J Dregni, Haifan Wu, Harrison K Wang, Jia Jin, Mei Hong, Pu Duan, William F DeGrado |
30795 | 2020-09-28 | Chemical Shifts: 1 set |
SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR | Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers | Alexander A Shcherbakov, Antonios Kolocouris, Aurelio J Dregni, Matthew J McKay, Mei Hong, Venkata S Mandala |
26536 | 2015-04-13 | Chemical Shifts: 1 set |
Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists. | Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists | Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok |
26538 | 2015-04-13 | Chemical Shifts: 1 set |
Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists. | Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists | Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok |
26537 | 2015-04-13 | Chemical Shifts: 1 set |
Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists. | Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists | Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok |
25517 | 2016-07-13 | Chemical Shifts: 1 set |
Short hydrophobic peptide, 11mer | Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists | Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok |
15603 | 2008-03-04 | Chemical Shifts: 1 set Spectral_peak_list: 4 sets |
SOLUTION NMR STRUCTURE OF LIPOPROTEIN SPR FROM ESCHERICHIA COLI K12. NORTHEAST STRUCTURAL GENOMICS TARGET ER541-37-162 | Solution NMR Structure of the NlpC/P60 Domain of Lipoprotein Spr from Escherichia coli: Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad | Burkhard Rost, Gaetano T Montelione, James M Aramini, Jessica Locke, Li Zhao, Masayori Inouye, Mei Jiang, Melissa Maglaqui, Paolo Rossi, Rajesh Nair, Rong Xiao, Thomas B Acton, Yuanpeng J Huang |
15476 | 2007-09-21 | Chemical Shifts: 1 set |
Solution NMR structure of the folded N-terminal fragment of UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384-1-46. | Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis | Burkhard Rost, Chi Kent Ho, Gaetano T Montelione, Gurla VT Swapna, James M Aramini, Jinfeng Liu, Karishma Shetty, Kellie Cunningham, Leah A Owens, Li-Chung Ma, Li Zhao, Mei Jiang, Micheal C Baran, Rong Xiao, Seema Sharma, Thomas B Acton, Yuanpeng J Huang |
7180 | 2007-11-21 | Chemical Shifts: 1 set |
NMR structure of UPF0301 PROTEIN SO3346 from Shewanella oneidensis: Northeast Structural Genomics Consortium target SOR39 | NMR structure of UPF0301 PROTEIN SO3346 from Shewanella oneidensis: Northeast Structural Genomics Consortium target SOR39 | A Eletsky, B Rost, D K Sukumaran, D Xu, G Liu, G T Montelione, J Mei, K Cunningham, K K Singarapu, L C Ma, R Xiao, S Ritu, T B Acton, T Szyperski |
6953 | 2007-10-15 | Chemical Shifts: 1 set |
NMR solution of rabbit Prion Protein (91-228) | 1H, 13C and 15N resonance assignments of rabbit prion protein (91-228) | D H Lin, F H Mei, G F Xiao, J Li |
4064 | 1998-02-25 | Chemical Shifts: 1 set |
Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase | Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase | Charlotte Urbano, Franklin J Moy, Loran M Killar, Mei-Li Sung, Michael R Pisano, Pranab K Chanda, Robert Powers |
1797 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 | 1995-07-31 | 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 |
1775 | 1995-07-31 | 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 |
1795 | 1995-07-31 | 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 |