| Year |
Citation |
Score |
| 2016 |
Kleinstreuer NC, Ceger P, Watt ED, Martin M, Houck K, Browne P, Thomas RS, Casey WM, Dix DJ, Allen D, Sakamuru S, Xia M, Huang R, Judson R. Development and Validation of a Computational Model for Androgen Receptor Activity. Chemical Research in Toxicology. PMID 27933809 DOI: 10.1021/Acs.Chemrestox.6B00347 |
0.303 |
|
| 2016 |
Nuzzio KM, Watt ED, Boettcher JM, Gajsiewicz JM, Morrissey JH, Rienstra CM. High-Resolution NMR Studies of Human Tissue Factor. Plos One. 11: e0163206. PMID 27657719 DOI: 10.1371/Journal.Pone.0163206 |
0.4 |
|
| 2015 |
Courtney JM, Ye Q, Nesbitt AE, Tang M, Tuttle MD, Watt ED, Nuzzio KM, Sperling LJ, Comellas G, Peterson JR, Morrissey JH, Rienstra CM. Experimental Protein Structure Verification by Scoring with a Single, Unassigned NMR Spectrum. Structure (London, England : 1993). PMID 26365800 DOI: 10.1016/J.Str.2015.07.019 |
0.362 |
|
| 2014 |
Watt ED, Rienstra CM. Recent advances in solid-state nuclear magnetic resonance techniques to quantify biomolecular dynamics. Analytical Chemistry. 86: 58-64. PMID 24313950 DOI: 10.1021/Ac403956K |
0.37 |
|
| 2011 |
Watt ED, Rivalta I, Whittier SK, Batista VS, Loria JP. Reengineering rate-limiting, millisecond enzyme motions by introduction of an unnatural amino acid. Biophysical Journal. 101: 411-20. PMID 21767494 DOI: 10.1016/J.Bpj.2011.05.039 |
0.659 |
|
| 2009 |
Doucet N, Watt ED, Loria JP. The flexibility of a distant loop modulates active site motion and product release in ribonuclease A. Biochemistry. 48: 7160-8. PMID 19588901 DOI: 10.1021/Bi900830G |
0.74 |
|
| 2008 |
Dethoff EA, Hansen AL, Musselman C, Watt ED, Andricioaei I, Al-Hashimi HM. Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesis. Biophysical Journal. 95: 3906-15. PMID 18621815 DOI: 10.1529/Biophysj.108.140285 |
0.465 |
|
| 2008 |
Croke RL, Sallum CO, Watson E, Watt ED, Alexandrescu AT. Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Science : a Publication of the Protein Society. 17: 1434-45. PMID 18493022 DOI: 10.1110/Ps.033803.107 |
0.334 |
|
| 2008 |
Loria JP, Berlow RB, Watt ED. Characterization of enzyme motions by solution NMR relaxation dispersion. Accounts of Chemical Research. 41: 214-21. PMID 18281945 DOI: 10.1021/Ar700132N |
0.701 |
|
| 2007 |
Watt ED, Shimada H, Kovrigin EL, Loria JP. The mechanism of rate-limiting motions in enzyme function. Proceedings of the National Academy of Sciences of the United States of America. 104: 11981-6. PMID 17615241 DOI: 10.1073/Pnas.0702551104 |
0.733 |
|
| 2006 |
Zhang Q, Sun X, Watt ED, Al-Hashimi HM. Resolving the motional modes that code for RNA adaptation. Science (New York, N.Y.). 311: 653-6. PMID 16456078 DOI: 10.1126/Science.1119488 |
0.408 |
|
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