| Year |
Citation |
Score |
| 2023 |
Zhang L, Brown MC, Mutter AC, Greenland KN, Cooley JW, Koder RL. Protein dynamics govern the oxyferrous state lifetime of an artificial oxygen transport protein. Biophysical Journal. PMID 37865818 DOI: 10.1016/j.bpj.2023.10.022 |
0.627 |
|
| 2023 |
McGuinness KN, Fehon N, Feehan R, Miller M, Mutter AC, Rybak LA, Nam J, AbuSalim JE, Atkinson JT, Heidari H, Losada N, Kim JD, Koder RL, Lu Y, Silberg JJ, et al. The energetics and evolution of oxidoreductases in deep time. Proteins. PMID 37596815 DOI: 10.1002/prot.26563 |
0.627 |
|
| 2019 |
Mutter AC, Tyryshkin AM, Campbell IJ, Poudel S, Bennett GN, Silberg JJ, Nanda V, Falkowski PG. De novo design of symmetric ferredoxins that shuttle electrons in vivo. Proceedings of the National Academy of Sciences of the United States of America. PMID 31262814 DOI: 10.1073/Pnas.1905643116 |
0.373 |
|
| 2015 |
Andersen EM, Koder RL, Mutter AC. Photosynthesis in a Single Protein Biophysical Journal. 108: 605a. DOI: 10.1016/J.Bpj.2014.11.3297 |
0.627 |
|
| 2014 |
Mutter AC, Norman JA, Tiedemann MT, Singh S, Sha S, Morsi S, Ahmed I, Stillman MJ, Koder RL. Rational design of a zinc phthalocyanine binding protein. Journal of Structural Biology. 185: 178-85. PMID 23827257 DOI: 10.1016/J.Bpj.2012.11.3785 |
0.66 |
|
| 2014 |
Raju G, Singh S, Mutter AC, Everson BH, Cerda JF, Koder RL. An extended scope synthesis of an artificial safranine cofactor Tetrahedron Letters. 55: 2487-2491. DOI: 10.1016/J.Tetlet.2014.03.010 |
0.645 |
|
| 2014 |
Raju G, Singh S, Mutter AC, Everson BH, Cerda JF, Koder RL. ChemInform Abstract: An Extended Scope Synthesis of an Artificial Safranine Cofactor. Cheminform. 45: no-no. DOI: 10.1002/CHIN.201438178 |
0.675 |
|
| 2013 |
Brown MC, Mutter A, Koder RL, JiJi RD, Cooley JW. Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy. Journal of Raman Spectroscopy : Jrs. 44: 957-962. PMID 27795611 DOI: 10.1002/Jrs.4316 |
0.647 |
|
| 2013 |
Brisendine JM, Mutter AC, Cerda JF, Koder RL. A three-dimensional printed cell for rapid, low-volume spectroelectrochemistry. Analytical Biochemistry. 439: 1-3. PMID 23583818 DOI: 10.1016/J.Ab.2013.03.036 |
0.593 |
|
| 2013 |
Everson BH, French CA, Mutter AC, Nanda V, Koder RL. Hemoprotein Design using Minimal Sequence Information Biophysical Journal. 104: 661a. DOI: 10.1016/J.Bpj.2012.11.3649 |
0.661 |
|
| 2013 |
Brown MC, Mutter AC, Koder RL, Jiji RD, Cooley JW. Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy Journal of Raman Spectroscopy. 44: 957-962. DOI: 10.1002/jrs.4316 |
0.565 |
|
| 2012 |
Punnoose A, McConnell LA, McConnell L, Liu W, Mutter AC, Koder RL, Koder R. Fundamental limits on wavelength, efficiency and yield of the charge separation triad. Plos One. 7: e36065. PMID 22675467 DOI: 10.1371/Journal.Pone.0036065 |
0.645 |
|
| 2012 |
Punnoose A, McConnell LA, Liu W, Mutter AC, Koder RL. Correction: Fundamental Limits on Wavelength, Efficiency and Yield of the Charge Separation Triad Plos One. 7. DOI: 10.1371/Annotation/7Db1B9Ef-C93C-4B02-B721-A8473D2Bb4E2 |
0.585 |
|
| 2012 |
Brown M, Cooley J, JiJi R, Koder R, Mutter A. Persistent α-Helical Content and Local Helical Structural Fluctuations from a Molten Globule to Ordered Peptide Transition Biophysical Journal. 102: 444a. DOI: 10.1016/J.Bpj.2011.11.2432 |
0.652 |
|
| 2011 |
Zhang L, Anderson JL, Ahmed I, Norman JA, Negron C, Mutter AC, Dutton PL, Koder RL. Manipulating cofactor binding thermodynamics in an artificial oxygen transport protein. Biochemistry. 50: 10254-61. PMID 22004125 DOI: 10.1021/Bi201242A |
0.647 |
|
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