Year |
Citation |
Score |
2020 |
Hsieh CL, Goldsmith JA, Schaub JM, DiVenere AM, Kuo HC, Javanmardi K, Le KC, Wrapp D, Lee AG, Liu Y, Chou CW, Byrne PO, Hjorth CK, Johnson NV, Ludes-Meyers J, ... ... Lavinder JJ, et al. Structure-based design of prefusion-stabilized SARS-CoV-2 spikes. Science (New York, N.Y.). PMID 32703906 DOI: 10.1126/Science.Abd0826 |
0.31 |
|
2018 |
Bowles DP, Yuan C, Stephany KR, Lavinder JJ, Hansen AL, Magliery TJ. Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop. Biomolecular Nmr Assignments. PMID 30159810 DOI: 10.1007/S12104-018-9837-0 |
0.639 |
|
2018 |
Bowles D, Yuan C, Lavinder J, Magliery T. Backbone 1H, 15N, 13C chemical shifts for Repressor of Primer (Rop) variant IVVA Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27451 |
0.561 |
|
2011 |
Magliery TJ, Lavinder JJ, Sullivan BJ. Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems. Current Opinion in Chemical Biology. 15: 443-51. PMID 21498105 DOI: 10.1016/J.Cbpa.2011.03.015 |
0.664 |
|
2011 |
Nie L, Lavinder JJ, Sarkar M, Stephany K, Magliery TJ. Synthetic approach to stop-codon scanning mutagenesis. Journal of the American Chemical Society. 133: 6177-86. PMID 21452871 DOI: 10.1021/Ja106894G |
0.619 |
|
2010 |
Hari SB, Byeon C, Lavinder JJ, Magliery TJ. Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics. Protein Science : a Publication of the Protein Society. 19: 670-9. PMID 20095056 DOI: 10.1002/Pro.342 |
0.677 |
|
2009 |
Gambin Y, Schug A, Lemke EA, Lavinder JJ, Ferreon AC, Magliery TJ, Onuchic JN, Deniz AA. Direct single-molecule observation of a protein living in two opposed native structures. Proceedings of the National Academy of Sciences of the United States of America. 106: 10153-8. PMID 19506258 DOI: 10.1073/Pnas.0904461106 |
0.651 |
|
2009 |
Lavinder JJ, Hari SB, Sullivan BJ, Magliery TJ. High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering. Journal of the American Chemical Society. 131: 3794-5. PMID 19292479 DOI: 10.1021/Ja8049063 |
0.659 |
|
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