| Year |
Citation |
Score |
| 2016 |
Tuttle MD, Comellas G, Nieuwkoop AJ, Covell DJ, Berthold DA, Kloepper KD, Courtney JM, Kim JK, Barclay AM, Kendall A, Wan W, Stubbs G, Schwieters CD, Lee VM, George JM, et al. Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Nature Structural & Molecular Biology. PMID 27018801 DOI: 10.1038/Nsmb.3194 |
0.761 |
|
| 2016 |
Tuttle M, Comellas G, Nieuwkoop A, Covell D, Berthold D, Kloepper K, Courtney J, Kim J, Schwieters C, Lee V, George J, Rienstra C. Atomic-resolution structure of alpha-synuclein fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25518 |
0.775 |
|
| 2012 |
Lemkau LR, Comellas G, Kloepper KD, Woods WS, George JM, Rienstra CM. Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics. The Journal of Biological Chemistry. 287: 11526-32. PMID 22334684 DOI: 10.1074/Jbc.M111.306902 |
0.762 |
|
| 2012 |
Lemkau L, Comellas G, Kloepper K, Woods W, George J, Rienstra C. A30P alpha-synuclein fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17214 |
0.775 |
|
| 2011 |
Comellas G, Lemkau LR, Nieuwkoop AJ, Kloepper KD, Ladror DT, Ebisu R, Woods WS, Lipton AS, George JM, Rienstra CM. Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites. Journal of Molecular Biology. 411: 881-95. PMID 21718702 DOI: 10.1016/J.Jmb.2011.06.026 |
0.72 |
|
| 2011 |
Comellas G, Lemkau L, Nieuwkoop A, Kloepper K, Ladror D, Ebisu R, Woods W, Lipton A, George J, Rienstra C. Partial 13C, 15N chemical shift assignments of A53T alpha-synuclein fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17649 |
0.738 |
|
| 2011 |
Comellas G, Kloepper K, Nieuwkoop A, Lemkau L, Ladror D, Ebisu R, Woods W, Lipton A, George J, Rienstra C. WT alpha-synuclein fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16939 |
0.741 |
|
| 2007 |
Kloepper KD, Hartman KL, Ladror DT, Rienstra CM. Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils. The Journal of Physical Chemistry. B. 111: 13353-6. PMID 17985869 DOI: 10.1021/Jp077036Z |
0.71 |
|
| 2007 |
Kloepper KD, Zhou DH, Li Y, Winter KA, George JM, Rienstra CM. Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils. Journal of Biomolecular Nmr. 39: 197-211. PMID 17899395 DOI: 10.1007/S10858-007-9189-Z |
0.67 |
|
| 2007 |
Woods WS, Boettcher JM, Zhou DH, Kloepper KD, Hartman KL, Ladror DT, Qi Z, Rienstra CM, George JM. Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy. The Journal of Biological Chemistry. 282: 34555-67. PMID 17893145 DOI: 10.1074/Jbc.M705283200 |
0.764 |
|
| 2007 |
Franks WT, Kloepper KD, Wylie BJ, Rienstra CM. Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins. Journal of Biomolecular Nmr. 39: 107-31. PMID 17687624 DOI: 10.1007/S10858-007-9179-1 |
0.737 |
|
| 2006 |
Zhou DH, Kloepper KD, Winter KA, Rienstra CM. Band-selective 13C homonuclear 3D spectroscopy for solid proteins at high field with rotor-synchronized soft pulses. Journal of Biomolecular Nmr. 34: 245-57. PMID 16645815 DOI: 10.1007/S10858-006-0026-6 |
0.621 |
|
| 2006 |
Kloepper KD, Woods WS, Winter KA, George JM, Rienstra CM. Preparation of alpha-synuclein fibrils for solid-state NMR: expression, purification, and incubation of wild-type and mutant forms. Protein Expression and Purification. 48: 112-7. PMID 16564705 DOI: 10.1016/J.Pep.2006.02.009 |
0.671 |
|
| Show low-probability matches. |