| Year |
Citation |
Score |
| 2020 |
Tenorio CA, Longo LM, Parker JB, Lee J, Blaber M. Ab initio Folding of a Trefoil-fold Motif Reveals Structural similarity with a β-propeller Blade Motif. Protein Science : a Publication of the Protein Society. PMID 32142181 DOI: 10.1002/Pro.3850 |
0.779 |
|
| 2016 |
Marzahn MR, Marada S, Lee J, Nourse A, Kenrick S, Zhao H, Ben-Nissan G, Kolaitis RM, Peters JL, Pounds S, Errington WJ, Privé GG, Taylor JP, Sharon M, Schuck P, et al. Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles. The Embo Journal. 35: 1254-75. PMID 27220849 DOI: 10.15252/Embj.201593169 |
0.351 |
|
| 2015 |
Pierce WK, Grace CR, Lee J, Nourse A, Marzahn MR, Watson ER, High AA, Peng J, Schulman BA, Mittag T. Multiple weak linear motifs enhance recruitment and processivity in SPOP-mediated substrate ubiquitination. Journal of Molecular Biology. PMID 26475525 DOI: 10.1016/J.Jmb.2015.10.002 |
0.341 |
|
| 2015 |
Marzahn MR, Lee J, Marada S, Nourse A, Zhao H, Schuck P, Ogden SK, Mittag T. The Role of Higher-Order SPOP Oligomers for Localization to Cellular “Bodies” and Ubiquitination Activity Biophysical Journal. 108: 390a. DOI: 10.1016/J.Bpj.2014.11.2135 |
0.357 |
|
| 2015 |
Marzahn MR, Lee J, Palud A, Marada S, Nourse A, Taylor JP, Ogden SK, Mittag T. The Role of Protein Disorder and Self-Association in the Formation of Cellular Bodies Biophysical Journal. 108: 6a. DOI: 10.1016/J.Bpj.2014.11.047 |
0.356 |
|
| 2013 |
Longo LM, Lee J, Tenorio CA, Blaber M. Alternative folding nuclei definitions facilitate the evolution of a symmetric protein fold from a smaller peptide motif. Structure (London, England : 1993). 21: 2042-50. PMID 24139990 DOI: 10.1016/J.Str.2013.09.003 |
0.798 |
|
| 2013 |
Longo LM, Lee J, Blaber M. Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein. Proceedings of the National Academy of Sciences of the United States of America. 110: 2135-9. PMID 23341608 DOI: 10.1073/Pnas.1219530110 |
0.786 |
|
| 2012 |
Longo L, Lee J, Blaber M. Experimental support for the foldability-function tradeoff hypothesis: segregation of the folding nucleus and functional regions in fibroblast growth factor-1. Protein Science : a Publication of the Protein Society. 21: 1911-20. PMID 23047594 DOI: 10.1002/Pro.2175 |
0.806 |
|
| 2012 |
Blaber M, Lee J, Longo L. Emergence of symmetric protein architecture from a simple peptide motif: evolutionary models. Cellular and Molecular Life Sciences : Cmls. 69: 3999-4006. PMID 22790181 DOI: 10.1007/S00018-012-1077-3 |
0.806 |
|
| 2012 |
Blaber M, Lee J. Designing proteins from simple motifs: opportunities in Top-Down Symmetric Deconstruction. Current Opinion in Structural Biology. 22: 442-50. PMID 22726756 DOI: 10.1016/J.Sbi.2012.05.008 |
0.733 |
|
| 2012 |
Alsenaidy MA, Wang T, Kim JH, Joshi SB, Lee J, Blaber M, Volkin DB, Middaugh CR. An empirical phase diagram approach to investigate conformational stability of "second-generation" functional mutants of acidic fibroblast growth factor-1. Protein Science : a Publication of the Protein Society. 21: 418-32. PMID 22113934 DOI: 10.1002/Pro.2008 |
0.765 |
|
| 2011 |
Lee J, Blaber SI, Dubey VK, Blaber M. A polypeptide "building block" for the β-trefoil fold identified by "top-down symmetric deconstruction". Journal of Molecular Biology. 407: 744-63. PMID 21315087 DOI: 10.1016/J.Jmb.2011.02.002 |
0.789 |
|
| 2011 |
Lee J, Blaber M. Experimental support for the evolution of symmetric protein architecture from a simple peptide motif. Proceedings of the National Academy of Sciences of the United States of America. 108: 126-30. PMID 21173271 DOI: 10.1073/Pnas.1015032108 |
0.739 |
|
| 2011 |
Lee J, Blaber SI, Dubey VK, Blaber M. Crystal structure of ""L44F/M67I/L73V/A103G/deletion 104-106/F108Y/V109L/L111I/C117V/R119G/deletion 120-122"" mutant form of Human acidic fibroblast growth factor Journal of Molecular Biology. 407: 744-763. DOI: 10.2210/Pdb3O3Q/Pdb |
0.712 |
|
| 2009 |
Meher AK, Blaber SI, Lee J, Honjo E, Kuroki R, Blaber M. Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 1136-40. PMID 19923735 DOI: 10.1107/S1744309109036987 |
0.767 |
|
| 2009 |
Lee J, Blaber SI, Irsigler A, Aspinwall E, Blaber M. X-ray structure and biophysical properties of rabbit fibroblast growth factor 1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 1097-104. PMID 19923726 DOI: 10.1107/S1744309109040287 |
0.702 |
|
| 2009 |
Kogot JM, Parker AM, Lee J, Blaber M, Strouse GF, Logan TM. Analysis of the dynamics of assembly and structural impact for a histidine tagged FGF1-1.5 nm Au nanoparticle bioconjugate. Bioconjugate Chemistry. 20: 2106-13. PMID 19810698 DOI: 10.1021/Bc900224D |
0.731 |
|
| 2009 |
Lee J, Blaber M. The interaction between thermodynamic stability and buried free cysteines in regulating the functional half-life of fibroblast growth factor-1. Journal of Molecular Biology. 393: 113-27. PMID 19695265 DOI: 10.1016/J.Jmb.2009.08.026 |
0.769 |
|
| 2009 |
Lee J, Blaber M. Structural basis of conserved cysteine in the fibroblast growth factor family: evidence for a vestigial half-cystine. Journal of Molecular Biology. 393: 128-39. PMID 19683004 DOI: 10.1016/J.Jmb.2009.08.007 |
0.752 |
|
| 2008 |
Lee J, Dubey VK, Longo LM, Blaber M. A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif. Journal of Molecular Biology. 377: 1251-64. PMID 18308335 DOI: 10.1016/J.Jmb.2008.01.055 |
0.812 |
|
| 2007 |
Yoon H, Laxmikanthan G, Lee J, Blaber SI, Rodriguez A, Kogot JM, Scarisbrick IA, Blaber M. Activation profiles and regulatory cascades of the human kallikrein-related peptidases. The Journal of Biological Chemistry. 282: 31852-64. PMID 17823117 DOI: 10.1074/Jbc.M705190200 |
0.738 |
|
| 2007 |
Dubey VK, Lee J, Somasundaram T, Blaber S, Blaber M. Spackling the crack: stabilizing human fibroblast growth factor-1 by targeting the N and C terminus beta-strand interactions. Journal of Molecular Biology. 371: 256-68. PMID 17570396 DOI: 10.1016/J.Jmb.2007.05.065 |
0.776 |
|
| 2006 |
Lee J, Dubey VK, Somasundaram T, Blaber M. Conversion of type I 4:6 to 3:5 beta-turn types in human acidic fibroblast growth factor: effects upon structure, stability, folding, and mitogenic function. Proteins. 62: 686-97. PMID 16355415 DOI: 10.1002/Prot.20808 |
0.801 |
|
| 2005 |
Dubey VK, Lee J, Blaber M. Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: thermodynamic and functional consequences of structural symmetry. Protein Science : a Publication of the Protein Society. 14: 2315-23. PMID 16081654 DOI: 10.1110/Ps.051494405 |
0.797 |
|
| 2005 |
Kim J, Lee J, Brych SR, Logan TM, Blaber M. Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor. Protein Science : a Publication of the Protein Society. 14: 351-9. PMID 15632285 DOI: 10.1110/Ps.041094205 |
0.776 |
|
| 2004 |
Brych SR, Dubey VK, Bienkiewicz E, Lee J, Logan TM, Blaber M. Symmetric primary and tertiary structure mutations within a symmetric superfold: a solution, not a constraint, to achieve a foldable polypeptide. Journal of Molecular Biology. 344: 769-80. PMID 15533444 DOI: 10.1016/J.Jmb.2004.09.060 |
0.794 |
|
| 2003 |
Kim J, Brych SR, Lee J, Logan TM, Blaber M. Identification of a key structural element for protein folding within beta-hairpin turns. Journal of Molecular Biology. 328: 951-61. PMID 12729767 DOI: 10.1016/S0022-2836(03)00321-8 |
0.8 |
|
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