Year |
Citation |
Score |
2015 |
Diamond MI, Cai S, Boudreau A, Carey CJ, Lyle N, Pappu RV, Swamidass SJ, Bissell M, Piwnica-Worms H, Shao J. Subcellular localization and Ser-137 phosphorylation regulate tumor-suppressive activity of profilin-1. The Journal of Biological Chemistry. 290: 9075-86. PMID 25681442 DOI: 10.1074/Jbc.M114.619874 |
0.465 |
|
2015 |
Holehouse AS, Garai K, Lyle N, Vitalis A, Pappu RV. Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. Journal of the American Chemical Society. 137: 2984-95. PMID 25664638 DOI: 10.1021/Ja512062H |
0.735 |
|
2014 |
Mittal A, Lyle N, Harmon TS, Pappu RV. Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins. Journal of Chemical Theory and Computation. 10: 3550-3562. PMID 25136274 DOI: 10.1021/Ct5002297 |
0.621 |
|
2014 |
Luan B, Lyle N, Pappu RV, Raleigh DP. Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47. PMID 24280003 DOI: 10.1021/Bi4008337 |
0.621 |
|
2014 |
Holehouse AS, Lyle N, Vitalis A, Thirumalai D, Pappu RV. Parsing the Contributions of Polypeptide Backbones and Sidechains to Denaturation in Concentrated Aqueous Solutions of Urea and Guanidinium Chloride Biophysical Journal. 106: 484a. DOI: 10.1016/J.Bpj.2013.11.2731 |
0.711 |
|
2013 |
Lyle N, Das RK, Pappu RV. A quantitative measure for protein conformational heterogeneity. The Journal of Chemical Physics. 139: 121907. PMID 24089719 DOI: 10.1063/1.4812791 |
0.632 |
|
2013 |
Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP. The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71. PMID 23480024 DOI: 10.1021/Bi301667U |
0.63 |
|
2013 |
Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV. Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8. PMID 23341588 DOI: 10.1073/Pnas.1216979110 |
0.65 |
|
2013 |
Mao AH, Lyle N, Pappu RV. Describing sequence-ensemble relationships for intrinsically disordered proteins. The Biochemical Journal. 449: 307-18. PMID 23240611 DOI: 10.1042/Bj20121346 |
0.71 |
|
2013 |
Lyle NJ, Pappu RV. Quantifying Disorder using Simulated Ensembles for Different Classes of Polypeptides Biophysical Journal. 104: 53a. DOI: 10.1016/J.Bpj.2012.11.335 |
0.637 |
|
2013 |
Khan S, Lyle N, Pappu RV. Coarse Grain Simulations Providing a Unifying Framework for Explaining Polyglutamine Aggregation Mechanism Biophysical Journal. 104: 388a-389a. DOI: 10.1016/J.Bpj.2012.11.2166 |
0.621 |
|
2013 |
Ruff K, Lyle N, Pappu RV. Modulation of Polyglutamine Conformations and Associations by C-Terminal Proline Rich Regions from Exon 1 of Huntingtin Biophysical Journal. 104: 233a. DOI: 10.1016/J.Bpj.2012.11.1317 |
0.598 |
|
2012 |
Lyle NJ, Meng W, Raleigh DP, Pappu RV. Simulations of Denatured Protein Ensembles Reproduce and Rationalize Experimental Observations of Persistent Contacts Between Residues Distal in Protein Sequence Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3433 |
0.665 |
|
2012 |
Ruff K, Lyle N, Pappu RV. Implications Of Cis Interactions Between Expanded Polyglutamine and the Proline Rich C-Terminal Domain of Huntingtin Exon 1 For the Loss- Versus Gain-Of-Function Models of Huntington's Disease Biophysical Journal. 102: 256a. DOI: 10.1016/J.Bpj.2011.11.1411 |
0.595 |
|
2011 |
Halfmann R, Alberti S, Krishnan R, Lyle N, O'Donnell CW, King OD, Berger B, Pappu RV, Lindquist S. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Molecular Cell. 43: 72-84. PMID 21726811 DOI: 10.1016/J.Molcel.2011.05.013 |
0.621 |
|
2011 |
Lyle NJ, Crick SL, Pappu RV. Alterations to the Conformational Ensemble and Intermolecular Associations of Polyglutamine Due to Charged Side Chains at the N- and C-Termini Biophysical Journal. 100: 63a. DOI: 10.1016/J.Bpj.2010.12.543 |
0.725 |
|
2010 |
Lyle NJ, Pappu RV. Parameter Refinement, Optimization, and Extension of the Absinth Implicit Solvation Model Biophysical Journal. 98: 574a. DOI: 10.1016/J.Bpj.2009.12.3118 |
0.593 |
|
2009 |
Vitalis A, Lyle N, Pappu RV. Thermodynamics of beta-sheet formation in polyglutamine. Biophysical Journal. 97: 303-11. PMID 19580768 DOI: 10.1016/J.Bpj.2009.05.003 |
0.686 |
|
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