Year |
Citation |
Score |
2020 |
Tang WS, Fawzi NL, Mittal J. Refining All-Atom Protein Force Fields for Polar-Rich, Prion-like, Low-Complexity Intrinsically Disordered Proteins. The Journal of Physical Chemistry. B. PMID 33078950 DOI: 10.1021/acs.jpcb.0c07545 |
0.307 |
|
2020 |
Ryan VH, Watters S, Amaya J, Khatiwada B, Venditti V, Naik MT, Fawzi NL. Weak binding to the A2RE RNA rigidifies hnRNPA2 RRMs and reduces liquid-liquid phase separation and aggregation. Nucleic Acids Research. PMID 32870271 DOI: 10.1093/Nar/Gkaa710 |
0.331 |
|
2020 |
Fawzi NL. Elastin phase separation — structure or disorder? Nature Reviews Molecular Cell Biology. 21: 1-1. PMID 32860012 DOI: 10.1038/S41580-020-00291-0 |
0.33 |
|
2020 |
Conicella AE, Dignon GL, Zerze GH, Schmidt HB, D'Ordine AM, Kim YC, Rohatgi R, Ayala YM, Mittal J, Fawzi NL. TDP-43 α-helical structure tunes liquid-liquid phase separation and function. Proceedings of the National Academy of Sciences of the United States of America. PMID 32132204 DOI: 10.1073/Pnas.1912055117 |
0.37 |
|
2020 |
Murthy AC, Fawzi NL. The (un)structural biology of biomolecular liquid-liquid phase separation using NMR spectroscopy. The Journal of Biological Chemistry. PMID 31911439 DOI: 10.1074/Jbc.Rev119.009847 |
0.401 |
|
2020 |
Mathews KL, Marglous J, Fawzi NL. Structural and Biophysical Characterization of Splicing-Associated Assemblies of the SMN Protein Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1228 |
0.382 |
|
2019 |
Ryan VH, Fawzi NL. Physiological, Pathological, and Targetable Membraneless Organelles in Neurons. Trends in Neurosciences. PMID 31493925 DOI: 10.1016/J.Tins.2019.08.005 |
0.314 |
|
2019 |
Stackpole EE, Akins MR, Ivshina M, Murthy AC, Fawzi NL, Fallon JR. EGFP insertional mutagenesis reveals multiple FXR2P fibrillar states with differing ribosome association in neurons. Biology Open. 8. PMID 31434643 DOI: 10.1242/Bio.046383 |
0.314 |
|
2019 |
Murthy AC, Dignon GL, Kan Y, Zerze GH, Parekh SH, Mittal J, Fawzi NL. Molecular interactions underlying liquid-liquid phase separation of the FUS low-complexity domain. Nature Structural & Molecular Biology. 26: 637-648. PMID 31270472 DOI: 10.1038/S41594-019-0250-X |
0.355 |
|
2019 |
Cable J, Brangwynne C, Seydoux G, Cowburn D, Pappu RV, Castañeda CA, Berchowitz LE, Chen Z, Jonikas M, Dernburg A, Mittag T, Fawzi NL. Phase separation in biology and disease-a symposium report. Annals of the New York Academy of Sciences. PMID 31199001 DOI: 10.1111/Nyas.14126 |
0.312 |
|
2018 |
Amaya J, Ryan VH, Fawzi NL. The SH3 domain of Fyn kinase interacts with and induces liquid-liquid phase separation of the low complexity domain of hnRNPA2. The Journal of Biological Chemistry. PMID 30397184 DOI: 10.1074/Jbc.Ra118.005120 |
0.316 |
|
2018 |
Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, et al. Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Cell. 173: 693-705.e22. PMID 29677513 DOI: 10.1016/J.Cell.2018.03.003 |
0.314 |
|
2018 |
Boeynaems S, Alberti S, Fawzi NL, Mittag T, Polymenidou M, Rousseau F, Schymkowitz J, Shorter J, Wolozin B, Van Den Bosch L, Tompa P, Fuxreiter M. Protein Phase Separation: A New Phase in Cell Biology. Trends in Cell Biology. PMID 29602697 DOI: 10.1016/J.Tcb.2018.02.004 |
0.349 |
|
2018 |
Wang A, Conicella AE, Schmidt HB, Martin EW, Rhoads SN, Reeb AN, Nourse A, Ramirez Montero D, Ryan VH, Rohatgi R, Shewmaker F, Naik MT, Mittag T, Ayala YM, Fawzi NL. A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing. The Embo Journal. PMID 29438978 DOI: 10.15252/Embj.201797452 |
0.382 |
|
2018 |
Ryan VH, Dignon GL, Zerze GH, Chabata CV, Silva R, Conicella AE, Amaya J, Burke KA, Mittal J, Fawzi NL. Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. Molecular Cell. PMID 29358076 DOI: 10.1016/J.Molcel.2017.12.022 |
0.343 |
|
2018 |
Venditti V, Fawzi NL. Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR. Methods in Molecular Biology (Clifton, N.J.). 1688: 243-255. PMID 29151213 DOI: 10.1007/978-1-4939-7386-6_12 |
0.399 |
|
2017 |
Janke AM, Seo DH, Rahmanian V, Conicella AE, Mathews KL, Burke KA, Mittal J, Fawzi NL. Lysines in RNA polymerase II C-terminal domain contribute to TAF15 fibril recruitment. Biochemistry. PMID 28945358 DOI: 10.1021/Acs.Biochem.7B00310 |
0.312 |
|
2017 |
Monahan Z, Ryan VH, Janke AM, Burke KA, Rhoads SN, Zerze GH, O'Meally R, Dignon GL, Conicella AE, Zheng W, Best RB, Cole RN, Mittal J, Shewmaker F, Fawzi NL. Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity. The Embo Journal. PMID 28790177 DOI: 10.15252/Embj.201696394 |
0.382 |
|
2017 |
Fawzi N. Visualizing Structural Details of Disordered Domain Phase Separation Associated with ALS and Cancers Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.046 |
0.333 |
|
2016 |
Conicella AE, Zerze GH, Mittal J, Fawzi NL. ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. Structure (London, England : 1993). PMID 27545621 DOI: 10.1016/J.Str.2016.07.007 |
0.371 |
|
2015 |
Burke KA, Janke AM, Rhine CL, Fawzi NL. Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II. Molecular Cell. PMID 26455390 DOI: 10.1016/J.Molcel.2015.09.006 |
0.405 |
|
2014 |
Fawzi NL, Libich DS, Ying J, Tugarinov V, Clore GM. Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening. Angewandte Chemie (International Ed. in English). 53: 10345-9. PMID 25130489 DOI: 10.1002/Anie.201405180 |
0.375 |
|
2014 |
Conicella AE, Fawzi NL. The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils. Biochemistry. 53: 3095-105. PMID 24773532 DOI: 10.1021/Bi500131A |
0.451 |
|
2013 |
Libich DS, Fawzi NL, Ying J, Clore GM. Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR. Proceedings of the National Academy of Sciences of the United States of America. 110: 11361-6. PMID 23798407 DOI: 10.1073/Pnas.1305715110 |
0.412 |
|
2012 |
Fawzi NL, Ying J, Torchia DA, Clore GM. Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy. Nature Protocols. 7: 1523-33. PMID 22814391 DOI: 10.1038/Nprot.2012.077 |
0.357 |
|
2012 |
Cellmer T, Fawzi NL. Coarse-grained simulations of protein aggregation. Methods in Molecular Biology (Clifton, N.J.). 899: 453-70. PMID 22735969 DOI: 10.1007/978-1-61779-921-1_27 |
0.403 |
|
2012 |
Venditti V, Fawzi NL, Clore GM. An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media. Journal of Biomolecular Nmr. 52: 191-5. PMID 22350951 DOI: 10.1007/S10858-012-9606-9 |
0.308 |
|
2012 |
Ball KA, Phillips AH, Fawzi NL, Wemmer DE, Head-Gordon T. Amyloid-Beta Heterogeneous Conformational Ensembles: Differences Between the 40- and 42-Residue Peptides and Implications for Dimer Polyamorphism Biophysical Journal. 102: 631a. DOI: 10.1016/J.Bpj.2011.11.3437 |
0.666 |
|
2011 |
Fawzi NL, Ying J, Ghirlando R, Torchia DA, Clore GM. Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR. Nature. 480: 268-72. PMID 22037310 DOI: 10.1038/Nature10577 |
0.424 |
|
2011 |
Venditti V, Fawzi NL, Clore GM. Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy. Journal of Biomolecular Nmr. 51: 319-28. PMID 21935714 DOI: 10.1007/S10858-011-9559-4 |
0.306 |
|
2011 |
Ball KA, Phillips AH, Nerenberg PS, Fawzi NL, Wemmer DE, Head-Gordon T. Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides. Biochemistry. 50: 7612-28. PMID 21797254 DOI: 10.1021/Bi200732X |
0.771 |
|
2011 |
Fawzi NL, Phillips AH, Ruscio JZ, Doucleff M, Wemmer DE, Head-Gordon T. Structure and dynamics of the Aβ 21-30 peptide from the interplay of NMR experiments and molecular simulations (Journal of the American Chemical Society (2008) 130 (6145-6158) DOI: 10.1021/ja710366c) Journal of the American Chemical Society. 133: 11816. DOI: 10.1021/ja204315n |
0.729 |
|
2010 |
Fawzi NL, Ying J, Torchia DA, Clore GM. Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation. Journal of the American Chemical Society. 132: 9948-51. PMID 20604554 DOI: 10.1021/Ja1048253 |
0.429 |
|
2010 |
Fawzi NL, Doucleff M, Suh JY, Clore GM. Mechanistic details of a protein-protein association pathway revealed by paramagnetic relaxation enhancement titration measurements. Proceedings of the National Academy of Sciences of the United States of America. 107: 1379-84. PMID 20080627 DOI: 10.1073/Pnas.0909370107 |
0.352 |
|
2010 |
Ruscio JZ, Fawzi NL, Head-Gordon T. How hot? Systematic convergence of the replica exchange method using multiple reservoirs. Journal of Computational Chemistry. 31: 620-7. PMID 19554556 DOI: 10.1002/Jcc.21355 |
0.694 |
|
2008 |
Fawzi NL, Yap EH, Okabe Y, Kohlstedt KL, Brown SP, Head-Gordon T. Contrasting disease and nondisease protein aggregation by molecular simulation. Accounts of Chemical Research. 41: 1037-47. PMID 18646868 DOI: 10.1021/Ar800062K |
0.749 |
|
2008 |
Fawzi NL, Phillips AH, Ruscio JZ, Doucleff M, Wemmer DE, Head-Gordon T. Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations. Journal of the American Chemical Society. 130: 6145-58. PMID 18412346 DOI: 10.1021/Ja710366C |
0.748 |
|
2008 |
Fawzi NL, Kohlstedt KL, Okabe Y, Head-Gordon T. Protofibril assemblies of the arctic, Dutch, and Flemish mutants of the Alzheimer's Abeta1-40 peptide. Biophysical Journal. 94: 2007-16. PMID 18032553 DOI: 10.1529/Biophysj.107.121467 |
0.614 |
|
2008 |
Yap EH, Fawzi NL, Head-Gordon T. A coarse-grained alpha-carbon protein model with anisotropic hydrogen-bonding. Proteins. 70: 626-38. PMID 17879350 DOI: 10.1002/Prot.21515 |
0.676 |
|
2007 |
Lin MS, Fawzi NL, Head-Gordon T. Hydrophobic potential of mean force as a solvation function for protein structure prediction. Structure (London, England : 1993). 15: 727-40. PMID 17562319 DOI: 10.1016/J.Str.2007.05.004 |
0.675 |
|
2007 |
Fawzi NL, Okabe Y, Yap EH, Head-Gordon T. Determining the critical nucleus and mechanism of fibril elongation of the Alzheimer's Abeta(1-40) peptide. Journal of Molecular Biology. 365: 535-50. PMID 17070840 DOI: 10.1016/J.Jmb.2006.10.011 |
0.704 |
|
2005 |
Marianayagam NJ, Fawzi NL, Head-Gordon T. Protein folding by distributed computing and the denatured state ensemble. Proceedings of the National Academy of Sciences of the United States of America. 102: 16684-9. PMID 16267133 DOI: 10.1073/Pnas.0506388102 |
0.59 |
|
2005 |
Fawzi NL, Chubukov V, Clark LA, Brown S, Head-Gordon T. Influence of denatured and intermediate states of folding on protein aggregation. Protein Science : a Publication of the Protein Society. 14: 993-1003. PMID 15772307 DOI: 10.1110/Ps.041177505 |
0.677 |
|
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