| Year |
Citation |
Score |
| 2018 |
Posey AE, Ruff KM, Harmon TS, Crick SL, Li A, Diamond MI, Pappu RV. Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers. The Journal of Biological Chemistry. PMID 29358329 DOI: 10.1074/Jbc.Ra117.000357 |
0.61 |
|
| 2013 |
Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-80. PMID 24282292 DOI: 10.1073/Pnas.1320626110 |
0.697 |
|
| 2013 |
Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-20080. DOI: 10.1073/pnas.1320626110 |
0.664 |
|
| 2012 |
Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. Proceedings of the National Academy of Sciences of the United States of America. 109: 6502-7. PMID 22493266 DOI: 10.1073/Pnas.1204161109 |
0.644 |
|
| 2012 |
Das RK, Crick SL, Pappu RV. N-terminal segments modulate the α-helical propensities of the intrinsically disordered basic regions of bZIP proteins. Journal of Molecular Biology. 416: 287-99. PMID 22226835 DOI: 10.1016/J.Jmb.2011.12.043 |
0.616 |
|
| 2012 |
Crick SL, Mao AH, Pappu RV. Inferring Aggregation Mechanisms of Polyglutamine Through Quantitative Studies of Phase Behavior Biophysical Journal. 102: 11a. DOI: 10.1016/J.Bpj.2011.11.081 |
0.769 |
|
| 2012 |
Crick SL, Pappu RV. Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins Protein and Peptide Folding, Misfolding, and Non-Folding. 413-440. DOI: 10.1002/9781118183373.ch14 |
0.584 |
|
| 2011 |
Das RK, Crick SL, Pappu RV. Intrinsic Helicity of Disordered Basic Regions of Bzip Transcription Factors: Implications For Mechanisms of DNA Binding Biophysical Journal. 100: 63a. DOI: 10.1016/J.Bpj.2010.12.544 |
0.557 |
|
| 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 |
0.775 |
|
| 2011 |
Das RK, Crick SL, Pappu RV. Intrinsic Disorder in the Basic Regions of bZIP Transcription Factors: What it Means to Be Disordered and Why it Might Matter! Biophysical Journal. 100: 519a. DOI: 10.1016/J.Bpj.2010.12.3033 |
0.544 |
|
| 2011 |
Crick SL, Pappu RV. Establishing a Reference State for Studying the Aggregation Kinetics of Polyglutamine Containing Systems Biophysical Journal. 100: 201a. DOI: 10.1016/J.Bpj.2010.12.1310 |
0.667 |
|
| 2010 |
Mustafi SM, Garai K, Crick SL, Baban B, Frieden C. Substoichiometric inhibition of Aβ1-40 aggregation by a tandem Aβ40-1-Gly8-1-40 peptide Biochemical and Biophysical Research Communications. 397: 509-512. PMID 20515649 DOI: 10.1016/J.Bbrc.2010.05.144 |
0.636 |
|
| 2010 |
Mao AH, Crick SL, Vitalis A, Chicoine CL, Pappu RV. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. 107: 8183-8. PMID 20404210 DOI: 10.1073/Pnas.0911107107 |
0.733 |
|
| 2010 |
Williamson TE, Vitalis A, Crick SL, Pappu RV. Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. Journal of Molecular Biology. 396: 1295-309. PMID 20026071 DOI: 10.1016/J.Jmb.2009.12.017 |
0.765 |
|
| 2010 |
Crick S, Pappu RV. Probing the Conformational Ensemble of Polyglutamine During the Initial Stages of Aggregation Biophysical Journal. 98: 424a. DOI: 10.1016/J.Bpj.2009.12.2297 |
0.657 |
|
| 2010 |
Mao AH, Crick SL, Chicoine CL, Pappu RV. Effects of pH on Conformational Equilibria of Intrinsically Disordered Proteins Biophysical Journal. 98: 256a. DOI: 10.1016/J.Bpj.2009.12.1390 |
0.745 |
|
| 2009 |
Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proceedings of the National Academy of Sciences of the United States of America. 106: 20324-20329. PMID 19910533 DOI: 10.1073/Pnas.0911281106 |
0.682 |
|
| 2009 |
Garai K, Crick SL, Mustafi SM, Frieden C. Expression and purification of amyloid-β peptides from Escherichia coli Protein Expression and Purification. 66: 107-112. PMID 19233290 DOI: 10.1016/J.Pep.2009.02.009 |
0.616 |
|
| 2009 |
Lee J, Crick S, Pappu R, Frieden C, Hu X. P1-004: Amyloid seeds formed by cellular uptake, concentration, and aggergation of the Abeta1-42
peptide Alzheimer's & Dementia. 5: P173-P173. DOI: 10.1016/J.Jalz.2009.04.007 |
0.663 |
|
| 2008 |
Pappu RV, Wang X, Vitalis A, Crick SL. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Archives of Biochemistry and Biophysics. 469: 132-41. PMID 17931593 DOI: 10.1016/J.Abb.2007.08.033 |
0.744 |
|
| 2006 |
Crick SL, Jayaraman M, Frieden C, Wetzel R, Pappu RV. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proceedings of the National Academy of Sciences of the United States of America. 103: 16764-16769. PMID 17075061 DOI: 10.1073/Pnas.0608175103 |
0.694 |
|
| 2006 |
Lee J, Hu X, Crick S, Song H, Yin K, Cirrito J, Bateman R, Hsu CY, Xu J, Hsu FF, Turk J, Pappu R, Holtzman DM, Yan P. O4-06-07: MMP-9 degrades fibrilllar abeta in vitro and compact plaques In situ Alzheimer's & Dementia. 2: S89-S89. DOI: 10.1016/J.Jalz.2006.05.342 |
0.534 |
|
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