Year |
Citation |
Score |
2022 |
Xiao Q, Jones ZB, Hatfield SC, Ashton DS, Dalley NA, Dyer CD, Evangelista JL, Price JL. Structural guidelines for stabilization of α-helical coiled coils PEG stapling. Rsc Chemical Biology. 3: 1096-1104. PMID 36128502 DOI: 10.1039/d1cb00237f |
0.324 |
|
2022 |
Stern KL, Dalley NA, McMurray NT, Billings WM, Loftus TJ, Jones ZB, Hadfield JR, Price JL. Prerequisites for Stabilizing Long-Range Synergistic Interactions among -, -, and -Residues in Coiled Coils. Biochemistry. PMID 35129961 DOI: 10.1021/acs.biochem.1c00760 |
0.323 |
|
2020 |
Xiao Q, Ashton DS, Jones ZB, Thompson KP, Price JL. Long-range PEG Stapling: Macrocyclization for Increased Protein Conformational Stability and Resistance to Proteolysis. Rsc Chemical Biology. 1: 273-280. PMID 33796855 DOI: 10.1039/d0cb00075b |
0.378 |
|
2020 |
Stern KL, Smith MS, Billings WM, Loftus TJ, Conover BM, Della Corte D, Price JL. Context-dependent stabilizing interactions among solvent-exposed residues along the surface of a trimeric helix bundle. Biochemistry. PMID 32270676 DOI: 10.1021/Acs.Biochem.0C00045 |
0.4 |
|
2019 |
Draper SRE, Ashton DS, Conover BM, Carter AJ, Stern KL, Xiao Q, Price JL. PEGylation near a patch of non-polar surface residues increases the conformational stability of the WW domain. The Journal of Organic Chemistry. PMID 31749365 DOI: 10.1021/Acs.Joc.9B02615 |
0.415 |
|
2019 |
Xiao Q, Draper SRE, Smith MS, Brown N, Pugmire NAB, Ashton DS, Carter AJ, Lawrence EEK, Price JL. Influence of PEGylation on the strength of protein surface salt bridges. Acs Chemical Biology. PMID 31188563 DOI: 10.1021/Acschembio.9B00432 |
0.452 |
|
2018 |
Xiao Q, Bécar NA, Brown NP, Smith MS, Stern KL, Draper SRE, Thompson KP, Price JL. Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect. Organic & Biomolecular Chemistry. PMID 30444518 DOI: 10.1039/C8Ob02535E |
0.476 |
|
2017 |
Draper SRE, Lawrence PB, Billings WM, Xiao Q, Brown NP, Becar NA, Matheson DJ, Stephens AR, Price JL. PEG-based Changes to β-sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location. Bioconjugate Chemistry. PMID 28972368 DOI: 10.1021/Acs.Bioconjchem.7B00281 |
0.422 |
|
2017 |
Jalan A, Kastner DW, Webber KGI, Smith MS, Price JL, Castle SL. Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides. Organic Letters. PMID 28910115 DOI: 10.1021/Acs.Orglett.7B02455 |
0.422 |
|
2017 |
Smith MS, Lawrence EEK, Billings WM, Price JL. An anion-π interaction strongly stabilizes the β-sheet protein WW. Acs Chemical Biology. PMID 28886246 DOI: 10.1021/Acschembio.7B00768 |
0.4 |
|
2017 |
Smith MS, Billings WM, Whitby FG, Miller MB, Price JL. Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids. Organic & Biomolecular Chemistry. PMID 28678274 DOI: 10.1039/C7Ob01198A |
0.395 |
|
2017 |
Kinghorn MJ, Valdivia-Berroeta GA, Chantry DR, Smith MS, Ence CC, Draper SRE, Duval JS, Masino BM, Cahoon SB, Flansburg RR, Conder CJ, Price JL, Michaelis DJ. Proximity-Induced Reactivity and Product Selectivity with a Rationally Designed Bifunctional Peptide Catalyst Acs Catalysis. 7: 7704-7708. DOI: 10.1021/Acscatal.7B02699 |
0.301 |
|
2016 |
Lawrence PB, Price JL. How PEGylation influences protein conformational stability. Current Opinion in Chemical Biology. 34: 88-94. PMID 27580482 DOI: 10.1016/J.Cbpa.2016.08.006 |
0.461 |
|
2016 |
Lawrence PB, Billings WM, Miller MB, Pandey BK, Stephens AR, Langlois MI, Price JL. Conjugation Strategy Strongly Impacts the Conformational Stability of a PEG-Protein Conjugate. Acs Chemical Biology. PMID 27191252 DOI: 10.1021/Acschembio.6B00349 |
0.466 |
|
2014 |
Lawrence PB, Gavrilov Y, Matthews SS, Langlois MI, Shental-Bechor D, Greenblatt HM, Pandey BK, Smith MS, Paxman R, Torgerson CD, Merrell JP, Ritz CC, Prigozhin MB, Levy Y, Price JL. Criteria for selecting PEGylation sites on proteins for higher thermodynamic and proteolytic stability. Journal of the American Chemical Society. 136: 17547-60. PMID 25409346 DOI: 10.1021/Ja5095183 |
0.465 |
|
2014 |
Pandey BK, Smith MS, Price JL. Cys(i)-Lys(i+3)-Lys(i+4) triad: a general approach for PEG-based stabilization of α-helical proteins. Biomacromolecules. 15: 4643-7. PMID 25387132 DOI: 10.1021/Bm501546K |
0.497 |
|
2014 |
Chao SH, Matthews SS, Paxman R, Aksimentiev A, Gruebele M, Price JL. Two structural scenarios for protein stabilization by PEG. The Journal of Physical Chemistry. B. 118: 8388-95. PMID 24821319 DOI: 10.1021/Jp502234S |
0.472 |
|
2014 |
Chao S, Price J, Aksimentiev A, Gruebele M. How Pegylation Stabilizes a Protein Biophysical Journal. 106: 667a. DOI: 10.1016/J.Bpj.2013.11.3693 |
0.464 |
|
2013 |
Pandey BK, Enck S, Price JL. Stabilizing impact of N-glycosylation on the WW domain depends strongly on the Asn-GlcNAc linkage. Acs Chemical Biology. 8: 2140-4. PMID 23937634 DOI: 10.1021/Cb4004496 |
0.435 |
|
2013 |
Chen W, Enck S, Price JL, Powers DL, Powers ET, Wong CH, Dyson HJ, Kelly JW. Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins. Journal of the American Chemical Society. 135: 9877-84. PMID 23742246 DOI: 10.1021/Ja4040472 |
0.718 |
|
2013 |
Pandey BK, Smith MS, Torgerson C, Lawrence PB, Matthews SS, Watkins E, Groves ML, Prigozhin MB, Price JL. Impact of site-specific PEGylation on the conformational stability and folding rate of the Pin WW domain depends strongly on PEG oligomer length. Bioconjugate Chemistry. 24: 796-802. PMID 23578107 DOI: 10.1021/Bc3006122 |
0.49 |
|
2013 |
Enck S, Chen W, Price J, Powers E, Wong C, Dyson H, Kelly J. NMR solution structure of Pin1 WW domain mutant 5-1g Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2M9E/Pdb |
0.705 |
|
2012 |
Price JL, Culyba EK, Chen W, Murray AN, Hanson SR, Wong CH, Powers ET, Kelly JW. N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability. Biopolymers. 98: 195-211. PMID 22782562 DOI: 10.1002/Bip.22030 |
0.756 |
|
2012 |
Price JL, Shental-Bechor D, Dhar A, Turner MJ, Powers ET, Gruebele M, Levy Y, Kelly JW. Correction to Context-Dependent Effects of Asparagine Glycosylation on Pin WW Folding Kinetics and Thermodynamics. Journal of the American Chemical Society. 134: 4450-4451. PMID 22500055 DOI: 10.1021/Ja300899D |
0.671 |
|
2011 |
Price JL, Powers ET, Kelly JW. N-PEGylation of a reverse turn is stabilizing in multiple sequence contexts, unlike N-GlcNAcylation. Acs Chemical Biology. 6: 1188-92. PMID 21939258 DOI: 10.1021/Cb200277U |
0.704 |
|
2011 |
Price JL, Powers DL, Powers ET, Kelly JW. Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts. Proceedings of the National Academy of Sciences of the United States of America. 108: 14127-32. PMID 21825145 DOI: 10.1073/Pnas.1105880108 |
0.723 |
|
2011 |
Bourgault S, Choi S, Buxbaum JN, Kelly JW, Price JL, Reixach N. Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs. Biochemical and Biophysical Research Communications. 410: 707-13. PMID 21557933 DOI: 10.1016/J.Bbrc.2011.04.133 |
0.721 |
|
2011 |
Culyba EK, Price JL, Hanson SR, Dhar A, Wong CH, Gruebele M, Powers ET, Kelly JW. Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science (New York, N.Y.). 331: 571-5. PMID 21292975 DOI: 10.1126/Science.1198461 |
0.722 |
|
2011 |
Bourgault S, Choi S, Buxbaum JN, Kelly JW, Price JL, Reixach N. Erratum to “Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs” [Biochem. Biophys. Res. Commun. 410 (2011) 707–713] Biochemical and Biophysical Research Communications. 412: 196. DOI: 10.1016/J.Bbrc.2011.07.093 |
0.712 |
|
2010 |
Price JL, Shental-Bechor D, Dhar A, Turner MJ, Powers ET, Gruebele M, Levy Y, Kelly JW. Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics. Journal of the American Chemical Society. 132: 15359-67. PMID 20936810 DOI: 10.1021/Ja106896T |
0.73 |
|
2010 |
Price JL, Horne WS, Gellman SH. Structural consequences of beta-amino acid preorganization in a self-assembling alpha/beta-peptide: fundamental studies of foldameric helix bundles. Journal of the American Chemical Society. 132: 12378-87. PMID 20718422 DOI: 10.1021/Ja103543S |
0.696 |
|
2010 |
Wiseman RL, Zhang Y, Lee KP, Harding HP, Haynes CM, Price J, Sicheri F, Ron D. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Molecular Cell. 38: 291-304. PMID 20417606 DOI: 10.1016/J.Molcel.2010.04.001 |
0.67 |
|
2010 |
Price JL, Hadley EB, Steinkruger JD, Gellman SH. Detection and analysis of chimeric tertiary structures by backbone thioester exchange: packing of an alpha helix against an alpha/beta-peptide helix. Angewandte Chemie (International Ed. in English). 49: 368-71. PMID 19967682 DOI: 10.1002/Anie.200904714 |
0.727 |
|
2009 |
Solomon JP, Yonemoto IT, Murray AN, Price JL, Powers ET, Balch WE, Kelly JW. The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic. Biochemistry. 48: 11370-80. PMID 19904968 DOI: 10.1021/Bi901368E |
0.661 |
|
2008 |
Horne WS, Price JL, Gellman SH. Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly. Proceedings of the National Academy of Sciences of the United States of America. 105: 9151-6. PMID 18587049 DOI: 10.1073/Pnas.0801135105 |
0.712 |
|
2008 |
Horne WS, Price JL, Gellman SH. Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly (Proceedings of the National Academy of Sciences of the United States of America (2008) 105, (9151-9156) DOI: 10.1073/pnas.0801135105) Proceedings of the National Academy of Sciences of the United States of America. 105: 17205. DOI: 10.1073/pnas.0808591105 |
0.449 |
|
2007 |
Price JL, Horne WS, Gellman SH. Discrete heterogeneous quaternary structure formed by alpha/beta-peptide foldamers and alpha-peptides. Journal of the American Chemical Society. 129: 6376-7. PMID 17465552 DOI: 10.1021/Ja071203R |
0.713 |
|
2007 |
Horne WS, Price JL, Keck JL, Gellman SH. Helix bundle quaternary structure from alpha/beta-peptide foldamers. Journal of the American Chemical Society. 129: 4178-80. PMID 17362016 DOI: 10.1021/Ja070396F |
0.693 |
|
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