Joshua L. Price, Ph.D. - Publications

Area:
Chemical Biology

38 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2006 Ziemer SP, Niederhauser TL, Price JL, Woolley EM. Thermodynamics of proton dissociations from aqueous alanine at temperatures from (278.15 to 393.15) K, molalities from (0.0075 to 1.0) mol · kg-1, and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of alanine, alaninium chloride, and sodium alaninate Journal of Chemical Thermodynamics. 38: 939-951. DOI: 10.1016/j.jct.2005.10.007  1
2006 Ziemer SP, Niederhauser TL, Merkley ED, Price JL, Sorenson EC, McRae BR, Patterson BA, Woolley EM. Thermodynamics of proton dissociations from aqueous serine at temperatures from (278.15 to 393.15) K, molalities from (0.01 up to 1.0) mol · kg-1, and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of serine, serinium chloride, and sodium serinate Journal of Chemical Thermodynamics. 38: 634-648. DOI: 10.1016/j.jct.2005.07.019  1
2006 Ziemer SP, Niederhauser TL, Merkley ED, Price JL, Sorenson EC, McRae BR, Patterson BA, Origlia-Luster ML, Woolley EM. Thermodynamics of proton dissociations from aqueous glycine at temperatures from 278.15 to 393.15 K, molalities from 0 to 1.0 mol·kg-1, and at the pressure 0.35 MPa: Apparent molar heat capacities and apparent molar volumes of glycine, glycinium chloride, and sodium glycinate Journal of Chemical Thermodynamics. 38: 467-483. DOI: 10.1016/j.jct.2005.06.017  1
2004 Seo Y, Ko J, Price JL. The determinants of job satisfaction among hospital nurses: a model estimation in Korea. International Journal of Nursing Studies. 41: 437-46. PMID 15050854 DOI: 10.1016/j.ijnurstu.2003.11.003  0.48
2003 Chu CI, Hsu HM, Price JL, Lee JY. Job satisfaction of hospital nurses: an empirical test of a causal model in Taiwan. International Nursing Review. 50: 176-82. PMID 12930286 DOI: 10.1046/j.1466-7657.2003.00165.x  0.48
2003 Price JL, Sorenson EC, Merkley ED, McRae BR, Woolley EM. Thermodynamics of proton dissociations from aqueous L-valine and L-2-amino-n-butanoic acid: Apparent molar volumes and apparent molar heat capacities of the protonated cationic, neutral zwitterionic, and deprotonated anionic species at temperatures from 278.15 ≤ T/K ≤ 393.15, at molalities 0.015 ≤ m/mol · kg-1 ≤ 0.67, and pressure p = 0.35 MPa Journal of Chemical Thermodynamics. 35: 1425-1467. DOI: 10.1016/S0021-9614(03)00113-7  1
2003 Sorenson EC, Price JL, McRae BR, Woolley EM. Thermodynamics of proton dissociations from aqueous L-proline: Apparent molar volumes and apparent molar heat capacities of the protonated cationic, zwitterionic, and deprotonated anionic forms at temperatures from 278.15 K to 393.15 K and at the pressure 0.35 MPa Journal of Chemical Thermodynamics. 35: 529-553. DOI: 10.1016/S0021-9614(02)00375-0  1
2003 Origlia-Luster ML, Ballerat-Busserolles K, Merkley ED, Price JL, McRae BR, Woolley EM. Apparent molar volumes and apparent molar heat capacities of aqueous phenol and sodium phenolate at temperatures from 278.15 to 393.15 K and at the pressure 0.35 MPa Journal of Chemical Thermodynamics. 35: 331-347. DOI: 10.1016/S0021-9614(02)00373-7  1
2001 Price JL. Reflections on the determinants of voluntary turnover International Journal of Manpower. 22: 600-624. DOI: 10.1108/EUM0000000006233  0.48
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