J. L. Price

发表

Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides.

S. Castle, J. Price, D. Kastner, 2017, Organic letters.

Exploring Pathways and Transitions between Juvenile and Adult Penal Institutions

J. Price, J. L. Price, 2019 .

Long-range PEG stapling: macrocyclization for increased protein conformational stability and resistance to proteolysis

Q. Xiao, J. Price, D. Ashton, 2020, RSC chemical biology.

Context-dependent stabilizing interactions among solvent-exposed residues along the surface of a trimeric helix bundle.

J. Price, Dennis Della Corte, W. M. Billings, 2020, Biochemistry.

Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids.

F. Whitby, J. Price, W. M. Billings, 2017, Organic & biomolecular chemistry.

Helix bundle quaternary structure from alpha/beta-peptide foldamers.

W Seth Horne, S. Gellman, J. Keck, 2007, Journal of the American Chemical Society.

Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect.

Q. Xiao, J. Price, K. L. Stern, 2018, Organic & biomolecular chemistry.

How PEGylation influences protein conformational stability.

J. Price, P. B. Lawrence, J. L. Price, 2016, Current opinion in chemical biology.

Impact of site-specific PEGylation on the conformational stability and folding rate of the Pin WW domain depends strongly on PEG oligomer length.

Maxim B. Prigozhin, S. S. Matthews, J. Price, 2013, Bioconjugate chemistry.

N-PEGylation of a reverse turn is stabilizing in multiple sequence contexts, unlike N-GlcNAcylation.

J. Kelly, E. Powers, J. Price, 2011, ACS chemical biology.

Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts

J. Kelly, E. Powers, J. Price, 2011, Proceedings of the National Academy of Sciences.

Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns

Chi-Huey Wong, Martin Gruebele, M. Gruebele, 2011, Science.

Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.

M. Gruebele, J. Kelly, E. Powers, 2010, Journal of the American Chemical Society.

Criteria for selecting PEGylation sites on proteins for higher thermodynamic and proteolytic stability.

Maxim B. Prigozhin, Minnie I Langlois, Y. Levy, 2014, Journal of the American Chemical Society.

Stabilizing impact of N-glycosylation on the WW domain depends strongly on the Asn-GlcNAc linkage.

Sebastian Enck, J. Price, B. K. Pandey, 2013, ACS chemical biology.

Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1.

F. Sicheri, Cole M. Haynes, D. Ron, 2010, Molecular cell.

Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs.

J. Kelly, Sungwook Choi, S. Bourgault, 2011, Biochemical and biophysical research communications.

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.

J. Kelly, E. Powers, W. Balch, 2009, Biochemistry.

Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins.

H. Dyson, Chi‐Huey Wong, Wentao Chen, 2013, Journal of the American Chemical Society.

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.

E. Powers, W. Balch, Isaac T. Yonemoto, 2009, Biochemistry.

Detection and analysis of chimeric tertiary structures by backbone thioester exchange: packing of an alpha helix against an alpha/beta-peptide helix.

S. Gellman, E. B. Hadley, Jay D. Steinkruger, 2010, Angewandte Chemie.

Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts

E. Powers, D. Powers, J. L. Price, 2011, Proceedings of the National Academy of Sciences.

Stabilizing impact of N-glycosylation on the WW domain depends strongly on the Asn-GlcNAc linkage.

Sebastian Enck, B. K. Pandey, J. L. Price, 2013, ACS chemical biology.

Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.

M. Gruebele, E. Powers, Y. Levy, 2010, Journal of the American Chemical Society.

Substance use and temporary assistance for needy families

J. Price, J. L. Price, 2016 .

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly

S. Gellman, J. L. Price, W. Horne, 2008, Proceedings of the National Academy of Sciences.

Substance use and participation in Temporary Assistance for Needy Families: the role of unobserved heterogeneity

J. Bray, J. L. Price, C. Swann, 2022, Journal of Substance Use.

Conjugation Strategy Strongly Impacts the Conformational Stability of a PEG-Protein Conjugate.

Minnie I Langlois, J. Price, B. K. Pandey, 2016, ACS Chemical Biology.

PEGylation near a patch of non-polar surface residues increases the conformational stability of the WW domain.

Q. Xiao, J. Price, A. J. Carter, 2019, The Journal of organic chemistry.

Influence of PEGylation on the strength of protein surface salt bridges.

Q. Xiao, J. Price, A. J. Carter, 2019, ACS chemical biology.

Polyethylene Glycol Based Changes to β-Sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location.

Q. Xiao, J. Price, P. B. Lawrence, 2017, Bioconjugate chemistry.

PEG-based Changes to β -sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location

J. Price, Brown, P. Nathaniel, 2019 .