Published in J Phys Chem B on June 24, 2010
Probing the effect of conformational constraint on phosphorylated ligand binding to an SH2 domain using polarizable force field simulations. J Phys Chem B (2012) 0.96
Bridging Calorimetry and Simulation through Precise Calculations of Cucurbituril-Guest Binding Enthalpies. J Chem Theory Comput (2014) 0.88
Computational Calorimetry: High-Precision Calculation of Host-Guest Binding Thermodynamics. J Chem Theory Comput (2015) 0.86
Calculating binding free energies of host-guest systems using the AMOEBA polarizable force field. Phys Chem Chem Phys (2016) 0.75
Classification of intrinsically disordered regions and proteins. Chem Rev (2014) 2.48
Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci U S A (2010) 2.16
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci U S A (2009) 2.14
NanoParticle Ontology for cancer nanotechnology research. J Biomed Inform (2010) 2.07
Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc Natl Acad Sci U S A (2006) 2.00
Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc Natl Acad Sci U S A (2013) 1.71
Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins. J Am Chem Soc (2008) 1.63
ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions. J Comput Chem (2009) 1.57
Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophys J (2007) 1.53
Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell (2011) 1.49
Characterizing the conformational ensemble of monomeric polyglutamine. Proteins (2006) 1.49
Role of solvent in determining conformational preferences of alanine dipeptide in water. J Am Chem Soc (2004) 1.46
Structural biology. Versatility from protein disorder. Science (2012) 1.46
Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. J Mol Biol (2008) 1.43
A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch Biochem Biophys (2007) 1.41
Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proc Natl Acad Sci U S A (2013) 1.39
Parameters of monovalent ions in the AMBER-99 forcefield: assessment of inaccuracies and proposed improvements. J Phys Chem B (2007) 1.31
Quantitative characterization of ion pairing and cluster formation in strong 1:1 electrolytes. J Phys Chem B (2007) 1.31
Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. J Mol Biol (2009) 1.30
Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins. Biochemistry (2005) 1.23
Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions. Biophys J (2006) 1.21
Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides. Biophys Chem (2011) 1.13
Thermodynamics of beta-sheet formation in polyglutamine. Biophys J (2009) 1.07
Simulations of RNA interactions with monovalent ions. Methods Enzymol (2009) 1.04
Molecular simulation studies of monovalent counterion-mediated interactions in a model RNA kissing loop. J Mol Biol (2009) 1.04
Describing sequence-ensemble relationships for intrinsically disordered proteins. Biochem J (2013) 1.00
Analysis of the conformational dependence of mass-metric tensor determinants in serial polymers with constraints. J Chem Phys (2004) 0.98
Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proc Natl Acad Sci U S A (2013) 0.96
Methods for Monte Carlo simulations of biomacromolecules. Annu Rep Comput Chem (2009) 0.94
N-terminal segments modulate the α-helical propensities of the intrinsically disordered basic regions of bZIP proteins. J Mol Biol (2011) 0.93
Ontologies for cancer nanotechnology research. Conf Proc IEEE Eng Med Biol Soc (2009) 0.92
Disordered binding of small molecules to Aβ(12-28). J Biol Chem (2011) 0.90
Unmasking functional motifs within disordered regions of proteins. Sci Signal (2012) 0.89
A quantitative measure for protein conformational heterogeneity. J Chem Phys (2013) 0.88
The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry (2013) 0.85
Crystal lattice properties fully determine short-range interaction parameters for alkali and halide ions. J Chem Phys (2012) 0.84
Satisfying the fluctuation theorem in free-energy calculations with Hamiltonian replica exchange. Phys Rev E Stat Nonlin Soft Matter Phys (2008) 0.83
Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. J Am Chem Soc (2015) 0.83
How is functional specificity achieved through disordered regions of proteins? Bioessays (2012) 0.82
Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies. Chembiochem (2009) 0.82
Improved atomistic Monte Carlo simulations demonstrate that poly-L-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks. J Phys Chem B (2012) 0.82
Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry (2013) 0.80
Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. J Am Chem Soc (2016) 0.77