Feng Ding

Orcid: 0000-0003-1850-6336

Affiliations:
  • Clemson University, Department of Chemical and Biomolecular Engineering, SC, USA
  • University of North Carolina, Department of Biochemistry and Biophysics, Chapel Hill, NC, USA (former)


According to our database1, Feng Ding authored at least 26 papers between 2005 and 2024.

Collaborative distances:
  • Dijkstra number2 of five.
  • Erdős number3 of four.

Timeline

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Bibliography

2024
Computational insights into the cross-talk between medin and A<i>β</i>: implications for age-related vascular risk factors in Alzheimer's disease.
Briefings Bioinform., January, 2024

Uncovering Intermolecular Interactions Driving the Liquid-Liquid Phase Separation of the TDP-43 Low-Complexity Domain via Atomistic Dimerization Simulations.
J. Chem. Inf. Model., 2024

Deciphering the Morphological Difference of Amyloid-β Fibrils in Familial and Sporadic Alzheimer's Diseases.
J. Chem. Inf. Model., 2024

Molecular Insights into the Effects of F16L and F19L Substitutions on the Conformation and Aggregation Dynamics of Human Calcitonin.
J. Chem. Inf. Model., 2024

Computational Investigation of Coaggregation and Cross-Seeding between Aβ and hIAPP Underpinning the Cross-Talk in Alzheimer's Disease and Type 2 Diabetes.
J. Chem. Inf. Model., 2024

2023
Unveiling Medin Folding and Dimerization Dynamics and Conformations via Atomistic Discrete Molecular Dynamics Simulations.
J. Chem. Inf. Model., October, 2023

Direct Observation of Seeded Conformational Conversion of hIAPP <i>In Silico</i> Reveals the Mechanisms for Morphological Dependence and Asymmetry of Fibril Growth.
J. Chem. Inf. Model., September, 2023

SEVI Inhibits Aβ Amyloid Aggregation by Capping the β-Sheet Elongation Edges.
J. Chem. Inf. Model., June, 2023

Dissecting the Self-assembly Dynamics of Imperfect Repeats in α-Synuclein.
J. Chem. Inf. Model., June, 2023

Structural Perturbation of Monomers Determines the Amyloid Aggregation Propensity of Calcitonin Variants.
J. Chem. Inf. Model., 2023

2022
Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation.
J. Chem. Inf. Model., 2022

2021
Direct Observation of β-Barrel Intermediates in the Self-Assembly of Toxic SOD128-38 and Absence in Nontoxic Glycine Mutants.
J. Chem. Inf. Model., 2021

Misfolding and Self-Assembly Dynamics of Microtubule-Binding Repeats of the Alzheimer-Related Protein Tau.
J. Chem. Inf. Model., 2021

2016
CSAR Benchmark of Flexible MedusaDock in Affinity Prediction and Nativelike Binding Pose Selection.
J. Chem. Inf. Model., 2016

2014
Structural and energetic determinants of tyrosylprotein sulfotransferase sulfation specificity.
Bioinform., 2014

2013
Predicting Binding Affinity of CSAR Ligands Using Both Structure-Based and Ligand-Based Approaches.
J. Chem. Inf. Model., 2013

Incorporating Backbone Flexibility in MedusaDock Improves Ligand-Binding Pose Prediction in the CSAR2011 Docking Benchmark.
J. Chem. Inf. Model., 2013

2011
Gaia: automated quality assessment of protein structure models.
Bioinform., 2011

2010
Polyglutamine Induced Misfolding of Huntingtin Exon1 is Modulated by the Flanking Sequences.
PLoS Comput. Biol., 2010

Rapid Flexible Docking Using a Stochastic Rotamer Library of Ligands.
J. Chem. Inf. Model., 2010

2008
Active Nuclear Receptors Exhibit Highly Correlated AF-2 Domain Motions.
PLoS Comput. Biol., 2008

iFoldRNA: three-dimensional RNA structure prediction and folding.
Bioinform., 2008

2006
Correction: Emergence of Protein Fold Families through Rational Design.
PLoS Comput. Biol., 2006

Emergence of Protein Fold Families through Rational Design.
PLoS Comput. Biol., 2006

iFold: a platform for interactive folding simulations of proteins.
Bioinform., 2006

2005
Molecular Origin of Polyglutamine Aggregation in Neurodegenerative Diseases.
PLoS Comput. Biol., 2005


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