Research graph
References from Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1080/17460441.2018.1403419
10.1080/17460441.2018.1403419 · External reference
Recent progress in molecular simulation methods for drug binding kinetics
10.1016/j.sbi.2020.06.022 · 2020 · External reference
10.1016/j.csbj.2019.07.010 · Admitted local publication
Visualizing protein folding and unfolding
10.1016/j.jmb.2019.02.026 · 2019 · External reference
10.1126/science.1208351
10.1126/science.1208351 · External reference
10.1002/prot.25759
10.1002/prot.25759 · External reference
10.1073/pnas.1811364115
10.1073/pnas.1811364115 · External reference
The role of post-translational modifications on the energy landscape of Huntingtin N-terminus
10.3389/fmolb.2019.00095 · 2019 · External reference
10.1016/j.bpj.2016.07.011
10.1016/j.bpj.2016.07.011 · External reference
10.1021/jp4126705
10.1021/jp4126705 · External reference
Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding
10.1021/jp209302e · 2012 · External reference
10.1021/ja211115q
10.1021/ja211115q · External reference
10.1021/acs.chemrev.8b00460
10.1021/acs.chemrev.8b00460 · External reference
Signal sensing and transduction by histidine kinases as unveiled through studies on a temperature sensor
10.1021/acs.accounts.6b00593 · 2017 · External reference
10.1111/mmi.13118
10.1111/mmi.13118 · External reference
Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding
10.1038/srep10549 · 2015 · External reference
10.1021/ct500718s
10.1021/ct500718s · External reference
Are current atomistic force fields accurate enough to study proteins in crowded environments?
10.1371/journal.pcbi.1003638 · 2014 · External reference
10.1021/ct501178z
10.1021/ct501178z · External reference
10.1021/ct500569b
10.1021/ct500569b · External reference
Comparison and evaluation of force fields for intrinsically disordered proteins
10.1021/acs.jcim.0c00762 · 2020 · External reference
Residue-specific force field improving the sample of intrinsically disordered proteins and folded proteins
10.1021/acs.jcim.9b00647 · 2019 · External reference
10.1111/cbdd.12314
10.1111/cbdd.12314 · External reference
Unresolved reference
2017 · External reference
The IDP-specific force field ff14IDPSFF improves the conformer sampling of intrinsically disordered proteins
10.1021/acs.jcim.7b00135 · 2017 · External reference
10.1038/nmeth.4067
10.1038/nmeth.4067 · External reference
ff19SB: amino-acid-specific protein backbone parameters trained against quantum mechanics energy surfaces in solution
10.1021/acs.jctc.9b00591 · 2019 · External reference
Developing a molecular dynamics force field for both folded and disordered protein states
10.1073/pnas.1800690115 · 2018 · External reference
10.1021/acs.jcim.0c01175
10.1021/acs.jcim.0c01175 · External reference
10.1016/j.sbi.2017.10.008
10.1016/j.sbi.2017.10.008 · External reference
Recent advances in atomic molecular dynamics simulation of intrinsically disordered proteins
10.1039/d0cp05818a · 2021 · External reference
10.1021/jp508971m
10.1021/jp508971m · External reference
10.1039/d0cp05484d
10.1039/d0cp05484d · External reference
10.1021/acs.jctc.5b00736
10.1021/acs.jctc.5b00736 · External reference
New developments in force fields for biomolecular simulations
10.1016/j.sbi.2018.02.002 · 2018 · External reference
10.1021/acs.jctc.5b00255
10.1021/acs.jctc.5b00255 · External reference
10.1021/acs.jctc.9b00251
10.1021/acs.jctc.9b00251 · External reference
10.1021/acs.jctc.8b01123
10.1021/acs.jctc.8b01123 · External reference
Thermodynamics of ubiquitin unfolding
10.1002/prot.340180305 · 1994 · External reference
10.1002/anie.201106190
10.1002/anie.201106190 · External reference
10.1021/la1034273
10.1021/la1034273 · External reference
Different force fields give rise to different amyloid aggregation pathways in molecular dynamics simulations
10.1021/acs.jcim.0c01063 · 2020 · External reference
10.1016/j.sbi.2020.10.019
10.1016/j.sbi.2020.10.019 · External reference
Mutant Exon1 Huntingtin aggregation is regulated by T3 phosphorylation-induced structural changes and crosstalk between T3 phosphorylation and acetylation at K6
10.1002/anie.201611750 · 2017 · External reference
Site-specific phosphorylation of Huntingtin exon 1 recombinant proteins enabled by the discovery of novel kinases
2020 · External reference
Structure and dynamics of the huntingtin Exon-1 N-terminus: a solution NMR perspective
10.1021/jacs.6b10893 · 2017 · External reference
10.1016/j.jmb.2018.03.031
10.1016/j.jmb.2018.03.031 · External reference
Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues
10.4161/pri.23807 · 2013 · External reference
Processing of the β-amyloid precursor protein and its regulation in Alzheimer’s disease
10.1046/j.1471-4159.1995.65041431.x · 1995 · External reference
10.1126/science.1105850
10.1126/science.1105850 · External reference
10.1073/pnas.1111305109
10.1073/pnas.1111305109 · External reference
10.1021/acs.jctc.0c00057
10.1021/acs.jctc.0c00057 · External reference
Polarizable atomic multipole-based AMOEBA force field for proteins
10.1021/ct4003702 · 2013 · External reference
10.1002/jcc.26067
10.1002/jcc.26067 · External reference
Polarizable force fields for biomolecular simulations: recent advances and applications
10.1146/annurev-biophys-070317-033349 · 2019 · External reference
10.1016/j.sbi.2019.12.012
10.1016/j.sbi.2019.12.012 · External reference
10.1021/ct500223p
10.1021/ct500223p · External reference